Human Secretary Phospholipase A2 Mutations and Their Clinical Implications

Mohd Imran Khan, Gururao Hariprasad Department of Biophysics, All India Institute of Medical Sciences, New Delhi 110029, IndiaCorrespondence: Gururao Hariprasad Tel +91-11-26594240Fax +91-11-26588663. Email g.hariprasad@rediffmail.comAbstract: Phospholipases A2 (PLA2s) belong to a superfamily of enz...

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Autores principales:	Khan MI, Hariprasad G
Formato:	article
Lenguaje:	EN
Publicado:	Dove Medical Press 2020
Materias:	secretary phospholipase a2 spla2 mutations clinical implications structure-function relationship Pathology RB1-214 Therapeutics. Pharmacology RM1-950
Acceso en línea:	https://doaj.org/article/0936663826ca4a11aca495ca274ab0df
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spelling	oai:doaj.org-article:0936663826ca4a11aca495ca274ab0df2021-12-02T10:12:20ZHuman Secretary Phospholipase A2 Mutations and Their Clinical Implications1178-7031https://doaj.org/article/0936663826ca4a11aca495ca274ab0df2020-09-01T00:00:00Zhttps://www.dovepress.com/human-secretary-phospholipase-a2-mutations-and-their-clinical-implicat-peer-reviewed-article-JIRhttps://doaj.org/toc/1178-7031Mohd Imran Khan, Gururao Hariprasad Department of Biophysics, All India Institute of Medical Sciences, New Delhi 110029, IndiaCorrespondence: Gururao Hariprasad Tel +91-11-26594240Fax +91-11-26588663. Email g.hariprasad@rediffmail.comAbstract: Phospholipases A2 (PLA2s) belong to a superfamily of enzymes responsible for hydrolysis of the sn-2 fatty acids of membrane phospholipids to release arachidonic acid. PLA2s are the rate limiting enzyme for the downstream synthesis of prostaglandins and leukotrienes that are the main mediators of inflammation. The extracellular forms of this enzyme are also called the secretary phospholipase A2 (sPLA2) and are distributed extensively in most of the tissues in the human body. Their integral role in inflammatory pathways has been the primary reason for the extensive research on this molecule. The catalytic mechanism of sPLA2 is initiated by a histidine/aspartic acid/calcium complex within the active site. Though they are known to have certain housekeeping functions, certain mutations of sPLA2 are known to be implicated in causation of certain pathologies leading to diseases such as atherosclerosis, cardiovascular diseases, benign fleck retina, neurodegeneration, and asthma. We present an overview of human sPLA2 and a comprehensive compilation of the mutations that result in various disease phenotypes. The study not only helps to have a holistic understanding of human sPLA2 mutations and their clinical implications, but is also a useful platform to initiate research pertaining to structure–function relationship of the mutations to develop effective therapies for management of these diseases.Keywords: secretary phospholipase A2, sPLA2, mutations, clinical implications, structure–function relationshipKhan MIHariprasad GDove Medical Pressarticlesecretary phospholipase a2spla2mutationsclinical implicationsstructure-function relationshipPathologyRB1-214Therapeutics. PharmacologyRM1-950ENJournal of Inflammation Research, Vol Volume 13, Pp 551-561 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	secretary phospholipase a2 spla2 mutations clinical implications structure-function relationship Pathology RB1-214 Therapeutics. Pharmacology RM1-950
spellingShingle	secretary phospholipase a2 spla2 mutations clinical implications structure-function relationship Pathology RB1-214 Therapeutics. Pharmacology RM1-950 Khan MI Hariprasad G Human Secretary Phospholipase A2 Mutations and Their Clinical Implications
description	Mohd Imran Khan, Gururao Hariprasad Department of Biophysics, All India Institute of Medical Sciences, New Delhi 110029, IndiaCorrespondence: Gururao Hariprasad Tel +91-11-26594240Fax +91-11-26588663. Email g.hariprasad@rediffmail.comAbstract: Phospholipases A2 (PLA2s) belong to a superfamily of enzymes responsible for hydrolysis of the sn-2 fatty acids of membrane phospholipids to release arachidonic acid. PLA2s are the rate limiting enzyme for the downstream synthesis of prostaglandins and leukotrienes that are the main mediators of inflammation. The extracellular forms of this enzyme are also called the secretary phospholipase A2 (sPLA2) and are distributed extensively in most of the tissues in the human body. Their integral role in inflammatory pathways has been the primary reason for the extensive research on this molecule. The catalytic mechanism of sPLA2 is initiated by a histidine/aspartic acid/calcium complex within the active site. Though they are known to have certain housekeeping functions, certain mutations of sPLA2 are known to be implicated in causation of certain pathologies leading to diseases such as atherosclerosis, cardiovascular diseases, benign fleck retina, neurodegeneration, and asthma. We present an overview of human sPLA2 and a comprehensive compilation of the mutations that result in various disease phenotypes. The study not only helps to have a holistic understanding of human sPLA2 mutations and their clinical implications, but is also a useful platform to initiate research pertaining to structure–function relationship of the mutations to develop effective therapies for management of these diseases.Keywords: secretary phospholipase A2, sPLA2, mutations, clinical implications, structure–function relationship
format	article
author	Khan MI Hariprasad G
author_facet	Khan MI Hariprasad G
author_sort	Khan MI
title	Human Secretary Phospholipase A2 Mutations and Their Clinical Implications
title_short	Human Secretary Phospholipase A2 Mutations and Their Clinical Implications
title_full	Human Secretary Phospholipase A2 Mutations and Their Clinical Implications
title_fullStr	Human Secretary Phospholipase A2 Mutations and Their Clinical Implications
title_full_unstemmed	Human Secretary Phospholipase A2 Mutations and Their Clinical Implications
title_sort	human secretary phospholipase a2 mutations and their clinical implications
publisher	Dove Medical Press
publishDate	2020
url	https://doaj.org/article/0936663826ca4a11aca495ca274ab0df
work_keys_str_mv	AT khanmi humansecretaryphospholipasea2mutationsandtheirclinicalimplications AT hariprasadg humansecretaryphospholipasea2mutationsandtheirclinicalimplications
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Human Secretary Phospholipase A2 Mutations and Their Clinical Implications

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