Adiponutrin Functions as a Nutritionally Regulated Lysophosphatidic Acid Acyltransferase
Numerous studies in humans link a nonsynonymous genetic polymorphism (I148M) in adiponutrin (ADPN) to various forms of fatty liver disease and liver cirrhosis. Despite its high clinical relevance, the molecular function of ADPN and the mechanism by which I148M variant affects hepatic metabolism are...
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| Published in | Cell metabolism Vol. 15; no. 5; pp. 691 - 702 |
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| Main Authors | , , , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
02.05.2012
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| Subjects | |
| Online Access | Get full text |
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| Abstract | Numerous studies in humans link a nonsynonymous genetic polymorphism (I148M) in adiponutrin (ADPN) to various forms of fatty liver disease and liver cirrhosis. Despite its high clinical relevance, the molecular function of ADPN and the mechanism by which I148M variant affects hepatic metabolism are unclear. Here we show that ADPN promotes cellular lipid synthesis by converting lysophosphatidic acid (LPA) into phosphatidic acid. The ADPN-catalyzed LPA acyltransferase (LPAAT) reaction is specific for LPA and long-chain acyl-CoAs. Wild-type mice receiving a high-sucrose diet exhibit substantial upregulation of Adpn in the liver and a concomitant increase in LPAAT activity. In Adpn-deficient mice, this diet-induced increase in hepatic LPAAT activity is reduced. Notably, the I148M variant of human ADPN exhibits increased LPAAT activity leading to increased cellular lipid accumulation. This gain of function provides a plausible biochemical mechanism for the development of liver steatosis in subjects carrying the I148M variant.
► Adiponutrin acts as a lysophosphatidic acid acyltransferase ► I148M variant of ADPN represents a gain-of-function mutation ► Adpn-deficient mice on high-sucrose diet exhibit diminished hepatic LPAAT activity ► Overexpression of I148M-ADPN causes increased FFA incorporation into glycerolipids |
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| AbstractList | Numerous studies in humans link a nonsynonymous genetic polymorphism (I148M) in adiponutrin (ADPN) to various forms of fatty liver disease and liver cirrhosis. Despite its high clinical relevance, the molecular function of ADPN and the mechanism by which I148M variant affects hepatic metabolism are unclear. Here we show that ADPN promotes cellular lipid synthesis by converting lysophosphatidic acid (LPA) into phosphatidic acid. The ADPN-catalyzed LPA acyltransferase (LPAAT) reaction is specific for LPA and long-chain acyl-CoAs. Wild-type mice receiving a high-sucrose diet exhibit substantial upregulation of Adpn in the liver and a concomitant increase in LPAAT activity. In Adpn-deficient mice, this diet-induced increase in hepatic LPAAT activity is reduced. Notably, the I148M variant of human ADPN exhibits increased LPAAT activity leading to increased cellular lipid accumulation. This gain of function provides a plausible biochemical mechanism for the development of liver steatosis in subjects carrying the I148M variant.Numerous studies in humans link a nonsynonymous genetic polymorphism (I148M) in adiponutrin (ADPN) to various forms of fatty liver disease and liver cirrhosis. Despite its high clinical relevance, the molecular function of ADPN and the mechanism by which I148M variant affects hepatic metabolism are unclear. Here we show that ADPN promotes cellular lipid synthesis by converting lysophosphatidic acid (LPA) into phosphatidic acid. The ADPN-catalyzed LPA acyltransferase (LPAAT) reaction is specific for LPA and long-chain acyl-CoAs. Wild-type mice receiving a high-sucrose diet exhibit substantial upregulation of Adpn in the liver and a concomitant increase in LPAAT activity. In Adpn-deficient mice, this diet-induced increase in hepatic LPAAT activity is reduced. Notably, the I148M variant of human ADPN exhibits increased LPAAT activity leading to increased cellular lipid accumulation. This gain of function provides a plausible biochemical mechanism for the development of liver steatosis in subjects carrying the I148M variant. Numerous studies in humans link a nonsynonymous genetic polymorphism (I148M) in adiponutrin (ADPN) to various forms of fatty liver disease and liver cirrhosis. Despite its high clinical relevance, the molecular function of ADPN and the mechanism by which I148M variant affects hepatic metabolism are unclear. Here we show that ADPN promotes cellular lipid synthesis by converting lysophosphatidic acid (LPA) into phosphatidic acid. The ADPN-catalyzed LPA acyltransferase (LPAAT) reaction is specific for LPA and long-chain acyl-CoAs. Wild-type mice receiving a high-sucrose diet exhibit substantial upregulation of Adpn in the liver and a concomitant increase in LPAAT activity. In Adpn-deficient mice, this diet-induced increase in hepatic LPAAT activity is reduced. Notably, the I148M variant of human ADPN exhibits increased LPAAT activity leading to increased cellular lipid accumulation. This gain of function provides a plausible biochemical mechanism for the development of liver steatosis in subjects carrying the I148M variant. Numerous studies in humans link a nonsynonymous genetic polymorphism (I148M) in adiponutrin (ADPN) to various forms of fatty liver disease and liver cirrhosis. Despite its high clinical relevance, the molecular function of ADPN and the mechanism by which I148M variant affects hepatic metabolism are unclear. Here we show that ADPN promotes cellular lipid synthesis by converting lysophosphatidic acid (LPA) into phosphatidic acid. The ADPN-catalyzed LPA acyltransferase (LPAAT) reaction is specific for LPA and long-chain acyl-CoAs. Wild-type mice receiving a high-sucrose diet exhibit substantial upregulation of Adpn in the liver and a concomitant increase in LPAAT activity. In Adpn-deficient mice, this diet-induced increase in hepatic LPAAT activity is reduced. Notably, the I148M variant of human ADPN exhibits increased LPAAT activity leading to increased cellular lipid accumulation. This gain of function provides a plausible biochemical mechanism for the development of liver steatosis in subjects carrying the I148M variant. ► Adiponutrin acts as a lysophosphatidic acid acyltransferase ► I148M variant of ADPN represents a gain-of-function mutation ► Adpn-deficient mice on high-sucrose diet exhibit diminished hepatic LPAAT activity ► Overexpression of I148M-ADPN causes increased FFA incorporation into glycerolipids |
| Author | Chitraju, Chandramohan Paar, Margret Scott, Sarah A. Eder, Sandra Rechberger, Gerald N. Wongsiriroj, Nuttaporn Rangrez, Ashraf Y. Nagy, Harald M. Kumari, Manju Lass, Achim Zimmermann, Robert Ivanova, Pavlina T. Brown, H. Alex Knittelfelder, Oskar Birner-Gruenberger, Ruth Schoiswohl, Gabriele Zechner, Rudolf Oberer, Monika Kershaw, Erin E. Cornaciu, Irina Haemmerle, Guenter |
| AuthorAffiliation | 5 Proteomics Core Facility, Institute of Pathology and Centre of Medical Research, Medical University of Graz, Graz, A-8010, Austria 4 Department of Pharmacology and Chemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-6600, USA 1 Institute of Molecular Biosciences, University of Graz, Graz, A-8010, Austria 2 Division of Endocrinology and Metabolism, Department of Medicine, University of Pittsburgh, Pittsburgh, PA 15261, USA 3 Department of Internal Medicine III, Cardiology and Angiology, University Hospital Schleswig-Holstein, Kiel, D-24105, Germany |
| AuthorAffiliation_xml | – name: 1 Institute of Molecular Biosciences, University of Graz, Graz, A-8010, Austria – name: 3 Department of Internal Medicine III, Cardiology and Angiology, University Hospital Schleswig-Holstein, Kiel, D-24105, Germany – name: 4 Department of Pharmacology and Chemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-6600, USA – name: 5 Proteomics Core Facility, Institute of Pathology and Centre of Medical Research, Medical University of Graz, Graz, A-8010, Austria – name: 2 Division of Endocrinology and Metabolism, Department of Medicine, University of Pittsburgh, Pittsburgh, PA 15261, USA |
| Author_xml | – sequence: 1 givenname: Manju surname: Kumari fullname: Kumari, Manju organization: Institute of Molecular Biosciences, University of Graz, Graz, A-8010, Austria – sequence: 2 givenname: Gabriele surname: Schoiswohl fullname: Schoiswohl, Gabriele organization: Institute of Molecular Biosciences, University of Graz, Graz, A-8010, Austria – sequence: 3 givenname: Chandramohan surname: Chitraju fullname: Chitraju, Chandramohan organization: Institute of Molecular Biosciences, University of Graz, Graz, A-8010, Austria – sequence: 4 givenname: Margret surname: Paar fullname: Paar, Margret organization: Institute of Molecular Biosciences, University of Graz, Graz, A-8010, Austria – sequence: 5 givenname: Irina surname: Cornaciu fullname: Cornaciu, Irina organization: Institute of Molecular Biosciences, University of Graz, Graz, A-8010, Austria – sequence: 6 givenname: Ashraf Y. surname: Rangrez fullname: Rangrez, Ashraf Y. organization: Department of Internal Medicine III, Cardiology and Angiology, University Hospital Schleswig-Holstein, Kiel, D-24105, Germany – sequence: 7 givenname: Nuttaporn surname: Wongsiriroj fullname: Wongsiriroj, Nuttaporn organization: Institute of Molecular Biosciences, University of Graz, Graz, A-8010, Austria – sequence: 8 givenname: Harald M. surname: Nagy fullname: Nagy, Harald M. organization: Institute of Molecular Biosciences, University of Graz, Graz, A-8010, Austria – sequence: 9 givenname: Pavlina T. surname: Ivanova fullname: Ivanova, Pavlina T. organization: Department of Pharmacology and Chemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-6600, USA – sequence: 10 givenname: Sarah A. surname: Scott fullname: Scott, Sarah A. organization: Department of Pharmacology and Chemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-6600, USA – sequence: 11 givenname: Oskar surname: Knittelfelder fullname: Knittelfelder, Oskar organization: Institute of Molecular Biosciences, University of Graz, Graz, A-8010, Austria – sequence: 12 givenname: Gerald N. surname: Rechberger fullname: Rechberger, Gerald N. organization: Institute of Molecular Biosciences, University of Graz, Graz, A-8010, Austria – sequence: 13 givenname: Ruth surname: Birner-Gruenberger fullname: Birner-Gruenberger, Ruth organization: Proteomics Core Facility, Institute of Pathology and Centre of Medical Research, Medical University of Graz, Graz, A-8010, Austria – sequence: 14 givenname: Sandra surname: Eder fullname: Eder, Sandra organization: Institute of Molecular Biosciences, University of Graz, Graz, A-8010, Austria – sequence: 15 givenname: H. Alex surname: Brown fullname: Brown, H. Alex organization: Department of Pharmacology and Chemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-6600, USA – sequence: 16 givenname: Guenter surname: Haemmerle fullname: Haemmerle, Guenter organization: Institute of Molecular Biosciences, University of Graz, Graz, A-8010, Austria – sequence: 17 givenname: Monika surname: Oberer fullname: Oberer, Monika organization: Institute of Molecular Biosciences, University of Graz, Graz, A-8010, Austria – sequence: 18 givenname: Achim surname: Lass fullname: Lass, Achim organization: Institute of Molecular Biosciences, University of Graz, Graz, A-8010, Austria – sequence: 19 givenname: Erin E. surname: Kershaw fullname: Kershaw, Erin E. organization: Division of Endocrinology and Metabolism, Department of Medicine, University of Pittsburgh, Pittsburgh, PA 15261, USA – sequence: 20 givenname: Robert surname: Zimmermann fullname: Zimmermann, Robert email: robert.zimmermann@uni-graz.at organization: Institute of Molecular Biosciences, University of Graz, Graz, A-8010, Austria – sequence: 21 givenname: Rudolf surname: Zechner fullname: Zechner, Rudolf email: rudolf.zechner@uni-graz.at organization: Institute of Molecular Biosciences, University of Graz, Graz, A-8010, Austria |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/22560221$$D View this record in MEDLINE/PubMed |
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| ContentType | Journal Article |
| Copyright | 2012 Elsevier Inc. Copyright © 2012 Elsevier Inc. All rights reserved. 2012 Elsevier Inc. 2012 |
| Copyright_xml | – notice: 2012 Elsevier Inc. – notice: Copyright © 2012 Elsevier Inc. All rights reserved. – notice: 2012 Elsevier Inc. 2012 |
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| Snippet | Numerous studies in humans link a nonsynonymous genetic polymorphism (I148M) in adiponutrin (ADPN) to various forms of fatty liver disease and liver cirrhosis.... |
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| SubjectTerms | 1-Acylglycerol-3-Phosphate O-Acyltransferase - genetics 1-Acylglycerol-3-Phosphate O-Acyltransferase - metabolism Acyl Coenzyme A - genetics Acyl Coenzyme A - metabolism Acyltransferases - genetics Acyltransferases - metabolism Animals Chlorocebus aethiops CHO Cells COS Cells Cricetinae Cysteine Endopeptidases - genetics Cysteine Endopeptidases - metabolism diet Dietary Sucrose - metabolism fatty liver Fatty Liver - genetics Fatty Liver - metabolism genetic polymorphism Hep G2 Cells Humans Lipid Metabolism - genetics Lipids - biosynthesis Lipids - genetics liver Liver - drug effects Liver - metabolism liver cirrhosis Lysophospholipids - genetics Lysophospholipids - metabolism Male Membrane Proteins - genetics Membrane Proteins - metabolism metabolism Mice Mice, Knockout Models, Molecular Phosphatidic Acids - genetics Phosphatidic Acids - metabolism Phospholipids - genetics Phospholipids - metabolism Polymorphism, Genetic Triglycerides - genetics Triglycerides - metabolism Up-Regulation |
| Title | Adiponutrin Functions as a Nutritionally Regulated Lysophosphatidic Acid Acyltransferase |
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