Mammalian Lipid Phosphate Phosphohydrolases

Brindley, David N.; Waggoner, David W.

doi:10.1074/jbc.273.38.24281

Cited by 245 publications

(247 citation statements)

References 52 publications

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“…At present little is known about the regulation of LPP activity, although it appears this enzyme could potentially be phosphorylated at the NH 2 or COOH terminus (25). Exposure of MLE12 cells to PMA for 5 min did not affect specific activity assayed with total membranes but resulted in an approximately threefold increase in LPP activity (4.8-14.5% of total) associated with DIGs (176).…”

Section: Lpp In Signaling Platformsmentioning

confidence: 99%

“…With this mechanism, PLD1 activation arises through PKC-␣-dependent phosphorylation in caveolae. It is thought that LPP may be phosphorylated (25), but whether phosphorylation affects LPP activity and whether this occurs in caveolae must still be demonstrated.…”

Section: Lpp In Signaling Platformsmentioning

confidence: 99%

“…Originally considered only for its role in glycerolipid biosynthesis, it has recently been demonstrated that this phosphohydrolase plays an important role as a modulator of cell signaling in relation to cell mobility, differentiation, growth, and survival (24,25,31,120,260).…”

mentioning

confidence: 99%

“…Unlike PAP1, which is highly specific for the Mg 2ϩ salts of PA and LPA, PAP2 degrades a number of lipid phosphates, including S1P, ceramide-1-phosphate (C1P), as well as PA and LPA, does not require specific ions, and is heat and sulphhydryl reagent resistant. It has consequently been suggested that PAP2 be designated lipid phosphate phosphatase (LPP) (25,107,260).…”

mentioning

confidence: 99%

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Pulmonary phosphatidic acid phosphatase and lipid phosphate phosphohydrolase

Nanjundan

Possmayer

2003

American Journal of Physiology-Lung Cellular and Molecular Phys

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The lung contains two distinct forms of phosphatidic acid phosphatase (PAP). PAP1 is a cytosolic enzyme that is activated through fatty acid-induced translocation to the endoplasmic reticulum, where it converts phosphatidic acid (PA) to diacylglycerol (DAG) for the biosynthesis of phospholipids and neutral lipids. PAP1 is Mg2+ dependent and sulfhydryl reagent sensitive. PAP2 is a six-transmembrane-domain integral protein localized to the plasma membrane. Because PAP2 degrades sphingosine-1-phosphate (S1P) and ceramide-1-phosphate in addition to PA and lyso-PA, it has been renamed lipid phosphate phosphohydrolase (LPP). LPP is Mg2+independent and sulfhydryl reagent insensitive. This review describes LPP isoforms found in the lung and their location in signaling platforms (rafts/caveolae). Pulmonary LPPs likely function in the phospholipase D pathway, thereby controlling surfactant secretion. Through lowering the levels of lyso-PA and S1P, which serve as agonists for endothelial differentiation gene receptors, LPPs regulate cell division, differentiation, apoptosis, and mobility. LPP activity could also influence transdifferentiation of alveolar type II to type I cells. It is considered likely that these lipid phosphohydrolases have critical roles in lung morphogenesis and in acute lung injury and repair.

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Section: Lpp In Signaling Platformsmentioning

confidence: 99%

Section: Lpp In Signaling Platformsmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Pulmonary phosphatidic acid phosphatase and lipid phosphate phosphohydrolase

Nanjundan

Possmayer

2003

American Journal of Physiology-Lung Cellular and Molecular Phys

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“…The action of phophatidylinositol phospholipase C provides both diacylglycerol and inositol trisphosphate. Other hydrolases include secreted and extracellular membrane-associated phosphatidic acid phosphatases which act on 1,2-diacyl,sn-glycerol phosphate to produce diacylglycerol and inorganic phosphate (Brindley & Waggoner, 1998), however, the membrane-associated hydrolases also act on a variety of phospholipids to generate anionic and/or neutral lipids (Nanjundan & Possmayer, 2003). These hydrolases may also be active against the rich phospholipid content of the cell wall of M.tb.…”

Section: Alveolar Epithelial Cellsmentioning

confidence: 99%

Broadening Our View About the Role of Mycobacterium tuberculosis Cell Envelope Components During Infection: A Battle for Survival

Torrelles¹

2012

Understanding Tuberculosis - Analyzing the Origin of Mycobacterium Tuberculosis Pathogenicity

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Induction of endothelial monolayer permeability by phosphatidate

et al. 1999

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Released into the vasculature from disrupted cells or transported to the surface of adjacent effectors, phosphatidate and related lipids may potentiate endothelial cell activation. However, the effect of these lipids on endothelial monolayer barrier integrity has not been reported. The present study documents the induction of endothelial monolayer permeability by phosphatidate. Both long (di-C18:1) and medium (di-C10; di-C8) chain length phosphatidates increased permeability of bovine pulmonary artery endothelial cell monolayers assessed using a well characterized assay system in vitro. Barrier disruption effected by dioctanoyl (di-C8) phosphatidate was markedly potentiated by the addition of propranolol, an inhibitor of endothelial cell "ecto"-phosphatidate phosphohydrolase (PAP), a lipid phosphate phosphohydrolase (LPP) that efficiently hydrolyzes extracellular substrate. Disruption of barrier function by phosphatidate did not result from its non-specific detergent characteristics, since a non-hydrolyzable but biologically inactive phosphonate analog of dioctanoyl phosphatidate, which retains the detergent characteristics of phosphatidate, did not induce permeability changes. Furthermore, neither diacylglycerol nor lyso-PA effected significant increases in monolayer permeability, indicating the observed response was due to phosphatidate rather than one of its metabolites. Phosphatidate-induced permeability was attenuated by preincubation of endothelial cells with the tyrosine kinase inhibitor, herbimycin A (10 microg/ml), and enhanced by the tyrosine phosphatase inhibitor, vanadate (100 microM), implicating a role for activation of intracellular tyrosine kinases in the response. In addition, phosphatidate increased the levels of intracellular free Ca(2+) in endothelial cells and ligated specific binding sites on endothelial cell plasma membranes, consistent with the presence of a phosphatidate receptor. Since phosphatidate generated within the plasma membrane of adherent effectors potentially interacts with endothelial membranes, we evaluated the influence of phosphatidate-enriched neutrophil plasma membranes on endothelial monolayer integrity. The effects of ectopic phosphatidate on endothelial monolayer permeability were mimicked by phosphatidate confined to neutrophil plasma membranes. We conclude that phosphatidate may be a physiologic modulator of endothelial monolayer permeability that exerts its effects by activating a receptor-linked, tyrosine kinase-dependent process which results in mobilization of intracellular stored Ca(2+)and consequent metabolic activation.

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Mammalian Lipid Phosphate Phosphohydrolases

Cited by 245 publications

References 52 publications

Pulmonary phosphatidic acid phosphatase and lipid phosphate phosphohydrolase

Pulmonary phosphatidic acid phosphatase and lipid phosphate phosphohydrolase

Broadening Our View About the Role of Mycobacterium tuberculosis Cell Envelope Components During Infection: A Battle for Survival

Induction of endothelial monolayer permeability by phosphatidate

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