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Stimulatory effect of basic fibroblast growth factor on induction of heat shock protein 27 in osteoblasts: role of protein kinase C.

Abstract：

:In a previous study we showed that basic fibroblast growth factor (bFGF) stimulates activation of protein kinase C through phosphoinositide hydrolysis by phospholipase C and phosphatidylcholine hydrolysis by phospholipase D in osteoblast-like MC3T3-E1 cells. In the present study, we investigated whether bFGF stimulates the induction of heat shock protein (HSP) 27, a low-molecular-weight HSP, and HSP70, a high-molecular-weight HSP, in MC3T3-E1 cells and the mechanism behind the induction. bFGF increased the level of HSP27 while having little effect on HSP70 level. bFGF stimulated the accumulation of HSP27 dose-dependently in the range between 1 and 30 ng/ml. bFGF induced an increase in the level of the mRNA for HSP27. The bFGF-stimulated accumulation of HSP27 was reduced by inhibitors of protein kinase C. The bFGF-induced HSP27 accumulation was reduced in protein kinase C-downregulated MC3T3-E1 cells. U-73122, an inhibitor of phospholipase C, and propranolol, a phosphatidic acid phosphohydrolase inhibitor, suppressed the bFGF-stimulated HSP27 accumulation. These results strongly suggest that bFGF stimulates HSP27 induction through protein kinase C activation in osteoblasts.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Kozawa O,Niwa M,Matsuno H,Ishisaki A,Kato K,Uematsu T

doi

10.1006/abbi.2000.2290

subject

Has Abstract

pub_date

2001-04-15 00:00:00

pages

237-42

issue

2

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(00)92290-2

journal_volume

388

pub_type

杂志文章

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