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GRF (1-43) (rat)

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GRF (1-43) (rat) is an indispensable peptide hormone deployed extensively in biomedical research to elicit an upsurge in the exudation of growth hormone.

Category

Peptide Inhibitors

Catalog number

BAT-015161

CAS number

86472-71-1

Molecular Formula

C225H361N77O66S

Molecular Weight

5232.89

Specification
Reference Reading

IUPAC Name

(4S)-4-[[2-[[(2S)-5-amino-2-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-5-amino-2-[[2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-amino-3-(1H-imidazol-5-yl)propanoyl]amino]propanoyl]amino]-3-carboxypropanoyl]amino]propanoyl]amino]-3-methylpentanoyl]amino]-3-phenylpropanoyl]amino]-3-hydroxybutanoyl]amino]-3-hydroxypropanoyl]amino]-3-hydroxypropanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-3-methylpentanoyl]amino]-4-methylpentanoyl]amino]acetyl]amino]-5-oxopentanoyl]amino]-4-methylpentanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]propanoyl]amino]-5-carbamimidamidopentanoyl]amino]hexanoyl]amino]-4-methylpentanoyl]amino]-4-methylpentanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]amino]-4-carboxybutanoyl]amino]-3-methylpentanoyl]amino]-4-methylsulfanylbutanoyl]amino]-3-carboxypropanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-oxopentanoyl]amino]-5-oxopentanoyl]amino]acetyl]amino]-5-[[(2S)-1-[[(2S)-4-amino-1-[[(2S)-5-amino-1-[[(2S)-1-[[(2S)-5-amino-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(1S)-3-amino-1-carboxy-3-oxopropyl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]amino]-1,5-dioxopentan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-1,5-dioxopentan-2-yl]amino]-1,4-dioxobutan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]amino]-5-oxopentanoic acid

Alternative CAS

95536-01-9; 100918-42-1; 108316-45-6

Synonyms

Growth Hormone-Releasing Hormone (rat); H-His-Ala-Asp-Ala-Ile-Phe-Thr-Ser-Ser-Tyr-Arg-Arg-Ile-Leu-Gly-Gln-Leu-Tyr-Ala-Arg-Lys-Leu-Leu-His-Glu-Ile-Met-Asn-Arg-Gln-Gln-Gly-Glu-Arg-Asn-Gln-Glu-Gln-Arg-Ser-Arg-Phe-Asn-OH; Rat hypothalamic growth hormone-releasing factor (1-43); GRF (rat); GHRF, rat; L-Histidyl-L-alanyl-L-α-aspartyl-L-alanyl-L-isoleucyl-L-phenylalanyl-L-threonyl-L-seryl-L-seryl-L-tyrosyl-L-arginyl-L-arginyl-L-isoleucyl-L-leucylglycyl-L-glutaminyl-L-leucyl-L-tyrosyl-L-alanyl-L-arginyl-L-lysyl-L-leucyl-L-leucyl-L-histidyl-L-α-glutamyl-L-isoleucyl-L-methionyl-L-asparaginyl-L-arginyl-L-glutaminyl-L-glutaminylglycyl-L-α-glutamyl-L-arginyl-L-asparaginyl-L-glutaminyl-L-α-glutamyl-L-glutaminyl-L-arginyl-L-seryl-L-arginyl-L-phenylalanyl-L-asparagine; Somatoliberin (human pancreatic islet), 1-L-histidine-8-L-serine-12-L-arginine-13-L-isoleucine-18-L-tyrosine-24-L-histidine-25-L-glutamic acid-28-L-asparagine-34-L-arginine-38-L-glutamine-39-L-arginine-40-L-serine-42-L-phenylalanine-43-L-asparagine-44-de-L-leucinamide-; Somatoliberin (rat hypothalamus); Rat hypothalamic GH-releasing factor(1-43); Rat somatoliberin

Appearance

White or Off-white Lyophilized Powder

Purity

≥95%

Sequence

HADAIFTSSYRRILGQLYARKLLHEIMNRQQGERNQEQRSRFN

Storage

Store at -20°C

Solubility

Soluble in Water

InChI

InChI=1S/C225H360N76O67S/c1-20-111(12)174(298-180(329)116(17)264-201(350)154(96-172(323)324)282-179(328)114(15)262-181(330)126(227)92-122-98-249-105-260-122)215(364)293-151(89-119-40-27-24-28-41-119)210(359)301-177(117(18)305)217(366)297-159(104-304)213(362)296-158(103-303)212(361)288-150(91-121-52-56-125(307)57-53-121)205(354)272-129(44-32-77-252-220(237)238)185(334)271-134(49-37-82-257-225(247)248)198(347)299-176(113(14)22-3)216(365)292-144(84-107(4)5)183(332)259-101-168(316)265-136(59-67-161(229)309)192(341)284-146(86-109(8)9)203(352)287-148(90-120-50-54-124(306)55-51-120)200(349)263-115(16)178(327)267-128(43-31-76-251-219(235)236)184(333)268-127(42-29-30-75-226)187(336)283-145(85-108(6)7)202(351)285-147(87-110(10)11)204(353)289-152(93-123-99-250-106-261-123)207(356)280-142(65-73-171(321)322)199(348)300-175(112(13)21-2)214(363)281-143(74-83-369-19)197(346)291-155(97-173(325)326)209(358)273-130(45-33-78-253-221(239)240)186(335)276-139(61-69-163(231)311)194(343)275-135(58-66-160(228)308)182(331)258-100-167(315)266-137(63-71-169(317)318)191(340)269-131(46-34-79-254-222(241)242)189(338)290-153(94-165(233)313)208(357)279-140(62-70-164(232)312)195(344)278-141(64-72-170(319)320)196(345)277-138(60-68-162(230)310)193(342)270-133(48-36-81-256-224(245)246)190(339)295-157(102-302)211(360)274-132(47-35-80-255-223(243)244)188(337)286-149(88-118-38-25-23-26-39-118)206(355)294-156(218(367)368)95-166(234)314/h23-28,38-41,50-57,98-99,105-117,126-159,174-177,302-307H,20-22,29-37,42-49,58-97,100-104,226-227H2,1-19H3,(H2,228,308)(H2,229,309)(H2,230,310)(H2,231,311)(H2,232,312)(H2,233,313)(H2,234,314)(H,249,260)(H,250,261)(H,258,331)(H,259,332)(H,262,330)(H,263,349)(H,264,350)(H,265,316)(H,266,315)(H,267,327)(H,268,333)(H,269,340)(H,270,342)(H,271,334)(H,272,354)(H,273,358)(H,274,360)(H,275,343)(H,276,335)(H,277,345)(H,278,344)(H,279,357)(H,280,356)(H,281,363)(H,282,328)(H,283,336)(H,284,341)(H,285,351)(H,286,337)(H,287,352)(H,288,361)(H,289,353)(H,290,338)(H,291,346)(H,292,365)(H,293,364)(H,294,355)(H,295,339)(H,296,362)(H,297,366)(H,298,329)(H,299,347)(H,300,348)(H,301,359)(H,317,318)(H,319,320)(H,321,322)(H,323,324)(H,325,326)(H,367,368)(H4,235,236,251)(H4,237,238,252)(H4,239,240,253)(H4,241,242,254)(H4,243,244,255)(H4,245,246,256)(H4,247,248,257)/t111-,112-,113-,114-,115-,116-,117+,126-,127-,128-,129-,130-,131-,132-,133-,134-,135-,136-,137-,138-,139-,140-,141-,142-,143-,144-,145-,146-,147-,148-,149-,150-,151-,152-,153-,154-,155-,156-,157-,158-,159-,174-,175-,176-,177-/m0/s1

InChI Key

ORNDKVCWLUZAQL-FOWIMTFFSA-N

Canonical SMILES

CCC(C)C(C(=O)NC(CC1=CC=CC=C1)C(=O)NC(C(C)O)C(=O)NC(CO)C(=O)NC(CO)C(=O)NC(CC2=CC=C(C=C2)O)C(=O)NC(CCCNC(=N)N)C(=O)NC(CCCNC(=N)N)C(=O)NC(C(C)CC)C(=O)NC(CC(C)C)C(=O)NCC(=O)NC(CCC(=O)N)C(=O)NC(CC(C)C)C(=O)NC(CC3=CC=C(C=C3)O)C(=O)NC(C)C(=O)NC(CCCNC(=N)N)C(=O)NC(CCCCN)C(=O)NC(CC(C)C)C(=O)NC(CC(C)C)C(=O)NC(CC4=CN=CN4)C(=O)NC(CCC(=O)O)C(=O)NC(C(C)CC)C(=O)NC(CCSC)C(=O)NC(CC(=O)O)C(=O)NC(CCCNC(=N)N)C(=O)NC(CCC(=O)N)C(=O)NC(CCC(=O)N)C(=O)NCC(=O)NC(CCC(=O)O)C(=O)NC(CCCNC(=N)N)C(=O)NC(CC(=O)N)C(=O)NC(CCC(=O)N)C(=O)NC(CCC(=O)O)C(=O)NC(CCC(=O)N)C(=O)NC(CCCNC(=N)N)C(=O)NC(CO)C(=O)NC(CCCNC(=N)N)C(=O)NC(CC5=CC=CC=C5)C(=O)NC(CC(=O)N)C(=O)O)NC(=O)C(C)NC(=O)C(CC(=O)O)NC(=O)C(C)NC(=O)C(CC6=CN=CN6)N

1. Thyrotropin-releasing hormone mediates growth hormone release induced by milk and nursing in neonatal rats

B Kacsóh,C E Grosvenor,B E Tóth J Neuroendocrinol . 1992 Dec;4(6):663-72. doi: 10.1111/j.1365-2826.1992.tb00217.x.

Previous evidence from this laboratory suggested that growth hormone (GH) release induced by milk in vitro and by nursing in vivo from neonatal rat pituitary glands is mediated by an alternative GH-releasing factor(s) (GRF) distinct from GH-releasing hormone (GHRH(1-43) ). In the present experiments we tested whether thyrotropin-releasing hormone (TRH) could fulfil the criteria of this alternative GRF in neonatal rats. The water-soluble fraction of rat milk (infranatant, prepared by ultracentrifugation) and its methanol/acetic acid extract (milk-borne peptides) stimulated GH release from perifused pituitary glands obtained from 2-day-old rats. Dialysis of the infranatant (mol wt cut-off: 2,000) against 500 volumes of culture medium at 4°C eliminated its GH-releasing activity in the perifusion system, while the infranatant retained its full GRF-like activity when incubated at 4°C without dialysis. The milk-borne GRF eluted as a single peak and coeluted with TRH in a combined gel permeation chromatography (Sephadex G-10) and perifusion set-up. Prolactin secretion was also stimulated simultaneously with the release of GH induced either by milk or by TRH. In a stepwise C(18) reversed-phase chromatography, milk-borne GRF was highly hydrophilic and coeluted with synthetic TRH. The in vitro GH-releasing bioactivities of synthetic TRH and a milk extract purified in C(18) reversed-phase chromatography were abolished by proline-specific endopeptidase. Thus, TRH and milk-borne GRF displayed similar molecular weights, hydropathic characteristics and proteolytic enzyme resistance. In vivo, nursing (which has been reported as a potent stimulus of GH secretion even in the absence of milk-intake) increased serum GH levels in 2-day-old pups. A supramaximal dose of TRH (10 ng/g intraperitoneally) stimulated GH release in 2-day-old pups separated from their mothers for 6 h to a similar extent as nursing. Nursing-induced levels of serum GH were not further elevated by TRH. This failure of TRH to further increase serum GH levels was not due to a maximal GH output by the neonatal pituitary gland, since the GH release induced by the serotonin precursor 5-hydroxy-L-tryptophan was augmented either by TRH or by nursing. These data provide evidence that the milk-borne GRF-like activity in vitro is indistinguishable from TRH, and suggest that TRH (probably of hypothalamic origin) might be the mediator of the nursing-induced release of GH in vivo as a physiological GRF in neonatal rats.

2. Semisynthesis of human growth hormone-releasing factor by trypsin catalyzed coupling of leucine amide to a C-terminal acid precursor

A M Felix,J Bongers,R M Campbell,E P Heimer,R E Offord Int J Pept Protein Res . 1992 Sep-Oct;40(3-4):268-73. doi: 10.1111/j.1399-3011.1992.tb00301.x.

Human growth hormone-releasing factor, GRF(1-44)-NH2, was synthesized by trypsin catalyzed coupling of Leu-NH2 to Arg43 of the precursor, GRF(1-43)-OH, prepared by solid phase peptide synthesis. The semisynthetic GRF(1-44)-NH2 was fully characterized and showed full potency in the rat pituitary in vitro bioassay. Conversion to GRF(1-44)-NH2 was limited to 60-70% in both 75% v:v N,N'-dimethylacetamide and 95% v:v 1,4-butanediol due to competing transpeptidations at Arg41 and Arg38 generating [Leu42]-GRF(1-42)-NH2 and [Leu39]-GRF(1-39)-NH2 side-products, respectively. The rates of formation and yields of GRF(1-44)-NH2 versus pH, Leu-NH2 concentration, and solvent composition were also studied.

3. Ontogenetic appearance of immunoreactive GRF-containing neurons in the rat hypothalamus

M Tokuzen,K Chihara,T Shibasaki,H Kawano,H Saito,S Daikoku,M Noguchi Cell Tissue Res . 1985;242(3):511-8. doi: 10.1007/BF00225416.

Ontogenetic development of GRF-containing neurons in the rat hypothalamus was studied employing antisera which were generated against hpGRF (1-44)NH2 and rhGRF(1-43)OH: anti-hpGRF-C and -rhGRF sera recognize the species-specific C-terminal portions of the peptides, and anti-hpGRF-MC and -N sera recognize hpGRF(27-44)NH2 and the N-terminal portion of hpGRF(1-44)NH2, respectively. The anti-hpGRF-C and -rhGRF sera stained different neuronal cell bodies, which were localized in distinct hypothalamic areas. The former serum did not stain the axonal terminals in the median eminence, but the latter stained them strongly. The anti-hpGRF-MC and -N sera stained neuronal cell bodies, some of which corresponded to those immunolabelled with anti-hpGRF-C or -rhGRF serum. The anti-rhGRF serum first demonstrated immunoreactive perikarya in the ventral-lateral border of the arcuate nucleus of 19.5-day-old fetuses that had received an intraventricular colchicine administration 24 h previously. The immunoreactive fibers were recognized first in the external layer of the median eminence of untreated fetuses on day 19.5 of gestation, and then they increased in amount with development. No immunoreactive fibers, however, were found in the median eminence of colchicine-treated animals during the fetal period. It is concluded that in rats GRF may be synthesized in the perikarya on day 18.5 of gestation and conveyed to the median eminence without delay via axonal flow.

4. Regional distribution of rat growth hormone releasing factor-like immunoreactivity in rat hypothalamus

H Kodama,K Chihara,N Minamitani,N Ling,H Kaji,Y Okimura,Y Kashio,T Fujita,T Kita,H Abe Endocrinology . 1985 Jan;116(1):259-62. doi: 10.1210/endo-116-1-259.

A heterologous RIA for rat GH-releasing factor (rGRF) was established using synthetic rGRF-(1-43)OH for both standard reference and radioiodination with the antiserum produced against human GRF-(1-44) NH2. The regional distribution of rGRF-like immunoreactivity (LI) in rat hypothalamus was examined according to the Palkovits microdissection method and compared with that of somatostatin (SRIF)-LI. Both rGRF- and SRIF-LI contents (mean +/- SE; nanograms per mg protein) were highest in the median eminence (rGRF, 32.28 +/- 11.42; SRIF, 109.9 +/- 19.2) and next most abundant in the arcuate nucleus (rGRF, 3.50 +/- 0.47; SRIF, 12.88 +/- 0.60). Only a small amount of rGRF-LI was found in the ventromedial (1.41 +/- 0.51) and dorsomedial (1.16 +/- 0.15) nuclei and the anterior hypothalamic area (1.29 +/- 0.42), whereas rGRF-LI was not detected in the other nuclei of the hypothalamus. A considerable amount of SRIF-LI was contained in the periventricular, ventromedial, and paraventricular nuclei and the anterior hypothalamic area, in accordance with other reports. Gel filtration chromatography revealed that hypothalamic extracts contained a major peak of rGRF-LI corresponding to rGRF-(1-43)OH and two peaks of SRIF-LI equivalent to SRIF-(1-28) and SRIF-(1-14), respectively. These findings indicate that rGRF-LI is localized in the median eminence and arcuate nucleus in the rat and that rGRF-, SRIF-(1-28)-, and SRIF-(1-14)-LI are present in a 1:2.10:6.29 ratio on a molar basis.