Abstract：
:The receptors for insulin and insulin-like growth factor (IGF)-I carry intrinsic tyrosine-specific protein kinases (TPK) in their cytoplasmic domains that show 84% homology. Our previous studies using tyrosine-containing synthetic polymers (Arch. Biochem. Biophys. 260, 416, 1988) revealed subtle differences between the two receptor TPKs. In the present study, low molecular weight kinase inhibitors were used to compare the two receptor TPKs purified from human placenta. Staurosporine was the most potent inhibitor of both receptor TPKs among the three inhibitors tested. It was 100 times more inhibitory to insulin receptor TPK (ED50 = 61nM) than IGF-I receptor TPK (ED50 = 6.2 microM). Apigenin and kaempferol showed approximately the same inhibitory potency toward both TPKs with a range of 10 approximately 1000 microM. Staurosporine is thus an excellent tool to biochemically characterize the two receptor TPKs as well as to selectively inhibit insulin-activated TPK in intact cells.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Fujita-Yamaguchi Y,Kathuria Sdoi
10.1016/s0006-291x(88)80967-7subject
Has Abstractpub_date
1988-12-30 00:00:00pages
955-62issue
3eissn
0006-291Xissn
1090-2104pii
S0006-291X(88)80967-7journal_volume
157pub_type
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