Investigation of the relationship between atherosclerosis and paraoxonase or homocysteine thiolactonase activity in patients with type 2 diabetes mellitus using a commercially available assay.
BACKGROUND
It is known that serum paraoxonase activity decreases in patients with atherosclerotic diseases such as type 2 diabetes mellitus. Paraoxonase hydrolyzes homocysteine thiolactone, which is thought to be an endogenous substrate. The relationship between the status of atherosclerosis and homocysteine thiolactonase activity in patients with type 2 diabetes mellitus was investigated.


METHODS
Serum homocysteine thiolactonase activities in 207 patients with type 2 diabetes mellitus were measured with a recently developed commercially available assay.


RESULTS
The coefficient of variation for the assay was <0.7%. Serum paraoxonase and arylesterase activities were dependent on the PON1 192 polymorphism expressed by the subjects but homocysteine thiolactonase activity was not affected. A tendency for a negative association between homocysteine thiolactonase activity and the thickness of the carotid intima media was observed in patients with type 2 diabetes mellitus.


CONCLUSIONS
The serum homocysteine thiolactonase activity may represent the status of atherosclerosis in patients with type 2 diabetes mellitus. Since the assay can be used with a routine analyzer, the activities of thousands of samples can be measured with excellent precision in a few hours.
Kosaka
Tetsuya
T
Diagnostic R and D Dept., R and D Headquarters, Alfresa Pharma Corporation, 2-24-3 Sho, Ibaraki-city, Osaka 567-0806, Japan. te-kosaka@alfresa-pharma.co.jp
Yamaguchi
Masahiro
M
Motomura
Takashi
T
Mizuno
Koji
K
D001161:Arteriosclerosis / Q000150:complications / Q000201:enzymology*; D043303:Aryldialkylphosphatase / Q000097:blood*; D003924:Diabetes Mellitus, Type 2 / Q000097:blood* / Q000150:complications; D005260:Female; D006801:Humans; D008297:Male; D008875:Middle Aged; D011933:Reagent Kits, Diagnostic
D011933:Reagent Kits, Diagnostic; D043303:Aryldialkylphosphatase