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Protein Kinase Activity of the Insulin Receptor Is Essential for Insulin-Regulated Gene Expression.

Abstract：

:Two Chinese hamster ovary (CHO) cell lines stably transfected with human insulin receptor cDNA, CHO-wt and CHO-mut, which express an equivalent number of normal and kinase-defective human insulin receptors, respectively, were used to assess the roles of insulin receptor tyrosine kinase activity in insulin-regulated gene expression. The effect of insulin on gene-33-promoter-driven chloramphenicol acetyltransferase (CAT), RSVLTR-driven beta-galactosidase (pRSVLTR-betagal) and SV40 late-promoter-driven hepatitis B surface antigen (pMLSV(2)HBsAg) were examined in CHO-wt and CHO-mut cells. Insulin-stimulated gene 33 promoter is 10- to 50-fold more effective in CHO-wt cells than that in parental CHO cells. However, no enhancement of insulin sensitivity of gene 33 promoter in CHO-mut cells relative to parental CHO cells was found. Similar phenomena were also observed, in that insulin regulated pRSVLTR-betagal and pMLSV(2)HBsAg in these three CHO lines. Our data indicated that the protein kinase activity of the insulin receptor is essential for the stimulatory activity of insulin toward the activities of different promoters. Copyright 1994 S. Karger AG, Basel

journal_name

J Biomed Sci

journal_title

Journal of biomedical science

authors

Lin SC,Chen MF,Chou CK

doi

10.1007/BF02258333

keywords:

subject

Has Abstract

pub_date

1994-12-01 00:00:00

pages

2-6

issue

1

eissn

1021-7770

issn

1423-0127

pii

jbs01002

journal_volume

1

pub_type

杂志文章

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