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Protein Kinase C is a mediator of the synthesis and secretion of osteoprotegerin in osteoblast-like cells.

Abstract：

:Osteoprotegerin (OPG) is a member of the TNF receptor superfamily and plays a critical role in the development of osteoclasts from precursor cells. OPG is produced by a variety of cells of mesenchymal origin and has been demonstrated to be present in osteoblasts and osteocytes. However, the mechanisms of regulation of OPG production and secretion are not known. Using a highly specific polyclonal antibody, we demonstrate that OPG is synthesized and secreted by osteoblast-like cells in culture. We further show that phorbol myristate acetate, an activator of protein kinase C, activated the secretion of OPG. Further, the increased secretion of OPG correlated well with a corresponding increase in OPG mRNA abundance. In addition, OPG promoter stably integrated into an osteoblast cell line was activated by phorbol myristate acetate. The increase in OPG expression was blocked by an inhibitor of protein kinase C, although the basal OPG expression was not altered. These results suggest that activation of the protein kinase C pathway may play a critical role in OPG expression.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Yang X,Halladay D,Onyia JE,Martin TJ,Chandrasekhar S

doi

10.1006/bbrc.2001.6176

subject

Has Abstract

pub_date

2002-01-11 00:00:00

pages

42-6

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006291X01961765

journal_volume

290

pub_type

杂志文章

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