| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 277, Issue 45, 43327-43334, November 8, 2002
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
,
From the Wellcome Trust Centre for Cell-Matrix Research, University
of Manchester, School of Biological Sciences, Stopford Building 2.205, Oxford Road, Manchester M13 9PT, United Kingdom
Bone morphogenetic protein (BMP)-1 is a
glycosylated metalloproteinase that is fundamental to the synthesis of
a normal extracellular matrix because it cleaves type I procollagen, as
well as other precursor proteins. Sequence analysis suggests that BMP-1
has six potential N-linked glycosylation sites
(i.e. NXS/T) namely: Asn91 (prodomain),
Asn142 (metalloproteinase domain), Asn332 and
Asn363 (CUB1 domain), Asn599 (CUB3 domain), and
Asn726 in the C-terminal-specific domain. In this study we
showed that all these sites are N-glycosylated with
complex-type oligosaccharides containing sialic acid, except
Asn726 presumably because proline occurs immediately
C-terminal of threonine in the consensus sequence. Recombinant BMP-1
molecules lacking all glycosylation sites or the three CUB-specific
sites were not secreted. BMP-1 lacking CUB glycosylation was
translocated to the proteasome for degradation. BMP-1 molecules lacking
individual glycosylation sites were efficiently secreted and
exhibited full procollagen C-proteinase activity, but N332Q and
N599Q exhibited a slower rate of cleavage. BMP-1 molecules lacking any
one of the CUB-specific glycosylation sites were sensitive to thermal denaturation. The study showed that the glycosylation sites in the CUB
domains of BMP-1 are important for secretion and stability of the molecule.
To whom correspondence should be addressed. Tel.: 44-161-275-6925;
Fax: 44-161-275-1505; E-mail: laure.garrigue-antar@man.ac.uk.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  M. Antenos, M. Stemler, I. Boime, and T. K. Woodruff N-Linked Oligosaccharides Direct the Differential Assembly and Secretion of Inhibin {alpha}- and {beta}A-Subunit Dimers Mol. Endocrinol., July 1, 2007; 21(7): 1670 - 1684. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. S. Ishmael, F. T. Ishmael, A. D. Jones, and J. S. Bond Protease Domain Glycans Affect Oligomerization, Disulfide Bond Formation, and Stability of the Meprin A Metalloprotease Homo-oligomer J. Biol. Chem., December 8, 2006; 281(49): 37404 - 37415. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
V. Petropoulou, L. Garrigue-Antar, and K. E. Kadler Identification of the Minimal Domain Structure of Bone Morphogenetic Protein-1 (BMP-1) for Chordinase Activity: CHORDINASE ACTIVITY IS NOT ENHANCED BY PROCOLLAGEN C-PROTEINASE ENHANCER-1 (PCPE-1) J. Biol. Chem., June 17, 2005; 280(24): 22616 - 22623. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
N. Hartigan, L. Garrigue-Antar, and K. E. Kadler Bone Morphogenetic Protein-1 (BMP-1). IDENTIFICATION OF THE MINIMAL DOMAIN STRUCTURE FOR PROCOLLAGEN C-PROTEINASE ACTIVITY J. Biol. Chem., May 9, 2003; 278(20): 18045 - 18049. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. Leighton and K. E. Kadler Paired Basic/Furin-like Proprotein Convertase Cleavage of Pro-BMP-1 in the trans-Golgi Network J. Biol. Chem., May 9, 2003; 278(20): 18478 - 18484. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Bernocco, B. M. Steiglitz, D. I. Svergun, M. V. Petoukhov, F. Ruggiero, S. Ricard-Blum, C. Ebel, C. Geourjon, G. Deleage, B. Font, et al. Low Resolution Structure Determination Shows Procollagen C-Proteinase Enhancer to be an Elongated Multidomain Glycoprotein J. Biol. Chem., February 21, 2003; 278(9): 7199 - 7205. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
