Insulin-like growth factor-binding protein-5 (IGFBP-5) stimulates phosphorylation of the IGFBP-5 receptor

被引:118
作者
Andress, DL
机构
[1] Vet Affairs Med Ctr, Med Serv, Seattle, WA 98108 USA
[2] Vet Affairs Med Ctr, Res Serv, Seattle, WA 98108 USA
[3] Univ Washington, Dept Med, Seattle, WA 98493 USA
来源
AMERICAN JOURNAL OF PHYSIOLOGY-ENDOCRINOLOGY AND METABOLISM | 1998年 / 274卷 / 04期
关键词
osteoblast;
D O I
10.1152/ajpendo.1998.274.4.E744
中图分类号
R5 [内科学];
学科分类号
1002 ; 100201 ;
摘要
The finding that insulin-like growth factor (IGF)-binding protein-5 (IGFBP-5) binding to mouse osteoblasts was capable of being downregulated by IGFBP-5 suggested that the 420-kDa membrane protein, which interacted with IGFBP-5, may be a signaling receptor (Andress, D. L. J. Biol. Chem. 270: 28289-28296, 1995). In the current study, a carboxy-terminal IGFBP-5 peptide, IGFBP-5-(201-218), which was found to competitively inhibit I-125-IGFBP-5 binding and to specifically bind to osteoblast monolayers, was used to affinity-purify the 420-kDa membrane protein. Coincubation of the affinity-purified membrane protein with [P-32]ATP resulted in autophosphorylation at serine residues. Serine phosphorylation of the 420-kDa protein was enhanced by intact IGFBP-5, IGFBP-5-(1-169), and IGFBP-5-(201-218). When the IGFBP-5 receptor was incubated with dephosphorylated casein in the presence of [P-32]ATP, casein became phosphorylated on serine residues. These data indicate that IGFBP-5 stimulates the phosphorylation of the IGFBP-5 receptor and suggest that serine/threonine kinase activation may be important in mediating some of the IGF-independent effects of IGFBP-5.
引用
收藏
页码:E744 / E750
页数:7
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