Still more complexity in mammalian basement membranes.

Research output: Contribution to journalJournal articleResearchpeer-review

A C Erickson, J R Couchman

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.
Original languageEnglish
JournalJournal of Histochemistry and Cytochemistry
Volume48
Issue number10
Pages (from-to)1291-306
Number of pages15
ISSN0022-1554
Publication statusPublished - 2000

Bibliographical note

Keywords: Agrin; Animals; Basement Membrane; Carrier Proteins; Cell Adhesion Molecules; Collagen; Humans; Laminin; Membrane Glycoproteins; Proteoglycans

ID: 5163313