GHRP-6 (acetate)
(Synonyms: 生长激素释放肽-6) 目录号 : GC45459
A growth hormone secretagogue and GHS-R agonist
Cas No.:145177-42-0
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
GHRP-6 is a synthetic growth hormone (GH) secretagogue and an agonist of the GH secretagogue receptor (GHS-R), which is also known as the ghrelin receptor.1,2,3,4 It inhibits binding of the GHS-R agonist MK-0677 to COS-7 cell membranes expressing human GHS-R type Ia (Ki = 1.9 nM) and binding of ghrelin to COS-7 cells expressing human GHS-R (Kd = 260 nM).2,3 GHRP-6 stimulates intracellular calcium mobilization in BHK cells expressing the human receptor (EC50 = 4.5 nM) and inositol phosphate production in COS-7 cells expressing the human receptor (EC50 = 0.83 nM).3 It also acts as a negative allosteric modulator of ghrelin signaling. GHRP-6 (0.03 μg/ml) induces release of GH, but not thyroid-stimulating hormone (TSH), luteinizing hormone (LH), or follicle-stimulating hormone (FSH), in isolated rat pituitary gland.1 It increases levels of GH, but not TSH, LH, FSH, or prolactin, in rat blood when administered subcutaneously at a dose of 50 μg. GHRP-6 increases food intake in rats when administered intracerebroventricularly at 0.3, 1, and 3 nmol.4
References
1. Bowers, C.Y., Momany, F.A., Reynolds, G.A., et al. On the in vitro and in vivo activity of a new synthetic hexapeptide that acts on the pituitary to specifically release growth hormone. Endocrinology 114(5), 1537-1545 (1984).
2. Howard, A.D., Feighner, S.D., Cully, D.F., et al. A receptor in pituitary and hypothalamus that functions in growth hormone release. Science 273(5277), 974-977 (1996).
3. Holst, B., Brandt, E., Bach, A., et al. Nonpeptide and peptide growth hormone secretagogues act both as ghrelin receptor agonist and as positive or negative allosteric modulators of ghrelin signaling. Mol. Endocrinol. 19(9), 2400-2411 (2005).
4. Wren, A.M., Small, C.J., Ward, H.L., et al. The novel hypothalamic peptide ghrelin stimulates food intake and growth hormone secretion. Endocrinology 141(11), 4325-4328 (2000).
| Cas No. | 145177-42-0 | SDF | |
| 别名 | 生长激素释放肽-6 | ||
| Canonical SMILES | O=C(N[C@H](CC1=CC=CC=C1)C(N[C@H](C(N)=O)CCCCN)=O)[C@@H](NC([C@H](C)NC([C@H](NC([C@H](CC2=CN=CN2)N)=O)CC3=CNC4=C3C=CC=C4)=O)=O)CC5=CNC6=C5C=CC=C6.CC(O)=O.CC(O)=O.CC(O)=O | ||
| 分子式 | C46H56N12O6.3C2H4O2 | 分子量 | 1053.2 |
| 溶解度 | DMF: 30 mg/ml,DMSO: 30 mg/ml,PBS (pH 7.2): 10 mg/ml | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 0.9495 mL | 4.7474 mL | 9.4949 mL |
| 5 mM | 0.1899 mL | 0.9495 mL | 1.899 mL |
| 10 mM | 0.0949 mL | 0.4747 mL | 0.9495 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Structure-activity relationships of GHRP-6 azapeptide ligands of the CD36 scavenger receptor by solid-phase submonomer azapeptide synthesis
J Am Chem Soc 2011 Aug 17;133(32):12493-506.PMID:21692501DOI:10.1021/ja203007u.
The cluster of differentiation 36 (CD36) class B scavenger receptor binds a variety of biologically endogenous ligands in addition to synthetic peptides (i.e., growth hormone-releasing peptides, GHRPs), which modulate biological function related to anti-angiogenic and anti-atherosclerotic activities. Affinity labeling had previously shown that GHRP-6 analogues such as hexarelin, [2-Me-W(2)]GHRP-6 (1), bind to the lysine-rich domain of the CD36 receptor. Moreover, the azapeptide analogue [aza-F(4)]GHRP-6, 2, exhibited a characteristic β-turn conformation as described by CD and NMR spectroscopy and a slightly higher CD36 binding affinity relative to hexarelin (1.34 and 2.37 μM, respectively), suggesting receptor binding was mediated by the conformation and the aromatic residues of these peptide sequences. Ligand-receptor binding interactions were thus explored using azapeptides to examine influences of side-chain diversity and backbone conformation. In particular, considering that aromatic cation interactions may contribute to binding affinity, we have explored the potential of introducing salt bridges to furnish GHRP-6 azapeptide ligands of the CD36 receptor. Fifteen aza-glutamic acid analogues related to 2 were prepared by submonomer solid-phase synthesis. The azapeptide side chains were installed by novel approaches featuring alkylation of resin-bound semicarbazone with Michael acceptors and activated allylic acetates in the presence of phosphazene base (BTPP). Moreover, certain Michael adducts underwent intramolecular cyclization during semicarbazone deprotection, leading to novel pyrrazoline and aza-pyroglutamate N-terminal residues. Structural studies indicated that contingent on sequence the [aza-Glu]GHRP-6 analogues exhibited CD spectra characteristic of random coil, polyproline type II and β-turn secondary structures in aqueous media. In covalent competition binding studies with the GHRP-6 prototype hexarelin bearing a radiotracer, certain [aza-Glu]GHRP-6 azapeptides retained relatively high (2-27 μM) affinity for the CD36 scavenger receptor.
The effect of GHRP-6 on the intracellular Na+ concentration of rat pituitary cells in primary culture
J Neuroendocrinol 1999 Oct;11(10):795-800.PMID:10520128DOI:10.1046/j.1365-2826.1999.00394.x.
The objective of the present study was to further investigate the ionic mechanism of the action of GHRP-6 on male rat pituitary cells in culture. A synthetic hexapeptide, GHRP-6 stimulates the secretion of growth hormone both in vivo and in vitro. It is generally accepted that Ca2+ and protein kinase C but not cAMP are involved in the signal transduction pathway of the action of GHRP-6. Ca2+-influx through voltage-gated Ca2+ channels and mobilization of internal stored Ca2+ are thought to be responsible for an increase in cytosolic Ca2+ concentration. For activation of the voltage-gated Ca2+ channels, however, it is not determined whether the membrane Na+ permeability plays a role. To answer this question, we measured intracellular Na+ concentration of the pituitary cells with ion imaging technique. We found that GHRP-6 increased [Na+]i; the Na+ response depended on the presence of extracellular Na+ and was blocked by Gd3+, known as a blocker of nonselective cation channels but not by tetrodotoxin, a blocker of the voltage-gated Na+ channel; thapsigargin, an inhibitor of endoplasmic reticulum Ca2+ ATPase, had no effect on the response; Ca2+ chelating agent, BAPTA had no inhibitory effect on the response; ouabain, an inhibitor of Na+-K+ ATPase, did not block the rise in [Na+]i induced by GHRP-6; somatostatin, which hyperpolarizes the cells by activating K+ channels, suppressed the response. These data clearly showed that GHRP-6 increased [Na+]i in the rat pituitary cells including somatotrophs. The rise in [Na+]i is likely to be due to an increase in the membrane Na+ permeability which should depolarize the cells, thereby activating the voltage-gated Ca2+ channels. This process leads to an influx of Ca2+ and subsequent increase in [Ca2+]i which results in an exocytotic release of GH.
GHRP-6 induces a biphasic calcium response in rat pituitary somatotrophs
Cell Calcium 1994 Mar;15(3):247-58.PMID:8194104DOI:10.1016/0143-4160(94)90064-7.
The mechanism of action of His-D-Trp-Ala-Trp-D-Phe-Lys-NH2 (GHRP-6), a synthetic peptide which specifically induces the secretion of growth hormone (GH) in rat somatotrophs, is still poorly understood. We have studied the effects of GHRP-6 on the cytosolic free calcium concentration ([Ca2+]i) of somatotrophs in primary culture. [Ca2+]i was monitored in individual somatotrophs by dual emission microspectrofluorimetry, using Indo-1 as the intracellular fluorescent Ca2+ probe. A short application of GHRP-6 (10(-5) M, 10 s) induced a biphasic Ca2+ response in most cells (44%), which consisted in a rapid and large rise in [Ca2+]i followed by sustained oscillations. This response is dose dependent in a range of concentrations from 10(-10) to 10(-5) M. The first phase of the GHRP-6 response persisted in the absence of Ca2+ in the extracellular medium, whereas the second phase was inhibited. The application of Ca2+ channel blockers like cadmium chloride (200 microM) or PN-200-110 (200 nM) also prevented the second phase. Conversely, when the cells were pretreated with thapsigargin (TG) (100 nM), the first phase of the GHRP-6 Ca2+ response was abolished, whereas the second phase alone was preserved. When the cells were depleted in PKC by incubation with 10(-6) M PMA for 24 h, the second phase of the GHRP-6 response was inhibited, and only the first phase was maintained. These results were corroborated by using phloretin, a PKC inhibitor. These data show that GHRP-6 induces a biphasic elevation of the [Ca2+]i in rat somatotrophs. The first phase is probably due to mobilization of the intracellular Ca2+ stores, whereas the second phase is a PKC-dependent process.
Antagonization of Ghrelin Suppresses Muscle Protein Deposition by Altering Gut Microbiota and Serum Amino Acid Composition in a Pig Model
Biology (Basel) 2022 May 30;11(6):840.PMID:35741361DOI:10.3390/biology11060840.
Ghrelin is an appetite-stimulating hormone that can increase food intake and has been reported to prevent muscle loss; however, the mechanism is not yet fully understood. In this study, [D-Lys3]-GHRP-6 (GHRP) was used to investigate the effects of the antagonization of ghrelin on muscle protein deposition, eating patterns and gut microbiota in a pig model. We found that the growth performance and muscle fiber cross-sectional area of pigs treated with GHRP were significantly reduced compared with the control (CON) group. Moreover, the levels of serum isoleucine, methionine, arginine and tyrosine in the GHRP group were lower than that of the CON group. The abundance of acetate-producing bacteria (Oscillospiraceae UCG-005, Parabacteroides and Oscillospiraceae NK4A214 group) and acetate concentration in the colons of pigs treated with GHRP were significantly reduced. In addition, the injection of GHRP down-regulated the mRNA expression of MCT-1 and mTOR, and it up-regulated the mRNA expression of HDAC1, FOXO1 and Beclin-1. In summary, the antagonization of ghrelin reduced the concentration of important signal molecules (Arg, Met and Ile) that activate the mTOR pathway, concurrently reduce the concentration of HDAC inhibitors (acetate), promote autophagy and finally reduce protein deposition in muscles.
Relationship between GHRP-6 and TPA in the regulation of growth hormone secretion by human pituitary somatotrophinomas
J Tongji Med Univ 1997;17(3):132-5.PMID:9812762DOI:10.1007/BF02888286.
Growth hormone releasing peptide (GHRP-6) is a synthetic hexapeptide which specifically stimulates secretion of growth hormone (GH) by pituitary somatotrophs. Phorbel ester, 1, 2 tetradecanoylphorbol 13 acetate (TPA) can also stimulate releasing of GH. The precise intracellular mechanism has not been entirely deciphered. We used cell cultures of human pituitary somatotrophinomas to investigate the relation between GHRP-6 and TPA on membrane phosphatidylinositol (PI) turnover and GH secretion. The results showed that the working mechanisms of GHRP-6 and TPA are not identical, although they all can stimulate GH secretion in human pituitary somatotrophinomas. This indicates that PI-PKC signal transduction system may play a crucial role in the regulation of GH secretion.