Publication:
Lead inhibits paraoxonase 2 but not paraoxonase 1 activity in human hepatoma HepG2 cells

2
0

Issued Date

2013

Resource Type

Article

File Type

application/pdf

ISSN

0260437X

DOI

10.1002/jat.1789

Other identifier(s)

2-s2.0-84878193221

Rights Holder(s)

มหาวิทยาลัยศรีนครินทรวิโรฒ

Bibliographic Citation

Journal of Applied Toxicology. Vol 33, No.7 (2013), p.631-637

Suggested Citation

Sukketsiri W., Porntadavity S., Phivthong-Ngam L., Lawanprasert S. Lead inhibits paraoxonase 2 but not paraoxonase 1 activity in human hepatoma HepG2 cells. Journal of Applied Toxicology. Vol 33, No.7 (2013), p.631-637. doi:10.1002/jat.1789 Retrieved from: https://hdl.handle.net/20.500.14740/6628

Title

Lead inhibits paraoxonase 2 but not paraoxonase 1 activity in human hepatoma HepG2 cells

Author(s)

Sukketsiri W.
 Porntadavity S.
 Phivthong-Ngam L.
 Lawanprasert S.

Abstract

Lead is an environmental toxicant of great concern for humans and animals. Lead-induced liver damage and malfunction are partly due to a disturbance of the cellular antioxidant balance. Paraoxonase 1 (PON1) and PON2 are highly expressed in the liver and have been proposed as antioxidative enzymes. In this study, the effects of lead on PON1 and PON2 activities were investigated in human hepatoma HepG2 cells by exposing the cells to various concentrations of lead acetate for 24, 48, or 72h. The results show that a significant increase in reactive oxygen species was observed even at the lowest concentration of lead treatment. However, only the highest concentration of lead significantly influenced cell viability. Lead had no influence on cell-associated PON1 activity, but it significantly decreased cytoplasmic PON2 activity in a concentration- and time-dependent manner. This reduction was rescued by the addition of calcium. A significant increase of PON2 transcript was observed by real-time polymerase chain reaction, while PON2 protein expression did not change in the western blot analysis. Taken together, these results indicate that lead reduces PON2, but not PON1, activity and that this reduction is reversed by calcium. Lead-induced oxidative stress and decreased PON2 activity lead to the upregulation of PON2 transcript. © 2012 John Wiley & Sons, Ltd.

Subject(s)

Aryldialkylphosphatase 1
 Aryldialkylphosphatase 2
 Calcium
 Lead acetate
 Reactive oxygen metabolite
 Adult
 Article
 Cancer cell culture
 Cell lysate
 Cell viability
 Concentration response
 Controlled study
 Cytotoxicity
 Enzyme activity
 Enzyme inhibition
 Hepatoma cell
 Human
 Human cell
 In vitro study
 Liver cell carcinoma
 Liver toxicity
 Molecular size
 Oxidative stress
 Priority journal
 Protein expression
 Real time polymerase chain reaction
 RNA extraction
 Spectrophotometry
 Treatment duration
 Upregulation
 Western blotting
 Aryldialkylphosphatase
 Blotting, Western
 Calcium Chloride
 Carcinoma, Hepatocellular
 Cell Line, Tumor
 Cell Survival
 Drug-Induced Liver Injury
 Enzyme Inhibitors
 Humans
 Indicators and Reagents
 Liver Neoplasms
 Organometallic Compounds
 Reactive Oxygen Species
 Real-Time Polymerase Chain Reaction
 RNA
 Animalia

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URI

https://hdl.handle.net/20.500.14740/6628

Collections

Scopus: Year 1983-2021

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