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Specific inhibition of type I and type II collagen fibrillogenesis by the small proteoglycan of tendon

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Vogel, K G, Paulsson, M, Heinegård, D·1984·Biochemical Journal

Abstract

The small dermatan sulphate proteoglycan of bovine tendon demonstrated a unique ability to inhibit fibrillogenesis of both type I and type II collagen from bovine tendon and cartilage respectively in an assay performed in vitro. None of the other proteoglycan populations from cartilage, tendon or aorta, even those similar in size and chemical structure, had this effect. Alkali treatment of the small proteoglycan of tendon eliminated its ability to inhibit fibrillogenesis, whereas chondroitinase digestion did not. This indicates that its interaction with collagen depends on the core protein. Fibrillogenesis of pepsin-digested collagens was affected similarly, indicating that interaction with the collagen telopeptides is not involved. The results suggest that interactions between collagen and proteoglycans may be quite specific both for the type of proteoglycan and its tissue of origin.

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Metadata

Authors
Vogel, K. G., Paulsson, M., & Heinegård, D.
Venue
Biochemical Journal
Published
1984-11-01
Volume
223
Issue
3
Pages
587-597
ISSN
  • 0264-6021 (ISSN-L)
  • 1470-8728
OpenAlex
W2151621078
Cited by
856
References
0
FWCI
7.88
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Specific inhibition of type I and type II collagen fibrillogenesis by the small proteoglycan of tendon. https://app.cochat.ai/papers/10.1042/bj2230587
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Vogel, K. G., Paulsson, M., & Heinegård, D. (1984). Specific inhibition of type I and type II collagen fibrillogenesis by the small proteoglycan of tendon. Biochemical Journal. https://doi.org/10.1042/bj2230587

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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.