Prolidase, paraoxonase-1, arylesterase activity in oral squamous cell carcinoma, a preliminary study.

INTRODUCTION: In many types of cancer, reactive oxygen and nitrogen products have been detected at high levels. Arylesterase, and paraoxonase1 are esterase enzymes that have strong antioxidant characteristics. The prolidase enzyme is a rate-limiting metalloenzyme which also plays a role in collagen turnover, and is dependent on its NO-activity. In this study, we aimed to investigate the possible relationship between serum paraoxonase1, arilesterase and prolidase enzyme activity in patients with squamous cell carcinoma of the oral cavity and to investigate the etiology and mechanism of oral cavity cancer.
METHODS: The study included 24 patients with oral cavity cancer, and 22 healthy age- and sex- matched individuals. Arylesterase, paraoxonase1 and prolidase activities were measured using spectrophotometry.
RESULTS: Paraoxonase1 activity was 11.6±2.32 nmol/l in the patient group and 29.46±6.18 nmol/l in the controls. Arylesterase activity was 32.2±14.57 nmol/l in the patient group and 80.71±7.23 nmol/l in the controls. Prolidase activity was 39.51±3.02 nmol/l in the patient group and 19.53±1.13 nmol/l in the controls.The mean paraoxonase1 and arylesterase levels in the patient group were statistically lower than the control group and the mean prolidase levels were high (p = 0.0001).
DISCUSSION AND CONCLUSION: In our study, arylesterase and paraoxonase1 enzyme activity was low in patients with oral cavity cancer. The prolidase activity was higher in the same group. As a result, paraoxonase1, arylesterase and prolidase enzyme activities play an important role in the etiopathogenesis of oral cavity cancers. In addition, more research should be done on both clinical and molecular levels of oral cavity cancer.