Osteogenic Protein-1 (OP-1) Expression and Processing in Chinese Hamster Ovary Cells: Isolation of a Soluble Complex Containing the Mature and Pro-Domains of OP-1
作者:
JonesWilliam K.,
RichmondEmilie A.,
WhiteKerry,
SasakHalina,
KusmikWilliam,
SmartJohn,
OppermannHermann,
RuegerDavid C.,
TuckerRonald F.,
期刊:
Growth Factors
(Taylor Available online 1994)
卷期:
Volume 11,
issue 3
页码: 215-225
ISSN:0897-7194
年代: 1994
DOI:10.3109/08977199409046919
出版商: Taylor&Francis
关键词: Osteogenic Protein 1 (OP-1);BMP-7;bone morphogenesis;growth factor;TGF-βfamily;protein processing
数据来源: Taylor
摘要:
AbstractWe have characterized the expression and processing of Osteogenic Protein-1 (hOP-1), a bone morphogenic protein of the TGF-βfamily, in Chinese hamster ovary cells. The hOP-1 is initially synthesized as a monomeric 50 kDa pro-protein that is dimerized, glycosylated, and then proteolytically cleaved at the Arg-Xaa-Xaa-Arg maturation site in an acidic cellular compartment before secretion into the medium. Of the four potential N-linked glycosylation sites two are used, one in the mature domain and one in the pro-domain. Gel permeation chromatography of secreted hOP-1 in physiological buffers yields an apparent molecular weight of 110-120 k, indicating that after proteolytic processing the two pro-domains remain non-covalently associated with the disulfide linked mature dimer in a complex termed soluble hOP-1. Purified soluble hOP-1 is significantly more soluble in physiological buffers than the purified mature OP-1.
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