Detail of "60514-48-9"

Reference

Diacylglycerols release LH: structure-activity relations reveal a role for protein kinase C

Diacylglycerols release LH: structure-activity relations reveal a role for protein kinase C. Conn, P. Michael; Ganong, Barry R.; Ebeling, James; Staley, Daphne; Neidel, James E.; Bell, Robert M. (Dep. Pharmacol., Univ. Iowa, Iowa City, IA 52242, USA). Biochem. Biophys. Res. Commun., 126(1), 532-9 (English) 1985.Several reagents such as 9026-43-1 is used here. CODEN: BBRCA9. 9026-43-1 which is the cas registry number is also used here. ISSN: 0006-291X. DOCUMENT TYPE: Journal CA Section: 2 (Mammalian Hormones) Section cross-reference(s): 7 A series of diacylglycerols were synthesized with varying lengths and substituents to establish the structure-activity relationship between each with activation of protein kinase [9026-43-1] C and stimulation of a biol. response system (pituitary LH [9002-67-9] release). This approach enables distinction between actions mediated by direct activation of protein kinase C and those due to other, presumably nonspecific, actions. The ability of diacylglycerols to function as regulators of a biol. response system and of protein kinase C was investigated with a series of sn-1,2 diacylglycerols contg. fatty acids 4-10 C in length and with analogs in which the 3'-hydroxyl was replaced with a chloro, H, or sulfhydryl moiety. Several diacylglycerols stimulated LH release in a saturable, time- and dose-dependent manner that was independent of extracellular Ca. Dioctanoylglycerol [60514-48-9] was the most effective of the diacylglycerols tested; 3'-analogs lacking the hydroxyl were inactive. The diacylglycerols activated protein kinase C in vitro, whereas the 3'-analogs did not. These data implicate protein kinase C in the mechanism of LH release, demonstrate that unsatd. fatty acyl moieties within the diacylglycerol are not required for protein kinase C activation, and establish diacylglycerol-protein kinase C structure-function relationships that should prove useful for investigations in other systems. ..

Protein kinase C activators suppress stimulation of capillary endothelial cell growth by angiogenic endothelial mitogens

Protein kinase C activators suppress stimulation of capillary endothelial cell growth by angiogenic endothelial mitogens. Doctrow, Susan R.; Folkman, Judah (Dep. Surg., Child. Hosp., Boston, MA 02115, USA). J. Cell Biol., 104(3), 679-87 (English) 1987. CODEN: JCLBA3. ISSN: 0021-9525. DOCUMENT TYPE: Journal CA Section: 2 (Mammalian Hormones) The protein kinase C activator b-phorbol 12,13-dibutyrate (PDBu) [37558-16-0] suppresses bovine capillary endothelial (BCE) cell proliferation and DNA synthesis in response to human hepatoma-derived growth factor, an angiogenic endothelial mitogen. In contrast, PDBu has no effect on the proliferation of bovine aortic endothelial cells and is mitogenic for bovine aortic smooth muscle and BALB/c 3T3 cells. Several observations indicate that the inhibition of human hepatoma-derived growth factor-stimulated BCE cell growth by PDBu is mediated through protein kinase C. Different phorbol compds. inhibit BCE cell growth according to their potencies as protein kinase C activators (12-O-tetradecanoylphorbol 13-acetate [16561-29-8] > PDBu >> b-phorbol 12,13-diacetate [24928-15-2] >>> b-phorbol; a-phorbol 12,13-dibutyrate; a-phorbol 12,13-didecanoate). PDBu binds to a single class of specific, saturable sites on the BCE cell with an apparent dissocn. const. of 8 nM, in agreement with reported affinities of PDBu for protein kinase C in other systems. Specific binding of PDBu to BCE cells is displaced by sn-1,2-dioctanoylglycerol [60514-48-9], a protein kinase C activator and an analog of the putative 2nd messenger activating this kinase in vivo. The weak protein kinase C activator, sn-1,2-dibutyrylglycerol, does not affect PDBu binding. A cytosolic ext.In this experiment, several chemicals are used like 24928-15-2 and 9026-43-1 from BCE cells contains a Ca/phosphatidylserine-dependent protein kinase that is activated by sn-1,2-dioctanoylglycerol and PDBu, but not by b-phorbol. Apparently, protein kinase C activation can cause capillary endothelial cells to become desensitized to angiogenic endothelial mitogens. This intracellular regulatory mechanism might be invoked during certain phases of angiogenesis, for example when proliferating endothelial cells become differentiated to organize into nongrowing tubes. .