Phosphatidic Acid-mediated Phosphorylation of the NADPH Oxidase Component p47-phox

Waite, Kristin; Wallin, Reidar; Qualliotine-Mann, Diane; McPhail, Linda C.

doi:10.1074/jbc.272.24.15569

Cited by 137 publications

(80 citation statements)

References 85 publications

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“…Other kinases recently shown to be activated by phospholipids include phosphatidic acid-activated protein kinase and Raf-1 by phosphatidic acid [15,16]. The present results demonstrating the activation of PKA by lysoplasmenylcholine represent another mechanism through which accelerated phospholipolysis may be coupled to protein kinases.…”

Section: Discussionmentioning

confidence: 50%

Activation of myocardial cAMP‐dependent protein kinase by lysoplasmenylcholine

Williams¹,

Ford²

1997

FEBS Letters

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Plasmalogen-specific, calcium-independent phospholipase A 2 (iPLA 2 ) is activated during myocardial ischemia. Accordingly, we have assessed the activation of myocardial protein kinases by the iPLA 2 product, lysoplasmenylcholine. Lysoplasmenylcholine-activated protein kinase activity from heart cytosol fractionated on a DE-52 column was identified as cAMP-dependent protein kinase (PKA) based on the following: (1) protein kinase activity stimulated by cAMP and lysoplasmenylcholine co-eluted on sequential chromatographic steps; (2) lysoplasmenylcholine-activated protein kinase activity was inhibited by the PKA inhibitor, PKI; and (3) the unprimed PKA form generated from the primed form of PKA was activated by cAMP and lysoplasmenylcholine. These results demonstrate a novel mechanism for PKA activation by lysoplasmenylcholine.z 1997 Federation of European Biochemical Societies.

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Section: Discussionmentioning

confidence: 50%

Activation of myocardial cAMP‐dependent protein kinase by lysoplasmenylcholine

Williams¹,

Ford²

1997

FEBS Letters

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“…Furthermore, blocking the Na ϩ /H ϩ antiport preferentially enhanced azurophilic degranulation, whereas specific degranulation was only mildly enhanced, consistent with a mechanism involving PLD because phosphatidic acid, the product of PLD lysis of phospholipids, has been shown to induce degranulation of azurophilic but not of specific granules when added to electropermeabilized PMN [15]. Although PLD activation is also required for PMN superoxide secretion [27][28][29], our results suggest that, at least in response to maximal Fc␥ receptor stimulation, neither PLD activation nor acidification is limiting. Perhaps for that secretory response, ⌬[Ca 2ϩ ] in plays a more important regulatory role because preventing such changes potently (Ͼ75%) inhibits PMN superoxide release [3].…”

Section: Discussionmentioning

confidence: 71%

Neutrophil degranulation and phospholipase D activation are enhanced if the Na+/H+ antiport is blocked

Gewirtz

Seetoo

Simons

1998

Journal of Leukocyte Biology

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To investigate the role of the pH transient in controlling degranulation, the Na ؉ /H ؉ antiport was inhibited either with 100 M dimethylamiloride (DMA) or by substituting N-methyl-glucamine for extracellular sodium. Blocking the antiport with DMA led to hyperacidified PMN, which exhibited an increase in degranulation, but did not affect generation of superoxide. DMA did not alter the ability of neutrophils to phagocytose and oxidize dichlorodihydrofluoresceinated HIC, suggesting the increase in degranulation was not the result of failed phagocytosis. Investigation into whether the observed increase in degranulation when the antiport was blocked was mediated by PLD or ⌬[Ca 2؉ ] in revealed that blocking the antiport increased HICinduced PLD activity but had no effect on HICinduced ⌬[Ca 2؉ ] in . Blocking the Na ؉ /H ؉ antiport by ion substitution caused similar effects on PMN signaling and secretion as was seen with DMA. These results indicate that Na ؉ /H ؉ antiport activity is not necessary for degranulation or superoxide release in HICstimulated PMN and that hyperacidification of the cytoplasm can modulate degranulation. Therefore, pH in , via its effect on PLD, may be a control point of degranulation and may represent one way that neutrophils achieve differential control of their antibacterial products. J. Leukoc. Biol. 64: 98-103; 1998.

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“…Although homologs of the gp91 phox catalytic subunit of the neutrophil NADPH oxidase (Keller et al, 1998;Torres et al, 1998) and putative homologs of the Rac small G protein regulatory subunit (Yang, 2002) are present in Arabidopsis, the genome does not encode homologs of the remaining components of the neutrophil NADPH oxidase, p22 phox , p67 phox , p47 phox , or p40 phox (Arabidopsis Genome Initiative, 2000). Therefore, triggering of ROS generation by PA in Arabidopsis is not likely to be achieved via the activation of the p22 phox and p47 phox , as found in neutrophils (Waite et al, 1997;Regier et al, 2000).…”

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confidence: 99%

Phosphatidic Acid Induces Leaf Cell Death in Arabidopsis by Activating the Rho-Related Small G Protein GTPase-Mediated Pathway of Reactive Oxygen Species Generation

Gu²,

et al. 2004

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Phosphatidic acid (PA) level increases during various stress conditions. However, the physiological roles of this lipid in stress response remain largely unknown. In this study, we report that PA induced leaf cell death and elevated the levels of reactive oxygen species (ROS) in the whole leaf and single cells. To further elucidate the mechanism of PA-induced cell death, we then examined whether Rho-related small G protein (ROP) 2, which enhanced ROS production in an in vitro assay, is involved in PA-induced ROS production and cell death. In response to PA, transgenic leaves of Arabidopsis expressing a constitutively active rop2 mutant exhibited earlier cell death and higher levels of ROS than wild type (WT), whereas those expressing a dominant-negative rop2 mutant exhibited later cell death and lower ROS. However, in the absence of exogenous PA, no spontaneous cell death or elevated ROS was observed in constitutively active rop2 plants, suggesting that the activation of ROP GTPase alone is insufficient to activate the ROP-mediated ROS generation pathway. These results suggest that PA modulates an additional factor required for the active ROP-mediated ROS generation pathway. Therefore, PA may be an important regulator of ROP-regulated ROS generation and the cell death process during various stress and defense responses of plants.Phosphatidic acid (PA) is implicated in numerous stress responses of plants. Intracellular PA levels increase under various biotic and abiotic stress conditions, including pathogen elicitation (Young et al., 1996;van der Luit et al., 2000), wounding Wang, 1996, 1998; Lee et al., 1997), freezing (Welti et al., 2002), hyperosmotic stress (Munnik et al., 2000), and water deficit (Frank et al., 2000;Munnik et al., 2000). It is suggested that PA is a second messenger in a broad range of stress-signaling pathways in plants and mediates important responses to stresses (Munnik, 2001).PA has many regulatory functions in animal cells, including the regulation of reactive oxygen species (ROS) generation, protein kinase, phosphatase, lipid kinase, phospholipases, intracellular Ca 2ϩ levels, vesicle trafficking, cell proliferation, and cytoskeletal rearrangement (Liscovitch et al., 2000). This lipid also regulates a wide range of important cellular processes in plants, including regulation of ROS generation (Sang et al., 2001a), MAPK activity (Lee et al., 2001), K ϩ channels (Jacob et al., 1999), and actin organization (Lee et al., 2003). Therefore, PA is likely to be involved in numerous physiological processes in plants, including stomatal movement (Jacob et al., 1999), leaf senescence (Fan et al., 1997), various stress responses, and hormone signaling (for review, see Munnik, 2001). In vivo roles of PA in leaf senescence and stomatal closing movement were demonstrated using PLD␣ antisense plants; this mutant plant is delayed in ABA-and ethylene-induced senescence (Ryu and Wang, 1995; Fan et al., 1997;Zien et al., 2001) and in ABA-induced stomatal closing movement (Sang et al., 2001b).A potentia...

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Phosphatidic Acid-mediated Phosphorylation of the NADPH Oxidase Component p47-phox

Cited by 137 publications

References 85 publications

Activation of myocardial cAMP‐dependent protein kinase by lysoplasmenylcholine

Activation of myocardial cAMP‐dependent protein kinase by lysoplasmenylcholine

Neutrophil degranulation and phospholipase D activation are enhanced if the Na+/H+ antiport is blocked

Phosphatidic Acid Induces Leaf Cell Death in Arabidopsis by Activating the Rho-Related Small G Protein GTPase-Mediated Pathway of Reactive Oxygen Species Generation

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