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Lipoquality control by phospholipase A(2) enzymes

The phospholipase A(2) (PLA(2)) family comprises a group of lipolytic enzymes that typically hydrolyze the sn-2 position of glycerophospholipids to give rise to fatty acids and lysophospholipids. The mammalian genome encodes more than 50 PLA(2)s or related enzymes, which are classified into several...

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Autor principal: MURAKAMI, Makoto
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Japan Academy 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5743847/
https://www.ncbi.nlm.nih.gov/pubmed/29129849
http://dx.doi.org/10.2183/pjab.93.043
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author MURAKAMI, Makoto
author_facet MURAKAMI, Makoto
author_sort MURAKAMI, Makoto
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description The phospholipase A(2) (PLA(2)) family comprises a group of lipolytic enzymes that typically hydrolyze the sn-2 position of glycerophospholipids to give rise to fatty acids and lysophospholipids. The mammalian genome encodes more than 50 PLA(2)s or related enzymes, which are classified into several subfamilies on the basis of their structures and functions. From a general viewpoint, the PLA(2) family has mainly been implicated in signal transduction, producing bioactive lipid mediators derived from fatty acids and lysophospholipids. Recent evidence indicates that PLA(2)s also contribute to phospholipid remodeling for membrane homeostasis or energy production for fatty acid β-oxidation. Accordingly, PLA(2) enzymes can be regarded as one of the key regulators of the quality of lipids, which I herein refer to as lipoquality. Disturbance of PLA(2)-regulated lipoquality hampers tissue and cellular homeostasis and can be linked to various diseases. Here I overview the current state of understanding of the classification, enzymatic properties, and physiological functions of the PLA(2) family.
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spelling pubmed-57438472018-01-04 Lipoquality control by phospholipase A(2) enzymes MURAKAMI, Makoto Proc Jpn Acad Ser B Phys Biol Sci Review The phospholipase A(2) (PLA(2)) family comprises a group of lipolytic enzymes that typically hydrolyze the sn-2 position of glycerophospholipids to give rise to fatty acids and lysophospholipids. The mammalian genome encodes more than 50 PLA(2)s or related enzymes, which are classified into several subfamilies on the basis of their structures and functions. From a general viewpoint, the PLA(2) family has mainly been implicated in signal transduction, producing bioactive lipid mediators derived from fatty acids and lysophospholipids. Recent evidence indicates that PLA(2)s also contribute to phospholipid remodeling for membrane homeostasis or energy production for fatty acid β-oxidation. Accordingly, PLA(2) enzymes can be regarded as one of the key regulators of the quality of lipids, which I herein refer to as lipoquality. Disturbance of PLA(2)-regulated lipoquality hampers tissue and cellular homeostasis and can be linked to various diseases. Here I overview the current state of understanding of the classification, enzymatic properties, and physiological functions of the PLA(2) family. The Japan Academy 2017-11-10 /pmc/articles/PMC5743847/ /pubmed/29129849 http://dx.doi.org/10.2183/pjab.93.043 Text en © 2017 The Japan Academy This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review
MURAKAMI, Makoto
Lipoquality control by phospholipase A(2) enzymes
title Lipoquality control by phospholipase A(2) enzymes
title_full Lipoquality control by phospholipase A(2) enzymes
title_fullStr Lipoquality control by phospholipase A(2) enzymes
title_full_unstemmed Lipoquality control by phospholipase A(2) enzymes
title_short Lipoquality control by phospholipase A(2) enzymes
title_sort lipoquality control by phospholipase a(2) enzymes
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5743847/
https://www.ncbi.nlm.nih.gov/pubmed/29129849
http://dx.doi.org/10.2183/pjab.93.043
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