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Growth hormone stimulates tyrosine phosphorylation of focal adhesion kinase (p125(FAK)) and actin stress fiber formation in human osteoblast-like cells, Saos2.

Abstract：

:Bone is one of the essential target tissues of growth hormone (GH). In bone remodeling, cell-matrix attachment is important where focal adhesion kinase (FAK) is involved. FAK plays a central role in determining the shape and motility of cells in response to the extracellular matrix stimuli. In the present study, we have demonstrated that GH stimulated tyrosine phosphorylation of FAK in human osteoblast-like cells, Saos2. Moreover, GH rapidly enhanced the formation of actin stress fibers. In Saos2, Jak2 was tyrosine phosphorylated by GH stimulation, and AG490, a Jak2 specific inhibitor, inhibited GH-induced tyrosine phosphorylation of FAK and actin stress fiber reorganization. These results suggest that GH activates FAK via Jak2, and stimulates the formation of actin stress fibers in Saos2. Activation of FAK and actin stress fiber formation induced by GH seem to be important for the physiological role of osteoblast.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Takahashi MO,Takahashi Y,Iida K,Okimura Y,Kaji H,Abe H,Chihara K

doi

10.1006/bbrc.1999.1314

subject

Has Abstract

pub_date

1999-09-16 00:00:00

pages

100-6

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006291X99913141

journal_volume

263

pub_type

杂志文章

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