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Journal of Histochemistry and Cytochemistry, Vol. 48, 1291-1306, October 2000, Copyright © 2000, The Histochemical Society, Inc.

REVIEW

Still More Complexity in Mammalian Basement Membranes

Anna C. Ericksona and John R. Couchmana
a Department of Cell Biology and Cell Adhesion and Matrix Research Center, University of Alabama at Birmingham, Birmingham, Alabama

Correspondence to: John R. Couchman, Dept. of Cell Biology and Cell Adhesion and Matrix Res. Center, U. of Alabama at Birmingham, 1670 University Blvd., VH 201C, Birmingham, AL 35294-0019. E-mail: jrcouchman@cellbio.bhs.uab.edu

At the epithelial/mesenchymal interface of most tissues lies the basement membrane (BM). These thin sheets of highly specialized extracellular matrix vary in composition in a tissue-specific manner, and during development and repair. For about two decades it has been apparent that all BMs contain laminins, entactin-1/nidogen-1, Type IV collagen, and proteoglycans. However, within the past few years this complexity has increased as new components are described. The entactin/nidogen (E/N) family has expanded with the recent description of a new isoform, E/N-2/osteonidogen. Agrin and Type XVIII collagen have been reclassified as heparan sulfate proteoglycans (HSPGs), expanding the repertoire of HSPGs in the BM. The laminin family has become more diverse as new {alpha}-chains have been characterized, increasing the number of laminin isoforms. Interactions between BM components are now appreciated to be regulated through multiple, mostly domain-specific mechanisms. Understanding the functions of individual BM components and their assembly into macromolecular complexes is a considerable challenge that may increase as further BM and cell surface ligands are discovered for these proteins.

(J Histochem Cytochem 48:1291–1306, 2000)

Key Words: basement membrane, entactin, nidogen, proteoglycan, agrin, collagen XVIII, laminin {alpha}-chain


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