Premium
Mammalian collagen IV
Author(s) -
Khoshnoodi Jamshid,
Pedchenko Vadim,
Hudson Billy G.
Publication year - 2008
Publication title -
microscopy research and technique
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.536
H-Index - 118
eISSN - 1097-0029
pISSN - 1059-910X
DOI - 10.1002/jemt.20564
Subject(s) - collagen, type i, alpha 1 , alport syndrome , basement membrane , biology , microbiology and biotechnology , gene , endoplasmic reticulum , extracellular matrix , chemistry , genetics , glomerulonephritis , kidney
Abstract Four decades have passed since the first discovery of collagen IV by Kefalides in 1966. Since then collagen IV has been investigated extensively by a large number of research laboratories around the world. Advances in molecular genetics have resulted in identification of six evolutionary related mammalian genes encoding six different polypeptide chains of collagen IV. The genes are differentially expressed during the embryonic development, providing different tissues with specific collagen IV networks each having unique biochemical properties. Newly translated α‐chains interact and assemble in the endoplasmic reticulum in a chain‐specific fashion and form unique heterotrimers. Unlike most collagens, type IV collagen is an exclusive member of the basement membranes and through a complex inter‐ and intramolecular interactions form supramolecular networks that influence cell adhesion, migration, and differentiation. Collagen IV is directly involved in a number of genetic and acquired disease such as Alport's and Goodpasture's syndromes. Recent discoveries have also highlighted a new and direct role for collagen IV in the development of rare genetic diseases such as cerebral hemorrhage and porencephaly in infants and hemorrhagic stroke in adults. Years of intensive investigations have resulted in a vast body of information about the structure, function, and biology of collagen IV. In this review article, we will summarize essential findings on the structural and functional relationships of different collagen IV chains and their roles in health and disease. Microsc. Res. Tech., 2008. © 2008 Wiley‐Liss, Inc.