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Arylesterase activity of paraoxonase 1 (PON1) on HDL(3) and HDL(2): Relationship with Q192R, C-108T, and L55M polymorphisms

BACKGROUND: Controversy exists regarding the role of the subfractions of high-density lipoproteins (HDL(2) and HDL(3)) in cardiovascular disease. The functionality of these particles, and their protective role, is due in part to the paraoxonase 1 (PON1) presence in them. The polymorphisms rs662 (Q19...

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Autores principales: Valencia C, Sandra Y., Isaza M, Carlos A., Henao B, Julieta, Beltrán A, Leonardo, Loango, Nelsy, Landázuri, Patricia
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7985468/
https://www.ncbi.nlm.nih.gov/pubmed/33778169
http://dx.doi.org/10.1016/j.bbrep.2021.100971
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author Valencia C, Sandra Y.
Isaza M, Carlos A.
Henao B, Julieta
Beltrán A, Leonardo
Loango, Nelsy
Landázuri, Patricia
author_facet Valencia C, Sandra Y.
Isaza M, Carlos A.
Henao B, Julieta
Beltrán A, Leonardo
Loango, Nelsy
Landázuri, Patricia
author_sort Valencia C, Sandra Y.
collection PubMed
description BACKGROUND: Controversy exists regarding the role of the subfractions of high-density lipoproteins (HDL(2) and HDL(3)) in cardiovascular disease. The functionality of these particles, and their protective role, is due in part to the paraoxonase 1 (PON1) presence in them. The polymorphisms rs662 (Q192R, A/G), rs854560 (L55 M, T/A), and rs705379 (C-108T) of the PON1 gene have been related to enzyme activity and, with the anti-oxidative capacity of the HDL. The objective was to determine the arylesterase PON1 activity in HDL(3) and HDL(2) and its relationship with the polymorphisms mentioned, in a young population. METHODS: The polymorphisms were determined through mini-sequencing (SnaPshot). The HDL subpopulations were separated via ionic precipitation, cholesterol was measured with enzymatic methods, and PON1 activity was measured through spectrophotometry. RESULTS: The results show that the PON1 polymorphisms do not influence the cholesterol in the HDL. A variation between 40.02 and 43.9 mg/dL was in all the polymorphisms without significant differences. Additionally, PON1 activity in the HDL(3) subfractions was greater (62.83 ± 20 kU/L) than with HDL(2) (35.8 ± 20.8 kU/L) in the whole population and in all the polymorphisms (p < 0.001), and it was independent of the polymorphism and differential arylesterase activity in the Q192R polymorphism (QQ > QR > RR). Thus, 115.90 ± 30.7, 88.78 ± 21.3, 65.29 ± 10.2, respectively, for total HDL, with identical behavior for HDL(3) and HDL(2). CONCLUSIONS: PON1 polymorphisms do not influence the HDL(-c), and the PON activity is greater in the HDL(3) than in the HDL(2), independent of the polymorphism, but it is necessary to delve into the functionality of these findings in different populations.
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spelling pubmed-79854682021-03-25 Arylesterase activity of paraoxonase 1 (PON1) on HDL(3) and HDL(2): Relationship with Q192R, C-108T, and L55M polymorphisms Valencia C, Sandra Y. Isaza M, Carlos A. Henao B, Julieta Beltrán A, Leonardo Loango, Nelsy Landázuri, Patricia Biochem Biophys Rep Research Article BACKGROUND: Controversy exists regarding the role of the subfractions of high-density lipoproteins (HDL(2) and HDL(3)) in cardiovascular disease. The functionality of these particles, and their protective role, is due in part to the paraoxonase 1 (PON1) presence in them. The polymorphisms rs662 (Q192R, A/G), rs854560 (L55 M, T/A), and rs705379 (C-108T) of the PON1 gene have been related to enzyme activity and, with the anti-oxidative capacity of the HDL. The objective was to determine the arylesterase PON1 activity in HDL(3) and HDL(2) and its relationship with the polymorphisms mentioned, in a young population. METHODS: The polymorphisms were determined through mini-sequencing (SnaPshot). The HDL subpopulations were separated via ionic precipitation, cholesterol was measured with enzymatic methods, and PON1 activity was measured through spectrophotometry. RESULTS: The results show that the PON1 polymorphisms do not influence the cholesterol in the HDL. A variation between 40.02 and 43.9 mg/dL was in all the polymorphisms without significant differences. Additionally, PON1 activity in the HDL(3) subfractions was greater (62.83 ± 20 kU/L) than with HDL(2) (35.8 ± 20.8 kU/L) in the whole population and in all the polymorphisms (p < 0.001), and it was independent of the polymorphism and differential arylesterase activity in the Q192R polymorphism (QQ > QR > RR). Thus, 115.90 ± 30.7, 88.78 ± 21.3, 65.29 ± 10.2, respectively, for total HDL, with identical behavior for HDL(3) and HDL(2). CONCLUSIONS: PON1 polymorphisms do not influence the HDL(-c), and the PON activity is greater in the HDL(3) than in the HDL(2), independent of the polymorphism, but it is necessary to delve into the functionality of these findings in different populations. Elsevier 2021-03-18 /pmc/articles/PMC7985468/ /pubmed/33778169 http://dx.doi.org/10.1016/j.bbrep.2021.100971 Text en © 2021 The Authors http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Research Article
Valencia C, Sandra Y.
Isaza M, Carlos A.
Henao B, Julieta
Beltrán A, Leonardo
Loango, Nelsy
Landázuri, Patricia
Arylesterase activity of paraoxonase 1 (PON1) on HDL(3) and HDL(2): Relationship with Q192R, C-108T, and L55M polymorphisms
title Arylesterase activity of paraoxonase 1 (PON1) on HDL(3) and HDL(2): Relationship with Q192R, C-108T, and L55M polymorphisms
title_full Arylesterase activity of paraoxonase 1 (PON1) on HDL(3) and HDL(2): Relationship with Q192R, C-108T, and L55M polymorphisms
title_fullStr Arylesterase activity of paraoxonase 1 (PON1) on HDL(3) and HDL(2): Relationship with Q192R, C-108T, and L55M polymorphisms
title_full_unstemmed Arylesterase activity of paraoxonase 1 (PON1) on HDL(3) and HDL(2): Relationship with Q192R, C-108T, and L55M polymorphisms
title_short Arylesterase activity of paraoxonase 1 (PON1) on HDL(3) and HDL(2): Relationship with Q192R, C-108T, and L55M polymorphisms
title_sort arylesterase activity of paraoxonase 1 (pon1) on hdl(3) and hdl(2): relationship with q192r, c-108t, and l55m polymorphisms
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7985468/
https://www.ncbi.nlm.nih.gov/pubmed/33778169
http://dx.doi.org/10.1016/j.bbrep.2021.100971
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