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• W1972697844 abstract "To clarify molecular mechanism for sustained activation of gamma protein kinase C (γPKC), a neuron-specific subtype, we investigated the involvement of phospholipase A2 (PLA2) products in the membrane association of γPKC 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 γPKC on the plasma membrane was determined by simultaneously monitoring two different fluorescence-tagged γPKCs and mutants in the same living CHO-K1 cells. Purinoceptor activation by UTP induced a transient translocation of γPKC from the cytoplasm to the plasma membrane. Interestingly, PLA2 inhibitors, bromoenol lactone (BEL) and arachidonyl-trifluoromethyl ketone (AACOF3), shortened the retention time of γPKC on the plasma membrane in cells treated with UTP, while a DAG kinase inhibitor did not affect it. The C1 domain deficient mutant (ΔC1-γPKC) also showed short membrane association compared with wild type γPKC, when cells are treated with UTP or arachidonic acid (AA) plus a Ca2+ ionophore. However, deletion of C1A or C1B subdomains (ΔC1A-γPKC or ΔC1B-γPKC) 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 γPKC 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 γPKC on the membrane was also confirmed using neuronal cell line, suggesting that these are part of molecular machinery for sustaining enzyme activity in neurons." @default.
• W1972697844 created "2016-06-24" @default.
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• W1972697844 date "2004-07-01" @default.
• W1972697844 modified "2023-10-11" @default.
• W1972697844 title "Phospholipase A2 products retain a neuron specific γ isoform of PKC on the plasma membrane through the C1 domain—a molecular mechanism for sustained enzyme activity" @default.
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• W1972697844 doi "https://doi.org/10.1016/j.neuint.2003.12.006" @default.
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