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Collagen fibrillogenesis: fibronectin, integrins, and minor collagens as organizers and nucleators

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Kadler, Karl E, Hill, Adele, Canty-Laird, Elizabeth G·2008·Current Opinion in Cell Biology

Abstract

Collagens are triple helical proteins that occur in the extracellular matrix (ECM) and at the cell-ECM interface. There are more than 30 collagens and collagen-related proteins but the most abundant are collagens I and II that exist as D-periodic (where D = 67 nm) fibrils. The fibrils are of broad biomedical importance and have central roles in embryogenesis, arthritis, tissue repair, fibrosis, tumor invasion, and cardiovascular disease. Collagens I and II spontaneously form fibrils in vitro, which shows that collagen fibrillogenesis is a selfassembly process. However, the situation in vivo is not that simple; collagen I-containing fibrils do not form in the absence of fibronectin, fibronectin-binding and collagen-binding integrins, and collagen V. Likewise, the thin collagen II-containing fibrils in cartilage do not form in the absence of collagen XI. Thus, in vivo, cellular mechanisms are in place to control what is otherwise a protein self-assembly process. This review puts forward a working hypothesis for how fibronectin and integrins (the organizers) determine the site of fibril assembly, and collagens V and XI (the nucleators) initiate collagen fibrillogenesis.

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Metadata

Authors
Kadler, K. E., Hill, A., & Canty-Laird, E. G.
Venue
Current Opinion in Cell Biology
Publisher
Elsevier BV
Published
2008-10
Volume
20
Issue
5
Pages
495-501
ISSN
0955-0674 (ISSN-L)
OpenAlex
W2046656677
Cited by
756
References
4
FWCI
1.09
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Collagen fibrillogenesis: fibronectin, integrins, and minor collagens as organizers and nucleators. https://app.cochat.ai/papers/10.1016/j.ceb.2008.06.008
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Kadler, K. E., Hill, A., & Canty-Laird, E. G. (2008). Collagen fibrillogenesis: fibronectin, integrins, and minor collagens as organizers and nucleators. Current Opinion in Cell Biology. https://doi.org/10.1016/j.ceb.2008.06.008

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.