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Article: Human podocytes adhere to the KRGDS motif of the α3α4α5 collagen IV network

TitleHuman podocytes adhere to the KRGDS motif of the α3α4α5 collagen IV network
Authors
Issue Date2008
Citation
Journal of the American Society of Nephrology, 2008, v. 19 n. 4, p. 677-684 How to Cite?
AbstractPodocyte adhesion to the glomerular basement membrane is required for proper function of the glomerular filtration barrier. However, the mechanism whereby podocytes adhere to collagen IV networks, a major component of the glomerular basement membrane, is poorly understood. The predominant collagen IV network is composed of triple helical protomers containing the α3α4α5 chains. The protomers connect via the trimeric noncollagenous (NC1) domains to form hexamers at the interface. Because the NC1 domains of this network can potentially support integrin-dependent cell adhesion, it was determined whether individual NC1 monomers or α3α4α5 hexamers support podocyte adhesion. It was found that, although human podocytes did not adhere to NC1 domains proper, they did adhere via integrin αvβ3 to a KRGDS motif located adjacent to α3NC1 domains. Because the KRGDS motif is a site of phosphorylation, its interactions with integrin αvβ33 may play a critical role in cell signaling in physiologic and pathologic states. Copyright © 2008 by the American Society of Nephrology.
Persistent Identifierhttp://hdl.handle.net/10722/195460
ISSN
2015 Impact Factor: 8.491
2015 SCImago Journal Rankings: 4.699
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorBorza, CM-
dc.contributor.authorBorza, D-B-
dc.contributor.authorPedchenko, V-
dc.contributor.authorSaleem, MA-
dc.contributor.authorMathieson, PW-
dc.contributor.authorSado, Y-
dc.contributor.authorHudson, HM-
dc.contributor.authorPozzi, A-
dc.contributor.authorSaus, J-
dc.contributor.authorAbrahamson, DR-
dc.contributor.authorZent, R-
dc.contributor.authorHudson, BG-
dc.date.accessioned2014-02-28T06:12:11Z-
dc.date.available2014-02-28T06:12:11Z-
dc.date.issued2008-
dc.identifier.citationJournal of the American Society of Nephrology, 2008, v. 19 n. 4, p. 677-684-
dc.identifier.issn1046-6673-
dc.identifier.urihttp://hdl.handle.net/10722/195460-
dc.description.abstractPodocyte adhesion to the glomerular basement membrane is required for proper function of the glomerular filtration barrier. However, the mechanism whereby podocytes adhere to collagen IV networks, a major component of the glomerular basement membrane, is poorly understood. The predominant collagen IV network is composed of triple helical protomers containing the α3α4α5 chains. The protomers connect via the trimeric noncollagenous (NC1) domains to form hexamers at the interface. Because the NC1 domains of this network can potentially support integrin-dependent cell adhesion, it was determined whether individual NC1 monomers or α3α4α5 hexamers support podocyte adhesion. It was found that, although human podocytes did not adhere to NC1 domains proper, they did adhere via integrin αvβ3 to a KRGDS motif located adjacent to α3NC1 domains. Because the KRGDS motif is a site of phosphorylation, its interactions with integrin αvβ33 may play a critical role in cell signaling in physiologic and pathologic states. Copyright © 2008 by the American Society of Nephrology.-
dc.languageeng-
dc.relation.ispartofJournal of the American Society of Nephrology-
dc.titleHuman podocytes adhere to the KRGDS motif of the α3α4α5 collagen IV network-
dc.typeArticle-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1681/ASN.2007070793-
dc.identifier.pmid18235087-
dc.identifier.scopuseid_2-s2.0-44349170641-
dc.identifier.volume19-
dc.identifier.issue4-
dc.identifier.spage677-
dc.identifier.epage684-
dc.identifier.isiWOS:000254659100009-

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