Lipid phosphate phosphatase (LPP3) and vascular development

H. Ren; M. Panchatcharam; P. Mueller; D. Escalante-Alcalde; A. J. Morris; S. S. Smyth

doi:10.1016/j.bbalip.2012.07.012

Lipid phosphate phosphatase (LPP3) and vascular development

H. Ren, M. Panchatcharam, P. Mueller, D. Escalante-Alcalde, A. J. Morris, S. S. Smyth

Internal Medicine

Research output: Contribution to journal › Review article › peer-review

38 Scopus citations

Abstract

Lipid phosphate phosphatases (LPP) are integral membrane proteins with broad substrate specificity that dephosphorylate lipid substrates including phosphatidic acid, lysophosphatidic acid, ceramide 1-phosphate, sphingosine 1-phosphate, and diacylglycerol pyrophosphate. Although the three mammalian enzymes (LPP1-3) demonstrate overlapping catalytic activities and substrate preferences in vitro, the phenotypes of mice with targeted inactivation of the Ppap2 genes encoding the LPP enzymes reveal nonredundant functions. A specific role for LPP3 in vascular development has emerged from studies of mice lacking Ppap2b. A meta-analysis of multiple, large genome-wide association studies identified a single nucleotide polymorphism in PPAP2B as a novel predictor of coronary artery disease. In this review, we will discuss the evidence that links LPP3 to vascular development and disease and evaluate potential molecular mechanisms. This article is part of a Special Issue entitled Advances in Lysophospholipid Research.

Original language	English
Pages (from-to)	126-132
Number of pages	7
Journal	Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids
Volume	1831
Issue number	1
DOIs	https://doi.org/10.1016/j.bbalip.2012.07.012
State	Published - Jan 2013

Bibliographical note

Funding Information:
The authors thank Matt Hazard for assistance with graphics. This work was supported in part by the National Center for Research Resources and the National Center for Advancing Translational Sciences ( UL1RR033173 ), the Heart Lung and Blood Institute ( R01HL078663 ), the National Center for Research Resources ( P20RR021954 ), the National Institute of General Medical Sciences ( P20GM103527 ) and by CONACYT and PAPIIT grants to D.E.-A. The content is solely the responsibility of the authors and does not necessarily represent the official views of the NIH. This material is also based on work supported in part by resources at the Lexington VA Medical Center. HR was supported in part by a Beginning Grant in Aid from the American Heart Association ; MP by a Scientist Development Award from the American Heart Association , and PM by T32HL072743 from the Heart Lung and Blood Institute .

Keywords

Endothelial cell
Lysophosphatidic acid
Lysophospholipid
Sphingosine-1-phosphate
Vascular development

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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10.1016/j.bbalip.2012.07.012

Cite this

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title = "Lipid phosphate phosphatase (LPP3) and vascular development",

abstract = "Lipid phosphate phosphatases (LPP) are integral membrane proteins with broad substrate specificity that dephosphorylate lipid substrates including phosphatidic acid, lysophosphatidic acid, ceramide 1-phosphate, sphingosine 1-phosphate, and diacylglycerol pyrophosphate. Although the three mammalian enzymes (LPP1-3) demonstrate overlapping catalytic activities and substrate preferences in vitro, the phenotypes of mice with targeted inactivation of the Ppap2 genes encoding the LPP enzymes reveal nonredundant functions. A specific role for LPP3 in vascular development has emerged from studies of mice lacking Ppap2b. A meta-analysis of multiple, large genome-wide association studies identified a single nucleotide polymorphism in PPAP2B as a novel predictor of coronary artery disease. In this review, we will discuss the evidence that links LPP3 to vascular development and disease and evaluate potential molecular mechanisms. This article is part of a Special Issue entitled Advances in Lysophospholipid Research.",

keywords = "Endothelial cell, Lysophosphatidic acid, Lysophospholipid, Sphingosine-1-phosphate, Vascular development",

author = "H. Ren and M. Panchatcharam and P. Mueller and D. Escalante-Alcalde and Morris, {A. J.} and Smyth, {S. S.}",

note = "Funding Information: The authors thank Matt Hazard for assistance with graphics. This work was supported in part by the National Center for Research Resources and the National Center for Advancing Translational Sciences ( UL1RR033173 ), the Heart Lung and Blood Institute ( R01HL078663 ), the National Center for Research Resources ( P20RR021954 ), the National Institute of General Medical Sciences ( P20GM103527 ) and by CONACYT and PAPIIT grants to D.E.-A. The content is solely the responsibility of the authors and does not necessarily represent the official views of the NIH. This material is also based on work supported in part by resources at the Lexington VA Medical Center. HR was supported in part by a Beginning Grant in Aid from the American Heart Association ; MP by a Scientist Development Award from the American Heart Association , and PM by T32HL072743 from the Heart Lung and Blood Institute .",

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AU - Ren, H.

AU - Panchatcharam, M.

AU - Mueller, P.

AU - Escalante-Alcalde, D.

AU - Morris, A. J.

AU - Smyth, S. S.

N1 - Funding Information: The authors thank Matt Hazard for assistance with graphics. This work was supported in part by the National Center for Research Resources and the National Center for Advancing Translational Sciences ( UL1RR033173 ), the Heart Lung and Blood Institute ( R01HL078663 ), the National Center for Research Resources ( P20RR021954 ), the National Institute of General Medical Sciences ( P20GM103527 ) and by CONACYT and PAPIIT grants to D.E.-A. The content is solely the responsibility of the authors and does not necessarily represent the official views of the NIH. This material is also based on work supported in part by resources at the Lexington VA Medical Center. HR was supported in part by a Beginning Grant in Aid from the American Heart Association ; MP by a Scientist Development Award from the American Heart Association , and PM by T32HL072743 from the Heart Lung and Blood Institute .

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N2 - Lipid phosphate phosphatases (LPP) are integral membrane proteins with broad substrate specificity that dephosphorylate lipid substrates including phosphatidic acid, lysophosphatidic acid, ceramide 1-phosphate, sphingosine 1-phosphate, and diacylglycerol pyrophosphate. Although the three mammalian enzymes (LPP1-3) demonstrate overlapping catalytic activities and substrate preferences in vitro, the phenotypes of mice with targeted inactivation of the Ppap2 genes encoding the LPP enzymes reveal nonredundant functions. A specific role for LPP3 in vascular development has emerged from studies of mice lacking Ppap2b. A meta-analysis of multiple, large genome-wide association studies identified a single nucleotide polymorphism in PPAP2B as a novel predictor of coronary artery disease. In this review, we will discuss the evidence that links LPP3 to vascular development and disease and evaluate potential molecular mechanisms. This article is part of a Special Issue entitled Advances in Lysophospholipid Research.

AB - Lipid phosphate phosphatases (LPP) are integral membrane proteins with broad substrate specificity that dephosphorylate lipid substrates including phosphatidic acid, lysophosphatidic acid, ceramide 1-phosphate, sphingosine 1-phosphate, and diacylglycerol pyrophosphate. Although the three mammalian enzymes (LPP1-3) demonstrate overlapping catalytic activities and substrate preferences in vitro, the phenotypes of mice with targeted inactivation of the Ppap2 genes encoding the LPP enzymes reveal nonredundant functions. A specific role for LPP3 in vascular development has emerged from studies of mice lacking Ppap2b. A meta-analysis of multiple, large genome-wide association studies identified a single nucleotide polymorphism in PPAP2B as a novel predictor of coronary artery disease. In this review, we will discuss the evidence that links LPP3 to vascular development and disease and evaluate potential molecular mechanisms. This article is part of a Special Issue entitled Advances in Lysophospholipid Research.

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KW - Sphingosine-1-phosphate

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Lipid phosphate phosphatase (LPP3) and vascular development

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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