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Cited by 324

The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.

COMP (cartilage oligomeric matrix protein) is structurally related to the thrombospondins.

Open access
Oldberg, A, Antonsson, P, Lindblom, K, Heinegård, D·1992·Journal of Biological Chemistry

Abstract

Cloning and sequence analysis of cartilage oligomeric matrix protein (COMP) cDNA, representing a cartilage pentameric protein, revealed a protein of 755 amino acid residues with a calculated molecular mass of 82,700 Da. Expression of the cDNA in COS cells showed that COMP is a homopolymer composed of five identical disulfide-linked subunits. COMP is homologous to the carboxyl-terminal half of thrombospondin, and the homologies include 89% and 54% of the residues in COMP and thrombospondin, respectively. The similarities are most pronounced in the carboxyl-terminal domains and in the calcium binding type 3 repeat domains in which about 60% of the amino acid residues are identical. In the type 2/epidermal growth factor repeat domains the two proteins contain 41% identical residues. The sequence of the amino-terminal 84-amino acid residues is unique for COMP. Comparison of the amino acid sequences in the type 2 and type 3 repeat domains of COMP and the thrombospondins shows that COMP is the product of a unique gene and not the result of an alternatively spliced thrombospondin gene.

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Metadata

Authors
Oldberg, A., Antonsson, P., Lindblom, K., & Heinegård, D.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1992-11
Volume
267
Issue
31
Pages
22346-22350
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1605960013
Cited by
324
References
26
FWCI
9.88
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: COMP (cartilage oligomeric matrix protein) is structurally related to the thrombospondins. https://app.cochat.ai/papers/10.1016/s0021-9258(18)41677-8
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Oldberg, A., Antonsson, P., Lindblom, K., & Heinegård, D. (1992). COMP (cartilage oligomeric matrix protein) is structurally related to the thrombospondins. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)41677-8

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