Integrins as receptors for laminins

• Published in: Microscopy research and technique Vol. 51; no. 3; pp. 280 - 301
• Main Authors: Belkin, Alexey M., Stepp, Mary Ann
• Format: Journal Article
• Language: English
• Published: New York John Wiley & Sons, Inc 01.11.2000
• Subjects: Animals; Basement Membrane - chemistry; Cell Adhesion - physiology; Cell Communication; epithelial cell adhesion; Epithelial Cells - metabolism; Humans; Integrins - chemistry; Integrins - metabolism; laminin; Laminin - metabolism; Muscles - metabolism; myoblast differentiation; Neoplasm Invasiveness - physiopathology; Protein Isoforms - metabolism; Receptors, Laminin - chemistry; Receptors, Laminin - metabolism
• ISSN: 1059-910X; 1097-0029
• DOI: 10.1002/1097-0029(20001101)51:3<280::AID-JEMT7>3.0.CO;2-O

Laminins are a family of trimeric glycoproteins present in the extracellular matrix and the major constituents of basement membranes. Integrins are αβ transmembrane receptors that play critical roles in both cell‐matrix and cell‐cell adhesion. Several members of the integrin family, including α1β1, α2β1, α3β1, α6β1 , α7β1 and α6β4 heterodimers serve as laminin receptors on a variety of cell types. This review summarizes recent advances in understanding the involvement of individual integrins in cell interactions with laminins and the roles of laminin‐binding integrins in adhesion‐mediated events in vertebrates, including embryonic development, cell migration and tumor cell invasiveness, cell proliferation and differentiation, as well as basement membrane assembly. We discuss the regulation of integrin function via alternative splicing of cytoplasmic domains of α and β subunits of the integrin receptors for laminins and present examples of functional collaboration between laminin‐binding integrins and non‐integrin laminin receptors. Advances in our understanding of the laminin‐binding integrins continue to demonstrate the essential roles these receptors play in maintaining cell polarity and tissue architecture. Microsc. Res. Tech. 51:280–301, 2000. © 2000 Wiley‐Liss, Inc.