Mammalian collagen IV

Khoshnoodi, Jamshid; Pedchenko, Vadim; Hudson, Billy G.

doi:10.1002/jemt.20564

Cited by 668Collagen: Extraction and CharacterizationConnective tissue disorders researchRenal Diseases and Glomerulopathies

Mammalian collagen IV

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Khoshnoodi, Jamshid, Pedchenko, Vadim, Hudson, Billy G.·2008·Microscopy Research and Technique

DOI 10.1002/jemt.20564PMC PMC4788096

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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.

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Collagen I has a high affinity for α2β1 integrin, whereas collagen IV binds more strongly to α1β1 integrin.
“Collagen I has a high affinity for α2β1 integrin, whereas collagen IV binds more strongly to α1β1 integrin93.”
From Towards organoid culture without Matrigel (2021) · cites this paper as [93]
Collagen IV tends to occur exclusively in basement membranes.
“Collagen IV tends to occur exclusively in basement membranes93.”
From Towards organoid culture without Matrigel (2021) · cites this paper as [93]

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Authors: Khoshnoodi, J., Pedchenko, V., & Hudson, B. G.
Affiliations: Vanderbilt University (US)
Corresponding author: Khoshnoodi, Jamshid
Hudson, Billy G.
ORCID: Hudson, Billy G.
Venue: Microscopy Research and Technique
Publisher: Wiley
Published: 2008-01-24
Volume: 71
Issue: 5
Pages: 357-370
ISSN: 1059-910X (ISSN-L)
1097-0029
DOI: 10.1002/jemt.20564
PMC: PMC4788096
OpenAlex: W2096252197
Cited by: 668
References: 188
Citations by year: 2026: 26 · 2025: 41 · 2024: 43 · 2023: 37 · 2022: 50 · 2021: 43 · 2020: 47 · 2019: 35 · 2018: 28 · 2017: 32 · 2016: 37 · 2015: 34 · 2014: 32 · 2013: 40 · 2012: 40
FWCI: 1.56
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: Microscopy Research and Technique (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health
National Institute of Diabetes and Digestive and Kidney Diseases (R37DK018381, P01DK065123, R-37DK18381, R01DK018381)
Topics: Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Connective tissue disorders research
Health Sciences › Medicine › Nephrology › Renal Diseases and Glomerulopathies
Keywords: type IV collagen, alpha chain, basement membrane, heterotrimers, embryonic development, cell adhesion, cell migration, Alport syndrome, Goodpasture's syndrome, cerebral hemorrhage, porencephaly, hemorrhagic stroke, genetic disorders
MeSH terms: Animals, Chromosomes, Human, Multigene Family, Humans, Mammals, Nephritis, Hereditary, Protein Conformation, Protein Processing, Post-Translational, Integrins, Gene Expression Regulation, Developmental, Anti-Glomerular Basement Membrane Disease, Collagen Type IV, Genetic Diseases, Inborn

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