Purinergic effects on Na,K-ATPase activity differ in rat and human skeletal muscle.
Purinergic effects on Na,K-ATPase activity differ in rat and human skeletal muscle.
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DOI：
10.1371/journal.pone.0091175
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发表时间：
2014
期刊：
影响因子：
3.7
通讯作者：
Bangsbo J
中科院分区：
文献类型：
--
作者：
Juel C;Nordsborg NB;Bangsbo J
P2 Y受体的激活可能与嘌呤类药物对大鼠肌肉Na，K-ATP酶体外最大活性的影响有关。用来自大鼠和人骨骼肌的膜研究了人骨骼肌中存在类似机制的假设。从大鼠和人肌肉中纯化的膜用于Na，K-ATP酶测定。用ADP、稳定的ADP类似物MeS-ADP和UDP孵育大鼠肌膜，可增加Na+依赖的Na，K-ATP酶活性，而人肌膜的类似处理则降低Na，K-ATP酶活性。UTP孵育导致人体Na，K-ATP酶活性不变，但与拮抗剂苏拉明预孵育导致UTP抑制，表明P2 Y受体参与。蛋白激酶A和蛋白激酶C的激活均能激活人和大鼠细胞膜上的Na，K-ATP酶。因此，蛋白激酶A和C的激活可以增加人肌肉中Na，K-ATP酶的活性，但不是通过P2 Y受体刺激。大多数嘌呤（UTP除外）在人体肌膜中的抑制作用可能是由于ATP水解的质量定律抑制。这种抑制作用在大鼠中可能由于受体介导的Na，K-ATP酶的激活而变得模糊。不同的作用可能与大鼠中ADP敏感的P2 Y1和P2 Y13受体的高密度有关，而UTP敏感的P2 Y11可能在人类中更丰富。另外，大鼠可能具有P2 Y受体和Na，K-ATP酶之间的蛋白质-蛋白质相互作用的机制，并且这种机制可能在人骨骼肌中不存在（可能除了UTP敏感的P2 Y11受体）。大鼠肌肉不是研究嘌呤能对人骨骼肌Na，K-ATP酶影响的可靠模型。
P2Y receptor activation may link the effect of purines to increased maximal in vitro activity of the Na,K-ATPase in rat muscle. The hypothesis that a similar mechanism is present in human skeletal muscle was investigated with membranes from rat and human skeletal muscle. Membranes purified from rat and human muscles were used in the Na,K-ATPase assay. Incubation with ADP, the stable ADP analogue MeS-ADP and UDP increased the Na+ dependent Na,K-ATPase activity in rat muscle membranes, whereas similar treatments of human muscle membranes lowered the Na,K-ATPase activity. UTP incubation resulted in unchanged Na,K-ATPase activity in humans, but pre-incubation with the antagonist suramin resulted in inhibition with UTP, suggesting that P2Y receptors are involved. The Na,K-ATPase in membranes from both rat and human could be stimulated by protein kinase A and C activation. Thus, protein kinase A and C activation can increase Na,K-ATPase activity in human muscle but not via P2Y receptor stimulation. The inhibitory effects of most purines (with the exception of UTP) in human muscle membranes are probably due to mass law inhibition of ATP hydrolysis. This inhibition could be blurred in rat due to receptor mediated activation of the Na,K-ATPase. The different effects could be related to a high density of ADP sensitive P2Y1 and P2Y13 receptors in rat, whereas the UTP sensitive P2Y11 could be more abundant in human. Alternatively, rat could possesses a mechanism for protein-protein interaction between P2Y receptors and the Na,K-ATPase, and this mechanism could be absent in human skeletal muscle (perhaps with the exception of the UTP sensitive P2Y11 receptor). Rat muscle is not a reliable model for purinergic effects on Na,K-ATPase in human skeletal muscle.
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