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  Matrix assembly, regulation, and survival functions of laminin and its receptors in embryonic stem cell differentiation

Li, S., Harrison, D., Carbonetto, S., Fässler, R., Smyth, N., Edgar, D., et al. (2002). Matrix assembly, regulation, and survival functions of laminin and its receptors in embryonic stem cell differentiation. Journal of Cell Biology, 157(7), 1279-1290.

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Genre: Zeitschriftenartikel
Alternativer Titel : J. Cell Biol.

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 Urheber:
Li, S., Autor
Harrison, D., Autor
Carbonetto, S., Autor
Fässler, R.1, Autor           
Smyth, N., Autor
Edgar, D., Autor
Yurchenco, P. D., Autor
Affiliations:
1Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565147              

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Schlagwörter: basement membrane; gastrulation; integrin; dystroglycan; apoptosis
 Zusammenfassung: Laminin-1 is essential for early embryonic basement membrane assembly and differentiation. Several steps can be distinguished, i.e., the expression of laminin and companion matrix components, their accumulation on the cell surface and assembly into basement membrane between endoderm and inner cell mass, and the ensuing differentiation of epiblast. In this study, we used differentiating embryoid bodies derived from mouse embryonic stem cells null for gamma1-laminin, beta1- integrin and alpha/beta-dystroglycan to dissect the contributions of laminin domains and interacting receptors to this process. We found that (a) laminin enables beta1-integrin- null embryoid bodies to assemble basement membrane and achieve epiblast with beta1-integrin enabling expression of the laminin alpha1 subunit; (b) basement membrane assembly and differentiation require laminin polymerization in conjunction with cell anchorage, the latter critically dependent upon a heparin-binding locus within LG module-4; (c) dystroglycan is not uniquely required for basement membrane assembly or initial differentiation; (d) dystroglycan and integrin cooperate to sustain survival of the epiblast and regulate laminin expression; and (e) laminin, acting via beta1-integrin through LG1-3 and requiring polymerization, can regulate dystroglycan expression.

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Sprache(n): eng - English
 Datum: 2002-06-24
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 31387
ISI: 000176528400016
 Art des Abschluß: -

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Titel: Journal of Cell Biology
  Alternativer Titel : J. Cell Biol.
Genre der Quelle: Zeitschrift
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Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 157 (7) Artikelnummer: - Start- / Endseite: 1279 - 1290 Identifikator: ISSN: 0021-9525