Hydrogen peroxide induces association between glyceraldehyde 3‐phosphate dehydrogenase and phospholipase D2 to facilitate phospholipase D2 activation in PC12 cells

• DOI: 10.1046/j.1471-4159.2003.01755.x
• Publication Date: 2003-05-14T09:03:10Z
• Authors: Jung Hwan Kim; Sukmook Lee; Jong Bae Park; Sang Do Lee; Jong Hyun Kim; Sang Hoon Ha; Keiji Hasumi; Akira Endo; Pann‐Ghill Suh; Sung Ho Ryu
• Keywords: Glyceraldehyde 3-phosphate dehydrogenase; PLD2; Phospholipase D; Glyceraldehyde

Abstract Oxidative stress or signaling is widely implicated in apoptosis, ischemia and mitogenesis. Previously, our group reported that the hydrogen peroxide (H 2 O )‐dependent activation of phospholipase D2 (PLD2) PC12 cells involved anti‐apoptotic effect. However, precise mechanism PLD2 by H was not revealed. To find ‐dependent PLD2‐regulating proteins, we immunoprecipitated from found glyceraldehyde 3‐phosphate dehydrogenase (GAPDH) coimmunoprecipitated with upon treatment. This interaction to be direct vitro reconstitution purified GAPDH PLD2. In studies also indicated PLD2‐associated modified on its reactive cysteine residues. Koningic acid, an alkylator catalytic residue, increased between two proteins enhanced activity cells. Blocking modification 3‐aminobenzamide resulted inhibition GAPDH/PLD2 attenuated ‐induced From results, suggest modifies residue only inactivate but endow ability bind resulting association regulation .