Faculty Collaboration Database

Evidence that a 550,000-dalton cartilage matrix glycoprotein is a chondrocyte membrane-associated protein closely related to ceruloplasmin. J Biol Chem 1993 Feb 25;268(6):4407-11

Date

02/25/1993

Pubmed ID

8440723

Scopus ID

2-s2.0-0027417404 (requires institutional sign-in at Scopus site)   12 Citations

Abstract

Cartilage matrix glycoprotein (CMGP) is a disulfide-bonded 550,000-dalton protein that is synthesized by chondrocytes and ciliary epithelial cells. We have purified the protein from bovine and porcine articular cartilage and have sequenced two peptides, which both have significant homology with human ceruloplasmin, a copper-binding oxidase. Immunolocation analysis indicates that a commercial polyclonal antiserum to human ceruloplasmin reacts with bovine cartilage CMGP. Chelating columns made with copper bind CMGP from bovine cartilage extracts. CMGP is present in bovine chondrocyte membrane preparations purified from sucrose density gradients. Oligonucleotide probes have been synthesized based on the published sequence of the 3'-untranslated region and a portion of the C terminus of human ceruloplasmin and have been used to amplify a cDNA fragment from bovine cartilage and human liver libraries. CMGP demonstrates oxidase activity towards p-phenylenediamine similar to that of ceruloplasmin. These studies suggest that CMGP is closely related to, if not identical with, ceruloplasmin. It is possible that CMGP may be involved in metal transport into and/or within the chondrocyte.

Author List

Fife RS, Kluve-Beckerman B, Houser DS, Proctor C, Liepnieks J, Masuda I, McCarty DJ, Ryan LM

MESH terms used to index this publication - Major topics in bold

Amino Acid Sequence
Animals
Cartilage Oligomeric Matrix Protein
Cartilage, Articular
Cattle
Ceruloplasmin
Extracellular Matrix Proteins
Glycoproteins
Humans
Matrilin Proteins
Membrane Glycoproteins
Membrane Proteins
Molecular Sequence Data
Molecular Weight
Sequence Homology, Amino Acid
Swine