Detail of "53697-27-1"

Reference

Specific interactions between peptide hormones and artificial lipid membranes

Specific interactions between peptide hormones and artificial lipid membranes. Schwyzer, Robert; Gremlich, Hans Ulrich; Gysin, Beat; Sargent, David F.; Fringeli, Urs Peter (Lab. Mol. Biol. Biophys., Swiss Fed. Inst. Technol., Zurich CH-8093, Switz.). Pept.: Struct. Funct., Proc. Am. Pept. Symp., 8th, 657-64. Edited by: Hruby, Victor J.; Rich, Daniel H. Pierce Chem. Co.: Rockford, Ill. (English) 1983. CODEN: 51KAAK. DOCUMENT TYPE: Conference CA Section: 2 (Mammalian Hormones) 1-24-ACTH [16960-16-0] was readily adsorbed to lecithin and dioleoylphosphatidylcholine [10015-85-7] bilayers, whereas 11-24-ACTH [4237-93-8] and 1-10-ACTH [2791-05-1] were not adsorbed. A model for this binding of 1-24-ACTH is presented. When 5-24-ACTH [39603-68-4], 7-24-ACTH [60348-26-7], 1-13-ACTH amide [53697-27-1], and acetyl 1-13-ACTH amide [581-05-5] were tested for labeling with the hydrophobic photolabel [125I]3-trifluoromethyl-3-(m-iodophenyl)diazirine in the presence of lipid vesicles, those fragments contg. residues 11-24 were strongly labeled. The intensity of the vesicle-mediated hydrophobic labeling of the ACTH peptides was correlated with their in vitro steroidogenic agonistic and antagonistic potencies. 1-13-Dynorphin [72957-38-1] bound hydrophobically to lipid vesicles analogously to 1-24-ACTH. Enkephalin peptides and their amides had weak hydrophobic interactions with lecithin-phosphatidic acid and phosphatidylserine vesicles. The free acids, such as leucine-enkephalin [58822-25-6], interact even more weakly with brain cerebroside sulfate vesicles, whereas the amides reacted strongly. Hydrophobic interactions and head group specificity were correlated with known pharmacol. properties of the peptides studied.

Suppression of basal and stress-induced prolactin release and stimulation of luteinizing hormone secretion by a-melanocyte-stimulating hormone

Suppression of basal and stress-induced prolactin release and stimulation of luteinizing hormone secretion by a-melanocyte-stimulating hormone. Newman, Connie B.; Wardlaw, Sharon L.; Frantz, Andrew G. (Coll. Physicians Surg., Columbia Univ., New York, NY 10032, USA). Life Sci., 36(17), 1661-8 (English) 1985. CODEN: LIFSAK. ISSN: 0024-3205. DOCUMENT TYPE: Journal CA Section: 2 (Mammalian Hormones) Basal LH [9002-67-9] secretion and basal and stress-induced prolactin [9002-62-4] release were studied in adult male rats after intraventricular injection of a-MSH [37213-49-3]. Each rat also received intraventricular saline in order to serve as its own control. a-MSH (18 mg) stimulated plasma LH from 16.5 ng/mL to peaks of 27.2 and 26.0 ng/mL at 5 and 10 min, resp., and suppressed prolactin from 3.5 ng/mL to 1.3 and 1.2 ng/mL at 15 and 30 min, resp. Intraventricular a-MSH also blunted the prolactin rise assocd. with the stress of swimming. At 10 and 20 min after the onset of swimming, prolactin levels in rats pretreated with a-MSH were diminished: 7.4 and 6.5 ng/mL vs. 23.8 and 15.2 ng/mL after normal saline. Similarly, des-acetyl a-MSH [53697-27-1], which is the predominant form of a-MSH in the hypothalamus, diminished the stress-induced prolactin rise from 18.4 and 11.2 ng/mL at 10 and 20 min to 10.0 and 5.5 ng/mL, resp. Thus, centrally administered a-MSH stimulates LH and suppresses basal and stress-induced prolactin release in male rats. These actions are opposite to those previously shown for b-endorphin, and suggest that a-MSH may antagonize the effects of b-endorphin on pituitary function.