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Perinuclear localization of cytosolic phospholipase A 2 α is important but not obligatory for coupling with cyclooxygenases
Author(s) -
Murakami Makoto,
Das Sudipto,
Kim Young-Jun,
Cho Wonhwa,
Kudo Ichiro
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00596-9
Subject(s) - cytosol , phospholipase a2 , colocalization , microbiology and biotechnology , transfection , phospholipase , phospholipase a , biology , alpha (finance) , mutant , eicosanoid , biochemistry , arachidonic acid , enzyme , medicine , construct validity , nursing , patient satisfaction , gene
In response to Ca 2+ signaling, cytosolic phospholipase A 2 α (cPLA 2 α) translocates from the cytosol to the perinuclear membrane, where downstream eicosanoid‐synthetic enzymes, such as cyclooxygenase (COX), are localized. Although the spatiotemporal perinuclear colocalization of cPLA 2 α and COXs has been proposed to be critical for their functional coupling leading to prostanoid production, definitive evidence for this paradigm has remained elusive. To circumstantiate this issue, we took advantage of a chimeric cPLA 2 α mutant harboring the C2 domain of protein kinase Cα, which translocates to the plasma membrane following cell activation. Transfection analyses of the native or chimeric cPLA 2 α in combination with COX‐1 or COX‐2 revealed that, even though the arachidonate‐releasing capacities of native and mutant cPLA 2 α were comparable, prostaglandin production by mutant cPLA 2 α was markedly impaired as compared with that by native cPLA 2 α. We thus conclude that the perinuclear localization of cPLA 2 α is preferential, even if not obligatory, for efficient coupling with COXs.