Hemorphin-7
目录号 : GC32489
Hemorphin-7是一种血啡肽(hemorphin)，是来源于血红蛋白β链的一种内源性阿片类物质。Hemorphin能够活化阿片类受体(opioidreceptor)以及抑制血管紧张素转化酶(angiotensin-convertingenzyme)，具有抗伤害、抗高血压的作用。
Cas No.:152685-85-3
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >99.50%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Hemorphin-7 is a hemorphin peptide, an endogenous opioid peptide derived from the β-chain of hemoglobin. Hemorphin peptides exhibits antinociceptive and antihypertensive activities, activating opioid receptors and inhibiting angiotensin-converting enzyme (ACE).
[1]. Dejouvencel T, et al. Hemorphin 7 reflects hemoglobin proteolysis in abdominal aortic aneurysm. Arterioscler Thromb Vasc Biol. 2010 Feb;30(2):269-75.
| Cas No. | 152685-85-3 | SDF | |
| Canonical SMILES | Tyr-Pro-Trp-Thr-Gln-Arg-Phe | ||
| 分子式 | C49H64N12O11 | 分子量 | 997.11 |
| 溶解度 | Water : 12.5 mg/mL (12.54 mM) | 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 | 1.0029 mL | 5.0145 mL | 10.029 mL |
| 5 mM | 0.2006 mL | 1.0029 mL | 2.0058 mL |
| 10 mM | 0.1003 mL | 0.5014 mL | 1.0029 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。
Serum Hemorphin-7 levels are decreased in obesity
Obesity (Silver Spring) 2013 Feb;21(2):378-81.PMID:23532992DOI:10.1002/oby.20280.
Objective: Hemorphin peptides exhibit biological activities that interfere with the endorphin system, the inflammatory response, and blood-pressure control. VV-hemorphin-7 and LVV-hemorphin-7 peptides exert a hypotensive effect, in particular, by inhibiting the renin-angiotensin system. Furthermore, levels of circulating Hemorphin-7 peptides have been found to be decreased in diseases such as type 1 and type 2 diabetes. Design and methods: Because type 2 diabetes and obesity share common features, such as insulin resistance, microinflammation, high glomerular-filtration rate (GFR), and cardiovascular risk, we evaluated serum VV-hemorphin-7 like immunoreactivity (VVH7-i.r.) levels, using an enzyme-linked immunosorbent assay method, on a group of 54 obese subjects without diabetes or hypertension, compared with a group of 33 healthy normal-weight subjects. Results: Circulating VVH7-i.r. levels were significantly decreased in the obese group compared with the control group (1.98 ± 0.19 vs. 4.86 ± 0.54 µmol/l, respectively, P < 0.01), and a significant negative correlation between VVH7-i.r. and diastolic blood pressure (DBP) was found in obese patients (r = -0.35, P = 0.011). There was no significant correlation between VVH7-i.r. level and insulin resistance, metabolic syndrome, or GFR. Conclusions: The decreased serum Hemorphin-7 found in obese subjects, as in diabetes, may contribute to the development of hypertension and to the cardiovascular risk associated with these metabolic diseases.
VV-hemorphin-7 and LVV-hemorphin-7 released during in vitro peptic hemoglobin hydrolysis are morphinomimetic peptides
Neuropeptides 1995 Apr;28(4):243-50.PMID:7596489DOI:10.1016/0143-4179(95)90028-4.
Two opioid peptides were generated by in vitro pepsin treatment of bovine hemoglobin. These peptides were identified using a GPI test and purified using HPLC chromatographic techniques. They correspond to fragments 31-40 (LVV-hemorphin-7) and 32-40 (VV-hemorphin-7) of the beta-chain of bovine hemoglobin. Binding experiments strongly confirm that VV-hemorphin-7 and LVV-hemorphin-7 are opioid peptides since they inhibited [3H]naloxone binding to rat brain membranes. Our results indicate that VV-hemorphin-7 and LVV-hemorphin-7 exhibit a lesser potency both in GPI and binding tests. Selectivity and affinity of these purified peptides and synthetic Hemorphin-7 for opioid receptors is discussed.
Modulation of peripheral inflammation by locally administered Hemorphin-7
Inflamm Res 1998 Feb;47(2):49-55.PMID:9535541DOI:10.1007/s000110050266.
Objective: Sensory nerves mediate peripheral inflammation via the release of sensory peptides at the site of tissue injury. Using a blister model of inflammation, we have previously documented that endogenous opioids modulate chronic but not acute inflammation. Hemorphins are nonclassical opioid peptides found in the region of the beta-chain of hemoglobin (Hb). The heptapeptide Hemorphin-7 is identical with residues 35-41 of the beta-chain of the human Hb. The aim of this study was to examine the effect of Hemorphin-7 on the inflammatory response in acute and chronic injury models. Methods: We have used a vacuum-induced blister model in the footpad of anaesthetized rats to induce an inflammatory response in naive skin by (a) electrical stimulation (ES) of the distal end of the cut sciatic nerve at 20 V, 5 Hz, 2 ms for 1 min or (b) superfusion of sensory peptides; substance P (SP) or calcitonin gene related peptide (CGRP) over the blister base. In addition, we examined the effect of Hemorphin-7 on the inflammatory response to SP induced in a previously injured but healed skin site (recurrent injury model) and in denervated skin site due to chronic nerve lesion (chronic injury model). Results: The results showed that prior and concomitant perfusion of Hemorphin-7 over the blister base inhibited the acute inflammatory response to ES of the sciatic nerve at C-fibre strength in a dose-dependent manner. Significant inhibition was achieved at 20 and 200 microM concentration of Hemorphin-7. When Hemorphin-7 (20 microM) was perfused prior to and together with SP or CGRP (both at 1 microM), over the base of acutely induced blister in naive skin, it significantly reduced the inflammatory response to SP (both plasma extravasation and vasodilatation), but was without effect on the vasodilatation response to CGRP. Naloxone, the general opioid antagonist at (1 mg/kg i.v.) reversed the inhibitory effect of Hemorphin-7 on the inflammatory response to SP. On the other hand, Hemorphin-7 had no effect on the inflammatory response to SP in the recurrent injury or the chronic injury models. Conclusions: The results of this study suggest that hemorphins might play a role in inhibiting the inflammatory response in acute, but not in recurrent or chronic injury conditions. Evidence is also provided that the modulatory inhibitory effect of Hemorphin-7 is mediated via activation of opioid receptor(s). The significance of this study in conjunction with our previous work, is that it raises the possibility that different endogenous inhibitory mechanisms may operate under different injury conditions - endogenous hemorphins and opioids may modulate acute and chronic inflammation, respectively.
Brain processing of Hemorphin-7 peptides in various subcellular fractions from rats
Peptides 2006 Dec;27(12):3331-40.PMID:17097762DOI:10.1016/j.peptides.2006.09.014.
Hemorphins are multifunctional peptides derived from hemoglobin or blood processing. They have been found at high levels within the central nervous system where they have a direct effect on neuronal cells via peptidergic receptors. As relatively few studies have examined their metabolic stability in the brain, such investigation was performed to locate the cellular distribution of enzymatic activity against these peptides. High-performance liquid chromatography (HPLC) combined with electrospray ionisation mass spectrometry (ESI-MS) allows identification of degradation products resulting from incubation of Hemorphin-7 peptides (LVV-hemorphin-7, VV-hemorphin-7 and Hemorphin-7) with subcellular fractions isolated from rat brain tissue. Metabolic activities were found against the three peptides in brain homogenate and subcellular fractions with the highest metabolic activity (<3% peptide remaining after 10 min) observed in the microsomal fraction which processed Hemorphin-7 peptides mainly into N-terminal fragments (giving LVVH5) suggesting action of brain-membrane enzymes with C-terminal specificity. Incubation of the ACE inhibitor captopril (0.2 microM) with microsomal fraction, together with LVVH7, decreased the processing of LVVH7 to form LVVH5 by 85%.
Serum levels of Hemorphin-7 peptides in patients with breast cancer
Clin Chim Acta 2003 Nov;337(1-2):59-67.PMID:14568181DOI:10.1016/j.cccn.2003.07.011.
Background: Increased expression of cathepsin D (CD) and B (CB) is found in some cancers and correlates with the development of clinical metastases. It was suggested that these cathepsins could be used as prognostic markers, especially CD in breast cancer. Because serum level of Hemorphin-7 (H7) peptides could reflect CD activity, we have hypothesised that it could be used as a prognostic factor in breast cancer. Methods: To verify this hypothesis, H7 serum levels from 62 breast cancer patients and 25 healthy controls were measured by ELISA. Results: The mean serum concentration of H7 was 2.27+/-0.63 mumol/l in breast cancer patients in comparison with 4.09+/-1.05 mumol/l in controls (p=0.002). This reduced level of H7 in breast cancer could be due to the over-expression of CB, which exhibits strong interaction with H7 in vitro, with a ratio K(cat)/K(m) estimated at 18000 s(-1) M(-1). Conclusions: Because H7 serum levels did not correlate with other parameters including age, CA15-3 and ACE markers, it seems that they might be used as independent markers for the diagnosis of breast cancer.