Cell adhesion to a population of laminin isoforms isolated from normal renal tissue

To assess whether cells react differently towards a population of several laminin isoforms, as found in vivo, vs. a single isoform, we have compared the biological activity of kidney laminins to that of pure laminin 1. The kidney laminin preparation contained laminin 1 and further isoforms. Both sub...

Full description

Saved in:

Bibliographic Details
Published in:	Matrix biology Vol. 18; no. 5; pp. 433 - 444
Main Authors:	Dogic, Dagmar, Hülsmann, Hanni, Sherman, Nicholas, Fox, Jay W., Broermann, Ralf, Paulsson, Mats, Aumailley, Monique
Format:	Journal Article
Language:	English
Published:	Netherlands Elsevier B.V 01-10-1999
Subjects:	Amino Acid Sequence Animals Cattle Cell Adhesion - drug effects Cell Adhesion - physiology Cells, Cultured Focal adhesions Humans Integrin alpha3beta1 Integrin alpha6beta1 Integrins Integrins - physiology Kidney - physiology Laminin - isolation & purification Laminin - pharmacology Laminin - physiology Laminins Protein Isoforms - isolation & purification Protein Isoforms - pharmacology Protein Isoforms - physiology Signal Transduction Tissue Distribution Laminins Focal adhesions Integrins
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

Description
Summary:	To assess whether cells react differently towards a population of several laminin isoforms, as found in vivo, vs. a single isoform, we have compared the biological activity of kidney laminins to that of pure laminin 1. The kidney laminin preparation contained laminin 1 and further isoforms. Both substrates induced adhesion of a large spectrum of cell types, with kidney laminins being the most active. Unfolding of the coil-coiled conformation of the kidney isoforms negatively affected cell adhesion-promoting activity, which indicated that conformation-dependent cell binding is a characteristic feature of many or all laminins. Cellular interactions with kidney laminins were mediated by α3β1 and α6β1 integrins, with the contribution of α3β1 being apparently lower than that of α6β1 integrins. Immunofluorescence staining of vinculin and integrin subunits decorated focal adhesions on kidney laminins which differed in morphology from those formed on laminin 1 alone, in spite of the presence of the latter in the kidney preparation. These observations collectively indicate that tissue specific but often overlapping expression of laminin isoforms might modulate cell behavior by the activation of distinct sets of integrins and by the induction of distinct molecular assemblies within the cell adhesion signaling complexes.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0945-053X 1569-1802
DOI:	10.1016/S0945-053X(99)00046-3