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The ubiquitin-proteasome system regulates the stability and activity of the glucose sensor glucokinase in pancreatic β-cells.
Biochem J
December 2013
*Institute of Clinical Biochemistry, Hannover Medical School, 30625 Hannover, Germany.
The ubiquitin-proteasome system is important to maintain pancreatic β-cell function. Inhibition of the proteasome significantly reduced glucose-induced insulin secretion. Key regulators of the stimulus/secretion cascade seem to be affected by protein misfolding if the proteasome is down-regulated as recently reported in humans with Type 2 diabetes.
View Article and Find Full Text PDFEffect of low temperatures on compound 48/80-induced intracellular Ca2+ changes and exocytosis of rat peritoneal mast cells.
Arch Histol Cytol
July 2000
Department of Cell Biology and Neuroanatomy, Iwate Medical University, Morioka, Japan.
It has been well documented that compound 48/80-induced exocytosis of mast cells is accompanied by changes in intracellular Ca2+ concentration ([Ca2+]i) showing a biphasic pattern: an initial phase which constitutes an abrupt increase, followed by a plateau phase. The former is caused by Ca2+ release from intracellular Ca2+ stores, and the latter is the result of secondary Ca2+ influx. Low temperatures lead to the inhibition of exocytosis, but the precise mechanism remains unclear.
View Article and Find Full Text PDFEnhanced phosphorylation of two specific protein bands accompanied catecholamine secretion from cultured bovine adrenal medulla cells stimulated by different secretagogues. Cells preincubated with 32Pi were treated with nicotine, veratridine, Ionomycin, or barium. Each of these secretagogues stimulated the phosphorylation of two protein bands with apparent molecular weights of 60,000 and 95,000.
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