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首页> 外文期刊>European Journal of Pharmacology: An International Journal >alpha,beta-MeATP augments the UTP contraction of rabbit basilar artery.
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alpha,beta-MeATP augments the UTP contraction of rabbit basilar artery.

机译:α,β-MeATP增强兔基底动脉的UTP收缩。

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摘要

The mechanism underlying the interaction between alpha,beta-methyleneadenosine 5'-triphosphate (alpha,beta-MeATP) and uridine 5'-triphosphate (UTP) was investigated using the basilar artery of a rabbit. UTP induced a concentration-dependent contraction, whereas P2X receptor agonists, such as alpha,beta-MeATP and 2-methylthioadenosine 5'-triphosphate (2-MeSATP), did not induce any contraction up to 100 microM. alpha,beta-MeATP augmented the UTP contraction two-fold, immediately and reversibly. This effect was observed with ectonucleotidase inhibition with 1 mM Ni(2+), the removal of extracellular Ca(2+) or Evans blue. The contractile response to adenosine 5'-O-(3-triphosphate) (ATPgammaS), a selective agonist for P2Y(4), was augmented by pretreatment with alpha,beta-MeATP also. ATPgammaS had no additional effect on the UTP contraction fully activated with alpha,beta-MeATP. UTP (100 microM) did not induce an increase in cytosolic Ca(2+) in a rabbit basilar arterial strip; however, in the presence of 1 mMalpha,beta-MeATP, UTP induced a significant increase in cytosolic Ca(2+). These results suggest that alpha,beta-MeATP facilitates the activation by UTP of the P2Y receptor (P2Y(4)) of the rabbit basilar artery through mechanisms other than nucleotidase inhibition, and that it does not do so via a P2X receptor.
机译:使用兔的基底动脉研究了α,β-亚甲基腺苷5'-三磷酸(α,β-MeATP)和尿苷5'-三磷酸(UTP)之间相互作用的潜在机制。 UTP诱导了浓度依赖性的收缩,而P2X受体激动剂,例如α,β-MeATP和2-甲基硫代腺苷5'-三磷酸(2-MeSATP),则不会诱导任何收缩,直至100 microM。 α,β-MeATP立即和可逆地使UTP收缩增加了两倍。通过使用1 mM Ni(2+)抑制胞外核苷酸酶,去除细胞外Ca(2+)或伊文思蓝观察到这种效果。对腺苷5'-O-(3-三磷酸)(ATPgammaS)(P2Y(4)的选择性激动剂)的收缩反应也通过用α,β-MeATP预处理而增强。 ATPgammaS对用α,β-MeATP完全激活的UTP收缩没有其他影响。 UTP(100 microM)不会诱导兔基底动脉条中胞质Ca(2+)的增加;但是,在1 mMalpha,β-MeATP的存在下,UTP诱导胞质Ca(2+)的显着增加。这些结果表明,α,β-MeATP通过除核苷酸酶抑制以外的其他机制促进了兔基底动脉P2Y受体(P2Y(4))的UTP激活,而它不是通过P2X受体进行的。

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