scholarly journals lazaro Encodes a Lipid Phosphate Phosphohydrolase that Regulates Phosphatidylinositol Turnover during Drosophila Phototransduction

Neuron ◽  
2006 ◽  
Vol 49 (4) ◽  
pp. 533-546 ◽  
Author(s):  
Isaac Garcia-Murillas ◽  
Trevor Pettitt ◽  
Elaine Macdonald ◽  
Hanneke Okkenhaug ◽  
Plamen Georgiev ◽  
...  
Keyword(s):  
Phosphatidylinositol Turnover ◽  
Lipid Phosphate ◽  
Lipid Phosphate Phosphohydrolase

scholarly journals Lipid phosphate phosphohydrolase type 1 (LPP1) degrades extracellular lysophosphatidic acid in vivo

2009 ◽  
Vol 419 (3) ◽  
pp. 611-618 ◽  
Author(s):  
Jose L. Tomsig ◽  
Ashley H. Snyder ◽  
Evgeny V. Berdyshev ◽  
Anastasia Skobeleva ◽  
Chifundo Mataya ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Lysophosphatidic Acid ◽  
Important Determinant ◽  
Lipid Mediator ◽  
Wild Type ◽  
Lipid Phosphate ◽  
Lipid Phosphate Phosphohydrolase ◽  
Catabolic Enzyme

LPA (lysophosphatidic acid) is a lipid mediator that stimulates cell proliferation and growth, and is involved in physiological and pathological processes such as wound healing, platelet activation, angiogenesis and the growth of tumours. Therefore defining the mechanisms of LPA production and degradation are of interest in understanding the regulation of these processes. Extracellular LPA synthesis is relatively well understood, whereas the mechanisms of its degradation are not. One route of LPA degradation is dephosphorylation. A candidate enzyme is the integral membrane exophosphatase LPP1 (lipid phosphate phosphohydrolase type 1). In the present paper, we report the development of a mouse wherein the LPP1 gene (Ppap2a) was disrupted. The homozygous mice, which are phenotypically unremarkable, generally lack Ppap2a mRNA, and multiple tissues exhibit a substantial (35–95%) reduction in LPA phosphatase activity. Compared with wild-type littermates, Ppap2atr/tr animals have increased levels of plasma LPA, and LPA injected intravenously is metabolized at a 4-fold lower rate. Our results demonstrate that LPA is rapidly metabolized in the bloodstream and that LPP1 is an important determinant of this turnover. These results indicate that LPP1 is a catabolic enzyme for LPA in vivo.

scholarly journals Peroxisome Proliferator-Activated ReceptorγRegulates the Expression of Lipid Phosphate Phosphohydrolase 1 in Human Vascular Endothelial Cells

PPAR Research ◽  
2014 ◽  
Vol 2014 ◽  
pp. 1-6 ◽  
Author(s):  
Yazi Huang ◽  
Beilei Zhao ◽  
Yahan Liu ◽  
Nanping Wang
Keyword(s):  
Endothelial Cells ◽  
Umbilical Vein ◽  
Mrna Level ◽  
Site Directed Mutagenesis ◽  
Luciferase Reporter ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor ◽  
Lipid Phosphate ◽  
Lipid Phosphate Phosphohydrolase

Lipid phosphate phosphohydrolase 1 (LPP1), a membrane ectophosphohydrolase regulating the availability of bioactive lipid phosphates, plays important roles in cellular signaling and physiological processes such as angiogenesis and endothelial migration. However, the regulated expression of LPP1 remains largely unknown. Here, we aimed to examine a role of peroxisome proliferator-activated receptorγ(PPARγ) in the transcriptional control ofLPP1gene expression. In human umbilical vein endothelial cells (HUVECs), quantitative reverse transcriptase polymerase chain reaction (qRT-PCR) demonstrated that activation of PPARγincreased the mRNA level of LPP1. Chromatin immunoprecipitation assay showed that PPARγbinds to the putative PPAR-responsive elements (PPREs) within the 5′-flanking region of the humanLPP1gene. Genomic fragment containing 1.7-kilobase of the promoter region was cloned by using PCR. The luciferase reporter assays demonstrated that overexpression of PPARγand rosiglitazone, a specific ligand for PPARγ, could significantly upregulate the reporter activity. However, site-directed mutagenesis of the PPRE motif abolished the induction. In conclusion, our results demonstrated that PPARγtranscriptionally activated the expression ofLPP1gene in ECs, suggesting a potential role of PPARγin the metabolism of phospholipids.

scholarly journals Lipid phosphate phosphohydrolase-1 degrades exogenous glycerolipid and sphingolipid phosphate esters

1999 ◽  
Vol 340 (3) ◽  
pp. 677 ◽  
Author(s):  
Renata JASINSKA ◽  
Qiu-Xia ZHANG ◽  
Carlos PILQUIL ◽  
Indrapal SINGH ◽  
James XU ◽  
...  
Keyword(s):  
Phosphate Esters ◽  
Lipid Phosphate ◽  
Lipid Phosphate Phosphohydrolase

Pulmonary lipid phosphate phosphohydrolase in plasma membrane signalling platforms

2001 ◽  
Vol 358 (3) ◽  
pp. 637-646 ◽  
Author(s):  
Meera NANJUNDAN ◽  
Fred POSSMAYER
Keyword(s):  
Cell Lines ◽  
Lung Tissue ◽  
Type Ii Cells ◽  
Type Ii ◽  
Rat Lung ◽  
Caveolin 1 ◽  
Type Ii Cell ◽  
Lipid Phosphate ◽  
Lipid Phosphate Phosphohydrolase ◽  
Isolated Rat

Lipid phosphate phosphohydrolase (LPP) has recently been proposed to have roles in signal transduction, acting sequentially to phospholipase D (PLD) and in attenuating the effects of phospholipid growth factors on cellular proliferation. In this study, LPP activity is reported to be enriched in lipid-rich signalling platforms isolated from rat lung tissue, isolated rat type II cells and type II cell-mouse lung epithelial cell lines (MLE12 and MLE15). Lung and cell line caveolin-enriched domains (CEDs), prepared on the basis of their detergent-insolubility in Triton X-100, contain caveolin-1 and protein kinase C isoforms. The LPP3 isoform was predominantly localized to rat lung CEDs. These lipid-rich domains, including those from isolated rat type II cells, were enriched both in phosphatidylcholine plus sphingomyelin (PC+SM) and cholesterol. Saponin treatment of MLE15 cells shifted the LPP activity, cholesterol, PC+SM and caveolin-1 from lipid microdomains to detergent-soluble fractions. Elevated LPP activity and LPP1/1a protein are present in caveolae from MLE15 cells prepared using the cationic-colloidal-silica method. In contrast, total plasma membranes had a higher abundance of LPP1/1a protein with low LPP activity. Phorbol ester treatment caused a 3.8-fold increase in LPP specific activity in MLE12 CEDs. Thus the activated form of LPP1/1a may be recruited into caveolae/rafts. Transdifferentiation of type II cells into a type I-like cell demonstrated enrichment in caveolin-1 levels and LPP activity. These results indicate that LPP is localized in caveolae and/or rafts in lung tissue, isolated type II cells and type II cell lines and is consistent with a role for LPP in both caveolae/raft signalling and caveolar dynamics.

scholarly journals Lipid phosphate phosphohydrolase-1 degrades exogenous glycerolipid and sphingolipid phosphate esters

1999 ◽  
Vol 340 (3) ◽  
pp. 677-686 ◽  
Author(s):  
Renata JASINSKA ◽  
Qiu-Xia ZHANG ◽  
Carlos PILQUIL ◽  
Indrapal SINGH ◽  
James XU ◽  
...  
Keyword(s):  
Plasma Membranes ◽  
Cell Signalling ◽  
Mitogen Activated Protein Kinase ◽  
C Terminus ◽  
Liver Cdna Library ◽  
Mitogen Activated Protein ◽  
Sphingosine 1 Phosphate ◽  
Lipid Phosphate ◽  
Lipid Phosphate Phosphohydrolase ◽  
Ceramide 1

Lipid phosphate phosphohydrolase (LPP)-1 cDNA was cloned from a rat liver cDNA library. It codes for a 32-kDa protein that shares 87 and 82% amino acid sequence identities with putative products of murine and human LPP-1 cDNAs, respectively. Membrane fractions of rat2 fibroblasts that stably expressed mouse or rat LPP-1 exhibited 3.1-3.6-fold higher specific activities for phosphatidate dephosphorylation compared with vector controls. Increases in the dephosphorylation of lysophosphatidate, ceramide 1-phosphate, sphingosine 1-phosphate and diacylglycerol pyrophosphate were similar to those for phosphatidate. Rat2 fibroblasts expressing mouse LPP-1 cDNA showed 1.6-2.3-fold increases in the hydrolysis of exogenous lysophosphatidate, phosphatidate and ceramide 1-phosphate compared with vector control cells. Recombinant LPP-1 was located partially in plasma membranes with its C-terminus on the cytosolic surface. Lysophosphatidate dephosphorylation was inhibited by extracellular Ca2+ and this inhibition was diminished by extracellular Mg2+. Changing intracellular Ca2+ concentrations did not alter exogenous lysophosphatidate dephosphorylation significantly. Permeabilized fibroblasts showed relatively little latency for the dephosphorylation of exogenous lysophosphatidate. LPP-1 expression decreased the activation of mitogen-activated protein kinase and DNA synthesis by exogenous lysophosphatidate. The product of LPP-1 cDNA is concluded to act partly to degrade exogenous lysophosphatidate and thereby regulate its effects on cell signalling.

Pulmonary phosphatidic acid phosphatase and lipid phosphate phosphohydrolase

2003 ◽  
Vol 284 (1) ◽  
pp. L1-L23 ◽  
Author(s):  
Meera Nanjundan ◽  
Fred Possmayer
Keyword(s):  
Acid Phosphatase ◽  
Phosphatidic Acid ◽  
Transmembrane Domain ◽  
Neutral Lipids ◽  
Alveolar Type ◽  
Type I ◽  
Sulfhydryl Reagent ◽  
Phosphatidic Acid Phosphatase ◽  
Lipid Phosphate ◽  
Lipid Phosphate Phosphohydrolase

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.

Murine lipid phosphate phosphohydrolase-3 acts as a cell-associated integrin ligand

2005 ◽  
Vol 335 (3) ◽  
pp. 906-919 ◽  
Author(s):  
Joseph O. Humtsoe ◽  
Rodney A. Bowling ◽  
Shu Feng ◽  
Kishore K. Wary
Keyword(s):  
A Cell ◽  
Lipid Phosphate ◽  
Integrin Ligand ◽  
Lipid Phosphate Phosphohydrolase

scholarly journals Decreased Peritoneal Ovarian Cancer Growth in Mice Lacking Expression of Lipid Phosphate Phosphohydrolase 1

PLoS ONE ◽  
2015 ◽  
Vol 10 (3) ◽  
pp. e0120071 ◽  
Author(s):  
John Nakayama ◽  
Timothy A. Raines ◽  
Kevin R. Lynch ◽  
Jill K. Slack-Davis
Keyword(s):  
Ovarian Cancer ◽  
Cancer Growth ◽  
Lipid Phosphate ◽  
Lipid Phosphate Phosphohydrolase

Enhancement of the Release Reaction Not Accompanied with Enhanced Phosphatidylinositol Turnover in the Reserpinized Rabbit Blood Platelets

1983 ◽  
Vol 50 (02) ◽  
pp. 595-600 ◽  
Author(s):  
Y Watanabe ◽  
M Soda ◽  
N Fukamachi ◽  
B Kobayashi
Keyword(s):  
Phosphatidic Acid ◽  
Blood Platelets ◽  
Specific Protein ◽  
The Other ◽  
Release Reaction ◽  
Rabbit Blood ◽  
Phosphatidylinositol Turnover ◽  
Activated State ◽  
32P Incorporation ◽  
Platelet Release

SummaryThrombin-induced platelet release reaction examined with secretion of calcium and N-acetylglucosaminidase was significantly enhanced in the platelets from reserpine-treated rabbits as compared with the control. On the other hand, 32P-incorporation into phosphatidic acid was suppressed in the reserpinized platelets in activated state. Thrombin induced phosphatidylinositol (PI)- breakdown, which was examined by decreases in radioactivity and content of PI, and an increase in diacylglycerol, was not enhanced in the reserpinized platelets as compared with the control. The phosphorylation of the specific protein coupled to thrombin- induced platelet PI-breakdown was not stimulated in the reserpinized platelets as compared with the control. In contrast to PI, PC-degradation by thrombin was significantly stimulated in the reserpinized platelets. Possible existence of pathway(s) other than that associated with an enhancement of Pl-tumover is conceivable as a mechanism involved in platelet release reaction.

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