Xie Z, Jack-Hays M, Wang Y, Periyasamy S M, Blanco G, Huang W H, Askari A
Department of Pharmacology, Medical College of Ohio, Toledo 43699.
Biochem Biophys Res Commun. 1995 Feb 6;207(1):155-9. doi: 10.1006/bbrc.1995.1166.
Inhibition of Na+/K(+)-ATPase by partially reduced oxygen metabolites is an early event in the course of cell injury caused by oxidative stress. We showed before that isoforms of the enzyme obtained from different sources have different oxidant sensitivities. To evaluate the role of tissue-specific impurities in this difference, cDNAs of alpha 1 and alpha 2 isoforms were expressed in Sf-9 insect cells, and the effects of H2O2 on the resulting isolated enzymes were studied. The expressed alpha 2 was significantly more sensitive than alpha 1 to H2O2. These findings, together with our previous data showing different oxidant sensitivities of alpha 1 and alpha 3 in a cardiac enzyme preparation, indicate that differential oxidant sensitivities of Na+/K(+)-ATPase isoforms of various tissues are dictated by the primary sequences of alpha 1, alpha 2, and alpha 3 subunits.
部分还原的氧代谢产物对Na+/K(+)-ATP酶的抑制作用是氧化应激导致细胞损伤过程中的早期事件。我们之前表明,从不同来源获得的该酶同工型具有不同的氧化剂敏感性。为了评估组织特异性杂质在这种差异中的作用,α1和α2同工型的cDNA在Sf-9昆虫细胞中表达,并研究了H2O2对所得分离酶的影响。表达的α2对H2O2的敏感性明显高于α1。这些发现,连同我们之前的数据表明心脏酶制剂中α1和α3具有不同的氧化剂敏感性,表明不同组织的Na+/K(+)-ATP酶同工型的不同氧化剂敏感性是由α1、α2和α3亚基的一级序列决定的。