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J. Biol. Chem., Vol. 276, Issue 32, 29899-29905, August 10, 2001

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Nuclear Translocation of Cytosolic Phospholipase A₂ Is Induced by ATP Depletion^*

Alice M. Sheridan^§¶, Adam Sapirstein^**, Nicole Lemieux, Brennan D. Martin, Dae Kyong Kim^§, and Joseph V. Bonventre^§

From the  Medical Service and  Anesthesia Service, Massachusetts General Hospital and the Departments of ^§ Medicine and ^** Anesthesia, Harvard Medical School, Charlestown, Massachusetts 02129

Phospholipase A₂ (PLA₂) enzymes may play a role in cellular injury due to ATP depletion. Renal Madin-Darby canine kidney cells were subjected to ATP depletion to assess the effects of cellular energy metabolism on cytosolic PLA₂ (cPLA₂) regulation. ATP depletion results in a decrease in soluble cPLA₂ activity and an increase in membrane-associated activity, which is reversed upon restoration of ATP levels by addition of dextrose. In ATP-depleted cells cPLA₂ mass shifts from cytosol to nuclear fractions. GFP-cPLA₂ is localized at the nuclear membrane of stably transfected ATP-depleted LLC-PK₁ cells under conditions where [Ca²⁺]_i is known to increase. cPLA₂ translocation does not occur if the increase in [Ca²⁺]_i increase is inhibited. If [Ca²⁺]_i is allowed to increase when ATP is depleted and the cells are then lysed, cPLA₂ remains associated with nuclear fractions even if the homogenate [Ca²⁺] is markedly reduced. In contrast, cPLA₂, which becomes associated with the nucleus when [Ca²⁺]_i is increased using ionophore, readily dissociates from the nuclear fractions of ATP-replete cells upon reduction of homogenate [Ca²⁺]. Okadaic acid inhibits the ATP depletion-induced association of cPLA₂ with nuclear fractions. Thus energy deprivation results in [Ca²⁺]-induced nuclear translocation, which is partially prevented by a phosphatase inhibitor.

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