The structural determination and anti-angiogenic activity of a Chondromodulin-I subtype that lacks the N-terminal domain.

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In this study, we extracted and purified the 14-kDa species of ChM-I from rat rib cartilage. Amino acid sequencing revealed a 14-kDa ChM-I lacks the N-terminal 37 residues of mature 25-kDa ChM-I. As demonstrated in vitro, 14-kDa ChM-I exhibited little anti-angiogenic activity. There is no 25-kDa ChM-I species present in the hypertrophic/calcified cartilage zone of cartilaginous bone precursors. Instead only the 14-kDa ChM-I species was detected. Taken together, our data suggest that ChM-I is inactivated by its N-terminal deletion of 37 residues during endochondral bone formation.