Detail of "88894-91-1"

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Growth hormone-releasing factor from ovine and caprine hypothalamus: isolation, sequence analysis and total synthesis

Growth hormone-releasing factor from ovine and caprine hypothalamus: isolation, sequence analysis and total synthesis. Brazeau, Paul; Bohlen, Peter; Esch, Frederick; Ling, Nicholas; Wehrenberg, William B.; Guillemin, Roger (Lab. Neuroendocrinol., Salk Inst. Biol. Stud., La Jolla, CA 92037, USA). Biochem. Biophys. Res. Commun., 125(2), 606-14 (English) 1984. CODEN: BBRCA9. ISSN: 0006-291X. DOCUMENT TYPE: Journal CA Section: 2 (Mammalian Hormones) Peptides with high intrinsic growth hormone-releasing activity were isolated from 2100 ovine and 2600 caprine (goat) hypothalami by means of acid extn., immunoaffinity chormatog., gel filtration and reverse-phase HPLC. Structural characterization by gas-liq. phase sequencing and peptide mapping established the primary structure of sheep growth hormone-releasing factor [94948-82-0] as Tyr-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-Tyr-Arg-Lys-Ile-Leu-Gly-Gln-Leu-S er-Ala-Arg-Lys-Leu-Leu-Gln-Asp-Ile-Met-Asn-Arg-Gln-Gln-Gly-Glu-Arg- Asn-Gln-Glu-Gln-Gly-Ala-Lys-Val-Arg-Leu-NH2. Goat growth hormone-releasing factor [88894-91-1] possessed the same sequence, except for the replacement of the isoleucine residue in position 13 with valine; thus, it was identical to bovine growth hormone-releasing factor.

GH releasing factor: isolation, characterization and physiology

GH releasing factor: isolation, characterization and physiology. Brazeau, Paul; Bohlen, Peter; Esch, Fred; Ling, Nicholas; Wehrenberg, William B.; Guillemin, Roger (Neuroendocrinol. Lab., Notre-Dame Hosp., Montreal, PQ H2L 4K8, Can.). Monoclonal Antibodies New Trends Immunoassays, Proc. Int. Symp. Radioimmunol., 6th, 211-18. Edited by: Bizollon, Charles A. Elsevier: Amsterdam, Neth. (English) 1984. CODEN: 53DAAX. DOCUMENT TYPE: Conference CA Section: 2 (Mammalian Hormones) In comparison with human growth hormone-releasing factor-44-NH2 (hGRF-44-NH2) [83930-13-6], rat growth hormone-releasing factor-43-OH (rGRF-43-OH) [95536-01-9] is equipotent in rat pituitary cell cultures, whereas porcine growth hormone-releasing factor-44-NH2 [88384-73-0] is 75% as potent and bovine growth hormone-releasing factor-44-NH2 [88894-91-1] is 62% as potent. The species differences in the activity of these growth hormone-releasing factors (GRFs) are explained by variations in the mol. structure within the C-terminal portion from residues 28-44. Rat growth hormone-releasing factor (rGRF) [9034-39-3], hGRF-44-NH2, and 20 analogs of hGRF-44-NH2 were tested for their relative potencies to release growth hormone (GH) [9002-72-6] in cultured rat pituitary cells. The most effective prepns. were hGRF-44-NH2, (Norval-27)-human growth hormone-releasing factor-40-OH [95685-56-6], and rGRF. A 2 min pulse with hGRF-44-NH2 caused a prompt monospecific stimulation of GH within 32 s, whereas a 1 h continuous stimulation with an 80% max. ED of the releasing factor caused an oscillatory hormonic type of GH secretion in which the oscillations slowed with increasing dose. 8-Bromine-cAMP [23583-48-4], perfused into the pituitary glands prevented these oscillations. Thus, cAMP [60-92-4] appears to be the mediator harmonizing the oscillatory secretion. Addnl., physiol. studies on GRF in humans and rats are reported. In humans, the max. i.v. dose of GRF was 0.5 mg/kg. Human hypopituitary dwarfism did not respond well to GRF, although the effects of pulsatile chronic injections are still being studied. Humans over 40 showed a reduced response to hGRF-44-NH2. This was probably due to an accumulation of somatostatin [51110-01-1] in somatotrophs, since the effect was not seen in the presence of anti-somatostatin antiserum. The results are discussed relative to species differences in the mols. of the various GRFs; however, these results in rat pituitary cells are probably not applicable to pituitary cells of other species.