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Biology of Secretory Phospholipase A(2)
INTRODUCTION: The secretory phospholipase A(2) (sPLA(2)) family provides a seemingly endless array of potential biological functions that is only beginning to be appreciated. In humans, this family comprises 9 different members that vary in their tissue distribution, hydrolytic activity, and phospho...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer US
2008
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7101564/ https://www.ncbi.nlm.nih.gov/pubmed/18853244 http://dx.doi.org/10.1007/s10557-008-6134-7 |
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author | Boyanovsky, Boris B. Webb, Nancy R. |
author_facet | Boyanovsky, Boris B. Webb, Nancy R. |
author_sort | Boyanovsky, Boris B. |
collection | PubMed |
description | INTRODUCTION: The secretory phospholipase A(2) (sPLA(2)) family provides a seemingly endless array of potential biological functions that is only beginning to be appreciated. In humans, this family comprises 9 different members that vary in their tissue distribution, hydrolytic activity, and phospholipid substrate specificity. Through their lipase activity, these enzymes trigger various cell-signaling events to regulate cellular functions, directly kill bacteria, or modulate inflammatory responses. In addition, some sPLA(2)’s are high affinity ligands for cellular receptors. OBJECTIVE: This review merely scratches the surface of some of the actions of sPLA(2)s in innate immunity, inflammation, and atherosclerosis. The goal is to provide an overview of recent findings involving sPLA(2)s and to point to potential pathophysiologic mechanisms that may become targets for therapy. |
format | Online Article Text |
id | pubmed-7101564 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | Springer US |
record_format | MEDLINE/PubMed |
spelling | pubmed-71015642020-03-31 Biology of Secretory Phospholipase A(2) Boyanovsky, Boris B. Webb, Nancy R. Cardiovasc Drugs Ther Review INTRODUCTION: The secretory phospholipase A(2) (sPLA(2)) family provides a seemingly endless array of potential biological functions that is only beginning to be appreciated. In humans, this family comprises 9 different members that vary in their tissue distribution, hydrolytic activity, and phospholipid substrate specificity. Through their lipase activity, these enzymes trigger various cell-signaling events to regulate cellular functions, directly kill bacteria, or modulate inflammatory responses. In addition, some sPLA(2)’s are high affinity ligands for cellular receptors. OBJECTIVE: This review merely scratches the surface of some of the actions of sPLA(2)s in innate immunity, inflammation, and atherosclerosis. The goal is to provide an overview of recent findings involving sPLA(2)s and to point to potential pathophysiologic mechanisms that may become targets for therapy. Springer US 2008-10-14 2009 /pmc/articles/PMC7101564/ /pubmed/18853244 http://dx.doi.org/10.1007/s10557-008-6134-7 Text en © Springer Science+Business Media, LLC 2008 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic. |
spellingShingle | Review Boyanovsky, Boris B. Webb, Nancy R. Biology of Secretory Phospholipase A(2) |
title | Biology of Secretory Phospholipase A(2) |
title_full | Biology of Secretory Phospholipase A(2) |
title_fullStr | Biology of Secretory Phospholipase A(2) |
title_full_unstemmed | Biology of Secretory Phospholipase A(2) |
title_short | Biology of Secretory Phospholipase A(2) |
title_sort | biology of secretory phospholipase a(2) |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7101564/ https://www.ncbi.nlm.nih.gov/pubmed/18853244 http://dx.doi.org/10.1007/s10557-008-6134-7 |
work_keys_str_mv | AT boyanovskyborisb biologyofsecretoryphospholipasea2 AT webbnancyr biologyofsecretoryphospholipasea2 |