Blood pressure-lowering peptides from neo-fermented buckwheat sprouts: a new approach to estimating ACE-inhibitory activity.

Blood pressure-lowering peptides from neo-fermented buckwheat sprouts: a new approach to estimating ACE-inhibitory activity.
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DOI:
10.1371/journal.pone.0105802
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发表时间:
2014
期刊:
影响因子:
3.7
通讯作者:
Nakamura K
Nakamura K
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Koyama M;Hattori S;Amano Y;Watanabe M;Nakamura K

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新发酵荞麦芽(neo-FBS)含有血管紧张素转换酶(ACE)抑制剂和血管扩张剂,具有降低自发性高血压大鼠(SHR)血压(BPL)的特性。在这项研究中,我们研究了六个BPL肽从neo-FBS(FBPs)分离的血管舒张试验和传统的在体外,在体内,和一个新的离体ACE抑制试验的降压机制。在SHR胸主动脉中,一些FBPs表现出中度内皮依赖性血管舒张作用,所有FBPs在体外均轻度抑制ACE。口服FBPs强烈抑制SHR组织中的ACE。为了研究FBPs在活体组织中抑制ACE的详细机制,我们使用从SHR分离的内皮剥脱的胸主动脉环进行了离体实验,结果表明,FBPs在低浓度下有效地抑制胸主动脉组织中的ACE,并抑制血管紧张素II介导的与BPL直接相关的血管收缩。这些结果表明,在活体组织中,FBP的主要BPL机制是ACE抑制,表明高的FBP生物利用度(包括吸收、组织亲和力和组织蓄积)是体内上级ACE抑制的原因。我们建议,我们的体外试验是一种有效和可靠的方法,用于评估ACE抑制机制负责BPL活性在体内。
Neo-fermented buckwheat sprouts (neo-FBS) contain angiotensin-converting enzyme (ACE) inhibitors and vasodilators with blood pressure-lowering (BPL) properties in spontaneously hypertensive rats (SHRs). In this study, we investigated antihypertensive mechanisms of six BPL peptides isolated from neo-FBS (FBPs) by a vasorelaxation assay and conventional in vitro, in vivo, and a new ex vivo ACE inhibitory assays. Some FBPs demonstrated moderate endothelium-dependent vasorelaxation in SHR thoracic aorta and all FBPs mildly inhibited ACE in vitro. Orally administered FBPs strongly inhibited ACE in SHR tissues. To investigate detailed ACE-inhibitory mechanism of FBPs in living body tissues, we performed the ex vivo assay by using endothelium-denuded thoracic aorta rings isolated from SHRs, which demonstrated that FBPs at low concentration effectively inhibited ACE in thoracic aorta tissue and suppressed angiotensin II-mediated vasoconstriction directly associated with BPL. These results indicate that the main BPL mechanism of FBP was ACE inhibition in living body tissues, suggesting that high FBP's bioavailability including absorption, tissue affinity, and tissue accumulation was responsible for the superior ACE inhibition in vivo. We propose that our ex vivo assay is an efficient and reliable method for evaluating ACE-inhibitory mechanism responsible for BPL activity in vivo.
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