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The HRASLS (PLA/AT) subfamily of enzymes
The H-RAS-like suppressor (HRASLS) subfamily consists of five enzymes (1–5) in humans and three (1, 3, and 5) in mice and rats that share sequence homology with lecithin:retinol acyltransferase (LRAT). All HRASLS family members possess in vitro phospholipid metabolizing abilities including phospholi...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4624172/ https://www.ncbi.nlm.nih.gov/pubmed/26503625 http://dx.doi.org/10.1186/s12929-015-0210-7 |
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author | Mardian, Emily B. Bradley, Ryan M. Duncan, Robin E. |
author_facet | Mardian, Emily B. Bradley, Ryan M. Duncan, Robin E. |
author_sort | Mardian, Emily B. |
collection | PubMed |
description | The H-RAS-like suppressor (HRASLS) subfamily consists of five enzymes (1–5) in humans and three (1, 3, and 5) in mice and rats that share sequence homology with lecithin:retinol acyltransferase (LRAT). All HRASLS family members possess in vitro phospholipid metabolizing abilities including phospholipase A(1/2) (PLA(1/2)) activities and O-acyltransferase activities for the remodeling of glycerophospholipid acyl chains, as well as N-acyltransferase activities for the production of N-acylphosphatidylethanolamines. The in vivo biological activities of the HRASLS enzymes have not yet been fully investigated. Research to date indicates involvement of this subfamily in a wide array of biological processes and, as a consequence, these five enzymes have undergone extensive rediscovery and renaming within different fields of research. This review briefly describes the discovery of each of the HRASLS enzymes and their role in cancer, and discusses the biochemical function of each enzyme, as well as the biological role, if known. Gaps in current understanding are highlighted and suggestions for future research directions are discussed. |
format | Online Article Text |
id | pubmed-4624172 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-46241722015-10-29 The HRASLS (PLA/AT) subfamily of enzymes Mardian, Emily B. Bradley, Ryan M. Duncan, Robin E. J Biomed Sci Review The H-RAS-like suppressor (HRASLS) subfamily consists of five enzymes (1–5) in humans and three (1, 3, and 5) in mice and rats that share sequence homology with lecithin:retinol acyltransferase (LRAT). All HRASLS family members possess in vitro phospholipid metabolizing abilities including phospholipase A(1/2) (PLA(1/2)) activities and O-acyltransferase activities for the remodeling of glycerophospholipid acyl chains, as well as N-acyltransferase activities for the production of N-acylphosphatidylethanolamines. The in vivo biological activities of the HRASLS enzymes have not yet been fully investigated. Research to date indicates involvement of this subfamily in a wide array of biological processes and, as a consequence, these five enzymes have undergone extensive rediscovery and renaming within different fields of research. This review briefly describes the discovery of each of the HRASLS enzymes and their role in cancer, and discusses the biochemical function of each enzyme, as well as the biological role, if known. Gaps in current understanding are highlighted and suggestions for future research directions are discussed. BioMed Central 2015-10-26 /pmc/articles/PMC4624172/ /pubmed/26503625 http://dx.doi.org/10.1186/s12929-015-0210-7 Text en © Mardian et al. 2015 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Review Mardian, Emily B. Bradley, Ryan M. Duncan, Robin E. The HRASLS (PLA/AT) subfamily of enzymes |
title | The HRASLS (PLA/AT) subfamily of enzymes |
title_full | The HRASLS (PLA/AT) subfamily of enzymes |
title_fullStr | The HRASLS (PLA/AT) subfamily of enzymes |
title_full_unstemmed | The HRASLS (PLA/AT) subfamily of enzymes |
title_short | The HRASLS (PLA/AT) subfamily of enzymes |
title_sort | hrasls (pla/at) subfamily of enzymes |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4624172/ https://www.ncbi.nlm.nih.gov/pubmed/26503625 http://dx.doi.org/10.1186/s12929-015-0210-7 |
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