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在免疫抑制大鼠的淋巴细胞和血小板中水解腺嘌呤核苷酸的酶。

Enzymes that hydrolyze adenine nucleotides in lymphocytes and platelets of immunosuppressed rats.

机构信息

Curso de Farmácia, Centro Universitário Franciscano, 97010-032, Santa Maria, RS, Brazil.

出版信息

Biomed Pharmacother. 2010 Jul;64(6):437-40. doi: 10.1016/j.biopha.2010.01.014. Epub 2010 Feb 25.

Abstract

NTPDase (EC 3.6.1.5) is an enzyme that hydrolyzes extracellular nucleoside tri-and/ or diphosphates to form ATP, which can serve as a substrate for ecto-5'- nucleotidase (EC 3.1.3.5), releasing adenosine, an inhibitor of platelet aggregation and an immunosuppressant agent. In this study, the activity of enzymes that hydrolyze adenine nucleotides was investigated in lymphocytes and platelets of immunosuppressed rats. NTPDase and ecto-5'-nucleotidase activities were determined by colorimetric assay with quantification of the inorganic phosphate released. A significant increase in NTPDase activity was observed in lymphocytes (about 30% in ATP hydrolysis and 80% in ADP hydrolysis, at p<0.05 and p<0.01, respectively). In platelets, there was a significant increase in 5'-nucleotidase activity in immunosuppressed rats (p<0.01) when compared with controls. These results suggest that the hydrolysis of adenine nucleotides is modified in the immunosuppressed state, possibly to compensate for alterations that occur and to avoid the adverse effects of therapy.

摘要

NTPDase(EC 3.6.1.5)是一种酶,能够将细胞外核苷三磷酸和/或二磷酸水解为 ATP,ATP 可作为外切 5′-核苷酸酶(EC 3.1.3.5)的底物,释放出腺苷,腺苷是血小板聚集的抑制剂和免疫抑制剂。在这项研究中,研究了免疫抑制大鼠的淋巴细胞和血小板中水解腺嘌呤核苷酸的酶的活性。通过比色法测定酶活性,定量测定释放的无机磷酸盐。结果发现,淋巴细胞中 NTPDase 活性显著增加(ATP 水解增加约 30%,ADP 水解增加 80%,均 p<0.05 和 p<0.01)。与对照组相比,免疫抑制大鼠血小板中 5′-核苷酸酶活性显著增加(p<0.01)。这些结果表明,在免疫抑制状态下,腺嘌呤核苷酸的水解发生了改变,可能是为了代偿发生的改变,并避免治疗的不良反应。

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