acetylator

acetylator

 [ah-set″ĭ-la´ter]
an organism capable of metabolic acetylation. Individuals that differ in their inherited ability to metabolize certain drugs, e.g., isoniazid, are termed fast or slow acetylators.
References in periodicals archive ?
Two studies evaluated the association between red meat and breast cancer stratified by patients' genotypes regarding N-acetyltransferase 2 acetylator. (Differences in activity of this enzyme are thought to modify the carcinogenic effect of meat.) The researchers did not observe any association among patients with either fast or slow N-acetyltransferase 2 acetylators.
On the other hand, the authors observed a higher frequency of rapid acetylator phenotype in patients affected.
Effects of dietary factors and the NAT2 acetylator status on gastric cancer in Koreans.
Polymorphisms in this gene are responsible for the N-acetylation process in which humans are segregated into rapid, intermediate or slow acetylator phenotypes.
Anti-histone antibodies were elevated at 2.8 units (>1.5 is positive) and her N-acetyltransferase 2 (NAT2) genotype was found to be "intermediate acetylator."
Risk factors that have been linked to hydralazine induced lupus include high daily doses (>200 mg), slow acetylator, HLA-DRw4 phenotypes, therapy longer than 3 months, female gender, and a family history of autoimmune disease.
This correlation was significantly higher for the BLCA-4 protein in the slow acetylator group (p [greater than or equal to] 0.001) than for IA and FA groups (Table 6).
There is need for vigilance regarding neurological effects of isoniazid in seemingly low-risk individuals in whom development of symptoms should raise the suspicion about slow acetylator status.
Moreover, they also show that miR-200b controls miR-146a and FN expression, via the histone acetylator p300, in hyperglycemic conditions not only in the retina but also in the heart and kidney.
Determination of human NAT2 acetylator genotype by restriction fragment-length polymorphism and allele-specific amplification.
Jain et al., "Mechanism of biochemical action of substituted 4-methylbenzopyran-2-ones--part 4: hyperbolic activation of rat liver microsomal NADPH-cytochrome C reductase by the novel acetylator 7,8-diacetoxy-4-methylcoumarin," Bioorganic and Medicinal Chemistry, vol.