Oxidative inactivation of lactonase activity of purified human paraoxonase 1 (PON1)
Paraoxonase1 (PON1), one of HDL-associated antioxidant proteins, is known to lose its activity in vivo systems under oxidative stress. Here, we examined the effect of various oxidants on lactonase activity of PON1, and tried to protect the lactonase activity from oxidative inactivation. Among the ox...
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| Published in | Biochimica et biophysica acta Vol. 1790; no. 3; pp. 155 - 160 |
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| Main Authors | , , , , |
| Format | Journal Article |
| Language | English |
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Netherlands
Elsevier B.V
01.03.2009
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| ISSN | 0304-4165 0006-3002 1872-8006 |
| DOI | 10.1016/j.bbagen.2008.11.009 |
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| Abstract | Paraoxonase1 (PON1), one of HDL-associated antioxidant proteins, is known to lose its activity in vivo systems under oxidative stress. Here, we examined the effect of various oxidants on lactonase activity of PON1, and tried to protect the lactonase activity from oxidative inactivation. Among the oxidative systems tested, the ascorbate/Cu
2+ system was the most potent in inactivating the lactonase activity of purified PON1; in contrast to a limited role of Fe
2+, Cu
2+ (0.05–1.0 µM) remarkably enhanced the inactivation of PON1 in the presence of ascorbate (0.02–0.1 mM). Moreover, Cu
2+ alone inhibited the lactonase activity at concentrations as low as 1 µM. The ascorbate/Cu
2+-mediated inactivation of PON1 lactonase activity was prevented by catalase, but not general hydroxyl radical scavengers, suggesting the implication of Cu
2+-bound hydroxyl radicals in the oxidative inactivation. Compared to arylesterase activity, lactonase activity appears to be more sensitive to Cu
2+-catalyzed oxidation. Separately, ascorbate/Cu
2+-mediated inactivation of lactonase activity was prevented by oleic acid as well as phoshatidylcholine. Taken together, our data demonstrate that Cu
2+-catalyzed oxidation may be a primary factor to cause the decrease of PON1 lactonase activity under oxidative stress and that lactonase activity of PON1 is most susceptible to ascorbate/Cu
2+ among PON1 activities. In addition, we have showed that radical-induced inactivation of lactonase activity is prevented by some lipids. |
|---|---|
| AbstractList | Paraoxonase1 (PON1), one of HDL-associated antioxidant proteins, is known to lose its activity in vivo systems under oxidative stress. Here, we examined the effect of various oxidants on lactonase activity of PON1, and tried to protect the lactonase activity from oxidative inactivation. Among the oxidative systems tested, the ascorbate/Cu(2+) system was the most potent in inactivating the lactonase activity of purified PON1; in contrast to a limited role of Fe(2+), Cu(2+) (0.05-1.0 microM) remarkably enhanced the inactivation of PON1 in the presence of ascorbate (0.02-0.1 mM). Moreover, Cu(2+) alone inhibited the lactonase activity at concentrations as low as 1 microM. The ascorbate/Cu(2+)-mediated inactivation of PON1 lactonase activity was prevented by catalase, but not general hydroxyl radical scavengers, suggesting the implication of Cu(2+)-bound hydroxyl radicals in the oxidative inactivation. Compared to arylesterase activity, lactonase activity appears to be more sensitive to Cu(2+)-catalyzed oxidation. Separately, ascorbate/Cu(2+)-mediated inactivation of lactonase activity was prevented by oleic acid as well as phoshatidylcholine. Taken together, our data demonstrate that Cu(2+)-catalyzed oxidation may be a primary factor to cause the decrease of PON1 lactonase activity under oxidative stress and that lactonase activity of PON1 is most susceptible to ascorbate/Cu(2+) among PON1 activities. In addition, we have showed that radical-induced inactivation of lactonase activity is prevented by some lipids.Paraoxonase1 (PON1), one of HDL-associated antioxidant proteins, is known to lose its activity in vivo systems under oxidative stress. Here, we examined the effect of various oxidants on lactonase activity of PON1, and tried to protect the lactonase activity from oxidative inactivation. Among the oxidative systems tested, the ascorbate/Cu(2+) system was the most potent in inactivating the lactonase activity of purified PON1; in contrast to a limited role of Fe(2+), Cu(2+) (0.05-1.0 microM) remarkably enhanced the inactivation of PON1 in the presence of ascorbate (0.02-0.1 mM). Moreover, Cu(2+) alone inhibited the lactonase activity at concentrations as low as 1 microM. The ascorbate/Cu(2+)-mediated inactivation of PON1 lactonase activity was prevented by catalase, but not general hydroxyl radical scavengers, suggesting the implication of Cu(2+)-bound hydroxyl radicals in the oxidative inactivation. Compared to arylesterase activity, lactonase activity appears to be more sensitive to Cu(2+)-catalyzed oxidation. Separately, ascorbate/Cu(2+)-mediated inactivation of lactonase activity was prevented by oleic acid as well as phoshatidylcholine. Taken together, our data demonstrate that Cu(2+)-catalyzed oxidation may be a primary factor to cause the decrease of PON1 lactonase activity under oxidative stress and that lactonase activity of PON1 is most susceptible to ascorbate/Cu(2+) among PON1 activities. In addition, we have showed that radical-induced inactivation of lactonase activity is prevented by some lipids. Paraoxonase1 (PON1), one of HDL-associated antioxidant proteins, is known to lose its activity in vivo systems under oxidative stress. Here, we examined the effect of various oxidants on lactonase activity of PON1, and tried to protect the lactonase activity from oxidative inactivation. Among the oxidative systems tested, the ascorbate/Cu 2+ system was the most potent in inactivating the lactonase activity of purified PON1; in contrast to a limited role of Fe 2+, Cu 2+ (0.05–1.0 µM) remarkably enhanced the inactivation of PON1 in the presence of ascorbate (0.02–0.1 mM). Moreover, Cu 2+ alone inhibited the lactonase activity at concentrations as low as 1 µM. The ascorbate/Cu 2+-mediated inactivation of PON1 lactonase activity was prevented by catalase, but not general hydroxyl radical scavengers, suggesting the implication of Cu 2+-bound hydroxyl radicals in the oxidative inactivation. Compared to arylesterase activity, lactonase activity appears to be more sensitive to Cu 2+-catalyzed oxidation. Separately, ascorbate/Cu 2+-mediated inactivation of lactonase activity was prevented by oleic acid as well as phoshatidylcholine. Taken together, our data demonstrate that Cu 2+-catalyzed oxidation may be a primary factor to cause the decrease of PON1 lactonase activity under oxidative stress and that lactonase activity of PON1 is most susceptible to ascorbate/Cu 2+ among PON1 activities. In addition, we have showed that radical-induced inactivation of lactonase activity is prevented by some lipids. Paraoxonase1 (PON1), one of HDL-associated antioxidant proteins, is known to lose its activity in vivo systems under oxidative stress. Here, we examined the effect of various oxidants on lactonase activity of PON1, and tried to protect the lactonase activity from oxidative inactivation. Among the oxidative systems tested, the ascorbate/Cu(2+) system was the most potent in inactivating the lactonase activity of purified PON1; in contrast to a limited role of Fe(2+), Cu(2+) (0.05-1.0 microM) remarkably enhanced the inactivation of PON1 in the presence of ascorbate (0.02-0.1 mM). Moreover, Cu(2+) alone inhibited the lactonase activity at concentrations as low as 1 microM. The ascorbate/Cu(2+)-mediated inactivation of PON1 lactonase activity was prevented by catalase, but not general hydroxyl radical scavengers, suggesting the implication of Cu(2+)-bound hydroxyl radicals in the oxidative inactivation. Compared to arylesterase activity, lactonase activity appears to be more sensitive to Cu(2+)-catalyzed oxidation. Separately, ascorbate/Cu(2+)-mediated inactivation of lactonase activity was prevented by oleic acid as well as phoshatidylcholine. Taken together, our data demonstrate that Cu(2+)-catalyzed oxidation may be a primary factor to cause the decrease of PON1 lactonase activity under oxidative stress and that lactonase activity of PON1 is most susceptible to ascorbate/Cu(2+) among PON1 activities. In addition, we have showed that radical-induced inactivation of lactonase activity is prevented by some lipids. |
| Author | Cheon-Ho, Park Hung, Nguyen Dang Ree, Kim Mee Nguyen, Su Duy Dai-Eun, Sok |
| Author_xml | – sequence: 1 givenname: Su Duy surname: Nguyen fullname: Nguyen, Su Duy organization: Laboratory of Lipid Biochemistry and Protein Interactions, Department of Molecular Cell Biology, KU Leuven, Herestraat 49, 3000 Leuven, Belgium – sequence: 2 givenname: Nguyen Dang surname: Hung fullname: Hung, Nguyen Dang organization: College of Pharmacy, Chungnam National University, Yuseong-Ku, Gung-Dong, Taejon 305-764, Republic of Korea – sequence: 3 givenname: Park surname: Cheon-Ho fullname: Cheon-Ho, Park organization: College of Pharmacy, Chungnam National University, Yuseong-Ku, Gung-Dong, Taejon 305-764, Republic of Korea – sequence: 4 givenname: Kim Mee surname: Ree fullname: Ree, Kim Mee organization: Department of Food and Nutrition, Chungnam National University, Yuseong-ku, Taejon, Republic of Korea – sequence: 5 givenname: Sok surname: Dai-Eun fullname: Dai-Eun, Sok email: daesok@cnu.ac.kr organization: College of Pharmacy, Chungnam National University, Yuseong-Ku, Gung-Dong, Taejon 305-764, Republic of Korea |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/19103263$$D View this record in MEDLINE/PubMed |
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| Keywords | Oxidative inactivation HDL Lactonase LDL Arylesterase PON1 Paraoxonase Reactive oxygen specie Antioxidant DOPC |
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| Snippet | Paraoxonase1 (PON1), one of HDL-associated antioxidant proteins, is known to lose its activity in vivo systems under oxidative stress. Here, we examined the... |
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| SubjectTerms | Antioxidant Aryldialkylphosphatase - antagonists & inhibitors Aryldialkylphosphatase - isolation & purification Aryldialkylphosphatase - metabolism Arylesterase Ascorbic Acid - pharmacology Catalysis Copper - pharmacology Enzyme Inhibitors - pharmacology Humans Lactonase Lipoproteins, HDL - metabolism Oxidation-Reduction Oxidative inactivation Paraoxonase Reactive oxygen specie |
| Title | Oxidative inactivation of lactonase activity of purified human paraoxonase 1 (PON1) |
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