Paraoxonase (PON1) in Health and Disease

Basic and Clinical Aspects

  • Lucio G. Costa
  • Clement E. Furlong

Table of contents

  1. Front Matter
    Pages i-xvii
  2. Bert N. La Du
    Pages 1-25
  3. Denis Josse, Patrick Masson, Cynthia Bartels, Oksana Lockridge
    Pages 27-52
  4. Victoria H. Brophy, Gail P. Jarvik, Clement E. Furlong
    Pages 53-77
  5. Michael I. Mackness, Paul N. Durrington, Bharti Mackness
    Pages 79-92
  6. Diana M. Shih, Srinivasa Reddy, Aldons J. Lusis
    Pages 93-123
  7. Mohamad Navab, Susan Y. Hama, Alan C. Wagner, Greg Hough, Andrew D. Watson, Srinivasa T. Reddy et al.
    Pages 125-136
  8. Ronald Zech, Jörg M. Chemnitius
    Pages 137-163
  9. Lucio G. Costa, Wan-Fen Li, Rebecca J. Richter, Diana M. Shih, Aldons J. Lusis, Clement E. Furlong
    Pages 165-183
  10. Bharti Mackness, Paul N. Durrington, Michael I. Mackness
    Pages 185-195
  11. Lucio G. Costa, Clement E. Furlong
    Pages 197-210
  12. Back Matter
    Pages 211-216

About this book


The paraoxonase or PON family of genes resides on human chromosome 7q2t-22 in the order PONt, PON3 and PON2. PONt was one of the early genes identified as an environmentally relevant gene, in that it is important in determining an individual's sensitivity or resistance to exposure from specific organophosphorus (OP) insecticides. Paraoxonase (PONt) is an A­ esterase (i. e. , not inhibited by OP compounds) initially identified for its ability to catalytically hydrolyze paraoxon, the toxic metabolite (oxon form) of the insecticide parathion. Evidence accumulated in the past several years has established that this enzyme, which is present at variable levels in liver and serum of different individuals, is an important determinant of sensitivity to toxicity of specific organophosphorus compounds including chlorpyrifos oxon and diazoxon. Recent experiments have pointed out that it is the catalytic efficiency of PONt together with the levels of PONt that are important in determining the degree of resistance. Surprisingly, even though PONt has a higher catalytic efficiency than PONtQ)92 for paraoxon RJ92 hydrolysis, it does not provide significant in vivo protection against an exposure to paraoxon. Interest in this enzyme has also emerged from the finding that it displays genetic polymorphisms in most populations, with a significant number of the individuals in a given population canying a PONt gene that puts them at risk for a specific OP exposure.


cardiovascular chlorpyrifos insecticide insecticides organophosphorus toxicology

Editors and affiliations

  • Lucio G. Costa
    • 1
    • 2
  • Clement E. Furlong
    • 3
  1. 1.Department of Environmental HealthUniversity of WashingtonSeattleUSA
  2. 2.Department of Pharmacology and PhysiologyUniversity of Roma “La Sapienza”RomaItaly
  3. 3.Departments of Genome Sciences and Medicine, Division of Medical GeneticsUniversity of WashingtonSeattleUSA

Bibliographic information