GRP (porcine)

Endogenous GRP receptor agonist CAS# 74815-57-9

GRP (porcine)

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Chemical structure

GRP (porcine)

3D structure

Chemical Properties of GRP (porcine)

Cas No. 74815-57-9 SDF Download SDF
PubChem ID 71308506 Appearance Powder
Formula C126H198N38O31S2 M.Wt 2805.31
Type of Compound N/A Storage Desiccate at -20°C
Synonyms Gastrin-releasing peptide (porcine)
Solubility Soluble to 1 mg/ml in water
Sequence APVSVGGGTVLAKMYPRGNHWAVGHLM

(Modifications: Met-27 = C-terminal amide)

SMILES CC(C)CC(C(=O)NC(CCSC)C(=O)N)NC(=O)C(CC1=CNC=N1)NC(=O)CNC(=O)C(C(C)C)NC(=O)C(C)NC(=O)C(CC2=CNC3=CC=CC=C32)NC(=O)C(CC4=CNC=N4)NC(=O)C(CC(=O)N)NC(=O)CNC(=O)C(CCCNC(=N)N)NC(=O)C5CCCN5C(=O)C(CC6=CC=C(C=C6)O)NC(=O)C(CCSC)NC(=O)C(CCCCN)NC(=O)C(C)NC(=O)C(CC(C)C)NC(=O)C(C(C)C)NC(=O)C(C(C)O)NC(=O)CNC(=O)CNC(=O)CNC(=O)C(C(C)C)NC(=O)C(CO)NC(=O)C(C(C)C)NC(=O)C7CCCN7C(=O)C(C)N
Standard InChIKey GLCDCQPXUJKYKQ-GZDVRPNBSA-N
Standard InChI InChI=1S/C126H198N38O31S2/c1-62(2)44-83(155-121(191)102(67(11)12)162-123(193)103(71(16)166)158-98(173)56-138-94(169)54-137-95(170)55-140-120(190)100(65(7)8)160-116(186)90(59-165)157-122(192)101(66(9)10)161-118(188)92-31-24-40-163(92)124(194)68(13)128)110(180)144-69(14)105(175)149-81(28-21-22-38-127)108(178)150-82(37-43-197-18)109(179)156-89(46-72-32-34-76(167)35-33-72)125(195)164-41-25-30-91(164)117(187)151-80(29-23-39-135-126(131)132)107(177)139-57-96(171)147-88(50-93(129)168)115(185)154-87(49-75-53-134-61-143-75)114(184)153-85(47-73-51-136-78-27-20-19-26-77(73)78)111(181)145-70(15)106(176)159-99(64(5)6)119(189)141-58-97(172)146-86(48-74-52-133-60-142-74)113(183)152-84(45-63(3)4)112(182)148-79(104(130)174)36-42-196-17/h19-20,26-27,32-35,51-53,60-71,79-92,99-103,136,165-167H,21-25,28-31,36-50,54-59,127-128H2,1-18H3,(H2,129,168)(H2,130,174)(H,133,142)(H,134,143)(H,137,170)(H,138,169)(H,139,177)(H,140,190)(H,141,189)(H,144,180)(H,145,181)(H,146,172)(H,147,171)(H,148,182)(H,149,175)(H,150,178)(H,151,187)(H,152,183)(H,153,184)(H,154,185)(H,155,191)(H,156,179)(H,157,192)(H,158,173)(H,159,176)(H,160,186)(H,161,188)(H,162,193)(H4,131,132,135)/t68-,69-,70-,71+,79-,80-,81-,82-,83-,84-,85-,86-,87-,88-,89-,90-,91-,92-,99-,100-,101-,102-,103-/m0/s1
General tips For obtaining a higher solubility , please warm the tube at 37 ℃ and shake it in the ultrasonic bath for a while.Stock solution can be stored below -20℃ for several months.
We recommend that you prepare and use the solution on the same day. However, if the test schedule requires, the stock solutions can be prepared in advance, and the stock solution must be sealed and stored below -20℃. In general, the stock solution can be kept for several months.
Before use, we recommend that you leave the vial at room temperature for at least an hour before opening it.
About Packaging 1. The packaging of the product may be reversed during transportation, cause the high purity compounds to adhere to the neck or cap of the vial.Take the vail out of its packaging and shake gently until the compounds fall to the bottom of the vial.
2. For liquid products, please centrifuge at 500xg to gather the liquid to the bottom of the vial.
3. Try to avoid loss or contamination during the experiment.
Shipping Condition Packaging according to customer requirements(5mg, 10mg, 20mg and more). Ship via FedEx, DHL, UPS, EMS or other couriers with RT, or blue ice upon request.

Biological Activity of GRP (porcine)

DescriptionMammalian bombesin-like peptide neurotransmitter that is an agonist for the gastrin-releasing peptide receptor (GRPR). GRP has been reported to activate GABAergic interneurons in the amygdala leading to increased GABA release and fear suppression in mice in vivo. Also involved in mitogenesis, and GI tract and appetite regulation.

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References on GRP (porcine)

A qualitative comparison of canine plasma gastroenteropancreatic hormone response to bombesin and the porcine gastrin-releasing peptide (GRP).[Pubmed:7029673]

Regul Pept. 1981 Sep;2(5):293-304.

The effect on plasma gastroenteropancreatic hormone levels on infusing the porcine gastrin-releasing peptide and bombesin into dogs demonstrated no qualitative difference in the spectrum of activity of the two peptides. Sustained elevation in plasma immunoreactive gastrin, pancreatic polypeptide, enteroglucagon, gastric inhibitory polypeptide, pancreatic glucagon and transient elevations in plasma insulin were seen during infusions of both peptides. The similar spectrum of activities and the structural homology between the two peptides suggests that the porcine gastrin releasing peptide is the porcine counterpart of the amphibian peptide bombesin.

Effects of porcine gastrin releasing peptide (GRP) on canine antral motility and gastrin release in vivo.[Pubmed:6482663]

Life Sci. 1984 Sep 24;35(13):1415-22.

The effect of GRP on the in vivo canine antrum was investigated. GRP caused a dose-dependent increase in antral gastrin output which was not significantly altered by administration of tetrodotoxin. The higher doses of GRP administered also caused excitation of antral motility which was abolished by tetrodotoxin, a finding in contrast to previous in vitro results demonstrating bombesin-induced antral smooth muscle contraction to be tetrodotoxin-resistant. These data suggest that in the in vivo canine model GRP causes antral gastrin release via non-neurally mediated mechanisms (probably by acting directly on the G-cell) and excites antral motility via neurally-mediated mechanisms.

Identification, characterization and release of GRP gene-associated peptides from the normal porcine and human gastro-intestinal tract.[Pubmed:1924888]

Regul Pept. 1991 Jul 9;34(3):197-209.

Using a radioimmunoassay directed towards human proGRP (42-53) on acetic acid extracts, immunoreactivity was measured throughout the porcine GI-tract in concentrations that were parallel to those of GRP (gastrin-releasing peptide or 'mammalian bombesin'). Gel filtration and HPLC studies of human and porcine tissue extracts revealed that the immunoreactivity was mainly due to a peptide with a molecular size of 8-9 kDa. The peptide did not contain the GRP sequence, making it a major fragment of the GRP C-flanking part of proGRP. Furthermore, a peptide of similar size with proGRP (42-53) immunoreactivity was released from isolated, perfused preparations of porcine antral and non-antral stomach and pancreas in parallel with GRP in response to electrical stimulation of the vagus nerves. Our results suggest that a processing of preproGRP occurs in normal, adult human and porcine tissues, that is similar to that previously demonstrated in small cell lung carcinomas and human fetal lungs. The finding that the immunoreactive proGRP fragment is released from the tissues upon appropriate stimulation raises the question of a possible physiological role for proGRP products other than GRP.

Dose-response comparisons of canine plasma gastroenteropancreatic hormone responses to bombesin and the porcine gastrin-releasing peptide (GRP).[Pubmed:6338565]

Regul Pept. 1983 Jan;5(2):125-37.

This study compares the potencies of the porcine gastrin-releasing peptide (pGRP) and bombesin, in causing elevations of canine plasma gastroenteropancreatic (GEP) levels. In the dose range 0-600 pmol . kg-1 . h-1, infusion of both peptides resulted in obvious dose-related elevations of plasma levels of gastrin, pancreatic polypeptide, enteroglucagon, immunoreactive pancreatic glucagon, and insulin. In this dose range, no significant difference in potency between the two peptides in elevating plasma levels of the above hormones was observed. The results of this study, demonstrating equimolar potency of pGRP and bombesin, are in contrast to previous studies reporting that pGRP was less potent than bombesin in causing certain bioactivities in the rat following intracranial administration of the two peptides.

Identification of a signaling network in lateral nucleus of amygdala important for inhibiting memory specifically related to learned fear.[Pubmed:12526815]

Cell. 2002 Dec 13;111(6):905-18.

We identified the Grp gene, encoding gastrin-releasing peptide, as being highly expressed both in the lateral nucleus of the amygdala, the nucleus where associations for Pavlovian learned fear are formed, and in the regions that convey fearful auditory information to the lateral nucleus. Moreover, we found that GRP receptor (GRPR) is expressed in GABAergic interneurons of the lateral nucleus. GRP excites these interneurons and increases their inhibition of principal neurons. GRPR-deficient mice showed decreased inhibition of principal neurons by the interneurons, enhanced long-term potentiation (LTP), and greater and more persistent long-term fear memory. By contrast, these mice performed normally in hippocampus-dependent Morris maze. These experiments provide genetic evidence that GRP and its neural circuitry operate as a negative feedback regulating fear and establish a causal relationship between Grpr gene expression, LTP, and amygdala-dependent memory for fear.

Bombesin receptors in the brain.[Pubmed:8602736]

Ann N Y Acad Sci. 1996 Mar 22;780:223-43.

We have shown that in the central nervous system BN receptors are closely associated with 5-HT systems. On a subpopulation of dorsal raphe neurons, NMB receptors are able to depolarize cells by reducing gK+. In one of the target regions of the dorsal raphe 5-HT neurons, the SCN, we have also shown that neurons are excited by BN-related peptides. In the SCN, the GRP receptors excite neurons by two different mechanisms: closure of gK+ and opening of an unidentified cation conductance. Expression of human BN receptors from the brain in CHO cells or Xenopus oocytes shows a very similar pharmacological profile to that seen in the rat brain slice preparations. In the CHO cell line, following BN receptor activation, a major second-messenger path involves hydrolysis of PIP2 by phospholipases to yield IP3, which releases Ca2+ from intracellular stores. In the oocyte expression system, a similar second messenger pathway is clearly apparent, and Ca2+-sensitive gCl- represents the last phase in a cascade of events. The final phase of the mechanism of action in the artificial systems does not involve gK+, suggesting a different second messenger cascade to that in neurons. However, the involvement of phospholipases and their phospholipid products have not been excluded in neurons.

Gastrin-releasing peptide is a transmitter mediating porcine gallbladder contraction.[Pubmed:1708207]

Am J Physiol. 1991 Apr;260(4 Pt 1):G577-85.

We studied the role of gastrin-releasing peptide (GRP) for porcine gallbladder motility. Immunohistochemistry visualized nerve fibers containing GRP-like immunoreactivity in muscularis. GRP concentration dependently stimulated contractions of muscularis strips (ED50, 2.9 nM). Neuromedin B was less potent (ED50, 0.1 microM), suggesting existence of GRP-preferring receptors. GRP-induced contractions were unaffected by muscarinic antagonism (1 microM atropine), axonal blockade (1 microM tetrodotoxin), cholecystokinin (CCK) receptor antagonism (10 microM MK-329), or substance P desensitization (1 microM), supporting the existence of myogenic GRP receptors. The bombesin (BN) analogue D-Phe6-BN-(6-13)propylamide (PA) stimulated contractions (ED50, 3.3 nM) with low efficacy (29% of that of GRP). D-Phe6-BN-(6-13)PA (1 microM) shifted GRP concentration-response curves one log to the right. D-Phe6-BN-(6-13)PA interacted specifically with GRP receptors; while abolishing responses to GRP (1 nM), responses to substance P (0.1 microM) and CCK-8 (1 nM) were unchanged. Electrical stimulation (10 Hz, 0.5 ms, 10 V) caused a rapid onset-slow offset, tetrodotoxin-sensitive excitation. Atropine reduced the amplitude to 58% and caused a delayed, slow onset-slow decline response. D-Phe6-BN-(6-13)PA reduced the amplitude to 59% and caused a very rapid onset-rapid decline response. Atropine plus D-Phe6-BN-(6-13)PA abolished responses to nerve stimulation. Nerve stimulation caused significant release of GRP-like immunoreactivity. Thus two neural inputs were defined: a cholinergic rapid onset-rapid offset excitation and a delayed, slow onset-slow offset excitation caused by release and subsequent binding of GRP to GRP-preferring receptors.

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