Chondrocalcin is identical with the C-propeptide of type II procollagen
- PMID: 3800925
- PMCID: PMC1147077
- DOI: 10.1042/bj2370923
Chondrocalcin is identical with the C-propeptide of type II procollagen
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.
Similar articles
-
Kniest dysplasia is characterized by an apparent abnormal processing of the C-propeptide of type II cartilage collagen resulting in imperfect fibril assembly.J Clin Invest. 1988 Feb;81(2):579-89. doi: 10.1172/JCI113356. J Clin Invest. 1988. PMID: 3276736 Free PMC article.
-
Chondrocalcin is internalized by chondrocytes and triggers cartilage destruction via an interleukin-1β-dependent pathway.Matrix Biol. 2013 Oct-Nov;32(7-8):443-51. doi: 10.1016/j.matbio.2013.06.002. Epub 2013 Jul 10. Matrix Biol. 2013. PMID: 23851124
-
Selective binding of anchorin CII (annexin V) to type II and X collagen and to chondrocalcin (C-propeptide of type II collagen). Implications for anchoring function between matrix vesicles and matrix proteins.FEBS Lett. 1992 Sep 28;310(2):143-7. doi: 10.1016/0014-5793(92)81316-e. FEBS Lett. 1992. PMID: 1397263
-
Chondrocalcin: Insights into its regulation and multi-function in cartilage and bone.Differentiation. 2025 May-Jun;143:100861. doi: 10.1016/j.diff.2025.100861. Epub 2025 Mar 24. Differentiation. 2025. PMID: 40157027 Review.
-
Chondrocalcin and the calcification of cartilage. A review.Clin Orthop Relat Res. 1986 Jul;(208):114-8. Clin Orthop Relat Res. 1986. PMID: 3522018 Review.
Cited by
-
A histochemical localization on Maclura pomifera lectin during osteogenesis.Histochemistry. 1989;92(3):225-30. doi: 10.1007/BF00500922. Histochemistry. 1989. PMID: 2777640
-
Proteomic analysis of Col11a1-associated protein complexes.Proteomics. 2011 Dec;11(24):4660-76. doi: 10.1002/pmic.201100058. Epub 2011 Nov 23. Proteomics. 2011. PMID: 22038862 Free PMC article.
-
Structural basis of fibrillar collagen trimerization and related genetic disorders.Nat Struct Mol Biol. 2012 Oct;19(10):1031-6. doi: 10.1038/nsmb.2389. Epub 2012 Sep 23. Nat Struct Mol Biol. 2012. PMID: 23001006 Free PMC article.
-
Diverse biological functions of extracellular collagen processing enzymes.J Cell Biochem. 2005 Dec 1;96(5):927-37. doi: 10.1002/jcb.20605. J Cell Biochem. 2005. PMID: 16167328 Free PMC article. Review.
-
ENU-induced missense mutation in the C-propeptide coding region of Col2a1 creates a mouse model of platyspondylic lethal skeletal dysplasia, Torrance type.Mamm Genome. 2011 Jun;22(5-6):318-28. doi: 10.1007/s00335-011-9329-3. Epub 2011 May 3. Mamm Genome. 2011. PMID: 21538020
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases