PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10353694-8 1999 Taken together the data indicate that GM-CSF rapidly activates PLD in adherent cells, which is responsible for the generation of PA. Protactinium 129-131 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 63-66 11744730-7 2002 To examine the role of PLD in the regulation of PI(4,5)P(2) synthesis, we used butanol to diminish the PLD-derived PA. Protactinium 115-117 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 103-106 11744730-14 2002 We therefore conclude that both PA derived from the PLD pathway and ARF proteins, by directly activating PIP 5-kinase, contribute to the regulation of PI(4,5)P(2) synthesis at the plasma membrane in HL60 cells. Protactinium 32-34 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 52-55 11706993-1 2001 Phospholipase D (PLD) catalyses the hydrolysis of phosphatidylcholine to generate the lipid second messenger, phosphatidate (PA) and choline. Protactinium 125-127 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 0-15 11706993-1 2001 Phospholipase D (PLD) catalyses the hydrolysis of phosphatidylcholine to generate the lipid second messenger, phosphatidate (PA) and choline. Protactinium 125-127 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 17-20 11706993-6 2001 A signalling role of phospholipase D via PA and indirectly via PIP2 in regulating membrane traffic and actin dynamics is indicated by the available data. Protactinium 41-43 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 21-36 12217395-1 2002 Phospholipase D (PLD) catalyses the hydrolysis of phosphatidylcholine to generate the lipid second messenger, phosphatidate (PA). Protactinium 125-127 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 0-15 12217395-1 2002 Phospholipase D (PLD) catalyses the hydrolysis of phosphatidylcholine to generate the lipid second messenger, phosphatidate (PA). Protactinium 125-127 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 17-20 12217395-4 2002 Primary alcohols specifically interfere with the production of PLD-derived PA and are found to be potent inhibitors of antigen-stimulated exocytosis. Protactinium 75-77 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 63-66 12217395-7 2002 ARF proteins and PLD-derived PA synergistically regulate the activity of a Type I PIP 5-kinasealpha. Protactinium 29-31 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 17-20 12217395-8 2002 It is suggested that ARF, by activating PLD and PIP 5-kinase activities regulate PA and PI(4,5)P(2) levels, and both are critical components of the exocytosis machinery in mast cells. Protactinium 81-83 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 40-43 10375402-2 1999 Purified human liver microsomal cytochromes P450 (P450)-P450 1A2 and P450 2E1-were shown to have appreciable PLD activity, hydrolyzing phosphatidylcholine but not other phospholipids, generating PA and choline. Protactinium 195-197 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 109-112 8843153-3 1996 By contrast, the PLD-induced generation of PA was significantly higher in the old than in the young. Protactinium 43-45 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 17-20 8855796-10 1996 We suggest that the PA generation induced by PLD stimulation could contribute to the stimulated H2O2 formation and iodide organification observed with the agonists inducing PtdBut accumulation. Protactinium 20-22 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 45-48 8805276-10 1996 In PAE cells, the stimulation of actin stress fibre formation was a consequence of PA generation and, therefore, PLD activation. Protactinium 3-5 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 113-116 8793299-2 1996 Neutrophils and HL60 cells secrete lysosomal enzymes from azurophilic granules; this secretion is inhibited by 1% ethanol, indicating that phosphatidate (PA) produced by phospholipase D (PLD) activity may be involved. Protactinium 154-156 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 170-185 8793299-2 1996 Neutrophils and HL60 cells secrete lysosomal enzymes from azurophilic granules; this secretion is inhibited by 1% ethanol, indicating that phosphatidate (PA) produced by phospholipase D (PLD) activity may be involved. Protactinium 154-156 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 187-190 8793299-3 1996 PLD can use primary alcohols in preference to water during the hydrolytic step, generating the corresponding phosphatidylalcohol instead of PA, its normal product. Protactinium 140-142 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 0-3 8793299-15 1996 In comparison, ARF1 activates PLD, producing PA, which is a known activator of phosphatidylinositol-4-phosphate 5 kinase, the enzyme responsible for PIP2 synthesis. Protactinium 45-47 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 30-33 8805276-1 1996 BACKGROUND: Agonist-stimulated phospholipase D (PLD) catalyzes the hydrolysis of phosphatidylcholine, generating the putative messenger phosphatidate (PA). Protactinium 151-153 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 31-46 8805276-1 1996 BACKGROUND: Agonist-stimulated phospholipase D (PLD) catalyzes the hydrolysis of phosphatidylcholine, generating the putative messenger phosphatidate (PA). Protactinium 151-153 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 48-51 8209783-4 1993 In all cases, secretion correlated with the activation of phospholipase D (PLD), as detected by the formation of [3H]phosphatidic acid (PA) in the absence of ethanol or of [3H]phosphatidylethanol (PEt) in the presence of ethanol. Protactinium 136-138 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 58-73 22097391-3 1996 First, PL D hydrolysis of stable 1,2-diacyl-sn-glycero-3-phosphocholine (PC) films by PL D generated a stable 1,2-diacyl-sn-glycero-3-phosphate (PA) film and water-soluble choline. Protactinium 145-147 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 7-11 22097391-3 1996 First, PL D hydrolysis of stable 1,2-diacyl-sn-glycero-3-phosphocholine (PC) films by PL D generated a stable 1,2-diacyl-sn-glycero-3-phosphate (PA) film and water-soluble choline. Protactinium 145-147 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 86-90 7882615-5 1995 Laminin-induced production of MMP-2 is attenuated by 1-butanol, a competitive substrate of PLD that reduces PLD-catalyzed production of PA. Protactinium 136-138 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 91-94 7882615-5 1995 Laminin-induced production of MMP-2 is attenuated by 1-butanol, a competitive substrate of PLD that reduces PLD-catalyzed production of PA. Protactinium 136-138 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 108-111 8338512-5 1993 Addition of ethanol inhibited both secretion and [3H]PA formation and led to the accumulation of [3H]phosphatidylethanol ([3H]PEt), indicating that [3H]PA was formed largely by activation of PLD. Protactinium 152-154 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 191-194 8394074-3 1993 In the presence of ethanol, PLD catalyzed a transphosphatidylation reaction in which LTB4 increased [3H]alkyl-phosphatidylethanol formation and simultaneously decreased LTB4-induced PA and DG accumulation. Protactinium 182-184 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 28-31 8473292-4 1993 Inhibition of GPI-PLD by PAs (IC50 approximately 1 microM) was relatively independent of the length or degree of unsaturation of the fatty acyl chains. Protactinium 25-28 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 14-21 8209783-4 1993 In all cases, secretion correlated with the activation of phospholipase D (PLD), as detected by the formation of [3H]phosphatidic acid (PA) in the absence of ethanol or of [3H]phosphatidylethanol (PEt) in the presence of ethanol. Protactinium 136-138 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 75-78 8209783-10 1993 The results suggest that PA formed by activation of PLD may mediate secretion from permeabilized platelets by PKC-dependent and independent mechanisms. Protactinium 25-27 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 52-55 8209783-11 1993 However, in intact platelets stimulated by thrombin, PLD accounted for only 10-20% of the total PA formed and can only play a major role in secretion if this PA fraction is distinct from that formed by the combined actions of PLC and DAG kinase. Protactinium 96-98 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 53-56 8209783-11 1993 However, in intact platelets stimulated by thrombin, PLD accounted for only 10-20% of the total PA formed and can only play a major role in secretion if this PA fraction is distinct from that formed by the combined actions of PLC and DAG kinase. Protactinium 158-160 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 53-56 3422154-7 1988 In contrast, [3H]PA arises from both PLD and diglyceride kinase activities. Protactinium 17-19 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 37-40 2130511-18 1990 Activation of phospholipase D (PLD) was demonstrated by the finding that phosphatidic acid increased in response to PMA or carbachol prior to the increase in PA. Protactinium 158-160 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 14-29 2130511-18 1990 Activation of phospholipase D (PLD) was demonstrated by the finding that phosphatidic acid increased in response to PMA or carbachol prior to the increase in PA. Protactinium 158-160 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 31-34 2505772-7 1989 By comparing the 3H/32P ratios of PA and PEt to that of PC, it is concluded that PA and PEt are formed exclusively by a PLD that catalyzes both hydrolysis and transphosphatidylation between PC and ethanol. Protactinium 34-36 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 120-123 2505772-7 1989 By comparing the 3H/32P ratios of PA and PEt to that of PC, it is concluded that PA and PEt are formed exclusively by a PLD that catalyzes both hydrolysis and transphosphatidylation between PC and ethanol. Protactinium 81-83 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 120-123 3165977-12 1988 These results constitute the first direct evidence for receptor-linked activation of PLD, leading to the generation of PA and PEt in an intact cell system. Protactinium 119-121 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 85-88 3422154-8 1988 Furthermore, PEt synthesis closely parallels PA formation and both are inhibited by an fMLP receptor antagonist, suggesting that both PA and PEt are derived from agonist-stimulated PLD action. Protactinium 134-136 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 181-184 19250975-2 2009 In particular, the LPPs are normally considered to regulate signaling by the phospholipase D (PLD) pathway by converting phosphatidate (PA) to diacylglycerol (DAG). Protactinium 136-138 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 77-92 29928916-7 2018 Compared with the serious hydrolysis in the free PLD (35.3% yield of PA), the side reaction was minimized in this work. Protactinium 69-71 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 49-52 25082152-7 2014 Such a PLD-based autophagy mechanism would involve two positive inputs: the generation of PA to help the initiation of the autophagosome and a protein-protein interaction between PLD and PKC that leads to enhanced PA. Protactinium 90-92 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 7-10 25082152-7 2014 Such a PLD-based autophagy mechanism would involve two positive inputs: the generation of PA to help the initiation of the autophagosome and a protein-protein interaction between PLD and PKC that leads to enhanced PA. Protactinium 214-216 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 7-10 25082152-7 2014 Such a PLD-based autophagy mechanism would involve two positive inputs: the generation of PA to help the initiation of the autophagosome and a protein-protein interaction between PLD and PKC that leads to enhanced PA. Protactinium 214-216 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 179-182 19250975-2 2009 In particular, the LPPs are normally considered to regulate signaling by the phospholipase D (PLD) pathway by converting phosphatidate (PA) to diacylglycerol (DAG). Protactinium 136-138 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 94-97 19250975-3 2009 LPP activities do modulate the accumulations of PA and DAG following PLD activation, but this could also involve an effect upstream of PLD activation. Protactinium 48-50 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 69-72 17540539-8 2007 Revealing that the PLD/PA pathway mediates survival of macrophages provides a potent strategy to inhibit P2X7R-mediated cytolysis by controlling PA metabolism. Protactinium 23-25 glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens 19-22