Calmodulin-stimulated phosphorylation of 17 beta-estradiol receptor on tyrosine.
نویسندگان
چکیده
منابع مشابه
Insulin-stimulated phosphorylation of calmodulin.
Calmodulin is phosphorylated in vitro by the insulin-receptor tyrosine kinase and a variety of serine/threonine kinases. Here we report that insulin stimulates the phosphorylation of calmodulin on average 3-fold in intact rat hepatocytes. Although calmodulin is constitutively phosphorylated, insulin increases phosphate incorporation into serine, threonine and tyrosine residues. We demonstrate t...
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CONTEXT Ovarian hormones modulate insulin sensitivity, but their exact role remains unclear. OBJECTIVE We tried to determine whether different doses of 17-beta-estradiol cause changes in the regulation of insulin receptor substrate (IRS-1) levels, and if so, the possible implications in insulin sensitivity. DESIGN Ovariectomized rats were treated with different doses of 17-beta-estradiol at...
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ACKNOWLEDGEMENTS Foremost, I would like to sincerely express my gratitude to my mentor Dr. James Simpkins for his continued support, encouragement, sound advice and for his strategic ideas that contributed to the betterment of my thesis work and helped me meet my timelines. This work would not have been possible without him. Also, I would like to sincerely appreciate Dr. Simpkins for his kind a...
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متن کاملInsulin-stimulated phosphorylation of calmodulin by rat liver insulin receptor preparations.
Insulin stimulates autophosphorylation of the beta subunit of its receptor and activates the associated tyrosine kinase. This kinase, in turn, phosphorylates a number of specific protein substrates; however, the functional and structural identity of these substrates is largely unknown. In this study, we demonstrate that insulin also stimulates the phosphorylation of calmodulin by rat hepatocyte...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1984
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.81.19.5921