Cited by 197Collagen: Extraction and CharacterizationConnective tissue disorders researchTGF-β signaling in diseases

Type V Collagen in Health, Disease, and Fibrosis

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Mak, Ki M., Png, Chien Yi M., Lee, Danielle J.·2016·The Anatomical Record

Abstract

Type V collagen (COLV) is a regulatory fibril‐forming collagen. It has at least three different molecular isoforms—α1(V)2 α2(V), α1(V)3, and α1(V)α2(V)α3(V)—formed by combinations of three different polypeptide α chains—α1(V), α2(V), and α3(V). COL V is a relatively minor collagen of the extracellular matrix (ECM). Morphologically, COLV occurs as heterotypic fibrils with type I collagen (COLI), microfilaments, or 12‐nm‐thick fibrils. COLV is synthesized in various mesenchymal cells and its gene expression is modulated by TGF‐β and growth factors. While resistant to digestion by interstitial collagenases, native and denatured COLV are degraded by metalloproteinases and gelatinases, thereby promoting ECM remodeling. COLV interacts with matrix collagens and structural proteins, conferring structural integrity to tissue scaffolds. It binds matrix macromolecules, modulating cellular behavior, and functions. COLV co‐assembles with COLI into heterotypic fibrils in the cornea and skin dermis, acting as a dominant regulator of collagen fibrillogenesis. COLV deficiency is associated with loss of corneal transparency and classic Ehlers–Danlos syndrome, while COLV overexpression is found in cancer, granulation tissue, inflammation, atherosclerosis, and fibrosis of lungs, skin, kidneys, adipose tissue, and liver. COLV isoform containing the α3(V) chain is involved in mediating pancreatic islet cell functions. In the liver, COLV is a minor but regular component of the ECM. Increases in COLV are associated with both early and advanced hepatic fibrosis. The neoepitopes of COLV have been shown to be a useful noninvasive serum biomarker for assessing fibrotic progression and resolution in experimental hepatic fibrosis. COLV is multifunctional in health, disease, and fibrosis. Anat Rec, 299:613–629, 2016. © 2016 Wiley Periodicals, Inc.

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Authors
Mak, K. M., Png, C. Y. M., & Lee, D. J.
Affiliations
Icahn School of Medicine at Mount Sinai (US)
Corresponding author
Mak, Ki M.
Venue
The Anatomical Record
Publisher
Wiley
Published
2016-03-15
Volume
299
Issue
5
Pages
613-629
ISSN
  • 1932-8486 (ISSN-L)
  • 1932-8494
OpenAlex
W2285081944
Cited by
197
References
130
Citations by year
2026: 12 · 2025: 31 · 2024: 22 · 2023: 23 · 2022: 25 · 2021: 19 · 2020: 19 · 2019: 19 · 2018: 13 · 2017: 10 · 2016: 4
FWCI
0.82
Type
journal article
Language
en
Open access
Locations
  • The Anatomical Record (publishedVersion, other-oa)
  • PubMed (publishedVersion)
Funders
Mount Sinai Health System
Topics
  • Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Connective tissue disorders research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
Keywords
type V collagen, collagen fibrillogenesis, extracellular matrix, collagen isoforms, Ehlers-Danlos syndrome, corneal transparency, liver fibrosis, serum biomarkers, TGF-beta, matrix metalloproteinases, collagen degradation, pancreatic islet cells, fibrosis
MeSH terms
Disease, Extracellular Matrix, Fibrosis, Humans, Collagen Type V

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