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为了研究锌对大鼠成骨细胞膜Ca2+ -ATP酶和Na+ 、K+ -ATP酶活性的影响及其机制,实验设对照组和3个补锌组。采用孔雀绿比色法同步测定膜Ca2+ -ATP酶和Na+ ,K+ -ATP酶活性,以研究Zn2+ 对酶活性的影响以及蛋白激酶C或钙调素特异性抑制剂对Zn2+ 诱导的成骨细胞膜Ca2+ -ATP酶活性的影响。结果表明,Zn2+ 可以显著提高成骨细胞膜Ca2+ -ATP酶活性,但对Na+ ,K+ -ATPase活性无影响;钙调素特异性抑制剂R24571对Zn2+ 诱导的Ca2+ -ATPase活性无影响,钙调素对膜Ca2+ -ATP酶基础活性也无激活作用;蛋白激酶C特异性抑制剂三氟拉嗪可使Zn2+ 诱导的Ca2+ -ATP酶的活性显著降低。因此,锌可能通过蛋白激酶C介导调节成骨细胞膜Ca2+ -ATP酶活性
In order to study the effect of zinc on the activity of Ca2 + -ATPase and Na +, K + -ATPase in rat osteoblasts and its mechanism, we set up control group and three zinc-supplementing groups. The activity of Ca2 + -ATPase and Na +, K + -ATPase were assayed synchronously by malachite green colorimetric assay to study the effect of Zn2 + on the enzyme activity and the effect of protein kinase C or calmodulin-specific inhibitor on Zn2 + -induced membrane Ca2 + -ATP enzyme activity. The results showed that Zn2 + could significantly increase the activity of Ca2 + -ATPase in osteoblasts, but had no effect on the activity of Na +, K + -ATPase. Calmodulin-specific inhibitor R24571 had no effect on the activity of Ca2 + -ATPase induced by Zn2 + Membrane Ca2 + -ATP enzyme basal activity also no activation; protein kinase C-specific inhibitor trifluoperazine Zn2 + -induced Ca2 + -ATPase activity was significantly reduced. Therefore, zinc may mediate the osteoblast Ca2 + -ATPase activity through protein kinase C