TY - JOUR
T1 - The human serum paraoxonase/arylesterase gene (PON1) is one member of a multigene family
AU - Primo-Parmo, Sérgio L.
AU - Sorenson, Robert C.
AU - Teiber, John
AU - La Du, Bert N.
N1 - Funding Information:
The human liver cDNA library was obtained with permission from Dr. S. Woo; the chicken liver cDNA library was kindly donated by Dr. Jerry Dodgson (Department of Microbiology, Michigan State University). We are indebted to Drs. Stephen W. Scherer and Lap-Chee Tsui (Department of Molecular and Medical Genetics, University of Toronto) for providing four cosmids containing human genomic PON1 inserts and to Dr. Steve Adkins (Department of Human Genetics, University of Michigan) for the electroelution of PCR products from agarose gels. This study was supported, in part, by Grant GM 46979 from the National Institute of General Medical Sciences to B.N.L. R.C.S. was supported by Grant T32 GM07863 from NIGMS to the Medical Scientist Training Program at the University of Michigan Medical School.
PY - 1996/5/1
Y1 - 1996/5/1
N2 - A physiological role for paraoxonase (PON1) is still uncertain, but it catalyzes the hydrolysis of toxic organophosphates. Evidence that the human genome contains two PON1-like genes, designated PON2 and PON3, is presented here. Human PON1 and PON2 each have nine exons, and the exon/intron junctions occur at equivalent positions. PON1 and PON2 genes are both on chromosome 7 in human and on chromosome 6 in the mouse. Turkey and chicken, like most birds, lack paraoxonase activity and are very susceptible to organophosphates. However, they have a PON-like gene with ~70% identity with human PON1, PON2, and PON3. Another unexpected finding is that the deduced amino acid sequences of PON2 in human, mouse, dog, turkey, and chicken and of human PON3 are all missing the amino acid residue 105, which is lysine in human PON1. The expanded number of PON genes will have important implications for future experiments designed to discover the individual functions, catalytic properties, and physiological roles of the paraoxonases.
AB - A physiological role for paraoxonase (PON1) is still uncertain, but it catalyzes the hydrolysis of toxic organophosphates. Evidence that the human genome contains two PON1-like genes, designated PON2 and PON3, is presented here. Human PON1 and PON2 each have nine exons, and the exon/intron junctions occur at equivalent positions. PON1 and PON2 genes are both on chromosome 7 in human and on chromosome 6 in the mouse. Turkey and chicken, like most birds, lack paraoxonase activity and are very susceptible to organophosphates. However, they have a PON-like gene with ~70% identity with human PON1, PON2, and PON3. Another unexpected finding is that the deduced amino acid sequences of PON2 in human, mouse, dog, turkey, and chicken and of human PON3 are all missing the amino acid residue 105, which is lysine in human PON1. The expanded number of PON genes will have important implications for future experiments designed to discover the individual functions, catalytic properties, and physiological roles of the paraoxonases.
UR - http://www.scopus.com/inward/record.url?scp=0029937118&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0029937118&partnerID=8YFLogxK
U2 - 10.1006/geno.1996.0225
DO - 10.1006/geno.1996.0225
M3 - Article
C2 - 8661009
AN - SCOPUS:0029937118
SN - 0888-7543
VL - 33
SP - 498
EP - 507
JO - Genomics
JF - Genomics
IS - 3
ER -