Mas7
(Synonyms: Mastoparan 7) 目录号 : GC36545
Mas7是mastoparan的结构类似物，是异源三聚体 Gi 蛋白及其下游效应物的活化剂。
Cas No.:145854-59-7
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
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- Purity: >98.00%
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Cell experiment: | Hippocampal neurons cultured in round 35?mm coverslips at a density of 160,000 cells/coverslip are transfected with EGFP at 11 DIV. Then, at 14 DIV the neurons are placed in the imaging chamber in an isotonic solution. The EGFP-positive neurons are imaged with microscope every 5?min for 45?min after the treatment with 1?μM Mas-7. The images are processed and analyzed using ImageJ software[1]. |
References: [1]. Bavec A, et al. Novel features of amphiphilic peptide Mas7 in signalling via heterotrimeric G-proteins. J Pept Sci. 2004 Nov;10(11):691-9. | |
Mas7, a structural analogue of mastoparan, is an activator of heterotrimeric Gi proteins and its downstream effectors.
Mas7 produces several biological effects in different cell types. The effect of Mas7 on endogenous mono-ADP-ribosyltransferase activity is in the micromolar range with a maximal activation of 205% over the basal. In pertussis treated plasma membranes, it is found that the effect of Mas7 on endogenous mono-ADP-ribosyltransferase is partially blocked, which suggests the involvement of G-proteins, such as Gi or G0[1]. Mas7 is a basic tetradecapeptide isolated from isp venom, which activates guanine nucleotide-binding regulatory proteins (G-proteins) and stimulates apoptosis. In smooth muscle cells, Mas7 leads to an increase in the perfusion pressure. Vascular contraction is induced by Mas7. The vasoconstriction triggered by mas-7 exhibited a slower increase compared to that simulated by phenylephrine or vasopressin[2]. Exposure of hippocampal neurons to a low dose of Mas-7 increases dendritic spine density and spine head width in a time-dependent manner. Additionally, Mas-7 enhances postsynaptic density protein-95 (PSD-95) clustering in neurites and activates Gαo signaling, increasing the intracellular Ca2+ concentration[3].
[1]. Bavec A, et al. Novel features of amphiphilic peptide Mas7 in signalling via heterotrimeric G-proteins. J Pept Sci. 2004 Nov;10(11):691-9. [2]. Grze•k G, et al. Direct regulation of vascular smooth muscle contraction by mastoparan-7. Biomed Rep. 2014 Jan;2(1):34-38. [3]. RamÍrez VT, et al. The Gαo Activator Mastoparan-7 Promotes Dendritic Spine Formation in Hippocampal Neurons. Neural Plast. 2016;2016:4258171.
| Cas No. | 145854-59-7 | SDF | |
| 别名 | Mastoparan 7 | ||
| 分子式 | C67H124N18O15 | 分子量 | 1421.81 |
| 溶解度 | Soluble in DMSO | 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 | 0.7033 mL | 3.5166 mL | 7.0333 mL |
| 5 mM | 0.1407 mL | 0.7033 mL | 1.4067 mL |
| 10 mM | 0.0703 mL | 0.3517 mL | 0.7033 mL |
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| 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 |
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| % DMSO % % Tween 80 % saline | ||||||||||
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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。
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Novel features of amphiphilic peptide Mas7 in signalling via heterotrimeric G-proteins
J Pept Sci 2004 Nov;10(11):691-9.PMID:15568683DOI:10.1002/psc.579.
Amphiphilic peptide Mas7, a structural analogue of mastoparan is a known activator of heterotrimeric Gi-proteins and its downstream effectors. This study investigated the functional interaction of Mas7 with a plasma membrane protein from CHO cells, the endogenous mono-ADP-ribosyltransferase. The substrate of endogenous mono-ADP-ribosyltransferase was the ADP-ribosylated protein with a molecular mass of 36 kDa, which corresponded to the beta subunit of heterotrimeric G-proteins. The effect of Mas7 on endogenous mono-ADP-ribosyltransferase activity was in the micromolar range with a maximal activation of 205% over the basal. In pertussis treated plasma membranes, it was found that the effect of Mas7 on endogenous mono-ADP-ribosyltransferase was partially blocked, which suggests the involvement of G-proteins, such as Gi or G0. In addition, an immunoassay was developed for the visualization of interaction between the a subunit and the betagamma dimer of G-protein on a Ni-NTA support. The physical interaction was tested of Mas7 with the heterotrimeric G-protein alphai2 subunit, which was overexpressed together with beta1gamma2-His6 subunits in sf9 cells. An interaction between Gi2 heterotrimer and Mas7 was not observed, which was not in accordance with previously reported results of mastoparan obtained for Gi-proteins from bovine brain. In conclusion, the signal is mediated from Mas7 to endogenous mono-ADP-ribosyltransferase via pertussis sensitive G-proteins. Furthermore, it is hypothesized that Gi2 G-proteins are not involved in the process.
Secretory vesicle swelling by atomic force microscopy
Methods Mol Biol 2006;319:317-30.PMID:16719363DOI:10.1007/978-1-59259-993-6_16.
The swelling of secretory vesicles has been implicated in exocytosis, but the underlying mechanism of vesicle swelling remained unknown. Earlier studies from our laboratory demonstrated the association of the alpha-subunit of heterotrimeric GTP-binding protein G(alphai3) with zymogen granule membrane and implicated its involvement in vesicle swelling. Mas7, an active mastoparan analog known to stimulate Gi proteins, was found to stimulate the GTPase activity of isolated zymogen granules and cause swelling. Increase in vesicle size in the presence of GTP, NaF, and Mas7 were irreversible and found to be KCl sensitive. However, Ca2+ had no effect on zymogen granule size. Taken together, these results indicated that zymogen granules, the membrane-bound secretory vesicles in exocrine pancreas, swell in response to GTP mediated by a G(alphai3) protein. Subsequently, our studies demonstrated that the water channel aquaporin-1 (AQP1) is also present at the zymogen granule membrane and participates in rapid GTP-induced and G(alphai3)-mediated vesicular water gating and swelling. Isolated zymogen granules exhibit low basal water permeability. However, exposure of granules to GTP results in a marked potentiation of water entry. Treatment of zymogen granules with the known water channel inhibitor Hg2+ is accompanied by a reversible loss in both the basal and GTP-stimulable water entry and vesicle swelling. Introduction of AQP1-specific antibody raised against the carboxy-terminal domain of AQP1 blocked GTP-stimulable swelling of vesicles. Our results demonstrate that AQPI associated at the zymogen granule membrane is involved in basal GTP-induced and G(alphai3)-mediated rapid gating of water into zymogen granules of the exocrine pancreas.
Pharmacological evidence that multiple phospholipid signaling pathways link Rhizobium nodulation factor perception in Medicago truncatula root hairs to intracellular responses, including Ca2+ spiking and specific ENOD gene expression
Plant Physiol 2004 Nov;136(3):3582-93.PMID:15489277DOI:10.1104/pp.104.051110.
Rhizobium nodulation (Nod) factors are specific lipochito-oligosaccharide signals essential for initiating in root hairs of the host legume developmental responses that are required for controlled entry of the microsymbiont. In this article, we focus on the Nod factor signal transduction pathway leading to specific and cell autonomous gene activation in Medicago truncatula cv Jemalong in a study making use of the Nod factor-inducible MtENOD11 gene. First, we show that pharmacological antagonists that interfere with intracellular ion channel and Ca2+ pump activities are efficient blockers of Nod factor-elicited pMtENOD11-beta-glucuronidase (GUS) expression in root hairs of transgenic M. truncatula. These results indicate that intracellular Ca2+ release and recycling activities, essential for Ca2+ spiking, are also required for specific gene activation. Second, pharmacological effectors that inhibit phospholipase D and phosphoinositide-dependent phospholipase C activities are also able to block pMtENOD11-GUS activation, thus underlining a central role for multiple phospholipid signaling pathways in Nod factor signal transduction. Finally, pMtENOD11-GUS was introduced into all three Nod-/Myc- dmi M. truncatula mutant backgrounds, and gene expression was evaluated in response to the mastoparan peptide agonist Mas7. We found that Mas7 elicits root hair MtENOD11 expression in dmi1 and dmi2 mutants, but not in the dmi3 mutant, suggesting that the agonist acts downstream of DMI1/DMI2 and upstream of DMI3. In light of these results and the recently discovered identities of the DMI gene products, we propose an integrated cellular model for Nod factor signaling in legume root hairs in which phospholipids play a key role in linking the Nod factor perception apparatus to downstream components such as Ca2+ spiking and ENOD gene expression.
Heterotrimeric G proteins are implicated in gibberellin induction of a-amylase gene expression in wild oat aleurone
Plant Cell 1998 Feb;10(2):245-54.PMID:9490747DOI:10.1105/tpc.10.2.245.
The role of heterotrimeric G proteins in gibberellin (GA) induction of a-amylase gene expression was examined in wild oat aleurone protoplasts. Mas7, a cationic amphiphilic tetradecapeptide that stimulates GDP/GTP exchange by heterotrimeric G proteins, specifically induced alpha-amylase gene expression and enzyme secretion in a very similar manner to GA1. In addition, Mas7 stimulated expression of an alpha-Amy2/54:GUS promoter and reporter construct in transformed protoplasts. Both Mas7 and GA1 induction of alpha-amylase mRNA were insensitive to pertussis toxin. Hydrolysis-resistant nucleotides were introduced into aleurone protoplasts during transfection with reporter gene constructs. GDP-beta-S, which inhibits GDP/GTP exchange by heterotrimeric G proteins, completely prevented GA1 induction of alpha-Amy2/54:GUS expression, whereas GTP-gamma-S, which activates heterotrimeric G proteins, stimulated expression very slightly. Novel cDNA sequences from Galpha and Gbeta subunits were cloned from wild oat aleurone cells. By using RNA gel blot analysis, we found that the transcripts were expressed at a low level. Heterotrimeric G proteins have been implicated in several events during plant growth and development, and these data suggest that they may be involved in GA regulation of alpha-amylase gene expression in aleurone.
Gi regulation of secretory vesicle swelling examined by atomic force microscopy
Proc Natl Acad Sci U S A 1997 Nov 25;94(24):13317-22.PMID:9371843DOI:10.1073/pnas.94.24.13317.
In the last decade, several monomeric and heterotrimeric guanine nucleotide binding proteins have been identified to associate with secretory vesicles and to be implicated in exocytosis. Vesicle volume also has been proposed to play a regulatory role in secretory vesicle fusion at the plasma membrane. However, the molecular mechanism of function of the guanine nucleotide binding proteins and of the regulation of secretory vesicle volume in the exocytotic process remains unclear. In this study, we report association of the secretory vesicle membrane with the alpha subunit of a heterotrimeric GTP binding protein G(alpha i3) and implicate its involvement in vesicle swelling. Using an atomic force microscope in combination with confocal microscopy, we were able to study the dynamics of isolated zymogen granules, the secretory vesicles in exocrine pancreas. Exposure of zymogen granules to GTP resulted in a 15-25% increase in vesicle height as measured by the atomic force microscope and a similar increase in vesicle diameter as determined by confocal microscopy. Mas7, an active mastoparan analog known to stimulate Gi proteins, was found to stimulate the GTPase activity of isolated zymogen granules and cause swelling. Increase in vesicle size in the presence of GTP, NaF, and Mas7 were irreversible and KCl-sensitive. Ca2+ had no effect on zymogen granule size. Taken together, the results indicate that G(alpha i3) protein localized in the secretory vesicle membrane mediates vesicle swelling, a potentially important prerequisite for vesicle fusion at the cell plasma membrane.