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- W1605960013 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." @default.
- W1605960013 created "2016-06-24" @default.
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- W1605960013 date "1992-11-01" @default.
- W1605960013 modified "2023-10-14" @default.
- W1605960013 title "COMP (cartilage oligomeric matrix protein) is structurally related to the thrombospondins." @default.
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- W1605960013 doi "https://doi.org/10.1016/s0021-9258(18)41677-8" @default.
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