HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Neame, P. J. Articles by Young, C. N. Search for Related Content PubMed PubMed Citation Articles by Neame, P. J. Articles by Young, C. N. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 265, Issue 17, 9628-9633, Jun, 1990

An 18-kDa glycoprotein from bovine nasal cartilage. Isolation and primary structure of small, cartilage-derived glycoprotein [published erratum appears in J Biol Chem 1990 Dec 15;265(35):22056]

PJ Neame, JT Treep and CN Young
Shriners Hospital for Crippled Children, Tampa, FL 33612.

A glycosylated protein (small, cartilage-derived glycoprotein, SCGP) of approximately 18 kDa with unknown function has been isolated from dissociative extracts of bovine nasal cartilage and its primary structure determined. The protein has 121 amino acids, giving a calculated protein molecular weight of 13,878, four disulfide bonds, two N-linked oligosaccharides and one O-linked oligosaccharide. In nasal cartilage, this glycoprotein is in molar concentrations equivalent to 1/5-1/2 that of the link protein of cartilage proteoglycan aggregates, and it has also been isolated from bovine articular cartilage and from bovine fetal epiphysis. The N-terminal, glycosylated region of the molecule is relatively rich in arginine, proline, glycine, and threonine. The C-terminal 82 amino acids (which contains all four of the disulfide bonds and none of the carbohydrate) can be found as a discrete entity in cartilage extracts, indicating that the N-terminal domain is readily removed by extracellular proteolytic attack.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				D. Docheva, E. B. Hunziker, R. Fassler, and O. Brandau Tenomodulin Is Necessary for Tenocyte Proliferation and Tendon Maturation Mol. Cell. Biol., January 15, 2005; 25(2): 699 - 705. [Abstract] [Full Text] [PDF]

				Y. Oshima, K. Sato, F. Tashiro, J.-i. Miyazaki, K. Nishida, Y. Hiraki, Y. Tano, and C. Shukunami Anti-angiogenic action of the C-terminal domain of tenomodulin that shares homology with chondromodulin-I J. Cell Sci., June 1, 2004; 117(13): 2731 - 2744. [Abstract] [Full Text] [PDF]

				O. Brandau, A. Aszodi, E. B. Hunziker, P. J. Neame, D. Vestweber, and R. Fassler Chondromodulin I Is Dispensable during Enchondral Ossification and Eye Development Mol. Cell. Biol., September 15, 2002; 22(18): 6627 - 6635. [Abstract] [Full Text] [PDF]

				Y. Hiraki, H. Inoue, K.-i. Iyama, A. Kamizono, M. Ochiai, C. Shukunami, S. Iijima, F. Suzuki, and J. Kondo Identification of Chondromodulin I as a Novel Endothelial Cell Growth Inhibitor. PURIFICATION AND ITS LOCALIZATION IN THE AVASCULAR ZONE OF EPIPHYSEAL CARTILAGE J. Biol. Chem., December 19, 1997; 272(51): 32419 - 32426. [Abstract] [Full Text] [PDF]

				A. Azizan, N. Holaday, and P. J. Neame Post-translational Processing of Bovine Chondromodulin-I J. Biol. Chem., June 22, 2001; 276(26): 23632 - 23638. [Abstract] [Full Text] [PDF]