Effects of Protein Phosphorylation on the Sulphonylurea Receptor of the Pancreatic β-Cell
There is evidence that protein phosphorylation may modulate the action of diazoxide on the β-cell K-ATP channel  and the sulphonylurea receptor [2–3]. In this paper, we have further investigated the role of phosphorylation in the action of diazoxide on the β-cell sulphonylurea receptor by carrying out time-course studies on inhibition of [3H]-gliben-clamide binding by MgATP and diazoxide, and by examining effects of phosphatase inhibitors on binding. We also investigated the presence of protein kinase and protein phosphatase activities in β-cell membrane fractions.
KeywordsProtein Phosphorylation Okadaic Acid Photoaffinity Label United Kingdom Introduction Sulphonylurea Receptor
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- 9.Kramer, W., Müller, G., Girbig, F., Gutjahr, U., Kowalewski, S., Hartz, D. and Summ, H.-D., 1994, Differential interaction of glimepiride and glibenclamide with the beta-cell sulfonylurea receptor. II. Photoaffinity labeling of a 65 kDa protein by [3H]glimepiride, Biochim. Biophys. Acta 1191: 278–290PubMedCrossRefGoogle Scholar