Lipid phosphate phosphatases and lipid phosphate signalling

2005 ◽  
Vol 33 (6) ◽  
pp. 1370 ◽  
Author(s):  
J.S. Long ◽  
S. Pyne ◽  
N.T. Ktistakis ◽  
N.J. Pyne
Keyword(s):  
Lipid Phosphate ◽  
Lipid Phosphate Phosphatases

scholarly journals Lysophosphatidic Acid-induced Mitogenesis Is Regulated by Lipid Phosphate Phosphatases and Is Edg-receptor Independent

2000 ◽  
Vol 276 (7) ◽  
pp. 4611-4621 ◽  
Author(s):  
Shelley B. Hooks ◽  
Webster L. Santos ◽  
Dong-Soon Im ◽  
Christopher E. Heise ◽  
Timothy L. Macdonald ◽  
...  
Keyword(s):  
Lysophosphatidic Acid ◽  
Lipid Phosphate ◽  
Lipid Phosphate Phosphatases

Abstract 203: Regulation of Lipid Phosphate Phosphatase 3 in Cardiac Ischemia/Reperfusion Injury and Hypertrophy

2016 ◽  
Vol 36 (suppl_1) ◽  
Author(s):  
Mini Chandra ◽  
Jonathan Fox ◽  
Wayne Orr ◽  
Christopher Kevil ◽  
Sumitra Miriyala ◽  
...  
Keyword(s):  
Ischemia Reperfusion Injury ◽  
Ischemia Reperfusion ◽  
Cardiac Injury ◽  
Negative Regulator ◽  
Cardiomyocyte Hypertrophy ◽  
Acute Mi ◽  
Lipid Phosphate ◽  
Lipid Phosphate Phosphatases ◽  
Old Mice

Generation of reactive oxygen species (ROS) has been implicated in myocardial infarction (MI), stroke and sudden cardiac death. Mitochondrial respiration is a major source of ROS production and lipids regulate mitochondrial oxidative metabolism and homeostasis through effects on mitochondrial fusion and fission and on the activity of mitochondrial membrane proteins. Lipid phosphate phosphatases (LPPs) control the conversion of bioactive lipid phosphates to their dephosphorylated counterparts. These include phosphatidic acid (PA), and lysophosphatidic acid (LPA). Oxidative stress was identified to transactivate microRNA-92a, which is a negative regulator of LPP3. We found that LPP3 expression was markedly down regulated in ischemic regions after ischemia/reperfusion (I/R) injury. We observed a similar trend in the myocardium from patients with acute MI at 24h. Our in vitro studies indicate that overexpression of LPP3 protects the cardiomyocyte against ROS-induced cardiac injury and reduction of LPP3 by conditional specific cardiac knockout of the LPP3 gene in mice increases cardiac dysfunction and mortality. These mice are viable and fertile but showed increased mortality ~8 months (Fig1). Blood pressure was similar in LPP3 fl/fl (96 ± 9 mmHg; n = 19) and Myh6- LPP3 Δ mice (92 ± 7 mmHg; n = 19), although heart rates were significantly higher in Myh6- LPP3 Δ 3 month old mice (642 ± 21 bpm, compared to LPP3 fl/fl with 600± 17 bpm; P<0.001). Knockdown of LPP3 enhanced cardiomyocyte hypertrophy induced by LPA based on analysis of sarcomere organization, cell surface area, levels of fetal genes ANP and BNP, and ANF release from nuclei, which are hallmarks of cardiomyocyte hypertrophy, indicating that LPP3 negatively regulates cardiomyocyte hypertrophy induced by LPA.

scholarly journals Control of lateral migration and germ cell elimination by the Drosophila melanogaster lipid phosphate phosphatases Wunen and Wunen 2

2005 ◽  
Vol 171 (4) ◽  
pp. 675-683 ◽  
Author(s):  
Hiroko Sano ◽  
Andrew D. Renault ◽  
Ruth Lehmann
Keyword(s):  
Drosophila Melanogaster ◽  
Axon Guidance ◽  
Germ Cells ◽  
Primordial Germ Cells ◽  
Lateral Migration ◽  
Migration Process ◽  
The Central Nervous System ◽  
Lipid Phosphate ◽  
Lipid Phosphate Phosphatases ◽  
Single Cluster

In most organisms, primordial germ cells (PGCs) arise far from the region where somatic gonadal precursors (SGPs) are specified. Although PGCs in general originate as a single cluster of cells, the somatic parts of the gonad form on each site of the embryo. Thus, to reach the gonad, PGCs not only migrate from their site of origin but also split into two groups. Taking advantage of high-resolution real-time imaging, we show that in Drosophila melanogaster PGCs are polarized and migrate directionally toward the SGPs, avoiding the midline. Unexpectedly, neither PGC attractants synthesized in the SGPs nor known midline repellents for axon guidance were required to sort PGCs bilaterally. Repellent activity provided by wunen (wun) and wunen-2 (wun-2) expressed in the central nervous system, however, is essential in this migration process and controls PGC survival. Our results suggest that expression of wun/wun-2 repellents along the migratory paths provides faithful control over the sorting of PGCs into two gonads and eliminates PGCs left in the middle of the embryo.

scholarly journals Lipid phosphate phosphatases and their roles in mammalian physiology and pathology

2015 ◽  
Vol 56 (11) ◽  
pp. 2048-2060 ◽  
Author(s):  
Xiaoyun Tang ◽  
Matthew G. K. Benesch ◽  
David N. Brindley
Keyword(s):  
Lipid Phosphate ◽  
Lipid Phosphate Phosphatases

Co-ordinate regulation of growth factor receptors and lipid phosphate phosphatase-1 controls cell activation by exogenous lysophosphatidate

2001 ◽  
Vol 29 (6) ◽  
pp. 825-830 ◽  
Author(s):  
C. Pilquil ◽  
Z.-C. Ling ◽  
I. Singh ◽  
K. Buri ◽  
Q.-X. Zhang ◽  
...  
Keyword(s):  
Growth Factor ◽  
Cell Activation ◽  
Growth Factor Receptors ◽  
Exogenous Lipid ◽  
Edg Receptors ◽  
Sphingosine 1 Phosphate ◽  
Lipid Phosphate ◽  
Lipid Phosphate Phosphatases ◽  
Differentiation Gene

The serum-derived lipid growth factors, lysophosphatidate (LPA) and sphingosine 1-phosphate (S1P), activate cells selectively through different members of a family of endothelial differentiation gene (EDG) receptors. Activation of EDG receptors by LPA and S1P provides a variety of signalling cascades depending upon the G-protein coupling of the different EDG receptors. This leads to chemotactic and mitogenic responses, which are important in wound healing. For example, LPA stimulates fibroblast division and S1P stimulates the chemotaxis and division of endothelial cells leading to angiogenesis. Counteracting these effects of LPA and S1P, are the actions of lipid phosphate phosphatases (LPP, or phosphatidate phosphohydrolases, Type 2). The isoform LPP-1 is expressed in the plasma membrane with its active site outside the cell. This enzyme is responsible for ‘ecto-phosphatase’ activity leading to the degradation of exogenous lipid phosphate mediators, particularly LPA. Expression of LPP-1 decreases cell activation by exogenous LPA. The mechanism for this is controversial and several mechanisms have been proposed. Evidence will be presented that the LPPs cross-talk with EDG and other growth factor receptors, thus, regulating the responses of the cells to lipid phosphate mediators of signal transduction.

scholarly journals Lipid Phosphate Phosphatases inArabidopsis

2001 ◽  
Vol 276 (23) ◽  
pp. 20300-20308 ◽  
Author(s):  
Olivier Pierrugues ◽  
Catherine Brutesco ◽  
June Oshiro ◽  
Manolo Gouy ◽  
Yves Deveaux ◽  
...  
Keyword(s):  
Lipid Phosphate ◽  
Lipid Phosphate Phosphatases

scholarly journals Lipid phosphate phosphatases form homo- and hetero-oligomers: catalytic competency, subcellular distribution and function

2008 ◽  
Vol 411 (2) ◽  
pp. 371-377 ◽  
Author(s):  
Jaclyn S. Long ◽  
Nigel J. Pyne ◽  
Susan Pyne
Keyword(s):  
Recombinant Expression ◽  
Catalytic Site ◽  
Wild Type ◽  
Catalytically Active ◽  
Exclusion Chromatography ◽  
Sphingosine 1 Phosphate ◽  
Lipid Phosphate ◽  
Extracellular Side ◽  
And Function ◽  
Lipid Phosphate Phosphatases

Lipid phosphate phosphatases (LPP1–LPP3) have been topographically modelled as monomers (molecular mass of 31–36 kDa) composed of six transmembrane domains and with the catalytic site facing the extracellular side of the plasma membrane or the luminal side of intracellular membranes. The catalytic motif has three conserved domains, termed C1, C2 and C3. The C1 domain may be involved in substrate recognition, whereas C2 and C3 domains appear to participate in the catalytic dephosphorylation of the substrate. We have obtained three lines of evidence to demonstrate that LPPs exist as functional oligomers. First, we have used recombinant expression and immunoprecipitation analysis to demonstrate that LPP1, LPP2 and LPP3 form both homo- and hetero-oligomers. Secondly, large LPP oligomeric complexes that are catalytically active were isolated using gel-exclusion chromatography. Thirdly, we demonstrate that catalytically deficient guinea-pig FLAG-tagged H223L LPP1 mutant can form an oligomer with wild-type LPP1 and that wild-type LPP1 activity is preserved in the oligomer. These findings suggest that, in an oligomeric arrangement, the catalytic site of the wild-type LPP can function independently of the catalytic site of the mutant LPP. Finally, we demonstrate that endogenous LPP2 and LPP3 form homo- and hetero-oligomers, which differ in their subcellular localization and which may confer differing spatial regulation of phosphatidic acid and sphingosine 1-phosphate signalling.

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