Lysosomal phospholipase A2.


Journal

Biochimica et biophysica acta. Molecular and cell biology of lipids
ISSN: 1879-2618
Titre abrégé: Biochim Biophys Acta Mol Cell Biol Lipids
Pays: Netherlands
ID NLM: 101731727

Informations de publication

Date de publication:
06 2019
Historique:
received: 17 06 2018
revised: 23 07 2018
accepted: 24 07 2018
pubmed: 5 8 2018
medline: 15 1 2020
entrez: 5 8 2018
Statut: ppublish

Résumé

Lysosomal phospholipase A2 (PLA2G15) is a ubiquitous enzyme uniquely characterized by a subcellular localization to the lysosome and late endosome. PLA2G15 has an acidic pH optimum, is calcium independent, and acts as a transacylase in the presence of N-acetyl-sphingosine as an acceptor. Recent studies aided by the delineation of the crystal structure of PLA2G15 have clarified further the catalytic mechanism, sn-1 versus sn-2 specificity, and the basis whereby cationic amphiphilic drugs inhibit its activity. PLA2G15 has recently been shown to hydrolyze short chain oxidized phospholipids which access the catalytic site directly based on their aqueous solubility. Studies on the PLA2G15 null mouse suggest a role for the enzyme in the catabolism of pulmonary surfactant. PLA2G15 may also have a role in host defense and in the processing of lipid antigens for presentation by CD1 proteins. This article is part of a Special Issue entitled Novel functions of phospholipase A2 Guest Editors: Makoto Murakami and Gerard Lambeau.

Identifiants

pubmed: 30077006
pii: S1388-1981(18)30182-3
doi: 10.1016/j.bbalip.2018.07.012
pmc: PMC6361722
mid: NIHMS1503190
pii:
doi:

Substances chimiques

Phospholipids 0
Phospholipases A2 EC 3.1.1.4

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S. Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

932-940

Subventions

Organisme : BLRD VA
ID : I01 BX002021
Pays : United States
Organisme : NIAMS NIH HHS
ID : R01 AR056991
Pays : United States
Organisme : NHLBI NIH HHS
ID : R01 HL122416
Pays : United States
Organisme : NINDS NIH HHS
ID : UH3 NS092981
Pays : United States

Informations de copyright

Published by Elsevier B.V.

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Auteurs

James A Shayman (JA)

Department of Internal Medicine, University of Michigan Medical School, University of Michigan, Ann Arbor, MI, USA. Electronic address: jshayman@umich.edu.

John J G Tesmer (JJG)

Department of Biological Sciences, Purdue University, West Lafayette, IN, USA.

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Classifications MeSH