Detail of "2623-82-7"

Reference

Increased diacylglycerol levels inhibit [20-3H]phorbol 12,13-dibutyrate binding and the glucocorticoid-mediated increase in glycerol phosphate dehydrogenase levels in C6 rat glioma cells

Increased diacylglycerol levels inhibit [20-3H]phorbol 12,13-dibutyrate binding and the glucocorticoid-mediated increase in glycerol phosphate dehydrogenase levels in C6 rat glioma cells. Bressler, Joseph (Surg. Neurol. Branch, NINCDS, Bethesda, MD 20205, USA). J. Neurochem., 48(1), 181-6 (English) 1987. CODEN: JONRA9. ISSN: 0022-3042. DOCUMENT TYPE: Journal CA Section: 4 (Toxicology) Whether the phorbol ester-mediated inhibition of glycerol 3-phosphate dehydrogenase (GPDH) [9075-65-4] induction could be mimicked by raising the cellular diacylglycerol levels was studied. Phorbol ester tumor promoters and diacylglycerols activate protein kinase [9026-43-1] C. An increase in radiolabeled diacylglycerol levels in C6 rat glioma cells was obsd. when cells were prelabeled overnight with 3H-labeled arachidonic acid [506-32-1] and treated with either phospholipase C [9001-86-9] (Clostridium perfringens) or 2-bromooctanoic acid [2623-82-7]. The increase was dose-dependent. The diacylglycerols competed with 20-3H-labeled phorbol 12,13-dibutyrate [37558-16-0] in binding to the phorbol ester receptor. A Scatchard anal. of the binding of cells treated with 0.There are some commonly used reagents with their cas registry numbers 37558-16-0 and 9075-65-4 in this article.1 unit/mL of phospholipase C demonstrated that the inhibition was mainly due to a decrease in binding affinity and not in the total no. of binding sites. 2-Bromooctanoate and phospholipase C, but not the synthetic diacylglycerol 1-oleoyl 2-acetyl glycerol [84746-00-9], inhibited the glucocorticoid induction of GPDH levels. Boiled phospholipase C, phospholipase A2 [9001-84-7], or phospholipase D [9001-87-0] were ineffective in inhibiting induction, a result suggesting that the inhibition was not due to nonspecific membrane perturbation. Thus, inhibition of the glucocorticoid-mediated increase in GPDH induction is most likely mediated by protein kinase C, and not by an alternate phorbol ester receptor. .

Starvation-induced secretory changes of insulin, somatostatin, and glucagon and their modification by 2-bromostearate

Starvation-induced secretory changes of insulin, somatostatin, and glucagon and their modification by 2-bromostearate. Tamarit-Rodriguez, J.; Vara, E.; Tamarit, J. (Fac. Med., Univ. Complutense, Madrid, Spain). Horm. Metab. Res., 16(3), 115-19 (English) 1984. CODEN: HMMRA2. ISSN: 0018-5043. DOCUMENT TYPE: Journal CA Section: 2 (Mammalian Hormones) Section cross-reference(s): 13 2-Bromostearate (BrS) [2623-82-7], a fatty acid (FFA)-oxidn. inhibitor, was tested on rat pancreatic islet secretion of insulin [9004-10-8], glucagon [9007-92-5], and somatostatin [51110-01-1] stimulated by glucose [50-99-7] or palmitate [57-10-3] under fasted or fed conditions. Starvation for 48 h blocked both the glucose-induced stimulation of insulin and the inhibition of somatostatin and glucagon secretion. BrS completely restored the insulin response and stimulated both somatostatin and glucagon-basal release, the latter inhibition by glucose being partially recovered. Palmitate transient stimulation of insulin and somatostatin and inhibition of glucagon release was turned into a sustained increase in all 3 cases by addn. of BrS. The potentiation by BrS of palmitate secretory effects in fed islets and of hormone release in fasted islets suggest that inhibition of FFA-oxidn. may play a role in the regulation of islet secretion.