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首页> 外文期刊>Canadian Journal of Physiology and Pharmacology >Restricted ability of human mast cell tryptase to activate proteinase-activated receptor-2 in rat aorta.
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Restricted ability of human mast cell tryptase to activate proteinase-activated receptor-2 in rat aorta.

机译：人肥大细胞类胰蛋白酶激活大鼠主动脉蛋白酶激活受体2的能力有限。

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摘要

We investigated the potential of human mast cell tryptase to induce relaxation of rat aorta. Trypsin and the selective PAR2-activating peptide (PAR2-AP) SLIGRL-NH2 stimulated robust relaxation of phenylephrine-precontracted rat aortic rings. However, human lung tryptase (1-100 nM) either in the presence or absence of heparin failed to induce any significant relaxation. Notwithstanding, incubation of the aorta with tryptase (100 nM), following the addition of a peptide corresponding to the cleavage/activation sequence of rat PAR2 (rPAR2), resulted in relaxation of precontracted tissue due to the proteolytic release of the PAR2-AP SLIGRL/ from the parent peptide. Thus, tryptase was enzymatically active in the bioassay system. Preincubation of aorta with neuraminidase to remove cell-surface sialic acid unmasked the ability of tryptase to induce relaxation of the aorta, but had no effect on relaxation induced by trypsin, SLIGRL-NH2, or acetylcholine (Ach). Like trypsin and SLIGRL-NH2, the tryptase-induced relaxation was inhibited by either removal of the endothelium or pretreatment of the tissue with NG-nitro-L-arginine methyl ester (L-NAME), suggesting an endothelium-derived nitric oxide mechanism. Interestingly, tryptase in the presence of heparin failed to induce relaxation of precontracted neuraminidase-treated rat aorta. We conclude that tryptase-induced relaxation of rat aorta, most likely via PAR2, is tightly regulated by heparin and cell-surface sialic acid.
机译：我们调查了人类肥大细胞类胰蛋白酶诱导大鼠主动脉松弛的潜力。胰蛋白酶和选择性PAR2激活肽（PAR2-AP）SLIGRL-NH2刺激了去氧肾上腺素预收缩的大鼠主动脉环的强烈松弛。但是，在有或没有肝素的情况下，人肺类胰蛋白酶（1-100 nM）都无法诱导任何明显的松弛。尽管如此，在添加与大鼠PAR2的裂解/激活序列相对应的肽（rPAR2）后，用胰蛋白酶（100 nM）孵育主动脉，由于PAR2-AP SLIGRL的蛋白水解释放，导致预收缩组织松弛。 /来自亲本肽。因此，类胰蛋白酶在生物测定系统中具有酶促活性。用神经氨酸酶对主动脉进行预温育以去除细胞表面唾液酸掩盖了类胰蛋白酶诱导主动脉松弛的能力，但对胰蛋白酶，SLIGRL-NH2或乙酰胆碱（Ach）诱导的松弛没有影响。像胰蛋白酶和SLIGRL-NH2一样，通过去除内皮或用NG-硝基-L-精氨酸甲酯（L-NAME）预处理组织，抑制了类胰蛋白酶诱导的松弛，提示内皮源性一氧化氮机制。有趣的是，在肝素存在下的类胰蛋白酶不能诱导预收缩的神经氨酸酶处理的大鼠主动脉松弛。我们得出的结论是，肝素和细胞表面唾液酸严格控制类胰蛋白酶诱导的大鼠主动脉松弛，这很可能是通过PAR2进行的。

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