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

scholarly journals Lipid Phosphate Phosphatases Regulate Lysophosphatidic Acid Production and Signaling in Platelets

2003 ◽  
Vol 278 (44) ◽  
pp. 43214-43223 ◽  
Author(s):  
Susan S. Smyth ◽  
Vicki A. Sciorra ◽  
Yury J. Sigal ◽  
Zehra Pamuklar ◽  
Zuncai Wang ◽  
...  
Keyword(s):  
Lysophosphatidic Acid ◽  
Acid Production ◽  
Lipid Phosphate ◽  
Lipid Phosphate Phosphatases

scholarly journals Autotaxin-LPA-LPP3 Axis in Energy Metabolism and Metabolic Disease

2021 ◽  
Vol 22 (17) ◽  
pp. 9575
Author(s):  
Anu Jose ◽  
Petra C. Kienesberger
Keyword(s):  
Metabolic Disease ◽  
Lysophosphatidic Acid ◽  
Fatty Liver Disease ◽  
Energy Homeostasis ◽  
Membrane Component ◽  
Metabolic Complications ◽  
Lpa Receptors ◽  
Lipid Phosphate ◽  
Lipid Phosphate Phosphatases

Besides serving as a structural membrane component and intermediate of the glycerolipid metabolism, lysophosphatidic acid (LPA) has a prominent role as a signaling molecule through its binding to LPA receptors at the cell surface. Extracellular LPA is primarily produced from lysophosphatidylcholine (LPC) through the activity of secreted lysophospholipase D, autotaxin (ATX). The degradation of extracellular LPA to monoacylglycerol is mediated by lipid phosphate phosphatases (LPPs) at the cell membrane. This review summarizes and interprets current literature on the role of the ATX-LPA-LPP3 axis in the regulation of energy homeostasis, insulin function, and adiposity at baseline and under conditions of obesity. We also discuss how the ATX-LPA-LPP3 axis influences obesity-related metabolic complications, including insulin resistance, fatty liver disease, and cardiomyopathy.

scholarly journals Lipid Phosphate Phosphatase 3 regulates Lysophosphatidic Acid mediated vascular response in diabetic vascular injury

2021 ◽  
Vol 35 (S1) ◽  
Author(s):  
Utsab Subedi ◽  
Susmita Bhattarai ◽  
Sudha Sharma ◽  
Hosne Ara ◽  
Md Shenuarin Bhuiyan ◽  
...  
Keyword(s):  
Vascular Injury ◽  
Lysophosphatidic Acid ◽  
Vascular Response ◽  
Lipid Phosphate

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

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 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.

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