Arylesterase activity of paraoxonase 1 (PON1) on HDL3 and HDL2: Relationship with Q192R, C-108T, and L55M polymorphisms
Background: Controversy exists regarding the role of the subfractions of high-density lipoproteins (HDL2 and HDL3) 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,...
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| Format: | Article |
| Language: | English |
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Elsevier
2021-07-01
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| Series: | Biochemistry and Biophysics Reports |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2405580821000650 |
| _version_ | 1818837205040234496 |
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| author | Sandra Y. Valencia C Carlos A. Isaza M Julieta Henao B Leonardo Beltrán A Nelsy Loango Patricia Landázuri |
| author_facet | Sandra Y. Valencia C Carlos A. Isaza M Julieta Henao B Leonardo Beltrán A Nelsy Loango Patricia Landázuri |
| author_sort | Sandra Y. Valencia C |
| collection | DOAJ |
| description | Background: Controversy exists regarding the role of the subfractions of high-density lipoproteins (HDL2 and HDL3) 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 HDL3 and HDL2 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 HDL3 subfractions was greater (62.83 ± 20 kU/L) than with HDL2 (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 HDL3 and HDL2. Conclusions: PON1 polymorphisms do not influence the HDL-c, and the PON activity is greater in the HDL3 than in the HDL2, independent of the polymorphism, but it is necessary to delve into the functionality of these findings in different populations. |
| first_indexed | 2024-12-19T03:18:48Z |
| format | Article |
| id | doaj.art-14568cf4469849f69d9b34ccb360a98f |
| institution | Directory Open Access Journal |
| issn | 2405-5808 |
| language | English |
| last_indexed | 2024-12-19T03:18:48Z |
| publishDate | 2021-07-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Biochemistry and Biophysics Reports |
| spelling | doaj.art-14568cf4469849f69d9b34ccb360a98f2022-12-21T20:37:49ZengElsevierBiochemistry and Biophysics Reports2405-58082021-07-0126100971Arylesterase activity of paraoxonase 1 (PON1) on HDL3 and HDL2: Relationship with Q192R, C-108T, and L55M polymorphismsSandra Y. Valencia C0Carlos A. Isaza M1Julieta Henao B2Leonardo Beltrán A3Nelsy Loango4Patricia Landázuri5Faculty of Health Sciences, Program of Nutrition, Universidad Libre, Colombia; Faculty of Medicine, Fundación Universitaria Autónoma de las Américas, Colombia; Faculty of Health Sciences, Universidad del Quindío, Colombia; Corresponding author. Faculty of Health Sciences, Program of Nutrition, Universidad Libre, Colombia.Faculty of Health Sciences, Universidad Tecnológica de Pereira, ColombiaFaculty of Health Sciences, Universidad Tecnológica de Pereira, ColombiaFaculty of Health Sciences, Universidad Tecnológica de Pereira, Colombia; Faculty of Health Sciences, Unidad Central del Valle del Cauca, ColombiaFaculty of Health Sciences, Universidad del Quindío, Colombia; Faculty of Basic Sciences and Technologies, Universidad del Quindío, ColombiaFaculty of Health Sciences, Universidad del Quindío, ColombiaBackground: Controversy exists regarding the role of the subfractions of high-density lipoproteins (HDL2 and HDL3) 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 HDL3 and HDL2 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 HDL3 subfractions was greater (62.83 ± 20 kU/L) than with HDL2 (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 HDL3 and HDL2. Conclusions: PON1 polymorphisms do not influence the HDL-c, and the PON activity is greater in the HDL3 than in the HDL2, independent of the polymorphism, but it is necessary to delve into the functionality of these findings in different populations.http://www.sciencedirect.com/science/article/pii/S2405580821000650HDL subfractionsHDL cholesterolPON1 polymorphismsCardiovascular diseaseAntioxidantArylesterase activity |
| spellingShingle | Sandra Y. Valencia C Carlos A. Isaza M Julieta Henao B Leonardo Beltrán A Nelsy Loango Patricia Landázuri Arylesterase activity of paraoxonase 1 (PON1) on HDL3 and HDL2: Relationship with Q192R, C-108T, and L55M polymorphisms Biochemistry and Biophysics Reports HDL subfractions HDL cholesterol PON1 polymorphisms Cardiovascular disease Antioxidant Arylesterase activity |
| title | Arylesterase activity of paraoxonase 1 (PON1) on HDL3 and HDL2: Relationship with Q192R, C-108T, and L55M polymorphisms |
| title_full | Arylesterase activity of paraoxonase 1 (PON1) on HDL3 and HDL2: Relationship with Q192R, C-108T, and L55M polymorphisms |
| title_fullStr | Arylesterase activity of paraoxonase 1 (PON1) on HDL3 and HDL2: Relationship with Q192R, C-108T, and L55M polymorphisms |
| title_full_unstemmed | Arylesterase activity of paraoxonase 1 (PON1) on HDL3 and HDL2: Relationship with Q192R, C-108T, and L55M polymorphisms |
| title_short | Arylesterase activity of paraoxonase 1 (PON1) on HDL3 and HDL2: Relationship with Q192R, C-108T, and L55M polymorphisms |
| title_sort | arylesterase activity of paraoxonase 1 pon1 on hdl3 and hdl2 relationship with q192r c 108t and l55m polymorphisms |
| topic | HDL subfractions HDL cholesterol PON1 polymorphisms Cardiovascular disease Antioxidant Arylesterase activity |
| url | http://www.sciencedirect.com/science/article/pii/S2405580821000650 |
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