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首页> 外文期刊>Neurochemistry International: The International Journal for the Rapid Publication of Critical Reviews, Preliminary and Original Research Communications in Neurochemistry >Phospholipase A2 products retain a neuron specific gamma isoform of PKC on the plasma membrane through the C1 domain--a molecular mechanism for sustained enzyme activity.
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Phospholipase A2 products retain a neuron specific gamma isoform of PKC on the plasma membrane through the C1 domain--a molecular mechanism for sustained enzyme activity.

机译：磷脂酶A2产物通过C1域在质膜上保留了神经元特有的PKCγ异构体-一种持续的酶活性的分子机制。

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摘要

To clarify molecular mechanism for sustained activation of gamma protein kinase C (gammaPKC), a neuron-specific subtype, we investigated the involvement of phospholipase A2 (PLA2) products in the membrane association of gammaPKC upon activation of G protein coupled purinoceptors in CHO-K1 and NG 108-15 cells. In addition, the functional domain responsible for PLA2-product mediated retention of gammaPKC on the plasma membrane was determined by simultaneously monitoring two different fluorescence-tagged gammaPKCs and mutants in the same living CHO-K1 cells. Purinoceptor activation by UTP induced a transient translocation of gammaPKC from the cytoplasm to the plasma membrane. Interestingly, PLA2 inhibitors, bromoenol lactone (BEL) and arachidonyl-trifluoromethyl ketone (AACOF3), shortened the retention time of gammaPKC on the plasma membrane in cells treated with UTP, while a DAG kinase inhibitor did not affect it. The C1 domain deficient mutant (DeltaC1-gammaPKC) also showed short membrane association compared with wild type gammaPKC, when cells are treated with UTP or arachidonic acid (AA) plus a Ca(2+) ionophore. However, deletion of C1A or C1B subdomains (DeltaC1A-gammaPKC or DeltaC1B-gammaPKC) did not alter the retention time on the plasma membrane, whereas PLA2 inhibitor shortened the retention times of both mutants. These results indicate that PLA2 products prolong the retention of gammaPKC on the plasma membrane through the C1A and/or C1B subdomain in purinoceptor-stimulated CHO-K1 cells. The importance of PLA2 product and C1 domain for the retention of gammaPKC on the membrane was also confirmed using neuronal cell line, suggesting that these are part of molecular machinery for sustaining enzyme activity in neurons.
机译：为了阐明持续激活神经元特异性亚型的γ蛋白激酶C（gammaPKC）的分子机制，我们研究了CHO-K1中G蛋白偶联嘌呤受体激活后磷脂酶A2（PLA2）产品参与γγPKC膜缔合的过程。和NG 108-15细胞。此外，负责PLA2产物介导的γ-PKC在质膜上的保留的功能域是通过同时监控两个相同的活CHO-K1细胞中带有荧光标记的γ-PKC和突变体来确定的。 UTP引起的嘌呤受体激活诱导了γPKC从细胞质到质膜的短暂转运。有趣的是，PLA2抑制剂，溴烯醇内酯（BEL）和花生四烯基-三氟甲基酮（AACOF3）缩短了UTP处理的细胞中gammaPKC在细胞膜上的保留时间，而DAG激酶抑制剂对此没有影响。当用UTP或花生四烯酸（AA）加Ca（2+）离子载体处理细胞时，与野生型gammaPKC相比，C1域缺陷突变体（DeltaC1-gammaPKC）还显示出短的膜缔合。但是，删除C1A或C1B子域（DeltaC1A-gammaPKC或DeltaC1B-gammaPKC）不会改变质膜上的保留时间，而PLA2抑制剂则缩短了两个突变体的保留时间。这些结果表明，PLA2产物通过嘌呤受体刺激的CHO-K1细胞中的C1A和/或C1B子域延长了gammaPKC在质膜上的保留。使用神经元细胞系也证实了PLA2产物和C1结构域对于在膜上保留gammaPKC的重要性，这表明它们是维持神经元酶活性的分子机制的一部分。

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