Matrix metalloproteinase-9 and paraoxonase 1 Q/R192 gene polymorphisms and the risk of coronary artery stenosis in Iranian subjects
✍ Scribed by Soudabeh Fallah; Morteza Seifi; Asghar Ghasemi; Mohsen Firoozrai; Ali Samadikuchaksaraei
- Publisher
- John Wiley and Sons
- Year
- 2010
- Tongue
- English
- Weight
- 103 KB
- Volume
- 24
- Category
- Article
- ISSN
- 0887-8013
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✦ Synopsis
Abstract
Purpose: To investigate the association of matrix metalloproteinase‐9 (MMP‐9) and paraoxonase 1 (PON1) 192 polymorphisms with susceptibility to coronary artery stenosis (CAS) and the number of diseased vessels in patients with CAS. Methods: The study population comprised 302 unrelated Iranian individuals, including 145 patients with CAS and 157 control subjects. Genotypes for MMP‐9 and PON1 192 polymorphisms were determined by polymerase chain reaction (PCR) and restriction fragment length polymorphism (RFLP). Results: In our study, distributions of the TT genotype of MMP‐9 and the RR genotype of PON1 192 were significantly higher in patients compared with healthy control subjects (P<0.05). Subsequent analysis demonstrated that a significant difference existed in the male (TT+TC vs. CC and RR+QR vs. QQ, P<0.01) but not in the female. The associations of these polymorphisms with the severity of stenosis were also evaluated, which according to results distribution of MMP‐9 and PON1 192 genotypes were not significantly different compared with the severity of stenosis (P>0.05). Conclusions: The observation indicates that the polymorphisms in the MMP‐9 and PON1 192 genes potentially play a role in the manifestation of coronary atherosclerosis but does not have any effect on the number of diseased vessels in Iran. J. Clin. Lab. Anal. 24:305–310, 2010. © 2010 Wiley‐Liss, Inc.
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## Abstract Paraoxonase 1 (PON 1) is a high‐density lipoprotein (HDL)‐associated enzyme with antioxidant function protecting low‐density lipoprotein (LDL) from oxidation. PON 1 has two amino acid polymorphisms in coding region; L/M 55 and Q/R 192. These polymorphisms modulate paraoxonase activity o