Chondrocalcin is identical with the C-propeptide of type II procollagen
- 1 August 1986
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 237 (3), 923-925
- https://doi.org/10.1042/bj2370923
Abstract
The primary structure of the cartilage matrix molecule chondrocalcin has been found to be identical with that of the C-propeptide of type II procollagen by comparing sequence analyses of the N-terminal regions and of tryptic peptides derived from chondrocalcin. This implies that in type II collagen the C-propeptide of type II collagen is employed not only in the assembly of the triple helix of type II collagen, as demonstrated previously, but in calcifying cartilage it may also be involved in those events leading to cartilage calcification, as earlier indicated.Keywords
This publication has 19 references indexed in Scilit:
- Type I procollagen carboxyl-terminal proteinase from chick embryo tendons. Purification and characterization.Journal of Biological Chemistry, 1985
- A unique low molecular weight collagen secreted by cultured chick embryo chondrocytes.Journal of Biological Chemistry, 1982
- A Comprehensive Approach to the Study of Collagen Primary Structure Based on High‐Performance Liquid ChromatographyEuropean Journal of Biochemistry, 1982
- Effects of matrix macromolecules on chondrocyte gene expression: synthesis of a low molecular weight collagen species by cells cultured within collagen gels.The Journal of cell biology, 1982
- Proteoglycans from bovine nasal cartilage. Properties of a soluble form of link protein.Journal of Biological Chemistry, 1979
- Collagen heterogeneity in human cartilage: Identification of several new collagen chainsBiochemical and Biophysical Research Communications, 1979
- Biosynthesis of proteoglycans and their assembly into aggregates in cultures of chondrocytes from the Swarm rat chondrosarcoma.Journal of Biological Chemistry, 1979
- The isolation and characterization of the link proteins from proteoglycan aggregates of bovine nasal cartilageJournal of Biological Chemistry, 1979
- Purification and characterization of a peptide from the carboxy-terminal region of chick tendon procollagen type IBiochemistry, 1977
- Formation of interchain disulfide bonds and helical structure during biosynthesis of procollagen by embryonic tendon cellsBiochemistry, 1974