Type V Collagen in Health, Disease, and Fibrosis
Open accessAbstract
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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Collagen V has a crucial role for embryonic development.
“Collagen V knockout mice synthesize and secrete normal amounts of collagen I, but collagen fibrils are absent, and the animals die at the onset of organogenesis, supporting the crucial role of collagen V for embryonic development [43].”
From Cellular and Molecular Mechanisms in the Pathogenesis of Classical, Vascular, and Hypermobile Ehlers‒Danlos Syndromes (2019) · cites this paper as [43]
Collagen V knockout mice synthesize and secrete normal amounts of collagen I, but collagen fibrils are absent, and the animals die at the onset of organogenesis.
“Collagen V knockout mice synthesize and secrete normal amounts of collagen I, but collagen fibrils are absent, and the animals die at the onset of organogenesis, supporting the crucial role of collagen V for embryonic development [43].”
From Cellular and Molecular Mechanisms in the Pathogenesis of Classical, Vascular, and Hypermobile Ehlers‒Danlos Syndromes (2019) · cites this paper as [43]
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The good and the bad collagens of fibrosis – Their role in signaling and organ function
Karsdal, M. A., Nielsen, S. H., Leeming, D. J., Langholm, L. L., Nielsen, M. J., Manon-Jensen, T., Siebuhr, A., Gudmann, N. S., Rønnow, S., Sand, J. M., et al. (2017) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2017.07.014 · Cited by 509 · see citing works
Bi, H., Ye, K., & Jin, S. (2020) · Biomaterials · doi:10.1016/j.biomaterials.2019.119673 · Cited by 105 · see citing works
Chiarelli, N., Ritelli, M., Zoppi, N., & Colombi, M. (2019) · Genes · doi:10.3390/genes10080609 · Cited by 82 · see citing works
The Matrisome, Inflammation, and Liver Disease
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Chiarelli, N., Carini, G., Zoppi, N., Ritelli, M., & Colombi, M. (2019) · PLOS ONE · doi:10.1371/journal.pone.0211647 · Cited by 35 · see citing works
- 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
- hybrid
- doi.org
- Licence
- 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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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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