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Here we report the structure and bioactivity of 25 kDa glycoprotein (chondromodulin-I) as a tissue-specific functional matrix component identified and cloned for the first time. Chondromodulin-I purified from fetal bovine cartilage markedly stimulated DNA synthesis of cultured growth-plate chondrocytes in the presence of basic fibroblast growth factor (FGF). Bovine chondromodulin-I cDNA revealed that the mature protein consists of 121 amino acids with three possible glycosylation sites and is coded as the C-terminal part of a larger precursor. On northern blot analysis, expression of chondromodulin-I mRNA was observed only in cartilage.


Y Hiraki, H Tanaka, H Inoue, J Kondo, A Kamizono, F Suzuki. Molecular cloning of a new class of cartilage-specific matrix, chondromodulin-I, which stimulates growth of cultured chondrocytes. Biochemical and biophysical research communications. 1991 Mar 29;175(3):971-7

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PMID: 1709014

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