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Updating Phospholipase A(2) Biology
The phospholipase A(2) (PLA(2)) superfamily contains more than 50 enzymes in mammals that are subdivided into several distinct families on a structural and biochemical basis. In principle, PLA(2) has the capacity to hydrolyze the sn-2 position of glycerophospholipids to release fatty acids and lysop...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7603386/ https://www.ncbi.nlm.nih.gov/pubmed/33086624 http://dx.doi.org/10.3390/biom10101457 |
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author | Murakami, Makoto Sato, Hiroyasu Taketomi, Yoshitaka |
author_facet | Murakami, Makoto Sato, Hiroyasu Taketomi, Yoshitaka |
author_sort | Murakami, Makoto |
collection | PubMed |
description | The phospholipase A(2) (PLA(2)) superfamily contains more than 50 enzymes in mammals that are subdivided into several distinct families on a structural and biochemical basis. In principle, PLA(2) has the capacity to hydrolyze the sn-2 position of glycerophospholipids to release fatty acids and lysophospholipids, yet several enzymes in this superfamily catalyze other reactions rather than or in addition to the PLA(2) reaction. PLA(2) enzymes play crucial roles in not only the production of lipid mediators, but also membrane remodeling, bioenergetics, and body surface barrier, thereby participating in a number of biological events. Accordingly, disturbance of PLA(2)-regulated lipid metabolism is often associated with various diseases. This review updates the current state of understanding of the classification, enzymatic properties, and biological functions of various enzymes belonging to the PLA(2) superfamily, focusing particularly on the novel roles of PLA(2)s in vivo. |
format | Online Article Text |
id | pubmed-7603386 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-76033862020-11-01 Updating Phospholipase A(2) Biology Murakami, Makoto Sato, Hiroyasu Taketomi, Yoshitaka Biomolecules Review The phospholipase A(2) (PLA(2)) superfamily contains more than 50 enzymes in mammals that are subdivided into several distinct families on a structural and biochemical basis. In principle, PLA(2) has the capacity to hydrolyze the sn-2 position of glycerophospholipids to release fatty acids and lysophospholipids, yet several enzymes in this superfamily catalyze other reactions rather than or in addition to the PLA(2) reaction. PLA(2) enzymes play crucial roles in not only the production of lipid mediators, but also membrane remodeling, bioenergetics, and body surface barrier, thereby participating in a number of biological events. Accordingly, disturbance of PLA(2)-regulated lipid metabolism is often associated with various diseases. This review updates the current state of understanding of the classification, enzymatic properties, and biological functions of various enzymes belonging to the PLA(2) superfamily, focusing particularly on the novel roles of PLA(2)s in vivo. MDPI 2020-10-19 /pmc/articles/PMC7603386/ /pubmed/33086624 http://dx.doi.org/10.3390/biom10101457 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Murakami, Makoto Sato, Hiroyasu Taketomi, Yoshitaka Updating Phospholipase A(2) Biology |
title | Updating Phospholipase A(2) Biology |
title_full | Updating Phospholipase A(2) Biology |
title_fullStr | Updating Phospholipase A(2) Biology |
title_full_unstemmed | Updating Phospholipase A(2) Biology |
title_short | Updating Phospholipase A(2) Biology |
title_sort | updating phospholipase a(2) biology |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7603386/ https://www.ncbi.nlm.nih.gov/pubmed/33086624 http://dx.doi.org/10.3390/biom10101457 |
work_keys_str_mv | AT murakamimakoto updatingphospholipasea2biology AT satohiroyasu updatingphospholipasea2biology AT taketomiyoshitaka updatingphospholipasea2biology |