Laminins are the most abundant structural non-collagenous glycoproteins ubi
quitously present in basement membranes. They are multidomain molecules con
stituting a family of possibly more than 50 members. Some members such as l
aminins 5, 6 and 10 are specific of the basal lamina present under stratifi
ed epithelia. Although only few intact laminin isoforms have been purified
from cultivated cells or tissues, genetic engineering has opened the way fo
r a rapid development of laminin structural biology. Moreover, the phenotyp
es resulting from gene targeting in mouse or from laminin defects in acquir
ed or inherited human diseases highlight the pivotal role of laminins in mo
rphogenesis, development, and physiology. Indeed, the laminins display a re
markable repertoire of functions, most importantly as structural elements f
orming a network throughout the basement membrane to which other collagenou
s or non-collagenous glycoproteins and proteoglycans attach. Furthermore, t
hey are signaling molecules providing adjacent cells with diverse informati
on by interacting with cell surface components. (C) 1999 Elsevier Science B
.V./International Society of Matrix Biology. All rights reserved.