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NCBIBookshelf.AserviceoftheNationalLibraryofMedicine,NationalInstitutesofHealth.

CooperGM.TheCell:AMolecularApproach.2ndedition.Sunderland(MA):SinauerAssociates2000.

CellWallsandtheExtracellularMatrix
Althoughcellboundariesaredefinedbytheplasmamembrane,manycellsaresurroundedbyan
insolublearrayofsecretedmacromolecules.Cellsofbacteria,fungi,algae,andhigherplantsare
surroundedbyrigidcellwalls,whichareanintegralpartofthecell.Althoughnotencasedincell
walls,animalcellsintissuesarecloselyassociatedwithanextracellularmatrixcomposedof
proteinsandpolysaccharides.Theextracellularmatrixnotonlyprovidesstructuralsupporttocells
andtissues,butalsoplaysimportantrolesinregulatingthebehaviorofcellsinmulticellular
organisms.
BacterialCellWalls
Therigidcellwallsofbacteriadeterminecellshapeandpreventthecellfromburstingasaresultof
osmoticpressure.Thestructureoftheircellwallsdividesbacteriaintotwobroadclassesthatcan
bedistinguishedbyastainingprocedureknownastheGramstain,developedbyChristianGramin
1884(Figure12.44).Asdescribedearlierinthischapter,Gramnegativebacteria(suchasE.coli)
haveadualmembranesystem,inwhichtheplasmamembraneissurroundedbyapermeableouter
membrane.Thesebacteriahavethincellwallslocatedbetweentheirinnerandoutermembranes.In
contrast,Grampositivebacteria(suchasthecommonhumanpathogenStaphylococcusaureus)
haveonlyasingleplasmamembrane,whichissurroundedbyamuchthickercellwall.
Figure12.44

Bacterialcellwalls.TheplasmamembraneofGramnegative
bacteriaissurroundedbyathincellwallbeneaththeouter
membrane.Grampositivebacterialackoutermembranesand
havethickcellwalls.

Despitethesestructuraldifferences,theprincipalcomponentofthecellwallsofbothGram
positiveandGramnegativebacteriaisapeptidoglycan(Figure12.45)consistingoflinear
polysaccharidechainscrosslinkedbyshortpeptides.Becauseofthiscrosslinkedstructure,the
peptidoglycanformsastrongcovalentshellaroundtheentirebacterialcell.Interestingly,the
uniquestructureoftheircellwallsalsomakesbacteriavulnerabletosomeantibiotics.Penicillin,for
example,inhibitstheenzymeresponsibleforformingcrosslinksbetweendifferentstrandsofthe
peptidoglycan,therebyinterferingwithcellwallsynthesisandblockingbacterialgrowth.
Figure12.45

ThepeptidoglycanofE.coli.Polysaccharidechainsconsistof
alternatingNacetylglucosamine(NAG)andNacetylmuramic
acid(NAM)residuesjoinedby(14)glycosidicbonds.
Parallelchainsarecrosslinkedbytetrapeptidesattachedto
(more...)
PlantCellWalls
Incontrasttobacteria,thecellwallsofeukaryotes(includingfungi,algae,andhigherplants)are
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composedprincipallyofpolysaccharides(Figure12.46).Thebasicstructuralpolysaccharideof
fungalcellwallsischitin(apolymerofNacetylglucosamineresidues),whichalsoformsthe
exoskeletonofarthropods(e.g.,theshellsofcrabs).Thecellwallsofmostalgaeandhigherplants
arecomposedprincipallyofcellulose,whichisthesinglemostabundantpolymeronEarth.
Celluloseisalinearpolymerofglucoseresidues,oftencontainingmorethan10,000glucose
monomers.Theglucoseresiduesarejoinedby(14)linkages,whichallowthepolysaccharide
toformlongstraightchains.Severaldozensuchchainsthenassociateinparallelwithoneanother
toformcellulosemicrofibrils,whichcanextendformanymicrometersinlength.
Figure12.46

Polysaccharidesoffungalandplantcellwalls.(A)Chitin(the
principalpolysaccharideoffungalcellwalls)isalinear
polymerofNacetylglucosamineresidues,whereascelluloseis
alinearpolymerofglucose.Thecarbohydratemonomersare
joined(more...)

Withinthecellwall,cellulosemicrofibrilsareembeddedinamatrixconsistingofproteinsandtwo
othertypesofpolysaccharides:hemicellulosesandpectins(Figure12.47).Hemicellulosesare
highlybranchedpolysaccharidesthatarehydrogenbondedtothesurfaceofcellulosemicrofibrils.
Thiscrosslinksthecellulosemicrofibrilsintoanetworkoftough,fibrousmolecules,whichis
responsibleforthemechanicalstrengthofplantcellwalls.Pectinsarebranchedpolysaccharides
containingalargenumberofnegativelychargedgalacturonicacidresidues.Becauseofthese
multiplenegativecharges,pectinsbindpositivelychargedions(suchasCa2+)andtrapwater
moleculestoformgels.Anillustrationoftheirgelformingpropertiesisprovidedbythefactthat
jamsandjelliesareproducedbytheadditionofpectinstofruitjuice.Inthecellwall,thepectins
formagellikenetworkthatisinterlockedwiththecrosslinkedcellulosemicrofibrils.Inaddition,
cellwallscontainavarietyofglycoproteinsthatareincorporatedintothematrixandarethoughtto
providefurtherstructuralsupport.
Figure12.47

Modelofaplantcellwall.(A)Structuresofarepresentative
hemicellulose(xyloglucan)andpectin(rhamnogalacturonan).
Xyloglucanconsistsofabackboneofglucose(Glc)residues
withsidechainsofxylose(Xyl),galactose(Gal),andfucose
(Fuc).(more...)
Boththestructureandfunctionofcellwallschangeasplantcellsdevelop.Thewallsofgrowing
plantcells(calledprimarycellwalls)arerelativelythinandflexible,allowingthecelltoexpandin
size.Oncecellshaveceasedgrowth,theyfrequentlylaydownsecondarycellwallsbetweenthe
plasmamembraneandtheprimarycellwall(Figure12.48).Suchsecondarycellwalls,whichare
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boththickerandmorerigidthanprimarywalls,areparticularlyimportantincelltypesresponsible
forconductingwaterandprovidingmechanicalstrengthtotheplant.
Figure12.48

Primaryandsecondarycellwalls.Secondarycellwallsarelaid
downbetweentheprimarycellwallandtheplasma
membrane.Secondarywallsfrequentlyconsistofthreelayers,
whichdifferintheorientationoftheircellulosemicrofibrils.
Electronmicrographs(more...)
Primaryandsecondarycellwallsdifferincompositionaswellasinthickness.Primarycellwalls
containapproximatelyequalamountsofcellulose,hemicelluloses,andpectins.Incontrast,the
morerigidsecondarywallsgenerallylackpectinandcontain50to80%cellulose.Manysecondary
wallsarefurtherstrengthenedbylignin,acomplexpolymerofphenolicresiduesthatisresponsible
formuchofthestrengthanddensityofwood.Theorientationofcellulosemicrofibrilsalsodiffers
inprimaryandsecondarycellwalls.Thecellulosefibersofprimarywallsappeartoberandomly
arranged,whereasthoseofsecondarywallsarehighlyordered(seeFigure12.48).Secondarywalls
arefrequentlylaiddowninlayersinwhichthecellulosefibersdifferinorientation,forminga
laminatedstructurethatgreatlyincreasescellwallstrength.
Oneofthecriticalfunctionsofplantcellwallsistopreventcellswellingasaresultofosmotic
pressure.Incontrasttoanimalcells,plantcellsdonotmaintainanosmoticbalancebetweentheir
cytosolandextracellularfluids.Consequently,osmoticpressurecontinuallydrivestheflowof
waterintothecell.Thiswaterinfluxistoleratedbyplantcellsbecausetheirrigidcellwallsprevent
swellingandbursting.Instead,aninternalhydrostaticpressure(calledturgorpressure)buildsup
withinthecell,eventuallyequalizingtheosmoticpressureandpreventingthefurtherinfluxof
water.
Turgorpressureisresponsibleformuchoftherigidityofplanttissues,asisreadilyapparentfrom
examinationofadehydrated,wiltedplant.Inaddition,turgorpressureprovidesthebasisforaform
ofcellgrowththatisuniquetoplants.Inparticular,plantcellsfrequentlyexpandbytakingup
waterwithoutsynthesizingnewcytoplasmiccomponents(Figure12.49).Cellexpansionbythis
mechanismissignaledbyplanthormones(auxins)thatweakenaregionofthecellwall,allowing
turgorpressuretodrivetheexpansionofthecellinthatdirection.Asthisoccurs,thewaterthat
flowsintothecellaccumulateswithinalargecentralvacuole,sothecellexpandswithout
increasingthevolumeofitscytosol.Suchexpansioncanresultina10to100foldincreaseinthe
sizeofplantcellsduringdevelopment.
Figure12.49

Expansionofplantcells.Turgorpressuredrivestheexpansion
ofplantcellsbytheuptakeofwater,whichisaccumulatedina
largecentralvacuole.

Ascellsexpand,newcomponentsofthecellwallaredepositedoutsidetheplasmamembrane.
Matrixcomponents,includinghemicellulosesandpectins,aresynthesizedintheGolgiapparatus
andsecreted.Cellulose,however,issynthesizedbyaplasmamembraneenzymecomplex
(cellulosesynthase).Inexpandingcells,thenewlysynthesizedcellulosemicrofibrilsaredeposited
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atrightanglestothedirectionofcellelongationanorientationthatisthoughttoplayanimportant
roleindeterminingthedirectionoffurthercellexpansion(Figure12.50).Interestingly,the
cellulosemicrofibrilsinelongatingcellwallsarelaiddowninparalleltocorticalmicrotubules
underlyingtheplasmamembrane.Thesemicrotubulesappeartodefinetheorientationofnewly
synthesizedcellulosemicrofibrils,possiblybydeterminingthedirectionofmovementofthe
cellulosesynthasecomplexesinthemembrane.Thecorticalmicrotubulesthusdefinethedirection
ofcellwallgrowth,whichinturndeterminesthedirectionofcellexpansionandultimatelythe
shapeoftheentireplant.
Figure12.50

Cellulosesynthesisduringcellelongation.Newcellulose
microfibrils,synthesizedbyaplasmamembraneenzyme
complex(cellulosesynthase),arelaiddownatrightanglesto
thedirectionofcellelongation.Thedirectionofcellulose
synthesisisparallel(more...)
TheExtracellularMatrix
Althoughanimalcellsarenotsurroundedbycellwalls,manyofthecellsintissuesofmulticellular
organismsareembeddedinanextracellularmatrixconsistingofsecretedproteinsand
polysaccharides.Theextracellularmatrixfillsthespacesbetweencellsandbindscellsandtissues
together.Onetypeofextracellularmatrixisexemplifiedbythethin,sheetlikebasallaminae,or
basementmembranes,uponwhichlayersofepithelialcellsrest(Figure12.51).Inadditionto
supportingsheetsofepithelialcells,basallaminaesurroundmusclecells,adiposecells,and
peripheralnerves.Extracellularmatrix,however,ismostabundantinconnectivetissues.For
example,thelooseconnectivetissuebeneathepithelialcelllayersconsistspredominantlyofan
extracellularmatrixinwhichfibroblastsaredistributed.Othertypesofconnectivetissue,suchas
bone,tendon,andcartilage,similarlyconsistlargelyofextracellularmatrix,whichisprincipally
responsiblefortheirstructureandfunction.
Figure12.51

Examplesofextracellularmatrix.Sheetsofepithelialcellsrest
onathinlayerofextracellularmatrixcalledabasallamina.
Beneaththebasallaminaislooseconnectivetissue,which
consistslargelyofextracellularmatrixsecretedbyfibroblasts.
(more...)

Extracellularmatricesarecomposedoftoughfibrousproteinsembeddedinagellike
polysaccharidegroundsubstanceadesignbasicallysimilartothatofplantcellwalls.Inaddition
tofibrousstructuralproteinsandpolysaccharides,theextracellularmatrixcontainsadhesion
proteinsthatlinkcomponentsofthematrixbothtooneanotherandtoattachedcells.The
differencesbetweenthevarioustypesofextracellularmatrixresultfromvariationsonthisgeneral
theme.Forexample,tendonscontainahighproportionoffibrousproteins,whereascartilage
containsahighconcentrationofpolysaccharidesthatformafirmcompressionresistantgel.In
bone,theextracellularmatrixishardenedbydepositionofcalciumphosphatecrystals.The
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sheetlikestructureofbasallaminaealsoresultsfromtheutilizationofmatrixcomponentsthatdiffer
fromthosefoundinconnectivetissues.
Themajorstructuralproteinoftheextracellularmatrixiscollagen,whichisthesinglemost
abundantproteininanimaltissues.Thecollagensarealargefamilyofproteins,containingatleast
19differentmembers.Theyarecharacterizedbytheformationoftriplehelicesinwhichthree
polypeptidechainsarewoundtightlyaroundoneanotherinaropelikestructure(Figure12.52).
ThetriplehelixdomainsofthecollagensconsistofrepeatsoftheaminoacidsequenceGlyXY.
Aglycine(thesmallestaminoacid,withasidechainconsistingonlyofahydrogen)isrequiredin
everythirdpositioninorderforthepolypeptidechainstopacktogethercloseenoughtoformthe
collagentriplehelix.ProlineisfrequentlyfoundintheXpositionandhydroxyprolineintheY
positionbecauseoftheirringstructure,theseaminoacidsstabilizethehelicalconformationsofthe
polypeptidechains.Theunusualaminoacidhydroxyprolineisformedwithintheendoplasmic
reticulumbymodificationofprolineresiduesthathavealreadybeenincorporatedintocollagen
polypeptidechains(Figure12.53).Lysineresiduesincollagenarealsofrequentlyconvertedto
hydroxylysines.Thehydroxylgroupsofthesemodifiedaminoacidsarethoughttostabilizethe
collagentriplehelixbyforminghydrogenbondsbetweenpolypeptidechains.Theseaminoacids
arerarelyfoundinotherproteins,althoughhydroxyprolineisalsocommoninsomeofthe
glycoproteinsofplantcellwalls.
Figure12.52

Structureofcollagen.(A)Threepolypeptidechainscoil
aroundoneanotherinacharacteristictriplehelixstructure.(B)
Theaminoacidsequenceofacollagentriplehelixdomain
consistsofGlyXYrepeats,inwhichXisfrequentlyproline
andYis(more...)

Figure12.53

Formationofhydroxyproline.Prolylhydroxylaseconverts
prolineresiduesincollagentohydroxyproline.

Themostabundanttypeofcollagen(typeIcollagen)isoneofthefibrilformingcollagensthatare
thebasicstructuralcomponentsofconnectivetissues(Table12.2).Thepolypeptidechainsofthese
collagensconsistofapproximatelyathousandaminoacidsor330GlyXYrepeats.Afterbeing
secretedfromthecell,thesecollagensassembleintocollagenfibrilsinwhichthetriplehelical
moleculesareassociatedinregularstaggeredarrays(Figure12.54).Thesefibrilsdonotform
withinthecell,becausethefibrilformingcollagensaresynthesizedassolubleprecursors
(procollagens)thatcontainnonhelicalsegmentsatbothendsofthepolypeptidechain.Procollagen
iscleavedtocollagenafteritssecretion,sotheassemblyofcollagenintofibrilstakesplaceonly
outsidethecell.Theassociationofcollagenmoleculesinfibrilsisfurtherstrengthenedbythe
formationofcovalentcrosslinksbetweenthesidechainsoflysineandhydroxylysineresidues.
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Frequently,thefibrilsfurtherassociatewithoneanothertoformcollagenfibers,whichcanbe
severalmicrometersindiameter.
Table12.2

RepresentativeMembersoftheCollagenFamily.
Figure12.54

Collagenfibrils.(A)Collagenmoleculesassembleinaregular
staggeredarraytoformfibrils.Themoleculesoverlapbyone
fourthoftheirlength,andthereisashortgapbetweentheN
terminusofonemoleculeandtheCterminusofthenext.The
assembly(more...)
Severalothertypesofcollagendonotformfibrilsbutplaydistinctrolesinvariouskindsof
extracellularmatrices.Inadditiontothefibrilformingcollagens,connectivetissuescontainfibril
associatedcollagens,whichbindtothesurfaceofcollagenfibrilsandlinkthembothtooneanother
andtoothermatrixcomponents.Basallaminaeformfromadifferenttypeofcollagen(typeIV
collagen),whichisanetworkformingcollagen(Figure12.55).TheGlyXYrepeatsofthese
collagensarefrequentlyinterruptedbyshortnonhelicalsequences.Becauseoftheseinterruptions,
thenetworkformingcollagensaremoreflexiblethanthefibrilformingcollagens.Consequently,
theyassembleintotwodimensionalcrosslinkednetworksinsteadoffibrils.Yetanothertypeof
collagenformsanchoringfibrils,whichlinksomebasallaminaetounderlyingconnectivetissues.
Figure12.55

TypeIVcollagen.(A)TheGlyXYrepeatstructureoftype
IVcollagen(yellow)isinterruptedbymultiplenonhelical
sequences(bars).(B)ElectronmicrographofatypeIV
collagennetwork.(B,P.D.YurchencoandJ.C.Schittny,
1990.FASEBJ.4:1577.)(more...)
Connectivetissuesalsocontainelasticfibers,whichareparticularlyabundantinorgansthat
regularlystretchandthenreturntotheiroriginalshape.Thelungs,forexample,stretcheachtimea
breathisinhaledandreturntotheiroriginalshapewitheachexhalation.Elasticfibersare
composedprincipallyofaproteincalledelastin,whichiscrosslinkedintoanetworkbycovalent
bondsformedbetweenthesidechainsoflysineresidues(similartothosefoundincollagen).This
networkofcrosslinkedelastinchainsbehaveslikearubberband,stretchingundertensionandthen
snappingbackwhenthetensionisreleased.
Thefibrousstructuralproteinsoftheextracellularmatrixareembeddedingelsformedfrom
polysaccharidescalledglycosaminoglycans,orGAGs,whichconsistofrepeatingunitsof
disaccharides(Figure12.56).OnesugarofthedisaccharideiseitherNacetylglucosamineorN
acetylgalactosamineandthesecondisusuallyacidic(eitherglucuronicacidoriduronicacid).With
theexceptionofhyaluronan,thesesugarsaremodifiedbytheadditionofsulfategroups.
Consequently,GAGsarehighlynegativelycharged.Likethepectinsofplantcellwalls,theybind
positivelychargedionsandtrapwatermoleculestoformhydratedgels,therebyproviding
mechanicalsupporttotheextracellularmatrix.
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Figure12.56

Majortypesofglycosaminoglycans.Glycosaminoglycansconsistofrepeating
disaccharideunits.Withtheexceptionofhyaluronan,thesugarsfrequently
containsulfate.Heparansulfateissimilartoheparinexceptthatitcontainsfewer
sulfategroups.(more...)
HyaluronanistheonlyGAGthatoccursasasinglelongpolysaccharidechain.Alloftheother
GAGsarelinkedtoproteinstoformproteoglycans,whichcanconsistofupto95%polysaccharide
byweight.ProteoglycanscancontainasfewasoneorasmanyasmorethanahundredGAG
chainsattachedtoserineresiduesofacoreprotein.Avarietyofcoreproteins(rangingfrom10to
>500kd)havebeenidentified,sotheproteoglycansareadiversegroupofmacromolecules.In
additiontobeingcomponentsoftheextracellularmatrix,someproteoglycansarecellsurface
proteinsthatfunctionincelladhesion.
Anumberofproteoglycansinteractwithhyaluronantoformlargecomplexesintheextracellular
matrix.Awellcharacterizedexampleisaggrecan,themajorproteoglycanofcartilage(Figure
12.57).Morethanahundredchainsofchondroitinsulfateareattachedtoacoreproteinofabout
250kd,formingaproteoglycanofabout3000kd.Multipleaggrecanmoleculesthenassociatewith
chainsofhyaluronan,forminglargeaggregates(>100,000kd)thatbecometrappedinthecollagen
network.Proteoglycansalsointeractwithbothcollagenandothermatrixproteinstoformgellike
networksinwhichthefibrousstructuralproteinsoftheextracellularmatrixareembedded.For
example,perlecan(themajorheparansulfateproteoglycanofbasallaminae)bindstobothtypeIV
collagenandtotheadhesionproteinlaminin,whichisdiscussedshortly.
Figure12.57

Complexesofaggrecanandhyaluronan.Aggrecanisalarge
proteoglycanconsistingofmorethan100chondroitinsulfate
chainsjoinedtoacoreprotein.Multipleaggrecanmolecules
bindtolongchainsofhyaluronan,forminglargecomplexesin
theextracellular(more...)

Adhesionproteins,thethirdclassofextracellularmatrixconstituents,areresponsibleforlinkingthe
componentsofthematrixbothtooneanotherandtothesurfacesofcells.Theprototypeofthese
moleculesisfibronectin,whichistheprincipaladhesionproteinofconnectivetissues.Fibronectin
isadimericglycoproteinconsistingoftwopolypeptidechains,eachcontainingnearly2500amino
acids(Figure12.58).Intheextracellularmatrix,fibronectinisfurthercrosslinkedintofibrilsby
disulfidebonds.FibronectinhasbindingsitesforbothcollagenandGAGs,soitcrosslinksthese
matrixcomponents.Adistinctsiteonthefibronectinmoleculeisrecognizedbycellsurface
receptorsandisthusresponsiblefortheattachmentofcellstotheextracellularmatrix.
Figure12.58

Structureoffibronectin.Fibronectinisadimerofsimilar
polypeptidechainsjoinedbydisulfidebondsneartheC
terminus.Sitesforbindingtoproteoglycans,cells,and
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collagenareindicated.Themoleculealsocontainsadditional
bindingsitesthat(more...)
Basallaminaecontainadistinctadhesionproteincalledlaminin(Figure12.59).LiketypeIV
collagen,lamininscanselfassembleintomeshlikepolymers.Suchlamininnetworksarethemajor
structuralcomponentsofthebasallaminaesynthesizedinveryearlyembryos,whichdonot
containcollagen.Thelamininsalsohavebindingsitesforcellsurfacereceptors,typeIVcollagen,
andperlecan.Inaddition,lamininsaretightlyassociatedwithanotheradhesionprotein,called
entactinornidogen,whichalsobindstotypeIVcollagen.Asaresultofthesemultiple
interactions,laminin,entactin,typeIVcollagen,andperlecanformcrosslinkednetworksinthe
basallamina.
Figure12.59

Structureoflaminin.Lamininconsistsofthreepolypeptide
chainsdesignatedA,B1,andB2.Someofthebindingsitesfor
entactin,typeIVcollagen,proteoglycans,andcellsurface
receptorsareindicated.

Themajorcellsurfacereceptorsresponsiblefortheattachmentofcellstotheextracellularmatrix
aretheintegrins.Theintegrinsareafamilyoftransmembraneproteinsconsistingoftwosubunits,
designatedand(Figure12.60).Morethan20differentintegrins,formedfromcombinationsof
18knownsubunitsand8knownsubunits,havebeenidentified.Theintegrinsbindtoshort
aminoacidsequencespresentinmultiplecomponentsoftheextracellularmatrix,including
collagen,fibronectin,andlaminin.Thefirstsuchintegrinbindingsitetobecharacterizedwasthe
sequenceArgGlyAsp,whichisrecognizedbyseveralmembersoftheintegrinfamily.Other
integrins,however,bindtodistinctpeptidesequences,includingrecognitionsequencesin
collagensandlaminin.Transmembraneproteoglycansonthesurfaceofavarietyofcellsalsobind
tocomponentsoftheextracellularmatrixandmodulatecellmatrixinteractions.
Figure12.60

Structureofintegrins.Theintegrinsareheterodimersoftwo
transmembranesubunits,designatedand.Thesubunit
bindsdivalentcations(M2+).Thematrixbindingregionis
composedofportionsofbothsubunits.

Inadditiontoattachingcellstotheextracellularmatrix,theintegrinsserveasanchorsforthe
cytoskeleton(Figure12.61).Theresultinglinkageofthecytoskeletontotheextracellularmatrixis
responsibleforthestabilityofcellmatrixjunctions.Distinctinteractionsbetweenintegrinsandthe
cytoskeletonarefoundattwotypesofcellmatrixjunctions,focaladhesionsandhemidesmosomes,
whichwerediscussedinChapter11.Focaladhesionsattachavarietyofcells,including
fibroblasts,totheextracellularmatrix.Thecytoplasmicdomainsofthesubunitsofintegrinsat
thesecellmatrixjunctionsanchortheactincytoskeletonbyassociatingwithbundlesofactin
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filaments.Hemidesmosomesarespecializedsitesofepithelialcellattachmentatwhichaspecific
integrin(designated64)interactswithintermediatefilamentsinsteadofwithactin.The64
integrinbindstolaminin,sohemidesmosomesanchorepithelialcellstothebasallamina.
Figure12.61

Junctionsbetweencellsandtheextracellularmatrix.Integrins
mediatetwotypesofstablejunctionsinwhichthecytoskeleton
islinkedtotheextracellularmatrix.Infocaladhesions,bundles
ofactinfilamentsareanchoredtothesubunits(more...)
Byagreementwiththepublisher,thisbookisaccessiblebythesearchfeature,butcannotbebrowsed.
Copyright2000,GeoffreyMCooper.
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