tailieunhanh - Báo cáo khoa học: Peroxiredoxin II functions as a signal terminator for H2O2-activated phospholipase D1

Phospholipase D1 (PLD1) is a signal-transduction regulated enzyme which regulates several cell intrinsic processes including activation of NAPDH oxidase, which elevates intracellular H2O2. Several proteins have been reported to interact with PLD1 in resting cells. We sought to identify pro-teins that interact with PLD1 after phorbol 12-myristate 13-acetate (PMA) stimulation. | ềFEBS Journal Peroxiredoxin II functions as a signal terminator for H2O2-activated phospholipase D1 Nianzhou Xiao Guangwei Du and Michael A. Frohman Department of Pharmacology and the Center for DevelopmentalGenetics University MedicalCenter at Stony Brook NY USA Keywords hydrogen peroxide peroxiredoxin II phosphatidic acid phospholipase D1 PMA Correspondence M. Frohman Center for Developmental Genetics 438 CMM Stony Brook NY 11794-5140 USA Fax 1 631 632 1692 Tel 1 631 632 1476 E-mail michael@ Received 4 May 2005 revised 3 June 2005 accepted 8 June 2005 doi Phospholipase D1 PLD1 is a signal-transduction regulated enzyme which regulates several cell intrinsic processes including activation of NAPDH oxidase which elevates intracellular H2O2. Several proteins have been reported to interact with PLD1 in resting cells. We sought to identify proteins that interact with PLD1 after phorbol 12-myristate 13-acetate PMA stimulation. A novel interaction with peroxiredoxin II PrxII an enzyme that eliminates cellular H2O2 which is a known stimulator of PLD1 was identified by PLD1-affinity pull-down and MS. PMA stimulation was confirmed to promote physical interaction between PLD1 and PrxII and to cause PLD1 and PrxII to colocalize subcellularly. Functional significance of the interaction was suggested by the observation that over-expression of PrxII specifically reduces the response of PLD1 to stimulation by H2O2. These results indicate that PrxII may have a signal-terminating role for PLD1 by being recruited to sites containing activated PLD1 after cellular stimulation involving production of H2O2. Mammalian phospholipase D PLD is a signal-transducing enzyme that hydrolyzes PtdCho to generate the membrane-bound lipid signal phosphatidic acid PA reviewed in 1 2 . PA is a second messenger and can be further converted into diacylglycerol. PLD is indirectly activated in response to cellular stimulation by various extracellular .

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