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{=0A= document.writeln('

3D"Click

');=0A= }=0A= =0A= function get_text_link(url, linktext)=0A= {=0A= document.writeln('' + = linktext + '');=0A= }=0A= =0A= function get_htmlftext_link(a, b) {=0A= document.writeln("" + = b + ", ");=0A= }=0A= =0A= ------=_NextPart_000_0000_01C99A9C.1FB151E0 Content-Type: application/octet-stream Content-Transfer-Encoding: quoted-printable Content-Location: http://www3.interscience.wiley.com/freeflow/js/personalisation.js /*=0A= * Project : Interscience Redesign=0A= * File : personalisation.js=0A= * Creation Date : 25th March 2003=0A= * Author : Jonathan Sugar=0A= *=0A= * Various functions to deliver personalisation functionality.=0A= */=0A= =0A= // Pre-declare userName so it's available when we need to test if the = page=0A= // assembler ran OK=0A= var userName =3D null;=0A= var shcrtCookie =3D null;=0A= =0A= // Browser detect globals:=0A= var uaStr =3D navigator.userAgent.toLowerCase();=0A= var uaVer =3D parseInt(navigator.appVersion);=0A= // for detecting netscape 4=0A= var netscape =3D (uaStr.indexOf("mozilla") > -1);=0A= var netscape4 =3D (netscape && uaVer < 5);=0A= =0A= // Factory Methods=0A= =0A= // Simple wraper object to encapsulate the data for a co-branding item.=0A= function coBrandingItem(image, imageAltText, href)=0A= {=0A= //alert("Making new coBrandingItem:\nImage: " + image + = "\nimageAltText" + imageAltText + "\nhref: " + href);=0A= this.image =3D image;=0A= this.imageAltText =3D imageAltText;=0A= this.href =3D href;=0A= }=0A= =0A= /*=0A= * Insert the 'Customer co-branding' section.=0A= * -----------------------------=0A= *=0A= * Author: Jonathan Sugar, March 2003.=0A= *=0A= * 1. Insert customer co branding. Loop through 'customerCoBranding' array=0A= * inserting XHTML where needed.=0A= *=0A= * NOTE: the array contains ONLY the resource location (the location of a = gif=0A= * on the file system), the required XHTML is then added where needed. = This way=0A= * we maintain the seperation between presentation and content.=0A= */=0A= function insertCustomerCoBranding(maxBranding)=0A= {=0A= if( customerCoBranding[0].image !=3D "none")=0A= {=0A= document.writeln('

');=0A= document.writeln('

');=0A= document.writeln('

' + imageAltText + '
' + imageAltText + = '
More Providers

');=0A= document.writeln('

');=0A= document.writeln('

3D""

');=0A= }=0A= }=0A= =0A= /*=0A= * Insert the 'My Area' section.=0A= * -----------------------------=0A= *=0A= * Author: Jonathan Sugar, March 2003.=0A= * Updated: Ben Marvell, April 2006=0A= *=0A= * My profile link absolute as this file isnt only run from w3 anymore.=0A= */=0A= function insertMyArea(userdata)=0A= {=0A= // just in case the page assembler isn't running.=0A= =0A= =0A= if (userName !=3D null)=0A= {=0A= document.writeln("

" + = userName.substring(0,33) + "..., access your
" + userName + = ", access your

My Profile"); =0A= } =0A= document.writeln(getLoginOutLink());=0A= //CR 3652 getAthenStatus() as added=0A= document.writeln(getAthenStatus());=0A= document.writeln("

");=0A= } else {=0A= if(typeof(environment)!=3D'undefined' && = environment=3D=3D'PRODUCTION') {=0A= document.writeln("

Log Out");=0A= document.writeln("

"); =0A= }=0A= }=0A= if (menuloadedflag){=0A= wisMenu();=0A= }=0A= }=0A= =0A= /*=0A= * Insert the Customer Admin 'Login/Logout' link=0A= * -----------------------------=0A= *=0A= * Author: Bobby Jack, December 2004.=0A= *=0A= */=0A= function insertAdminLink(page)=0A= {=0A= val =3D getCookie("AID");=0A= =0A= if (val && val !=3D "-1")=0A= {=0A= document.writeln('

Logout');=0A= }=0A= else=0A= {=0A= document.writeln('

');=0A= }=0A= }=0A= =0A= /*=0A= * Insert the username section.=0A= * -----------------------------=0A= *=0A= * Author: Jonathan Sugar, March 2003.=0A= *=0A= * 1. Insert the username.=0A= */=0A= function insertUserName()=0A= {=0A= document.write(userName);=0A= }=0A= =0A= /*=0A= * Return the appropriate link to the login/logout cgi=0A= * ---------------------------------------------------=0A= *=0A= * Author: Jonathan Sugar, March 2003.=0A= * Updated: Ben Marvell, April 2006=0A= * Had to change the links absolute as this file isnt only run from w3 = anymore.=0A= */=0A= function getLoginOutLink()=0A= {=0A= if(userName !=3D "")=0A= {=0A= return "

";=0A= }else=0A= {=0A= return "

";=0A= }=0A= }=0A= =0A= /*=0A= * Return the appropriate link to the shopping cart content page=0A= * ---------------------------------------------------=0A= *=0A= * Author: Zhiming & Warrell June 2007=0A= */=0A= function getShCrtLink(logged)=0A= {=0A= if(logged =3D=3D true )=0A= return "

";=0A= else=0A= return "

";=0A= }=0A= =0A= function toggleShCrtLink()=0A= {=0A= shcrtCookie =3D readCookie("SHCRT");=0A= if(shcrtCookie !=3D null)=0A= {=0A= if(document.all)=0A= {=0A= return true;=0A= }=0A= else=0A= {=0A= document.getElementById("shcrt_id").style.display =3D "block";=0A= }=0A= }=0A= else=0A= {=0A= if(document.all)=0A= {=0A= return true;=0A= }=0A= else=0A= {=0A= document.getElementById("shcrt_id").style.display =3D "none";=0A= }=0A= }=0A= }=0A= =0A= =0A= =0A= function readCookie(name)=0A= {=0A= var nameEQ =3D name + "=3D";=0A= var ca =3D document.cookie.split(';');=0A= for(var i=3D0; iYou are logged in = to Athens';=0A= }=0A= else=0A= {=0A= return "

";=0A= }=0A= =0A= } ------=_NextPart_000_0000_01C99A9C.1FB151E0 Content-Type: application/octet-stream Content-Transfer-Encoding: quoted-printable Content-Location: http://www3.interscience.wiley.com/freeflow/js/site.js /************************************************************************= ***************************=0A= FILE: site.js=0A= AUTHOR: Jonathan Sugar, Chris Neatby-Smith and Digital Pulp. July = 2003.=0A= =0A= DESCRIPTION: Javascript relating to site wide functionality across =0A= InterScience.=0A= =0A= INCLUDES FUNCTIONS=0A= =3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=0A= =0A= Search Functions=0A= ----------------=0A= =0A= selectAndSubmit() - for deciding where to submit a query based on the = state of the form.=0A= processallContentSearch() - for validating form input for an all = content search.=0A= processTitleSearch() - for validating form input for a Title search.=0A= checkCitationSearch() - for validating the citation search form.=0A= selectAll() - check all the checkboxes in a form.=0A= do_popup() - stasa Acronym Finder window popup function.=0A= =0A= =0A= Other Functions=0A= ---------------=0A= =0A= fixInlineLists() - fix netscape 4.x bug where

tags with images = display both an image and=0A= the default bullet. =0A= =0A= = *************************************************************************= **************************/=0A= =0A= var http =3D false;=0A= if(navigator.appName =3D=3D "Microsoft Internet Explorer") {=0A= http =3D new ActiveXObject("Microsoft.XMLHTTP");=0A= } else {=0A= http =3D new XMLHttpRequest();=0A= } =0A= =0A= // Global Variables=0A= var debug =3D false;=0A= var first =3D true;=0A= =0A= // Browser detect globals:=0A= var uaStr =3D navigator.userAgent.toLowerCase();=0A= var uaVer =3D parseInt(navigator.appVersion);=0A= // for detecting netscape 4=0A= var netscape =3D (uaStr.indexOf("mozilla") > -1);=0A= var netscape4 =3D (netscape && uaVer < 5);=0A= =0A= /*=0A= * Used to switch search mode between APS and TitleFinder on quicksearch = boxes=0A= * = -------------------------------------------------------------------------= --=0A= *=0A= * 1. Decides which search is required based on the value of the radio = buttons=0A= * in 'document.formSelector.whichForm'.=0A= *=0A= * 2. Calls individual functions to process the forms and submit them.=0A= *=0A= */=0A= function selectAndSubmit()=0A= {=0A= var formSelection;=0A= =0A= // find out which form we need to process.=0A= var selector =3D document.formSelector.whichForm;=0A= for (var i =3D 0; i < selector.length; i++){=0A= if (selector[i].checked){=0A= formSelection =3D selector[i].value;=0A= }=0A= }=0A= =0A= // Call the relevent function to process the required form.=0A= if(formSelection =3D=3D "allContentSearch"){=0A= processallContentSearch(document.allContentSearchForm, = document.formSelector)=0A= }=0A= else if(formSelection =3D=3D "searchTitles"){=0A= processTitleSearch(document.searchTitles, document.formSelector)=0A= }=0A= else{=0A= return false;=0A= }=0A= =0A= //@@@DM It was anoying me this error =0A= return false;=0A= }=0A= =0A= /*=0A= *Process the ADS search form=0A= *=0A= */=0A= function trim(str)=0A= {=0A= return str.replace(/(^\s*)|(\s*$)/g,"");=0A= }=0A= =0A= function ADSquery(t) {=0A= var keyword =3D trim(t.getElementsByTagName("input")[0].value);=0A= if (keyword!=3D"") {=0A= = window.open("","popup","toolbar=3Dyes,location=3Dyes,status=3Dyes,menubar= =3Dno,scrollbars=3Dyes,resizable=3Dyes,width=3D800,height=3D500");=0A= t.target=3D"popup";=0A= t.qsearch.value=3Dkeyword;=0A= return true;=0A= = //processADSSearch(document.ADSSearchForm,document.ADSQueryForm,keyword);=0A= } else {=0A= alert("Please input a keyword for ADS searching before clicking go");=0A= return false;=0A= }=0A= }=0A= /*=0A= function processADSSearch(hiddenForm ,queryForm , str) {=0A= var terms =3D str;=0A= var formToSubmit =3D hiddenForm;=0A= var formToProcess =3D queryForm;=0A= formToSubmit.qsearch.value =3D terms;=0A= = window.open("","popup","toolbar=3Dyes,location=3Dyes,status=3Dyes,menubar= =3Dno,scrollbars=3Dyes,resizable=3Dyes,width=3D800,height=3D500");=0A= formToSubmit.action =3D = "http://adsabs.harvard.edu/cgi-bin/nph-basic_connect"=0A= formToSubmit.target =3D "popup";=0A= formToSubmit.submit();=0A= }=0A= */=0A= =0A= /*=0A= * Process the allContentSearch form=0A= * ---------------------------------=0A= * 1. Perform form validation, checking for empty fields.=0A= * Give the user a relevent message if required.=0A= *=0A= * 2. Process/Assign the appropriate form elements and submit the form.=0A= */=0A= function processallContentSearch(hiddenForm, queryForm)=0A= {=0A= var formToSubmit =3D hiddenForm;=0A= var formToProcess =3D queryForm;=0A= =0A= // Do some basic form validation=0A= if(formToProcess.terms.value !=3D "")=0A= {=0A= formToSubmit.WISsearch1.value =3D formToProcess.terms.value;=0A= formToSubmit.submit(); =0A= }=0A= else=0A= {=0A= alert("You must enter a search term in the text box before you click = go.");=0A= }=0A= }=0A= =0A= /*=0A= * Process the Title Search form=0A= * -----------------------------=0A= * 1. Perform form validation, checking for empty fields.=0A= * Give the user a relevent message if required.=0A= *=0A= * 2. Process/Assign the appropriate form elements and submit the form.=0A= */=0A= =0A= function processTitleSearch(hiddenForm, queryForm)=0A= {=0A= var formToSubmit =3D hiddenForm;=0A= var formToProcess =3D queryForm;=0A= =0A= // Do some basic form validation=0A= if(formToProcess.terms.value !=3D "")=0A= {=0A= formToSubmit.query.value =3D formToProcess.terms.value;=0A= formToSubmit.submit();=0A= }=0A= else=0A= {=0A= alert("You must enter a search term in the text box before you click = go.");=0A= }=0A= }=0A= =0A= function doCitationSearch()=0A= {=0A= var form =3D document.citsearchform;=0A= if(checkCitationSearch())=0A= {=0A= form.action =3D "/search/allsearch";=0A= form.submit();=0A= }=0A= }=0A= =0A= // Preprocesses the arguments sent to CitationSearch and checks validity = of user inputs.=0A= function checkCitationSearch()=0A= {=0A= var supplementFound =3D 0; //increment if found;=0A= var hyphenFound =3D 0; //increment if found;=0A= var fm =3D document.citsearchform;=0A= var errmsg =3D "Please use the valid digits '0' to '9'";=0A= // remove all spaces=0A= fm.volume.value =3D fm.volume.value.replace(/ /g, "");=0A= fm.issue.value =3D fm.issue.value.replace(/ /g, "");=0A= fm.pages.value =3D fm.pages.value.replace(/ /g, "");=0A= =0A= if (fm.issn.value.length > 0 && fm.volume.value.length > 0 && = fm.pages.value.length > 0)=0A= {=0A= // check page range=0A= var pageRange =3D fm.pages.value;=0A= var volume =3D fm.volume.value;=0A= var issue =3D fm.issue.value;=0A= var continueFlag =3D 0;=0A= //check the volume=0A= // if (isNaN(volume))=0A= // {=0A= // // volume failed checking=0A= // alert("Volume is invalid. "+errmsg+".");=0A= // return false;=0A= // }=0A= //check the issue=0A= if ((issue.length !=3D 0) && isNaN(issue))=0A= {=0A= // issue failed checking=0A= alert("Issue is invalid. "+errmsg+" or leave blank.");=0A= return false;=0A= }=0A= //check the page range=0A= if (isNaN(pageRange))=0A= {=0A= var isValid =3D false;=0A= // check for hyphen=0A= var hyphenIndex =3D pageRange.indexOf("-");=0A= if ((hyphenIndex !=3D -1) && (hyphenIndex =3D=3D = pageRange.lastIndexOf("-")))=0A= {=0A= // we have only one hyphen, so extract each number=0A= var firstNum =3D pageRange.substring(0, hyphenIndex);=0A= var secondNum =3D pageRange.substring(hyphenIndex + 1);=0A= // check for S=0A= var firstS =3D firstNum.indexOf("S");=0A= var secondS =3D secondNum.indexOf("S");=0A= if (firstS =3D=3D secondS)=0A= {=0A= if ((firstS =3D=3D -1) && isNum(firstNum) && isNum(secondNum) && = (firstNum.length > 0) && (secondNum.length > 0))=0A= isValid =3D true; // both inputs are digits=0A= else if (firstS =3D=3D 0)=0A= {=0A= var firstNumNoS =3D firstNum.substring(1);=0A= var secondNumNoS =3D secondNum.substring(1);=0A= if (isNum(firstNumNoS) && isNum(secondNumNoS) && = (firstNumNoS.length > 0) && (secondNumNoS.length > 0))=0A= isValid =3D true; // both inputs are Sdigits=0A= }=0A= =0A= }=0A= }=0A= if (isValid)=0A= {=0A= return true;=0A= }=0A= else=0A= {=0A= alert("The page range is invalid. "+errmsg+" and a hyphen '-' if = required.");=0A= return false;=0A= }=0A= }=0A= return true;=0A= }=0A= else=0A= {=0A= alert("Volume and pages are required fields. Please make sure data has = been entered for both fields.");=0A= return false;=0A= }=0A= }=0A= =0A= // returns true if a is an Integer.=0A= function isNum(a)=0A= { return !(isNaN(a)); }=0A= =0A= function fixInlineLists() {=0A= if (!document.getElementById) return;=0A= var allLIs =3D document.getElementsByTagName('li');=0A= var bulletNode =3D document.createElement('img');=0A= bulletNode.src =3D"/images/icon.bullet.gif";=0A= =0A= for (var i=3D0; iAbstract | References';=0A= }=0A= //alert("URL: " + loc + "\nStart Index: " + startIndex + "\nEnd Index: = " + endIndex + "\nPage: " + page + "\nLink Text: " + links);=0A= return links;=0A= }=0A= =0A= =0A= function selectAll(fm)=0A= {=0A= //var fm =3D document.viewSelectedForm;=0A= =0A= for (var i =3D 0; i < fm.elements.length; i++)=0A= {=0A= if (fm.elements[i].type =3D=3D 'checkbox' /*&& fm.elements[i].name = =3D=3D 'ID'*/)=0A= {=0A= fm.elements[i].checked =3D true;=0A= }=0A= }=0A= }=0A= =0A= =0A= function do_popup(file)=0A= {=0A= var w =3D window.open(file, 'popWin', = 'width=3D350,height=3D500,scrollbars=3Dyes');=0A= =0A= }=0A= =0A= =0A= function mailTool(itemID, useurl, skin)=0A= {=0A= //var url =3D "/cgi-bin/mailform?item=3D"+itemID;=0A= var url =3D "/cgi-bin/mailform?item=3D" + itemID + "&skin=3D" + skin;=0A= var parameters =3D = 'status=3Dno,scrollbars=3Dno,resizable=3Dyes,width=3D400,height=3D475';=0A= =0A= if (useurl !=3D "")=0A= {=0A= url +=3D "&useurl=3D"+useurl;=0A= }=0A= =0A= if ((isNaN(parseInt(itemID))=3D=3Dtrue)||(arguments.length >=3D 4 && = arguments[3] =3D=3D 'cluster'))=0A= {=0A= url +=3D '&type=3Dcluster';=0A= }=0A= =0A= //check whether the last 2 arguments is used for urllink.=0A= // urllink is needed to open up mail form for mrw pages on tomcat = port=0A= if (arguments.length>=3D5 && = arguments[arguments.length-2]=3D=3D'urllink' && = arguments[arguments.length-1]!=3D'')=0A= {=0A= url =3D arguments[arguments.length-1] + url;=0A= }=0A= =0A= if (arguments.length>=3D5 && arguments[3]=3D=3D'currentlink' && = arguments[4]!=3D'')=0A= {=0A= url =3D url + '¤tLink=3D' + arguments[4];=0A= =0A= //processing specific cases=0A= if (arguments[4]=3D=3D'jcatalogjsphdr')=0A= {=0A= //get the issn and pass it the next stage for processing=0A= var currloc =3D location.href;=0A= var issnloc =3D currloc.indexOf("&issn=3D");=0A= if (issnloc !=3D -1)=0A= {=0A= url =3D url + '¤tISSN=3D' + = currloc.substring(issnloc+6);=0A= }=0A= }=0A= // issn is needed for cocoon rendered mrw to form the final url.=0A= else if ( (arguments[4]=3D=3D'cocoonmrwhome') || = (arguments[4]=3D=3D'cocoonmrwarticle') )=0A= {=0A= if (arguments.length>=3D7 && arguments[5]=3D=3D'issn' && = arguments[6]!=3D'')=0A= {=0A= url =3D url + '¤tISSN=3D' + arguments[6];=0A= }=0A= //getting the parameters of the currently shown mrw from the = url=0A= //the method used here is a little crude, it extracts the = values from the current url of the page the user is in =0A= //to pass it to the background program to reconstruct the = requred url=0A= if (arguments[4]=3D=3D'cocoonmrwhome')=0A= {=0A= var currloc =3D location.href;=0A= var mrwParamArr =3D currloc.split("/");=0A= if (mrwParamArr.length >=3D 7)=0A= {=0A= url =3D url + '&mrwPath=3D' + mrwParamArr[5];=0A= var mrwFileParam =3D mrwParamArr[6];=0A= var seploc =3D mrwFileParam.indexOf("#");=0A= if (seploc !=3D -1)=0A= {=0A= url =3D url + '&mrwSection=3D' + = mrwFileParam.substring(seploc+1);=0A= mrwFileParam =3D = mrwFileParam.substring(0,seploc);=0A= }=0A= seploc =3D mrwFileParam.indexOf("?");=0A= if (seploc !=3D -1)=0A= {=0A= url =3D url + '&mrwUrlParam=3D' + = mrwFileParam.substring(seploc+1);=0A= url =3D url + '&mrwDocType=3D' + = mrwFileParam.substring(0,seploc);=0A= }=0A= else=0A= {=0A= url =3D url + '&mrwDocType=3D' + mrwFileParam;=0A= }=0A= }=0A= =0A= }=0A= else if (arguments[4]=3D=3D'cocoonmrwarticle')=0A= {=0A= var currloc =3D location.href;=0A= var mrwParamArr =3D currloc.split("/");=0A= if (mrwParamArr.length >=3D 7)=0A= {=0A= url =3D url + '&mrwPath=3D' + mrwParamArr[5];=0A= url =3D url + '&mrwAid=3D' + mrwParamArr[7];=0A= url =3D url + '&mrwVersion=3D' + mrwParamArr[8];=0A= var mrwFileParam =3D mrwParamArr[9];=0A= var seploc =3D mrwFileParam.indexOf("#");=0A= if (seploc !=3D -1)=0A= {=0A= url =3D url + '&mrwSection=3D' + = mrwFileParam.substring(seploc+1);=0A= url =3D url + '&mrwDocType=3D' + = mrwFileParam.substring(0,seploc);=0A= }=0A= else=0A= {=0A= url =3D url + '&mrwDocType=3D' + mrwFileParam;=0A= }=0A= }=0A= }=0A= }=0A= }=0A= =0A= //checking if a html file exists in the url=0A= var tmpfname =3D location.href;=0A= var loc =3D tmpfname.indexOf("?");=0A= if (loc !=3D -1)=0A= {=0A= tmpfname =3D tmpfname.substring(0,loc);=0A= }=0A= loc =3D tmpfname.indexOf(".html");=0A= if (loc !=3D -1)=0A= {=0A= loc =3D tmpfname.lastIndexOf("/");=0A= if (loc !=3D -1)=0A= {=0A= tmpfname =3D tmpfname.substring(loc+1);=0A= url =3D url + '¤tFile=3D' + tmpfname;=0A= }=0A= }=0A= =0A= if (arguments.length>=3D7 && arguments[5]=3D=3D'currentyear' && = arguments[6]!=3D'')=0A= {=0A= url =3D url + '¤tYear=3D' + arguments[6];=0A= }=0A= =0A= eval("wileyMailTool =3D = window.open('"+url+"','MailTool','"+parameters+"')");=0A= =0A= // If object exists ensure has focus=0A= if (eval("wileyMailTool") && window.focus)=0A= eval("wileyMailTool").focus();=0A= }=0A= =0A= =0A= /*=0A= * 1. Find the links we need to alter.=0A= * 2. For each link apply the new styles we need.=0A= */=0A= function fixAbsRefRendering()=0A= { =0A= var table =3D document.getElementById('prerendered');=0A= var anchors =3D table.getElementsByTagName('a');=0A= for (var i =3D 1; i < anchors.length; i++)=0A= {=0A= if(anchors[i].href !=3D"") =0A= { =0A= applyAbsRefStyleCorrection(anchors[i]);=0A= =0A= }=0A= }=0A= }=0A= =0A= function applyAbsRefStyleCorrection(currentLink)=0A= {=0A= currentLink.style["color"] =3D "#369";=0A= currentLink.style["fontWeight"] =3D "normal";=0A= currentLink.style["marginLeft"] =3D "3px";=0A= currentLink.style["marginRight"] =3D "5px";=0A= }=0A= =0A= function populatePage(formName)=0A= {=0A= if (formName.Page.value =3D=3D '')=0A= {=0A= formName.Page.value =3D document.location;=0A= }=0A= }=0A= =0A= function equalizeColumnWidth(numFeatures)=0A= {=0A= var numberOfFeatures =3D numFeatures; =0A= // Percentage width of table to use for each column.=0A= var percentPerFeature =3D Math.floor(100 / numberOfFeatures); =0A= // Number of columns in total. Content cols + seperators. =0A= =0A= document.writeln("");=0A= for(var i =3D 0; i < numberOfFeatures; i++)=0A= { =0A= document.writeln(' 3D"blank"

');=0A= }=0A= document.writeln("");=0A= }=0A= =0A= function old_equalizeColumnWidth(numFeatures)=0A= {=0A= var numberOfFeatures =3D numFeatures; =0A= // Percentage width of table to use for each column.=0A= var percentPerFeature =3D Math.floor(100 / numberOfFeatures); =0A= // Number of columns in total. Content cols + seperators. =0A= =0A= if(debug)=0A= {=0A= alert("Number of feature boxes: " + numberOfFeatures + "\nPercent per = feature: " + percentPerFeature);=0A= }=0A= =0A= document.writeln("");=0A= for(var i =3D 0; i < numberOfFeatures; i++)=0A= { =0A= if (netscape4 =3D=3D false)=0A= {=0A= document.writeln(' 3D"blank"

'); =0A= }=0A= }=0A= document.writeln("");=0A= }=0A= =0A= function writeFBoxCell()=0A= {=0A= if(first)=0A= {=0A= document.write('');=0A= }else=0A= {=0A= document.write('');=0A= }=0A= numFeatures ++;=0A= }=0A= =0A= =0A= //=0A= // escape apostrophe characters within a string=0A= //=0A= function encode(str)=0A= {=0A= out =3D '';=0A= =0A= for (a =3D 0; a < str.length; a++)=0A= {=0A= c =3D str.charAt(a);=0A= =0A= if (c =3D=3D "'")=0A= {=0A= out +=3D '\\';=0A= }=0A= =0A= out +=3D c;=0A= }=0A= =0A= return out;=0A= }=0A= =0A= =0A= //=0A= //=0A= //=0A= function escapeEntities(str)=0A= {=0A= while (str.indexOf("'") > -1)=0A= {=0A= pos =3D str.indexOf("'");=0A= str =3D str.substr(0, pos) + '\\\'' + str.substr(pos + 6);=0A= }=0A= =0A= return str;=0A= }=0A= =0A= =0A= // new popup function less intrusive just uses the DOM to pickup links = with an exwin class.=0A= // currently implemented for Figure popups on D&T homepage.=0A= =0A= function exLinks()=0A= {=0A= if (document.getElementById)=0A= {=0A= var aObject =3D document.getElementsByTagName("a");=0A= for (var x=3D0; x" + = liels[j].innerHTML + "

You do not have = anything saved in this menu.

";=0A= else=0A= tmpinnerhtml +=3D "

" = + liels[j].innerHTML + "

"; =0A= } =0A= } else {=0A= //setup var to see if more is required=0A= var more =3D (subnodeslength < lilength) ? true : = false; =0A= var flag =3D true;=0A= for (var j=3D0; j" + liels[j].innerHTML + = "";=0A= } else if (j > lilength-3){=0A= if (j =3D=3D lilength-2){=0A= var url =3D liels[j].innerHTML.split('"')[1];=0A= tmpinnerhtml +=3D "

" + liels[j].innerHTML + "

";=0A= } else {=0A= tmpinnerhtml +=3D "

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"; =0A= } =0A= } =0A= }=0A= // set last two menu items to have no rollover and = a border at the top =0A= }=0A= menu.childNodes[x].childNodes[y].innerHTML =3D = tmpinnerhtml;=0A= // set default menu elements with diff style=0A= if (flag){=0A= if (more){=0A= liels[liels.length-3].style.borderTop =3D "1px solid = #DDDDDD";=0A= liels[liels.length-3].className =3D "noroll";=0A= liels[liels.length-2].style.borderTop =3D "1px solid = #DDDDDD";=0A= liels[liels.length-2].className =3D "noroll";=0A= liels[liels.length-1].className =3D "noroll";=0A= more =3D false;=0A= } else {=0A= liels[liels.length-2].style.borderTop =3D "1px solid = #DDDDDD";=0A= liels[liels.length-2].className =3D "noroll";=0A= liels[liels.length-1].className =3D "noroll";=0A= } =0A= flag =3D false; =0A= } =0A= =0A= // set sub menu title for the msnu=0A= liels[0].className =3D "hoverTitle";=0A= // apply rollover functions to hide/show sub menus=0A= if (classname =3D=3D "menuDOM"){=0A= menu.childNodes[x].onmouseover =3D function(){=0A= // safari doesnt handle auto in absoulte = positioning correctly so this code makes the menus display correctly.=0A= if (navigator.userAgent.indexOf("Safari") !=3D -1){=0A= if(!window.devicePixelRatio) {=0A= this.getElementsByTagName("UL")[0].style.marginTop =3D "20px";=0A= this.getElementsByTagName("UL")[0].style.marginLeft =3D "0";=0A= }=0A= }=0A= this.className =3D"menuhover domArrowOver";=0A= if(document.all) = this.getElementsByTagName("iframe")[0].style.height=3Dthis.getElementsByT= agName("ul")[0].offsetHeight;=0A= }=0A= menu.childNodes[x].onmouseout=3Dfunction() {=0A= this.className =3D "domArrowOut";=0A= }=0A= }=0A= =0A= if(document.all) {=0A= var newIframe =3D document.createElement("iframe");=0A= newIframe.style.filter =3D = "progid:DXImageTransform.Microsoft.Alpha(style=3D0,opacity=3D0)";=0A= menu.childNodes[x].appendChild(newIframe);=0A= }=0A= =0A= } =0A= }=0A= // deletes the sub menus on the IEMAC as they have a = background bug, will still remain on NS6=0A= if ((navigator.userAgent.indexOf("Mac") !=3D -1) && = (navigator.userAgent.indexOf("MSIE") !=3D -1)){=0A= menu.childNodes[x].innerHTML =3D = menu.childNodes[x].innerHTML.split(""=0A= var menu =3D document.all["menu"].children[0];=0A= menu.style.marginBottom =3D "-3px";=0A= for (var x=3D1; 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Journal of Neurochemistry

ISSN: 1471-4159 (Online)

ISSN: 0022-3042 (Print)

Volume 9999, Issue 9999, 2009.

Pages: ???=96???

Top of Page
Abstract
Materials and methods
Results
Discussion
Acknowledgements
References

List of=20 Images

Abstract=20 Only

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3D"About

Online ISSN: = 1096-9896 Print ISSN: 0022-3417
The Journal of = Pathology
Volume 214, Issue 3, 2008. Pages: 328-336

Copyright =C2=A9 2007 Pathological Society of Great = Britain and Ireland. Published by John Wiley & Sons, Ltd.

'); } =0A= function copyright(hwnd) {var title =3D pagetitle(); = hwnd.document.write(title.bold() + '
Copyright Journal compilation = © 2009 International Society for Neurochemistry

'); } =0A= function imagelink(hwnd, iname) {if (iname.indexOf(' ') > -1) {var = images =3D iname.split(' ');for (var i =3D 0; i < images.length; ++i) = {hwnd.document.write('

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'); } =0A= =0A= =0A= function caption_f1(hwnd) = {hwnd.document.write('Fig. 1 (a) Comparison of the = PKCζ expression in MDA-MB-231, LN-229, and U87 cells by western = blotting; 20 μg of protein was loaded on each lane. (b) = Western blotting and RT-PCR analysis of PKCζ expression in LN-229 = cells. β-Actin, and GAPDH were used as internal control. (c) = Quantitative PCR analyses showed the relative levels of PKCζ mRNA = expression in LN-229, scr/LN-229 and siPKCζ/LN-229 cells. Data = are given as mean ± SEM, n =3D 3. = *p < 0.05, two-way anova. (d) Protein = expression of EGFR in U87, LN-229 cells, and their transfected groups by = western blotting analysis; 5 × 10⁵ cells = were lysed and separated by 8% SDS-PAGE.'); }=0A= function display_f1(size) { var i =3D new Array(); i[0] =3D 'nf1'; i[1] = =3D 'nf1'; var hwnd =3D newfigwin(); dochead(hwnd, ''); copyright(hwnd); = otherlinks(hwnd, 'f1', size); imagelink(hwnd, i[size]); = caption_f1(hwnd); doctail(hwnd); hwnd.document.close(); hwnd.focus(); }=0A= function caption_f2(hwnd) = {hwnd.document.write('Fig. 2 Involvement of atypical = PKC in EGF-induced chemotaxis in glioblastoma cell lines and = PKCζ-deficient LN-229 cells display decreased motility. (a) = EGF-elicited chemotaxis assay at the presence of Gö6850 (0 nM, = 20 nM, 50 nM, 100 nM) and Chel. C. (0 μM, = 2 μM, 5 μM, 10 μM). EGF was used at = 10 ng/mL. (Data from three independent experiments summarized as = mean ± SEM, n =3D 3. = *p < 0.05, = **p < 0.01, = ***p < 0.001, two-way anova.) (b) = EGF-elicited chemotaxis of LN-229, U87 cells, and their siPKCζ = transfected groups. (Data from three independent experiments summarized = as mean ± SEM, n =3D 3. = **p < 0.01, two-way anova.) (c) Images of = scratch assay of scr/LN-229 and siPKCζ/LN-229 cells at 0 h, = 12 h, and 24 h (100×). LN-229 cells were grown to = confluence on a 10-cm cell culture dish and the monolayer was wounded = with a 10-μL pipette tip. (Data from three independent = experiments.) (d) The migrating distance of the scr/LN-229 and = siPKCζ/LN-229 cells at different time points in the scratch = assay. (Data from three independent experiments, two-way anova analysis, = p < 0.05.)'); }=0A= function display_f2(size) { var i =3D new Array(); i[0] =3D 'nf2'; i[1] = =3D 'nf2'; var hwnd =3D newfigwin(); dochead(hwnd, ''); copyright(hwnd); = otherlinks(hwnd, 'f2', size); imagelink(hwnd, i[size]); = caption_f2(hwnd); doctail(hwnd); hwnd.document.close(); hwnd.focus(); }=0A= function caption_f3(hwnd) = {hwnd.document.write('Fig. 3 Disruption of PKCζ = by siRNA impaired actin polymerization in LN-229 cells. (a) Cytoskeleton = rearrangement in scr/LN-229 cells and siPKCζ/LN-229 cells were = imaged by fluorescence staining. The data were collected by = representative images from three repeated experiments (400×). (b) = Time course of relative F-actin content in scr/LN-229 cells and = siPKCζ/LN-229 cells. Cells were treated with 10 ng/mL EGF = for various times before fixation and staining of F-actin by using = phalloidin conjugated to Alexa Flour 568. Data from three independent = experiments (n =3D 3). (c) Western blotting analysis of = phosphorylated LIMK and cofilin in total cell lysates from scr/LN-229 = and siPKCζ/LN-229 cells after stimulating with 50 ng/mL EGF = for 0 s, 5 s, 10 s, 15 s, and 60 s. LIMK1 and = cofilin were used as loading control respectively. Data from three = independent experiments (n =3D 3). (d) = Immuno-precipitation analysis of LIMK1 and PKCζ. LN-229 cells = were stimulated with 10 ng/mL EGF for 0 min, 2 min, and = 5 min. Lane NC, immuno-precipitation without PKCζ or LIMK1 = antibodies as negative control. Lane WCL, whole cell lysates. Each = immuno-precipitation is a representative of three independent = experiments.'); }=0A= function display_f3(size) { var i =3D new Array(); i[0] =3D 'nf3'; i[1] = =3D 'nf3'; var hwnd =3D newfigwin(); dochead(hwnd, ''); copyright(hwnd); = otherlinks(hwnd, 'f3', size); imagelink(hwnd, i[size]); = caption_f3(hwnd); doctail(hwnd); hwnd.document.close(); hwnd.focus(); }=0A= function caption_f4(hwnd) = {hwnd.document.write('Fig. 4 Disruption of PKCζ = by siRNA impaired adhesion of LN-229 cells. (a) Comparison of = 10 ng/mL EGF-induced adhesion at 5 min, 15 min, and = 30 min of scr/LN-229 cells to that of siPKCζ/LN-229 cells on = fibronectin-coated coverslips. Cell numbers in each high power field = (HPF) were counted in five fields on every coverslips under microscopy = (200×) (Data from three independent experiments summarized as = mean ± SEM, n =3D 3. = *p < 0.05, two-way anova.) (b) Western = blotting analysis of phosphorylated integrin β1 in total cell = lysates from scr/LN-229 and siPKCζ/LN-229 cells after stimulating = with 10 ng/mL EGF for 0 min, 2 min, and 5 min. = Integrin β1 was used as a loading control.'); }=0A= function display_f4(size) { var i =3D new Array(); i[0] =3D 'nf4'; i[1] = =3D 'nf4'; var hwnd =3D newfigwin(); dochead(hwnd, ''); copyright(hwnd); = otherlinks(hwnd, 'f4', size); imagelink(hwnd, i[size]); = caption_f4(hwnd); doctail(hwnd); hwnd.document.close(); hwnd.focus(); }=0A= function caption_f5(hwnd) = {hwnd.document.write('Fig. 5 Specific PKCζ = pseudosubstrates blocked EGF-induced chemotaxis and adhesion in = glioblastoma cells. (a) Blockage of chemotaxis in LN-229 cells by = myristoylated PKCζ pseudosubstrate peptide under EGF stimulation = (Data from three independent experiments summarized as = mean ± SEM, n =3D 3. = *p < 0.05, = **p < 0.01, = ***p < 0.001, two-way anova.) (b) Inhibitory = effect of 50 μM PKCζ pseudosubstrates on EGF-induced = LN-229 and U87 glioblastoma cells chemotaxis. (Data from three = independent experiments summarized as mean ± SEM, = n =3D 3. **p < 0.01, two-way = anova.) Cells were collected and incubated with myristoylated = pseudosubstrate peptide, non-myristoylated peptide, or PBS at 37°C = for 45 min before chemotaxis assay for (a) or (b). (c) The = impairment on cell adhesion with pseudosubstrate treatment. LN-229 and = U87 cells were pre-treated with myristoylated pseudosubstrate peptide, = non-myristoylated peptide, or PBS at 37°C for 45 min before = 10 ng/mL EGF stimulation. (Data from three independent experiments = summarized as mean ± SEM, n =3D 3. = **p < 0.01, two-way anova.)'); }=0A= function display_f5(size) { var i =3D new Array(); i[0] =3D 'nf5'; i[1] = =3D 'nf5'; var hwnd =3D newfigwin(); dochead(hwnd, ''); copyright(hwnd); = otherlinks(hwnd, 'f5', size); imagelink(hwnd, i[size]); = caption_f5(hwnd); doctail(hwnd); hwnd.document.close(); hwnd.focus(); }=0A= function caption_f6(hwnd) = {hwnd.document.write('Fig. 6 Disruption of PKCζ = by siRNA impaired invasion into matrigel in LN-229 cells and also = impaired the invasion of glioblastoma cells in vivo. (a) Invasion = was measured as described in \'Materials and Methods.\' The cells that = invaded through matrigel-coated transwell inserts toward chemoattractant = were stained. Photographs were taken at a magnification of 200×. = (b) The cells invading through the matrigel were counted under = microscope in five pre-determined fields at 400×. Data are shown = as mean ± SEM, n =3D 3. = **p < 0.01, two-way anova. (c) Western = blotting analysis of MMP-2 and MMP-9 expression in scr/LN-229 cells and = siPKCζ/LN-229 cells. β-Actin was used as a loading = control. (d) LN-229 cells were transfected with either control or = PKCζ siRNA plasmid followed by the isolation of stable clones. = Cell lysates of each representative clone were analyzed by western = blotting using anti-PKCζ antibody and anti-β-actin = antibody. (e) Frequency of xenograft invasion in control group and three = clones of the PKCζ knockdown groups (10 mice for each group, = *p < 0.05, Chi-square Test). (f) = Glioblastoma-xenografted tumors were sectioned for H&E staining to = identify tumor regions. (i) and (ii): tumors of = scr/LN-229-cells-injected mice group. (iii) and (iv): tumors of = siPKCζ/LN-229-cells-injected mice group. Panel (v) and (vi) are = enlarged figures of (i) and (ii), respectively. (Arrows indicate the = invasive scr/LN-229 cells). Top row, 100×; bottom row, = 200×.'); }=0A= function display_f6(size) { var i =3D new Array(); i[0] =3D 'nf6'; i[1] = =3D 'nf6'; var hwnd =3D newfigwin(); dochead(hwnd, ''); copyright(hwnd); = otherlinks(hwnd, 'f6', size); imagelink(hwnd, i[size]); = caption_f6(hwnd); doctail(hwnd); hwnd.document.close(); hwnd.focus(); }=0A= =0A= =0A= function imagelist() {var hwnd =3D newfigwin(); dochead(hwnd, 'List of = Images - '); copyright(hwnd); =0A= hwnd.document.write('');=0A= =0A= =0A= hwnd.document.write('');=0A= hwnd.document.write('');=0A= hwnd.document.write('');=0A= hwnd.document.write('');=0A= hwnd.document.write('');=0A= hwnd.document.write('');hwnd.document.write('

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3D""=20

Reduction of protein kinase C ζ = inhibits=20 migration and invasion of human glioblastoma cells

Hua=20 Guo*^,=86^,1,=20 Feng Gu=87,1, = Wenliang Li=A7, Baogang Zhang*,=20 Ruifang Niu*, Li Fu=87, Ning Zhang* and Yongjie Ma*

*Department of=20 Core Laboratory, Tianjin Medical University Cancer Institute and = Hospital,=20 Tianjin, China
=86Tianjin Medical=20 College, Tianjin, China
=87Department of=20 Breast Cancer Pathology, Tianjin Medical University Cancer = Institute and=20 Hospital, Tianjin, China
=A7Department of=20 Neurosurgery, Tianjin Medical University Cancer Institute and = Hospital,=20 Tianjin, China

Address correspondence and = reprint=20 requests to Yongjie Ma and Ning Zhang, Department of Core = Laboratory,=20 Tianjin Medical University, Cancer Institute and Hospital, = Huanhuxi Road,=20 Hexi District, Tianjin, China, 300060. E-mail: yongjiemagu@yahoo.com.cn

=20 ¹ These = authors=20 contributed equally to this study.

Copyright Journal compilation =A9 2009 = International Society for Neurochemistry

KEYWORDS

adhesion =95 F-actin =95 integrin β1 = =95=20 invasion

ABSTRACT

3DAbstract=20

=

=

=

=

=

Glioblastomas are the most aggressive forms of = primary brain=20 tumors with their tendency to invade surrounding healthy brain = tissues,=20 rendering them largely incurable. In this report, we used=20 small-interference RNA technology to knock down the expression of = protein=20 kinase C (PKC) ζ, which resulted in specific and massive = impairment of=20 glioblastoma cell migration and invasion. We also explained the=20 fundamental molecular processes of glioblastoma migration and = invasion in=20 which PKCζ is a participant. The silence of PKCζ = expression likewise=20 impaired the phosphorylation of LIN-11, Isl1 and MEC-3 protein = domain=20 kinase (LIMK) and cofilin, which is a critical step in cofilin = recycling=20 and actin polymerization. Consistent with the defects in cell = adhesion,=20 phosphorylation of integrin β1 was also dampened. Therefore, = PKCζ=20 regulated both cytoskeleton rearrangement and cell adhesion, which = contributed to cell migration. Additionally, there was = down-regulation of=20 matrix metalloprotease-9 expression in siPKCζ/LN-229 cells, = which=20 coincided with decreased invasion both in = vitro and=20 in vivo. These results indicate that = PKCζ is involved=20 in the control of glioblastoma cell migration and invasion by = regulating=20 the cytoskeleton rearrangement, cell adhesion, and matrix=20 metalloprotease-9 expression. Collectively, these findings suggest = that=20 PKCζ is a potential therapeutic target for glioblastoma=20 infiltration.

Received October 10, 2008; revised manuscript = received=20 January 18, 2009; accepted January 21, 2009.

DIGITAL OBJECT IDENTIFIER (DOI)

10.1111/j.1471-4159.2009.05946.x About=20 DOI

=20

=20

Article Text

Among the malignant tumors of the adult CNS, = glioblastomas=20 are the most common; they have a median survival of less than one = year.=20 The highly lethal nature of this tumor is the consequence of an = invasive=20 phenotype, allowing tumor cells to infiltrate surrounding brain = tissues.=20 The initial treatment for many glioblastomas is maximal surgical=20 resection; however, the widespread migration and invasion of tumor = cells=20 into the surrounding brain tissues render complete removal = virtually=20 impossible. Additionally, the molecular mechanisms that regulate=20 glioblastoma invasion from primary tumor sites to the surrounding = normal=20 brain tissues remain poorly understood. Therefore, a better = understanding=20 of the glioblastoma cells' migratory and invasive mechanisms may = result in=20 new therapeutic approaches.

An over-expressed or hyperactive protein kinase C = (PKC) is=20 reported as one of the malignant CNS tumors' most distinguishing=20 characteristics (da=20 Rocha et al. 2002). PKC consists = of 12=20 different isoforms, which can be sorted into three subfamilies = based on=20 their activation mechanisms: classic, novel and atypical PKC. = PKCζ,=20 belonging to the atypical PKC family, which has higher expression = in=20 glioblastoma cell lines than normal astrocytes has been reported = to have=20 an important role in glioblastomas (Acevedo-Duncan=20 et al. 2004). Schih et al. reported that when human glioblastoma = cell line=20 U373 cells were transfected with anti-sense oligonucleotide = sequences to=20 the translation start sites of PKCα, β, γ, δ, = ε, or ζ isoforms, only PKCζ=20 and PKCα anti-sense oligonucleotide showed inhibition of = vascular=20 endothelial growth factor (VEGF) expression (Shih=20 et al. 1999). PKCζ also plays = an important=20 role in determining cell polarity (Joberty=20 et al. 2000). The isozyme-specific = inhibitors demonstrated that PKCζ is involved in = chemokine-triggered cell=20 adhesion and actin assembly in polymorphonuclear cells (Laudanna=20 et al. 1998; Giagulli=20 et al. 2004). The potential = importance of=20 PKCζ as a downstream mediator in the Phosphatidyl inositol = 3-kinase (PI3K)=20 pathway has been emphasized by our recent finding, that is, it can = itself=20 function as a migration regulator in human breast cancers (Sun=20 et al. 2005). However, it is not = known=20 whether PKCζ is necessary in glioblastoma cells motility and = invasion.=20 Likewise, the downstream events involved in atypical PKC-mediated = motility=20 have not been determined.

In the present study, we tested the hypothesis = that PKCζ=20 directly participates in glioblastoma cell migration and invasion. = We=20 down-regulated the PKCζ expression in glioblastoma LN-229 and = U87 cells by=20 PKCζ small interference RNA (siRNA); this effectively = inhibited migration=20 and invasion in vitro and in=20 vivo. Our data further demonstrated that several key = proteins,=20 including integrin β1, cofilin, LIN-11, Isl1 and MEC-3 = protein domain=20 kinase (LIMK), and matrix metalloprotease (MMP)-9, were involved = in PKCζ=20 signaling pathways, which are critical for glioblastoma cell = migration and=20 invasion. Thus, our study suggests that PKCζ is required in = glioblastoma=20 migration and invasion, and is a potential therapeutic target = molecule for=20 glioblastoma infiltration.

=20

=20

Materials and methods

=

=

=

=

=

=20

=20

Cell culture and reagents

Cells from the human glioblastoma cell lines = LN-229 and U87=20 were obtained from American Type Culture Collection (Manassas, VA, = USA)=20 and were cultured in Roswell Park Memorial Institute (RPMI) 1640 = with 10%=20 Fetal Bovine Serum (FBS) (complete medium). The microboyden = chambers and=20 membranes were acquired from Neuroprobe (Gaithersburg, MD, USA). = The=20 recombinant human epithelial growth factor (EGF) was obtained from = R&D=20 systems (Minneapolis, MN, USA), G=F66850 and chelerythrine = chloride from=20 Alexis Biochemicals (San Diego, CA, USA), the myristoylated and=20 non-myristoylated pseudopeptides for PKCζ from Calbiochem (La = Jolla, CA,=20 USA). The antibodies against cofilin, P-cofilin, integrin β1, = P-LIMK,=20 LIMK1, β-actin, EGFR and PKCζ were acquired from Santa = Cruz Biotechnology,=20 Inc. (Santa Cruz, CA, USA). Antibodies against P-integrin β1 = (T788,=20 ZP0351) were bought from ABZOOM (Dallas, TX, USA).

=20

=20

RNA interference

Following the manufacturer's instruction, = transfection was=20 performed by using Lipofectamine2000 (Invitrogen) with = PKCζ-specific siRNA=20 (insert GAGGAAGTGAGAGACATGTGT) and scramble sequence siRNA from = Genescript=20 (Piscataway, NJ, USA). The transfected cells were selected on the = basis of=20 their resistance to Hygromycin B (BD Biosciences, San Jose, CA, = USA), and=20 their expression level of PKCζ protein was monitored by = western blotting=20 to establish the cell lines stably expressed by the mutant = proteins.=20 Clones, in which the expression of PKCζ was effectively = suppressed, were=20 selected and used for the in vivo invasion=20 study.

=20

=20

RT-PCR

Total RNA from cells was extracted using Trizol = (Invitrogen,=20 Carlsbad, CA, USA) and was reverse-transcribed and PCR-amplified = using the=20 One Step RNA PCR Kit (AMV) from TaKaRa Biotechnology Co., Ltd. = (Dalian,=20 China). The PCR procedure both with Glyceraldehyde-3-phosphate=20 dehydrogenase (GAPDH) and PKCζ was done in 95=B0C for = 1 min, 57=B0C for=20 1 min and 72=B0C for 1 min with a total of 35 cycles. = The primer=20 sequences were as follows: GAPDH (forward: = 5'-ACCACAGTCCATGCCATCAC-3';=20 reverse: 5'-TCCACCACCCTGTTGCTGTA-3'), PKCζ (forward:=20 5'-CTGAGGAGCACGCCAGGTT-3'; reverse:=20 5'-ACGGGCTCGCTGGTGAACT-3').

=20

=20

Quantitative RT-PCR

Total RNA was extracted using Trizol (Invitrogen). = cDNA was=20 prepared using the First Strand Synthesis kit (Roche Molecular=20 Biochemicals, Indianapolis, IN, USA). For the quantitative RT-PCR = (qPCR),=20 the iQ SYBR Green kit was used (Bio-Rad, Hercules, CA, USA). The = GAPDH=20 gene was the internal control for all the qPCR experiments. The = data were=20 from three independent experiments, and the mean values with SD = are=20 presented. For PKCζ qPCR, the primers used are as = follows:

forward:TTTACGCCATGAAAGTGGTGAAGA;

reverse: CAGGAGTGTAATCCGACCAGGAA.

=20

=20

Immunoprecipitation assay

Immunoprecipitation analysis was done as described = (Fernandis=20 et al. 2003). Details were shown = in Appendix=20 S1.

=20

=20

EGF activation and western = blotting assay

Western blotting assay was performed as described = by Sun=20 et al. (2005). PKCζ = activation assay was=20 done by serum starving the cells for at least 3 h and = subsequently=20 activating them with 10 ng/mL EGF at different times. More = details=20 were shown in Appendix S1.

=20

=20

Chemotaxis assay

Chemotaxis assay was performed in a 48-well Boyden = chamber=20 as described by Sun=20 et al. (2005). Details were shown = in=20 Appendix S1.

=20

=20

Invasion assay

A Boyden chamber invasion assay was performed as = previously=20 described by Albini=20 et al. (1987). Details were shown = in=20 Appendix S1.

=20

=20

Scratch assay

One day before assay, cells were plated in 35-mm = dishes at a=20 density of 1 =D7 10⁶ cells/mL to = form a=20 monolayer. An even trace was then lined out in the middle using a=20 10 μL pipette tip (Pixley=20 et al. 2001). The cells were then = incubated=20 at 37=B0C in 5% CO₂, and the wounds were=20 photographed at intervals until they were occluded by migrating=20 cells.

=

=20

Adhesion assay

This assay was performed as described by Sun=20 et al. (2005). Details were shown = in=20 Appendix S1.

=20

=20

Cellular F-actin measurement

Cellular F-actin measurement was carried out as = described=20 previously (Sun=20 et al. 2005). Details were shown = in Appendix=20 S1.

=20

=20

Fluorescence microscopy

The cells were cultured one day prior to staining = and=20 starved in serum-free medium for 3 h. After stimulation with=20 50 ng/mL EGF at 37=B0C for 1 min, cells were fixed and = then were=20 incubated with Alexa-fluro 568 phalloidin for 30 min. = Fluorescence of=20 cells were visualized with the Nikon inverted fluorescent = microscope=20 (Nikon, Inc., Tokyo, Japan).

=20

=20

Tumor invasion assay in=20 vivo

The invasion of glioblastoma cells was analyzed = in vivo by subcutaneous inoculation as previously = described=20 (Blazquez=20 et al. 2008). Male athymic Nu/Nu = mice, 4- to=20 6-weeks-old, were purchased from Wei Tong Li Hua Experimental = Animal Co.=20 Ltd. (Beijing, China). All animals received human care according = to the=20 criteria outlined in the Guide for the Care and Use of Laboratory = Animals,=20 prepared by the National Academy of Sciences and published by the = National=20 Institutes of Health. A total of = 2 =D7 10⁶=20 cells were inoculated subcutaneously into the mice's left flank. = After=20 28 days, the tumors were excised. These were then fixed with = 4%=20 paraformaldehyde and embedded in paraffin after which they were = sectioned=20 to a thickness of 5 μm with a microtome, mounted on = glass slides, and=20 processed for H&E staining. A group of ten mice were used for = each=20 data point.

=20

=20

Statistical analysis

Prism 3.0 software (San Diego, CA, USA) was used = for data=20 analysis. Chi-square Test was used for in = vivo=20 analysis and the two-way anova = were used=20 for two groups of data in vitro. All the = results were=20 generated from three independent experiments.

=20

=20

Results

=

=

=

=

=20

=20

Reduction of PKCζ impaired = LN-229 cells=20 migration

We first examined the expression of PKCζ in = two glioblastoma=20 cell lines, LN-229 and U87 cells. Western blotting analysis = revealed the=20 expression of PKCζ in both LN-229 and U87 cells at a level = comparable to=20 that of MDA-MB-231 cells, a type of human breast cancer cells (Fig. 1a).=20 Regarding the specific involvement of PKCζ in EGF-induced = migration of=20 glioblastoma cells, we applied the siRNA technology to inhibit = PKCζ=20 expression. Specifically, LN-229 cells transfected with PKCζ = siRNA plasmid=20 were designated as siPKCζ/LN-229 cells, while siRNA construct = containing a=20 scrambled sequence was transfected into LN-229 cells to generate = control=20 cells, which were designated as scr/LN-229 cells. Transfected = cells were=20 selected by Hygromycin B resistance to establish cell lines that = stably=20 down-regulated PKCζ expression. Following Hygromycin B = selection, infected=20 cells were screened for PKCζ expression using western = blotting analysis.=20 As shown in Fig. 1(b),=20 almost 70=9680% of PKCζ protein levels were reduced in = siPKCζ/LN-229 cells=20 compared with those in scrambled scr/LN-229 cells or = non-transfected=20 cells. In addition, subsequent experiments using at least three=20 independent batches of siPKCζ/LN-229 cells showed at least = 70% PKCζ=20 protein reduction. Meanwhile, the RT-PCR analysis detected a = marked loss=20 of PKCζ mRNA in siPKCζ/LN-229 cells, but not in = scr/LN-229 cells or=20 non-transfected cells which was consistent with the result of = quantitive=20 RT-PCR (Fig. 1b=20 and c). On the other hand, western blotting analysis was = applied to=20 identify whether the transfection down-regulates cell surface EGFR = expression. The analysis revealed considerable expression of EGFR = on the=20 cell surface of both glioblastoma and PKCζ down-regulated = cell lines,=20 while siRNA plasmid transfection did not induce any detectable = loss of=20 surface EGFR (Fig. 1d).

=20

= Fig. 1 = (a)=20 Comparison of the PKCζ expression in MDA-MB-231, = LN-229, and U87=20 cells by western blotting; 20 μg of protein was = loaded on each=20 lane. (b) Western blotting and RT-PCR analysis of PKCζ = expression in=20 LN-229 cells. β-Actin, and GAPDH were used as internal = control. (c)=20 Quantitative PCR analyses showed the relative levels of = PKCζ mRNA=20 expression in LN-229, scr/LN-229 and siPKCζ/LN-229 = cells. Data are=20 given as mean =B1 SEM, n =3D 3.=20 *p < 0.05,=20 two-way anova. (d) = Protein=20 expression of EGFR in U87, LN-229 cells, and their = transfected=20 groups by western blotting analysis;=20 5 =D7 10⁵ cells were lysed = and=20 separated by 8% SDS-PAGE.

[Normal=20 View ]

Migration contributes to several important = pathological=20 processes, including immunity, wound repair, tumor formation, and=20 metastasis. In order to examine how PKCζ affects cell = migration, we=20 performed cell chemotaxis assay and wound healing assay. = Chemotaxis refers=20 to directional cell movement dependent on a concentration = gradient. A=20 48-well chemotaxis model was applied to perform EGF-induced 3-h = cell=20 chemotaxis. To test the hypothesis that atypical PKCζ plays = an important=20 role in glioblastoma cells chemotaxis we first examined the role = of PKC=20 family members in EGF-mediated chemotaxis using the specific = inhibitors of=20 different subtypes. As shown in Fig. 2(a),=20 LN-229 cells were pre-treated for 1 h with a spectrum of PKC=20 inhibitors before being tested in 10 ng/mL EGF-induced = chemotaxis=20 assays. Chelerythrine chloride (Chel. C.), a specific inhibitor of = all the=20 PKC isotypes, severely impaired the EGF-induced chemotaxis in a=20 dose-dependent manner, indicating that PKC isozymes were required. = However, G=F66850, a specific inhibitor for classic and novel = types of PKC,=20 failed to inhibit chemotaxis. These results suggested that it was = the=20 atypical PKC and not the classic or novel PKC isotypes that was = involved=20 in the LN-229 cell chemotaxis. In contrast, Fig. 2(b)=20 illustrates robust chemotaxis of the parental LN-229 cells and = scr/LN-229=20 cells induced by EGF in a bell-shaped manner, although the = chemotaxis of=20 siPKCζ/LN-229 cells was impaired in response to PKCζ = reduction. Also,=20 EGF-induced chemotaxis in U87 cells was detected, consistent with = our=20 chemotaxis data in LN-229 cells. These results revealed that = PKCζ was=20 required for glioblastoma cell chemotaxis, while a concentration = gradient=20 was required for efficient migration of glioblastoma cells in = response to=20 EGF.

=20

= Fig. 2=20 Involvement of atypical PKC in EGF-induced = chemotaxis=20 in glioblastoma cell lines and PKCζ-deficient LN-229 = cells display=20 decreased motility. (a) EGF-elicited chemotaxis assay at the = presence of G=F66850 (0 nM, 20 nM, 50 nM, = 100 nM)=20 and Chel. C. (0 μM, 2 μM, = 5 μM, 10 μM). EGF was=20 used at 10 ng/mL. (Data from three independent = experiments=20 summarized as mean =B1 SEM, n =3D 3. *p < 0.05, **p < 0.01, ***p < 0.001, two-way=20 anova.) (b) EGF-elicited = chemotaxis=20 of LN-229, U87 cells, and their siPKCζ transfected = groups. (Data=20 from three independent experiments summarized as=20 mean =B1 SEM, n =3D 3. **p < 0.01, two-way=20 anova.) (c) Images of = scratch assay=20 of scr/LN-229 and siPKCζ/LN-229 cells at 0 h, = 12 h, and=20 24 h (100=D7). LN-229 cells were grown to confluence on = a 10-cm=20 cell culture dish and the monolayer was wounded with a = 10-μL pipette=20 tip. (Data from three independent experiments.) (d) The = migrating=20 distance of the scr/LN-229 and siPKCζ/LN-229 cells at = different time=20 points in the scratch assay. (Data from three independent=20 experiments, two-way anova=20 analysis, p < 0.05.)=20

[Normal View=20 ]

Scratch assay, an in vitro=20 wound-healing assay, is another method of evaluating cell = migration=20 capacity. It was observed that scr/LN-229 cells migrated into the = wound=20 and resulted in wound closure within 26 h, whereas = siPKCζ/LN-229=20 cells were significantly less motile (Fig. 2c)=20 as supported by the delay in the mean distance of closure (Fig. 2d).=20 Both the scr/LN-229 and siPKCζ/LN-229 cells were maintained = in a medium=20 supplemented with 0.5% FBS to block cell proliferation, which = could=20 otherwise account for gap closure. Taken together, our results = obviously=20 showed that PKCζ reduction by siRNA impaired the EGF-induced = migration and=20 that PKCζ was required for migration of glioblastoma = cells.

=20

=20

Reduction of PKCζ impaired = F-actin=20 polymerization of LN-229 cells

The actin cytoskeleton is a key mediator of cell=20 polarization and the directed migration of cells toward a = chemoattractant.=20 The ability of cells to move implies dynamic remodeling of the = actin=20 cytoskeleton that governs the extension of cell protrusions and = the=20 retraction of the cell body (Ridley=20 et al. 2003). Chemotaxis requires=20 cytoskeletal reorganization and formation of filamentous actin = (F-actin).=20 In this regard, the F-actin polymerization assay was carried out = to prove=20 the hypothesis that the reduction of PKCζ could impair LN-229 = cell=20 migration by reducing the F-actin polymerization. In particular, = LN-229=20 cells were stimulated at 0 s, 15 s, 30 s, = 1 min,=20 2 min, 5 min with 50 ng/mL EGF. The cells were = stained with=20 Alexa-fluro 568 phalloidin and the levels of F-actin = polymerization were=20 detected by microplate fluorescence reader. An increase of the = F-actin=20 contents induced by EGF could be observed in scr/LN-229 cells but = not in=20 siPKCζ/LN-229 cells (Fig. 3a).=20 Actin polymerization is most pronounced within 2 min after = EGF=20 stimulation, and two phases of typical actin polymerization were = observed=20 in the scr/LN-229 cells (Fig. 3b).=20 The first phase peaked at 15 s and the second phase peaked at = 60 s, which is consistent with previous reports (Chen=20 et al. 2003; Wang=20 et al. 2008). These two phases of = actin=20 polymerization display different dependencies and have unique = roles during=20 chemotaxis. Mouneimne et al. = demonstrated that=20 the first peak depended on phospholipase C (PLC)-γ and = cofilin (Mouneimne=20 et al. 2004) and the second peak = depended on=20 PI3K activity (Hill=20 et al. 2000; Chen=20 et al. 2003). In = siPKCζ/LN-229 cells, the=20 two phases were delayed and the two peaks were both lower than the = control. As actin polymerization induced by EGF was significantly = reduced=20 in siPKCζ/LN-229 cells, this signified that PKCζ was = required for=20 EGF-induced rearrangement of the cytoskeleton.

=20

= Fig. 3=20 Disruption of PKCζ by siRNA impaired actin = polymerization in LN-229 cells. (a) Cytoskeleton = rearrangement in=20 scr/LN-229 cells and siPKCζ/LN-229 cells were imaged by = fluorescence=20 staining. The data were collected by representative images = from=20 three repeated experiments (400=D7). (b) Time course of = relative=20 F-actin content in scr/LN-229 cells and siPKCζ/LN-229 = cells. Cells=20 were treated with 10 ng/mL EGF for various times before = fixation and staining of F-actin by using phalloidin = conjugated to=20 Alexa Flour 568. Data from three independent experiments = (n =3D 3). (c) Western blotting = analysis of=20 phosphorylated LIMK and cofilin in total cell lysates from=20 scr/LN-229 and siPKCζ/LN-229 cells after stimulating = with=20 50 ng/mL EGF for 0 s, 5 s, 10 s, = 15 s, and=20 60 s. LIMK1 and cofilin were used as loading control=20 respectively. Data from three independent experiments (n =3D 3). (d) = Immuno-precipitation analysis=20 of LIMK1 and PKCζ. LN-229 cells were stimulated with = 10 ng/mL=20 EGF for 0 min, 2 min, and 5 min. Lane NC,=20 immuno-precipitation without PKCζ or LIMK1 antibodies = as negative=20 control. Lane WCL, whole cell lysates. Each = immuno-precipitation is=20 a representative of three independent experiments.=20

[Normal View=20 ]

LIM kinase and cofilin are the two critical = factors involved=20 in the regulation of F-actin dynamics; their phosphorylation = mediates the=20 regulation of chemoattractants inducing actin polymerization. To = test the=20 hypothesis that PKCζ mediates EGF-induced activation of LIMK = and cofilin,=20 which in turn regulates actin polymerization, we detected evidence = for=20 LIMK and cofilin activation. As seen in Fig. 3(c),=20 reduction of PKCζ-inhibited EGF induced phosphorylation of = LIMK and=20 cofilin consistent with their defects in actin polymerization. = Together,=20 these findings indicated that the down-regulation of PKCζ = expression in=20 LN-229 cells resulted in a major cytoskeletal reorganization = defect in=20 response to EGF, possibly through regulation of LIMK/cofilin=20 phosphorylation.

Our previous report has shown that the inhibition = of PKCζ=20 could impair the activation of LIMK in lung cancer cells (Liu=20 et al. 2008). In this study, we = examined the=20 possibility of PKCζ interacting with LIMK1 directly. = Immuno-precipitation=20 analysis showed that treatment with EGF at 10 ng/mL for = 2 min=20 and 5 min induced co-precipitation of LIMK1 with PKCζ.. = LIMK2 was not=20 pulled down by PKCζ (data not shown). LIMK1 was = co-precipitated with PKCζ=20 by the anti-PKCζ antibody (Fig. 3d=20 top panel), and PKCζ was co-precipitated with LIMK1 by the = anti-LIMK1=20 antibody (Fig. 3d=20 low panel). Lane whole cell lysates indicated that sufficient = LIMK1 and=20 PKCζ were present in cell lysates during immuno-precipitation = assays.=20 These results suggested that EGF induced direct interaction of = PKCζ with=20 LIMK1.

=

=20

Reduction of PKCζ impaired = adhesion of LN-229=20 cells

The rate of cell migration can be limited by the = rate of=20 rear retraction, and thus the dynamic formation and disassembly of = cell=96matrix adhesions are critical to cell migration (Ridley=20 et al. 2003). We have shown = F-actin=20 polymerization changes induced by reduction of PKCζ in LN-229 = cells; we=20 also observed the effect of PKCζ on cell adhesion in LN-229 = cells.=20 Specifically, EGF at 10 ng/mL induced a more than two fold = increase=20 in the numbers of adhesive scr/LN-229 cells compared with = siPKCζ/LN-229=20 cells at 5 min (p < 0.05). Disruption of PKCζ resulted in = a marked=20 reduction in numbers of adhesive cells in 5 min and = 15 min.=20 Although the numbers of adherent cells in scr/LN-229 cells and=20 siPKCζ/LN-229 cells increased after incubated with EGF for = 30 min,=20 there was no statistically significant difference between these = two groups=20 (Fig. 4a).=20 Integrin β1 is the main adhesion mediating molecule in tumor = cells and its=20 phosphorylation can promote cell attachment. Thus, we examined the = EGF-induced activation of integrin β1 by western blotting = analysis. As=20 shown in Fig. 4(b),=20 EGF-induced phosphorylation of integrin β1 was severely = impaired in=20 siPKCζ/LN-229 cells, consistent with the reduction in = adhesion. Our=20 results suggested that the PKCζ directly mediated migration = signal=20 pathways through regulation of EGF-induced cell adhesion in LN-229 = cells.

=20

= Fig. 4=20 Disruption of PKCζ by siRNA impaired = adhesion of LN-229=20 cells. (a) Comparison of 10 ng/mL EGF-induced adhesion = at=20 5 min, 15 min, and 30 min of scr/LN-229 cells = to that=20 of siPKCζ/LN-229 cells on fibronectin-coated = coverslips. Cell=20 numbers in each high power field (HPF) were counted in five = fields=20 on every coverslips under microscopy (200=D7) (Data from = three=20 independent experiments summarized as = mean =B1 SEM, n =3D 3. *p < 0.05, two-way=20 anova.) (b) Western = blotting=20 analysis of phosphorylated integrin β1 in total cell = lysates from=20 scr/LN-229 and siPKCζ/LN-229 cells after stimulating = with=20 10 ng/mL EGF for 0 min, 2 min, and = 5 min.=20 Integrin β1 was used as a loading control. =

[Normal=20 View ]

=20

=20

PKCζ pseudosubstrate blocked = EGF-induced=20 chemotaxis

To further confirm our observation by PKCζ = siRNA (Fig. 2a),=20 we investigated the role of PKCζ in glioblastoma cells by = using a=20 myristoylated pseudosubstrate, which is a proven specific = inhibitor of=20 PKCζ. Myristoylation of this pseudosubstrate was required to = deliver this=20 polypeptide through the plasma membrane (Laudanna=20 et al. 1998). As shown in Fig. 5(a),=20 the non-myristoylated peptide at 50 μM, which served as = a negative=20 control, had no detectible effect on EGF-induced chemotaxis in = LN-229=20 cells. However, the addition of specific myristoylated peptide = could=20 apparently inhibit EGF-induced chemotaxis in a dose-dependent = manner. The=20 inhibitory effects were further confirmed by EGF-induced = chemotaxis in U87=20 cells (Fig. 5b).=20 Following this, we evaluated the inhibitory effect of a specific=20 pseudosubstrate on cell adhesion. Within 5 min, treatment = with=20 10 ng/mL EGF significantly impaired cell adhesion after the = specific=20 myristoylated PKCζ pseudosubstrate treated these two = glioblastoma cell=20 lines (Fig. 5c).=20 Altogether, the results suggested that PKCζ was specifically = required for=20 EGF-induced cell migration and adhesion.

=20

= Fig. 5 = Specific=20 PKCζ pseudosubstrates blocked EGF-induced chemotaxis = and adhesion in=20 glioblastoma cells. (a) Blockage of chemotaxis in LN-229 = cells by=20 myristoylated PKCζ pseudosubstrate peptide under EGF = stimulation=20 (Data from three independent experiments summarized as=20 mean =B1 SEM, n =3D 3. *p < 0.05, **p < 0.01, ***p < 0.001, two-way=20 anova.) (b) Inhibitory = effect of=20 50 μM PKCζ pseudosubstrates on EGF-induced = LN-229 and U87=20 glioblastoma cells chemotaxis. (Data from three independent=20 experiments summarized as mean =B1 SEM, n =3D 3. **p < 0.01, two-way=20 anova.) Cells were = collected and=20 incubated with myristoylated pseudosubstrate peptide,=20 non-myristoylated peptide, or PBS at 37=B0C for 45 min = before=20 chemotaxis assay for (a) or (b). (c) The impairment on cell = adhesion=20 with pseudosubstrate treatment. LN-229 and U87 cells were=20 pre-treated with myristoylated pseudosubstrate peptide,=20 non-myristoylated peptide, or PBS at 37=B0C for 45 min = before=20 10 ng/mL EGF stimulation. (Data from three independent=20 experiments summarized as mean =B1 SEM, n =3D 3. **p < 0.01, two-way=20 anova.) =

[Normal=20 View ]

=20

=20

Reduction of PKCζ expression = impaired=20 glioblastoma cells invasion

Cell migration is essential in tumor invasion and=20 metastasis. We have demonstrated that PKCζ plays a key role = in LN-229=20 cells migration, hence we hypothesize that PKCζ has a pivotal = effect on=20 glioblastoma cells invasion. To measure the effects of PKCζ = on=20 glioblastoma cell invasiveness, we employed a Transwell invasion = system.=20 The system consisted of two fluid-filled stacked compartments = separated by=20 a porous membrane filter coated with Matrigel. It was then = observed that=20 the siPKCζ/LN-229 cells that invaded through the Matrigel = were much less=20 compared to the scr/LN-229 cells (Fig. 6a).=20 The quantitative analysis of cell numbers revealed that the = siPKCζ/LN-229=20 cells had a 4.3-fold lower invasion rate than that of the = scr/LN-229 cells=20 in response to the 10 ng/mL EGF (Fig. 6b).

=20

= Fig. 6=20 Disruption of PKCζ by siRNA impaired = invasion into=20 matrigel in LN-229 cells and also impaired the invasion of=20 glioblastoma cells in vivo. (a) = Invasion was=20 measured as described in 'Materials=20 and Methods.' The cells that invaded through = matrigel-coated=20 transwell inserts toward chemoattractant were stained. = Photographs=20 were taken at a magnification of 200=D7. (b) The cells = invading=20 through the matrigel were counted under microscope in five=20 pre-determined fields at 400=D7. Data are shown as=20 mean =B1 SEM, n =3D 3. **p < 0.01, two-way=20 anova. (c) Western = blotting=20 analysis of MMP-2 and MMP-9 expression in scr/LN-229 cells = and=20 siPKCζ/LN-229 cells. β-Actin was used as a loading = control. (d)=20 LN-229 cells were transfected with either control or = PKCζ siRNA=20 plasmid followed by the isolation of stable clones. Cell = lysates of=20 each representative clone were analyzed by western blotting = using=20 anti-PKCζ antibody and anti-β-actin antibody. (e) = Frequency of=20 xenograft invasion in control group and three clones of the = PKCζ=20 knockdown groups (10 mice for each group, *p < 0.05,=20 Chi-square Test). (f) Glioblastoma-xenografted tumors were = sectioned=20 for H&E staining to identify tumor regions. (i) and = (ii): tumors=20 of scr/LN-229-cells-injected mice group. (iii) and (iv): = tumors of=20 siPKCζ/LN-229-cells-injected mice group. Panel (v) and = (vi) are=20 enlarged figures of (i) and (ii), respectively. (Arrows = indicate the=20 invasive scr/LN-229 cells). Top row, 100=D7; bottom row, = 200=D7.=20

[Normal View=20 ]

Processes of tumor cell invasion into the stromal = tissues=20 are closely related to the interactions between tumor cells and = the=20 extracellular matrix (ECM). MMPs degrade the ECM at tumor-invasive = fronts=20 to overcome the ECM barrier, and subsequently enabling tumor cells = to=20 penetrate into adjacent brain structures. In the MMP family, the = MMP-2 and=20 MMP-9 are two of its important members. It has been reported that = MMP-9=20 protein expression was inhibited by PI3K/Akt down-regulation (Lungu=20 et al. 2008). In our current = study, in order=20 to detect the fundamental response of MMP-2 and MMP-9 to PKCζ = deficiency,=20 we applied western blot to show the protein levels of them in = LN-229=20 cells. Of the two, we found that MMP-9 expression in = siPKCζ/LN-229 cells=20 was significantly inhibited, while the MMP-2 expression remained = almost=20 unchanged (Fig. 6c).=20 This is consistent with the previous report (Esteve=20 et al. 2002).

=20

=20

Disruption of PKCζ by siRNA = inhibited the=20 invasion of glioblastoma cells in vivo

After we demonstrated, through the above results, = that=20 disruption of PKCζ decreased migration and invasion of LN-229 = and U87=20 cells in vitro, we next used the = subcutaneous mouse=20 xenograft model to validate the role of PKCζ in glioblastoma = invasion=20 in vivo. In particular, the LN-229 cells = were=20 transfected with plasmid expressing either PKCζ siRNA or = control plasmid,=20 and several independent stable clones were isolated. Clone 3 = showed about=20 40% reduction of PKCζ, while clone 16 and 9 presented about = 70% and 85%=20 reduction of PKCζ, respectively, compared with the LN-229 = cells (Fig. 6d).=20 Clones 3, 9, 16 and the scr/LN-229 clone cells were chosen for = further=20 in vivo tumor invasion assays. The = frequency of=20 xenograft invasion of 10 Nu/Nu mice in each group was compared. = Group of=20 clone 3 and clone 16 showed small differences compared with the = control=20 group, respectively (p =3D 0.65, = p =3D 0.37); the frequency of xenograft = invasion in=20 clone 9 group was greatly decreased (p =3D 0.02) (Fig. 6e).=20 Representative tissue sections of Haematoxylin and Eosin (HE) = staining=20 showed that multiple invasion sites of tumors were observed = surrounding=20 the tumor boundary in scr/LN-229 clone group, but not in mice = injected=20 with clone 9 cells (Fig. 6f).

=20

=20

Discussion

=

=

=

Protein kinase C is a family of enzymes that = mediates the=20 normal cellular signaling pathways downstream of growth factors = receptors.=20 It controls many cellular key functions, such as cell = proliferation,=20 survival, and migration (Donson=20 et al. 2000). PKCζ, an = atypical subtype of=20 the PKC family, has been found to be involved in migration of = breast=20 cancer cells (Sun=20 et al. 2005). The expression of = PKCζ in=20 glioblastomas was reported to be two times higher than the level = in normal=20 glial cells (Acevedo-Duncan=20 et al. 2004). Although protein = levels do not=20 represent enzyme activity levels, the over-expression of PKCζ = suggests it=20 is involved in the malignant phenotype of glioblastomas. = Therefore,=20 elucidation of PKCζ signals associated with glioblastoma = migration and=20 invasion is crucial in revealing the mechanisms behind = glioblastoma=20 infiltration. In this study, we have shown that PKCζ is a key = effector of=20 migration and invasion in human glioblastoma cells. In addition, = we also=20 illustrated the fundamental molecular processes of glioblastoma = migration=20 and invasion in which PKCζ is a participant.

Directed cell migration and cell polarity are = crucial in=20 many biological processes, including wound healing and immune = responses,=20 as well as in pathological phenomena such as tissue invasion and=20 metastasis formation. In our study, the down-regulation of = PKCζ expression=20 by siRNA in the chemotaxis and scratch assays severely impaired = the=20 migration ability of the LN-229 cells. This result suggested the = general=20 involvement of PKCζ in glioblastoma cell migration. In = addition, actin=20 polymerization and the subsequent formation of membrane = protrusions are=20 required for cell migration. This remodeling of the actin = cytoskeleton is=20 important for the motility and chemotaxis of cancer cells as it=20 consequently influences the metastatic capability of these cells. = Our=20 results showed that PKCζ participates in actin polymerization = to mediate=20 cytoskeletal rearrangement, which plays an important role in = glioblastoma=20 cells migration and invasion.

Indeed, the cytoskeleton inside the cell assumes a = significant task in cell migration and invasion. Regulation of = actin=20 polymerization of the cytoskeleton allows cells to control their = shape and=20 to move. Many studies have shown that LIMK phosphorylates cofilin, = in turn=20 regulates actin polymerization (Arber=20 et al. 1998; Yang=20 et al. 1998). Our results showed = that the=20 down-regulation of PKCζ expression in LN-229 cells resulted = in attenuated=20 phosphorylation of both LIMK and cofilin. Thus, PKCζ = regulates=20 phosphorylation of LIMK and cofilin in actin polymerization, which = in turn=20 influences migration of gliblastoma cells. Moreover, integrin = β1 is a key=20 adhesion molecule in regulating cell=96cell and cell=96matrix = adhesions,=20 thereby playing a critical role in different aspects of tumor = formation=20 and invasion. Results in our current study demonstrated that the = PKCζ=20 reduction led to the decrease in phosphorylation of integrin = β1 in LN-229=20 cells. As a result, we speculate that the inhibition of PKCζ = activation=20 will further enhance a drastic decrease in integrin β1 = recycling and=20 finally lead to the impairment of cells adhesion. Taken together = with our=20 previous reports (Sun=20 et al. 2005; Wang=20 et al. 2008), we propose a simple = signaling=20 model: EGF-induced activation of PI3K/Akt/PKCζ pathways = leading to=20 rearrangement of cell cytoskeleton through LIMK/cofilin, and cell = adhesion=20 through integrin β1.

In the present study, not only did the cellular = experiments=20 in vitro indicate the reduction of = PKCζ inhibited=20 invasion of glioblastoma cells but the animal experiments as well. = By=20 invasion detection in vivo, the frequency = of=20 xenograft invasion in mice significantly decreased after PKCζ = was=20 significantly knocked down compared with the control. The = efficiency of=20 the PKCζ knockdown correlated with the extent of suppression = of invasion.=20 The invasive characteristics of glioblastoma cells depend mainly = on the=20 degradation of ECM by proteases and the induction of cell motility = and=20 invasion (Nakada=20 et al. 2003). MMPs secreted by = tumor cells=20 can degrade the ECM at tumor-invasive fronts to overcome the ECM = barrier.=20 In fact, it is proposed that the high levels of MMP expression = observed in=20 high-grade gliomas serve to facilitate the tumor cells' invasion = (Fillmore=20 et al. 2001). MMP-2 and MMP-9 are = considered=20 to be particularly efficient with their ability to cleave type IV=20 collagen, a major component of basement membrane (Timpl=20 1989). Moreover, increased production of MMP-2 and MMP-9 = appeared to=20 correlate with the malignant progression of human glioma in=20 vivo (Forsyth=20 et al. 1999; Wild-Bode=20 et al. 2001). We demonstrated the=20 significant decrease of MMP-9 expression in siPKCζ/LN-229 = cells, while=20 MMP-2 expression was constant. Of note, the involvement of MMP-9 = in the=20 PKCζ signaling pathway has been reported in various cell = types, such as=20 human breast cancer, pituitary adenoma, and non-small cell lung = cancer (Wang=20 et al. 2006; Hussaini=20 et al. 2007; Lungu=20 et al. 2008). While MMP-2 = regulated by PKCα,=20 PKCβ and PKCε were established in human melanoma, = cardiac microvascular=20 endothelial cells, and ciliary muscle cells, respectively. = Accordingly,=20 the functions of MMP-2 and MMP-9 most likely depend on different = cell=20 types or PKC isoforms. It has been reported that MMP-9 can form = complex=20 with β integrin, which is a part of the mechanism guiding = migration in=20 human THP-1 cells and microvascular endothelial cells and such = migration=20 is blocked by inhibitors of MMP-9 or β integrin, (Stefanidakis=20 et al. 2004). In the present = study, we=20 speculated that the inhibition of MMP-9 expression by reduction of = PKCζ=20 maybe explains the inhibitory effect of PKCζ on glioblastoma = cells=20 invasion.

PI3K/t-strain from AKR/J mouse (AKT)/PKCζ and = the=20 Ras/Raf/mitogen activated protein kinase kinase = (MEK)/Extracellular=20 signal-regulated protein kinase (ERK) (MAPK) are the two most = important=20 signaling cascades frequently dysregulated in cancer. There is = cross-talk=20 between two such pathways (Grant=20 2008). Two research groups, Waugh Kinkade et al. and Carracedo et al.,=20 observed that the simultaneous inhibition of MEK/ERK and the = downstream=20 factor of PI3K/AKT/PKCζ resulted in substantially enhanced = anti-tumor=20 effects both in vivo and in = vitro (Carracedo=20 et al. 2008; Kinkade=20 et al. 2008). Furthermore, = Alejandro J.=20 demonstrated that over-expression of PKCζ modulates = clonogenicity, cell=20 adhesiveness, motility, and proteases secretion of normal murine = mammary=20 cells through the activation of the ERK/MAPK pathway (Urtreger=20 et al. 2005). In our groups, the = precise=20 relationship between PI3K and MAPK signaling pathways remains = under=20 investigation.

In summary, we demonstrated that PKCζ is = required for=20 glioblastoma cell migration and invasion. These findings are = highly=20 important when contemplating novel treatments for glioblastomas, = which=20 have a tendency to diffuse, conveyed by single cells leaving the = core=20 lesion and invading healthy brain tissues, eventually creating = recurrent=20 tumors. Although the mechanism of PKCζ function in = glioblastomas requires=20 further clarification, our results potentially suggest that = inhibition of=20 PKCζ function would bring about progress in glioblastoma=20 therapy.

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=20

Acknowledgements

=

=

This work was supported by project grants from = China 973=20 program (2006CB705600) and 863 program (2006AA02Z19C) = (2007AA021802),=20 National Scientific Foundation of China (30700253) and (30800355), = Tianjin=20 Medical University Research Project (2006KY21), China program of=20 Changjiang scholar and innovative research team in University, = China=20 project of 2008 SRF for ROCS SEM.

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