Detail of "7266-47-9"

Reference

Carboxypeptidase B-like converting enzyme activity in secretory granules of rat pituitary

Carboxypeptidase B-like converting enzyme activity in secretory granules of rat pituitary. Hook, Vivian Y. H.; Loh, Y. Peng (Lab. Cell Biol., Natl. Inst. Ment. Health, Bethesda, MD 20205, USA). Proc. Natl. Acad. Sci. U. S. A., 81(9), 2776-80 (English) 1984. CODEN: PNASA6. ISSN: 0027-8424. DOCUMENT TYPE: Journal CA Section: 2 (Mammalian Hormones) Section cross-reference(s): 7 The existence of a carboxypeptidase B (I) [9025-24-5] activity in purified secretory granules from anterior, intermediate, and neural lobes of rat pituitary was examd. A I activity that cleaved the C-terminal -Lys-Lys-Arg residues from the ACTH fragment ACTH-(1-17) [7266-47-9] (a potential hormone product liberated from pro-opiocortin by a trypsin-like enzyme) was detected in anterior and intermediate lobe granules. A similar I activity was also present in purified secretory granules from rat pituitary neural lobes that cleaved the -Lys-Arg residues from [Arg8]vasopressin-Gly-Lys-Arg [90846-53-0], a potential product cleaved from provasopressin. Secretory granule carboxypeptidase(s) from the 3 lobes of the pituitary cleaved 125I-labeled [Met]enkephalin-Arg6 [76310-14-0] to form 125I-labeled methionine enkephalin as well. 125I-labeled methionine enkephalin was used as a model substrate for the quant. assay of pituitary carboxypeptidase activity. The I in secretory granules from all 3 lobes was active at pH 5.5, but not at pH 7.4. Inhibition by the Zn metallocarboxypeptidase inhibitors guanidinopropylsuccinic acid, aminomercaptosuccinic acid, benzylsuccinic acid, 2-mercaptomethyl-3-guanidinoethylthiopropanoic acid, and the potato I inhibitor and inhibition by the metal chelators EDTA and 1,10-phenanthroline demonstrate metal ion dependence of the pituitary granule I activities. However, Co2+ stimulated the secretory granule I activities. Thiol protease inhibitors such as Cu2+ and p-chloromercuriphenylsulfonic acid also inhibited the activity. Thus, the secretory granule I-like activities in all 3 lobes of the pituitary appear to be similar thiol-metallopeptidases that differ from other carboxypeptidase activities previously described and may play an exclusive role in hormone biosynthesis in the pituitary.

Effect of ACTH 1-17 at different circadian stages on [3H]TdR incorporation into DNA

Effect of ACTH 1-17 at different circadian stages on [3H]TdR incorporation into DNA. Scheving, L. E.; Tsai, T. H.; Pauly, J. E.; Halberg, F. (Dep. Anat., Univ. Arkansas Med. Sci., Little Rock, AR 72205, USA). Peptides (Fayetteville, N. Y.), 5(3), 507-18 (English) 1984. CODEN: PPTDD5. ISSN: 0196-9781. DOCUMENT TYPE: Journal CA Section: 2 (Mammalian Hormones) The effect of ACTH 1-17 [7266-47-9] on the incorporation of [3H]TdR into DNA (DNA synthesis) in the tongue, esophagus, and stomach of CD2F1 mice standardized to 12 h of light alternating with 12 h of darkness was examd. in relation to the time of administration. The response was complex as ACTH 1-17 increased the incorporation of [3H]TdR into DNA at certain times, decreased it at other times, or had no effect at still another time. In general the most marked effects of 20 IU/kg of ACTH 1-17 was to decrease DNA synthesis of as much as 60% 4 h after administration at the end of the dark or beginning of the light span. A 2- and 3-way anal. of variance supported the conclusion that the kind-of-treatment, time-of-treatment and the interval-to-kill (Sampling time) as well as their interactions are important factors when detg. any response of ACTH 1-17 or placebo.