5-Aminosalicylate stimulates phospholipase D activity in macrophages

Gómez-Muñoz, Antonio; O’Brien, Lori; Salh, Baljinder; Steinbrecher, Urs P.

doi:10.1016/s1388-1981(01)00149-4

Cited by 28 publications

(38 citation statements)

References 41 publications

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“…[21][22][23][24][25][26] The results suggest that phospholipids play a role in protecting DG-CPT from inactivation by detergents. Although the effect of PA on mammalian DG-CPT has not been described, yeast DG-CPT, which shares a homologous structure with that of mammalian DG-CPT, 27) is reported to be activated by PA with other phospholipids including lysophospholipids.…”

Section: Discussionmentioning

confidence: 99%

Regulation of Activities of Cytidine 5'-Diphospho-Choline: 1-O-Alkyl-2-Acetyl-sn-Glycerol Cholinephosphotransferase, an Enzyme Responsible for de novo Synthesis of Platelet-Activating Factor, by Membrane Phospholipids.

Satoh

Harada

Yokoyama

et al. 2003

JOURNAL OF HEALTH SCIENCE

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Cytidine 5′-diphospho (CDP)-choline: 1-O-alkyl-2-acetyl-sn-glycerol cholinephosphotransferase (AAG-CPT), an enzyme responsible for de novo synthesis of platelet-activating factor (PAF), was solubilized from porcine spleen microsomes using digitonin. Although the activity of the solubilized enzyme was relatively stable, further purification by sequential chromatography on Toyopearl HW-65 gel filtration and diethylaminoethyl (DEAE)-Toyopearl 650 caused a remarkable decrease in enzyme activity, which was partially recovered by the exogenously addition of phospholipids such as egg phosphatidylcholine, dioleoylphosphatidylcholine (DOPC), dioleoylphosphatidylethanolamine, dioleoylphosphatidylglycerol, and dioleoylphosphatidylserine. In contrast, dioleoylphosphatidic acid (DOPA) showed an inhibitory effect on enzyme activity. In addition, lysophospholipids such as monooleoylphosphatidylcholine, monooleoylphosphatidylethanolamine, monooleoylphosphatidylglycerol, and monooleoylphosphatidic acid showed an inhibitory effect on the enzyme activity. When DOPA was concomitantly added with DOPC, the enzyme activity reactivated by DOPC decreased with the ratio of DOPA to DOPC. Furthermore, we examined whether phosphatidic acid (PA) or lysophospholipids had an inhibitory effect on AAG-CPT activity under more physiological conditions. Treatment of microsomes with exogenously added phospholipase D or phospholipase A 2 resulted in a decrease in AAG-CPT. In addition, when endogenous phospholipase D was activated by fatty acids such as oleic acid and arachidonic acid to generate PA in the porcine microsomes, the enzyme activity was significantly inhibited. The molecular weight of the enzyme solubilized from porcine spleen microsomes was estimated to be 440 kDa based on gel-filtration column chromatography on Toyopearl HW-65, suggesting that this enzyme formed a complex with other protein molecules and membrane phospholipids, and that these phospholipids were necessary to maintain the enzyme activity. Our results indicate that environmental membrane phospholipids containing PA and/or lysophospholipids are important factors in the regulation of the enzyme for de novo synthesis of PAF.

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Section: Discussionmentioning

confidence: 99%

Regulation of Activities of Cytidine 5'-Diphospho-Choline: 1-O-Alkyl-2-Acetyl-sn-Glycerol Cholinephosphotransferase, an Enzyme Responsible for de novo Synthesis of Platelet-Activating Factor, by Membrane Phospholipids.

Satoh

Harada

Yokoyama

et al. 2003

JOURNAL OF HEALTH SCIENCE

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“…Chemoattractant (McMurray et al, 1993;Ryborg et al, 1994;Radu et al, 2004) IL-2Rα↑/thymidine uptake↑ (Asaoka et al, 1991;Asaoka et al, 1992) HB-EGF↑ (Nishi et al, 1997), IFN-γ↑ CD40 ligand↑ (Sakata-Kaneko et al, 1998), CXCR4↑, IL-2↑ (Han et al, 2004) Antibody formation↑, most notably IgA (Huang et al, 1999) Apoptosis↑/ROS generation↑ (Zurgil et al, 2007) p56 lck and ZAP 70 phosphorylation↑, [Ca2+] i ↑ in Jurkat cells (Legradi et al, 2004) Monocyte/macrophage Chemoattractant (Quinn et al, 1988) Activates p38 and p42/44 MAPKs in THP-1 cells (Jing et al, 2000) Mitogenic effects of acetylated LDL↑ (Sakai et al, 1994) Mature dendritic cell generation↑/CD86↑ (Coutant et al, 2002) Adhesion↑/activation of CD11b (Weber et al, 1995) IFN-γ↑ (Nakano et al, 1994), IL-1 β↑ (Liu-Wu et al, 1998), TNF-α↑ (Huang et al, 1999), MIP2↑ in RAW264.7 cells (Olofsson et al, 2008), arachidonic acid ↑ in THP-1 and Mono Mac6 cells (Oestvang et al, 2003) Phospholipase D (PLD) activity ↑ (Gómez- Muñoz et al, 1999) Extracellular acidification ↑ in RAW264.7 cells (De Vries et al, 1998) EC-SOD ↑ in U937 cells (Yamamoto et al, 2002) Ca 2+ influx ↑ in U937 human monocytes (Yun et al, 2004) De-ramification of murine microglia↑/nonselective cation current↑, calcium-activated potassium current↑/ hyperpolarization↑ (Schilling et al, 2004) …”

Section: Lymphocytementioning

confidence: 99%

“…LPC (1 µg/ml) increases phospholipase D (PLD) activity in mouse peritoneal macrophages. This effect was inhibited by down-regulation of PKC activity (with prolonged incubation with PMA), or inhibitors of tyrosine kinase (genistein) and PAFR (WEB-2086) (Gómez-Muñoz et al, 1999). Because PLD activity produces phosphatidic acid which can activate PLA 2 (Bauldry et al, 1997), PLD could be involved in LPCinduced release of arachidonic acid from THP-1 and Mono Mac6 cells (Oestvang et al, 2003).…”

Section: Neutrophilmentioning

confidence: 99%

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Immunomodulatory Actions of Lysophosphatidylcholine

Hong¹,

Song²

2008

Biomolecules and Therapeutics

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“…The molecules usually implicated in death of plaque macrophages are cytocidal lipids, 54,55 but some components of oxidized LDL can promote survival. 56 The first evidence for the oxidized lipid hypothesis appears to be an observation in the 1970s that rabbits fed purified cholesterol developed limited disease, but rabbits fed chow with "brown" cholesterol taken from a laboratory reagent bottle developed large lesions with necrotic cores.…”

Section: How Do Macrophages Die In the Plaque?mentioning

confidence: 99%

Role of Caspases in Death and Survival of the Plaque Macrophage

Nhan

Liles

2005

ATVB

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Abstract-This review considers the role of macrophage cell death in formation of the necrotic core and in plaque progression, and lists many of the possible mediators of macrophage cell death. Among these, perhaps the most cited toxic agent is oxidized low-density lipoprotein (oxLDL). Whereas oxLDL can kill macrophage, and whereas the form of death is morphologically apoptotic, caspase inhibitors appear to be ineffective in preventing death. This finding is consistent with recent literature showing how the canonical caspase pathways are used for physiological cellular functions other than cell death. Plaque macrophages appear to be among the cells with this nonapoptotic signaling function for activated caspases. In many of the other cell types, caspase activation appears to play a critical role in cell differentiation. We discuss possible functions of plaque macrophage using the nondeath caspase pathway. Recent literature shows that physiological and developmental functions of many cell types require active caspases without progressing to cell death. We discuss the role of macrophage cell death in plaque progression, possible mediators of macrophage cell death, and the possible functions of plaque macrophage using the nondeath caspase pathway.

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5-Aminosalicylate stimulates phospholipase D activity in macrophages

Cited by 28 publications

References 41 publications

Regulation of Activities of Cytidine 5'-Diphospho-Choline: 1-O-Alkyl-2-Acetyl-sn-Glycerol Cholinephosphotransferase, an Enzyme Responsible for de novo Synthesis of Platelet-Activating Factor, by Membrane Phospholipids.

Regulation of Activities of Cytidine 5'-Diphospho-Choline: 1-O-Alkyl-2-Acetyl-sn-Glycerol Cholinephosphotransferase, an Enzyme Responsible for de novo Synthesis of Platelet-Activating Factor, by Membrane Phospholipids.

Immunomodulatory Actions of Lysophosphatidylcholine

Role of Caspases in Death and Survival of the Plaque Macrophage

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