Human Paraoxonase-2 (PON2): Protein Functions and Modulation

PON1, PON2, and PON3 belong to a family of lactone hydrolyzing enzymes endowed with various substrate specificities. Among PONs, PON2 shows the highest hydrolytic activity toward many acyl-homoserine lactones (acyl-HL) involved in bacterial quorum-sensing signaling. Accordingly, defense against path...

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Detalles Bibliográficos
Autores principales: Manco, Giuseppe, Porzio, Elena, Carusone, Teresa Maria
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7915308/
https://www.ncbi.nlm.nih.gov/pubmed/33562328
http://dx.doi.org/10.3390/antiox10020256
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author Manco, Giuseppe
Porzio, Elena
Carusone, Teresa Maria
author_facet Manco, Giuseppe
Porzio, Elena
Carusone, Teresa Maria
author_sort Manco, Giuseppe
collection PubMed
description PON1, PON2, and PON3 belong to a family of lactone hydrolyzing enzymes endowed with various substrate specificities. Among PONs, PON2 shows the highest hydrolytic activity toward many acyl-homoserine lactones (acyl-HL) involved in bacterial quorum-sensing signaling. Accordingly, defense against pathogens, such as Brevundimonas aeruginosa (B. aeruginosa), was postulated to be the principal function of PON2. However, recent findings have highlighted the importance of PON2 in oxidative stress control, inhibition of apoptosis, and the progression of various types of malignancies. This review focuses on all of these aspects of PON2.
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spelling pubmed-79153082021-03-01 Human Paraoxonase-2 (PON2): Protein Functions and Modulation Manco, Giuseppe Porzio, Elena Carusone, Teresa Maria Antioxidants (Basel) Review PON1, PON2, and PON3 belong to a family of lactone hydrolyzing enzymes endowed with various substrate specificities. Among PONs, PON2 shows the highest hydrolytic activity toward many acyl-homoserine lactones (acyl-HL) involved in bacterial quorum-sensing signaling. Accordingly, defense against pathogens, such as Brevundimonas aeruginosa (B. aeruginosa), was postulated to be the principal function of PON2. However, recent findings have highlighted the importance of PON2 in oxidative stress control, inhibition of apoptosis, and the progression of various types of malignancies. This review focuses on all of these aspects of PON2. MDPI 2021-02-07 /pmc/articles/PMC7915308/ /pubmed/33562328 http://dx.doi.org/10.3390/antiox10020256 Text en © 2021 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
Manco, Giuseppe
Porzio, Elena
Carusone, Teresa Maria
Human Paraoxonase-2 (PON2): Protein Functions and Modulation
title Human Paraoxonase-2 (PON2): Protein Functions and Modulation
title_full Human Paraoxonase-2 (PON2): Protein Functions and Modulation
title_fullStr Human Paraoxonase-2 (PON2): Protein Functions and Modulation
title_full_unstemmed Human Paraoxonase-2 (PON2): Protein Functions and Modulation
title_short Human Paraoxonase-2 (PON2): Protein Functions and Modulation
title_sort human paraoxonase-2 (pon2): protein functions and modulation
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7915308/
https://www.ncbi.nlm.nih.gov/pubmed/33562328
http://dx.doi.org/10.3390/antiox10020256
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