GASTRIN RELEASING PEPTIDE, HUMAN manufacturers
|
| Product Name: | GASTRIN RELEASING PEPTIDE, HUMAN | | Synonyms: | GRP (HUMAN);GRP;H-VAL-PRO-LEU-PRO-ALA-GLY-GLY-GLY-THR-VAL-LEU-THR-LYS-MET-TYR-PRO-ARG-GLY-ASN-HIS-TRP-ALA-VAL-GLY-HIS-LEU-MET-NH2;GASTRIN RELEASING AGENT, HUMAN;GASTRIN RELEASING PEPTIDE;GASTRIN RELEASING PEPTIDE, HUMAN;VAL-PRO-LEU-PRO-ALA-GLY-GLY-GLY-THR-VAL-LEU-THR-LYS-MET-TYR-PRO-ARG-GLY-ASN-HIS-TRP-ALA-VAL-GLY-HIS-LEU-MET-NH2;VPLPAGGGTVLTKMYPRGNHWAVGHLM-NH2 | | CAS: | 93755-85-2 | | MF: | C130H204N38O31S2 | | MW: | 2859.38 | | EINECS: | | | Product Categories: | Neuromedins and related;Peptide | | Mol File: | 93755-85-2.mol |  |
| | GASTRIN RELEASING PEPTIDE, HUMAN Chemical Properties |
| density | 1.46±0.1 g/cm3(Predicted) | | storage temp. | −20°C | | form | Powder | | Water Solubility | Soluble to 1 mg/ml in water | | Sequence | H-Val-Pro-Leu-Pro-Ala-Gly-Gly-Gly-Thr-Val-Leu-Thr-Lys-Met-Tyr-Pro-Arg-Gly-Asn-His-Trp-Ala-Val-Gly-His-Leu-Met-NH2 |
| | GASTRIN RELEASING PEPTIDE, HUMAN Usage And Synthesis |
| Discovery | First isolated from the porcine stomach and named
gastrin-releasing peptide (GRP),1 GRP was originally
believed to be a mammalian counterpart of the amphibian peptide, bombesin. Its structure has been determined
in many mammals, including pigs, rats, mice, guinea
pigs, dogs, and humans. In addition, GRP18–27, a possible
fragment of mature GRP, was later isolated from the porcine spinal cord and originally called neuromedin C,2
although a more appropriate name is either GRP-10 or
GRP18–27. GRP orthologs have been identified in birds,
reptiles, amphibians, and teleost fish. On
the other hand, it is reported that frogs have both GRP
and bombesin, which are genetically distinct peptides,
suggesting that GRP is not mammalian bombesin.
 | | Structure | The human GRP precursor consists of 148 aa residues
(rat, 147 aa). A predicted preproGRP translation product
consists of a signal peptide, GRP1–27, and a C-terminal extended peptide termed proGRP31–125. Most GRP peptides have a common sequence motif,
GXHWAVGHLM amide (X=N or S), at their
C-terminus. Although the N-terminal
sequences are less conserved across vertebrate species,
many identified GRP peptides in mammals consist of
27 aa residues, excluding rats and mice (29 aa). In nonmammals, the amphibian GRP peptide consists of 29 aa
residues, the reptile peptide of 28 aa residues, and the
avian peptide of 27 aa residues while the teleost peptide
appears to be shorter (24–25 aa residues).
 | | Gene, mRNA, and precursor | The human GRP gene is located on chromosome
18 (18q21.32), and consists of three exons (mRNA, 850
bp long ) . Its mRNA produces a 125-aa preproGRP precursor protein. In chickens, the grp gene is
located on chromosome Z. In Xenopus, the grp gene is predicted to be located on chromosome 1. In zebrafish, the
grp gene is predicted to be located on chromosome
21 (CH211-233A1). GRP mRNA is produced in the CNS, stomach, intestine, pancreas, and lung in humans as well as other mammals. The expression of GRP mRNA is detected in the
limbic system, including the amygdala as well as the
hippocampus,8 and an overexpression in patients suffering from small cell lung cancer has been reported. | | Synthesis and release | In the CNS, bombesin or GRP immunoreactivity was
detected in approximately 5% of dorsal root ganglion
neurons and approximately 10% of trigeminal ganglion
neurons. In the brain, abundant GRP immunoreactivity
was observed in the cerebral cortex, hypothalamus, and
medulla oblongata. In the gastrointestinal tract, abundant
GRP-immunoreactive fibers were observed in the stomach, suggesting gastrin release, and the small intestine,
colon, and pancreas. In addition, the overexpression of
GRP has been demonstrated at both the mRNA and protein levels in various types of tumors, including lung,
prostate, breast, stomach, pancreas, and colon. | | Receptors | GRPR is a GPCR superfamily with a seventransmembrane domain. GRPR is coupled to the Gq
protein, and GRPR activation leads to an increase in intracellular Ca2+ and stimulation of the PLC/PKC and ERK/
MAPK pathways. In mammals, bombesin-like peptides
act on a family of at least three GPCRs: the GRP-preferring receptor (GRPR), the neuromedin
B-preferring receptor (NMBR), and the bombesin receptor subtype-3 (BRS-3), which is considered an orphan
receptor at present. Human GRP binds GRPR (BB2 receptor) with a higher binding affinity (Ki of 1.8 - 0.4 nM)
than that of NMBR (BB1 receptor) (Ki of 15 - 0.4 nM). | | Agonists and Antagonists | A fragment of the C-terminal of human GRP, GRP18–27
(GRP-10), is reported to be a selective and potent agonist
for GRPR. The central administration of GRP-10
induces many physiological responses, similar to that
with mature GRP. RC3095 has been reported as a selective and potent
antagonist of GRPR. The central administration of
RC-3095 attenuates many physiological responses. | | Biological functions | GRP functions via GRPR, which is highly expressed in
the pancreas, and is also expressed in the stomach, adrenal cortex, and brain. Considerable evidence indicates
that GRP plays a role in many physiological processes,
including food intake, male sexual functions,circadian rhythms, sigh control, and fear-memory consolidation in the mammalian CNS. In addition, the itch
sensation is a major biological function of GRP in mammals. In chicks, GRP functions as an anorexigenic factor
in the brain. | | Clinical implications | GRP and GRPR often excessively express in endocrinerelated cancer cells such as small cell lung cancer, prostate
cancer, and gastrointestinal tract cancer. ProGRP is
known to be a specific tumor marker for the small cell
lung cancer because the half-life of proGRP in the circulation is much longer than that of GRP. GRPR is also
important in prostate cancer growth and progression in
an androgen-dependent manner. | | Description | Gut-brain peptides are widely conserved in vertebrates,
GRP is a neuropeptide that modulates the autonomic system.
It is an anorexigenic factor in the brain, regulates male sexual
function at the spinal cord level, conveys the itch sensation,
and is also involved in many autonomic regulations in the
brain. The expression of GRP is also a specific tumor marker
for small cell lung cancer. It has the GXHWAVGHLM
amide (X=N or S) sequence at its C-terminus. | | Uses | GRP (gastrin releasing peptide) has been used for absorption/neutralization of anti-GRP antibody prior to the tyramide signal amplification (TSA) procedure. | | General Description | GRP (gastrin releasing peptide) is the mammalian homolog of bombesin (BBS) and functions as a mitogen for multiple cancers, such as neuroblastoma. It is a ligand for GRPR (GRP receptor) and is expressed in a subtype of peptidergic dorsal root ganglion neurons. | | Biochem/physiol Actions | GRP (gastrin releasing peptide) functions as an autocrine growth factor for nueroblastoma. It facilitates cell survival in PI3K/AKT (phosphatidylinositol-3-kinase/ v-Akt murine thymoma viral oncogene)-mediated manner and cell proliferation and angiogenesis in neuroblastoma. This peptide is involved in the release of gastrin and the control of gastric acid secretion and motor function. In patients with atopic dermatitis, the serum levels of this peptide are linked with pruritus. | | Clinical Use | GRP mRNA is overexpressed in patients suffering
from small cell lung cancer. Clinically, therefore, a higher
level of circulating proGRP31–125 is a specific tumor
marker for small cell lung cancer (higher than ~81.0 pg/mL in the plasma). In addition, intravenous
infusions of GRP decrease spontaneous food intake in
healthy men, suggesting GRP acts as a satiety signal in
humans. GRP has not yet been used much clinically
as a therapeutic agent. | | storage | Store at -20°C |
| | GASTRIN RELEASING PEPTIDE, HUMAN Preparation Products And Raw materials |
|