Acetyltransferase in Humans: Development and Tissue Distribution

Pacifici, Gian Maria; Franchi, M; Colizzi, Cesare; Giuliani, L.; Rane, A

doi:10.1159/000138181

Cited by 109 publications

(47 citation statements)

References 10 publications

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“…However, on the basis of the available literature it seems that the drugmetabolizing enzymes generally are well ex pressed in the kidney. This is particularly true for conjugating enzymes such as glucuronyl transferase [11,42], acetyltransferasc [11,34], glutathionetransfcrase [11,31], sulphotransferase [11,35], and thiomcthyltransferase and thiopurinemethyltransferase [present work].…”

Section: Discussionmentioning

confidence: 99%

Profile of Drug-Metabolizing Enzymes in the Cortex and Medulla of the Human Kidney

et al. 1989

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The cortex and medulla were isolated from kidneys whose donors (5 men and 1 woman, aged between 44 and 68 years) were undergoing nephrectomy to remove a tumor. Kidneys with normal architecture for at least two thirds of the organ were included in the study. Tissue specimens used in our experiments were free from pathological changes. The activities of the following enzymes of phase INADPH cytochrome c reductase, aminopyrine N-demethylase, ethoxycoumarin O-deethylase, ethoxyresorufin O-deethylase, microsomal and cytosolic epoxide hydrolases, glutathione reductase and glutathione peroxidase, and those of the following enzymes of phase II glutathione transferase, glucuronyl transferase, sulphotransferase, acetyltransferase, thiomethyltransferase, thiopurinemethyltransferase, thioltransferase and glyoxalase were measured. The activity in renal cortex was significantly higher than in medulla for NADPH cytochrome c reductase, cytosolic epoxide hydrolase, glutathione reductase and glutathione peroxidase (phase I enzymes), and glutathione transferase, acetyltransferase, thiomethyltransferase, thiopurinemethyltransferase, thioltransferase and glyoxalase (phase II enzymes). The other enzymes had similar activity in cortex and medulla. The distribution pattern of drug-metabolizing enzymes in the human kidney cannot be considered as a single pattern because of the observed enzyme-dependent differences between cortex and medulla.

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Section: Discussionmentioning

confidence: 99%

Profile of Drug-Metabolizing Enzymes in the Cortex and Medulla of the Human Kidney

et al. 1989

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“…Expression of human NAT1 www.intechopen.com has been detected in adult liver, bladder, digestive system, blood cells, placenta, skin, skeletal muscles, gingiva (Dupret & Lima, 2005), mammary tissue, prostate, and lung by a number of methods (Sim et al, 2008). A notable difference between the two isoenzymes is the presence of NAT1 activity in fetal and neonatal tissue, such as lungs, kidneys, and adrenal glands (Pacifici et al, 1986). By contrast, NAT2 is not evident until about 12 months after birth (Pariente-Khayat et al, 1991).…”

Section: N-acetyltransferasesmentioning

confidence: 99%

Phase II Drug Metabolism

Jančová¹,

Siller²

2012

Topics on Drug Metabolism

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“…Studies had shown expression of both NAT1 and NAT2 in human colon (Kirlin et al, 1991;Turesky et al, 1991;Ilett et al, 1994), intestine (Hickman et al, 1998) and widespread tissue distribution of human NAT1 and NAT2 mRNA (Windmill et al, 2000;Boukouvala and Sim, 2005). Although extrahepatic expression of N-acetyltransferase activities have been reported in humans (Pacifici et al, 1986), rat (Hein et al, 1991a), mouse (Chung et al, 1993;Stanley et al, 1997;Sugamori et al, 2003) and Syrian hamster (Hein et al, 1991b(Hein et al, , 1994a) models, substrates were not selective for NAT1 and NAT2. NAT2-dependent ABP-and BNA N-acetyltransferase activities have been reported in human urinary bladder Frederickson et al, 1992Frederickson et al, , 1994Pink et al, 1992;Badawi et al, 1995).…”

Section: Phenotypic Expression Of the Nat2 Polymorphismmentioning

confidence: 99%

N-acetyltransferase 2 genetic polymorphism: effects of carcinogen and haplotype on urinary bladder cancer risk

2006

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A role for the N-acetyltransferase 2 (NAT2) genetic polymorphism in cancer risk has been the subject of numerous studies. Although comprehensive reviews of the NAT2 acetylation polymorphism have been published elsewhere, the objective of this paper is to briefly highlight some important features of the NAT2 acetylation polymorphism that are not universally accepted to better understand the role of NAT2 polymorphism in carcinogenic risk assessment. NAT2 slow acetylator phenotype(s) infer a consistent and robust increase in urinary bladder cancer risk following exposures to aromatic amine carcinogens. However, identification of specific carcinogens is important as the effect of NAT2 polymorphism on urinary bladder cancer differs dramatically between monoarylamines and diarylamines. Misclassifications of carcinogen exposure and NAT2 genotype/phenotype confound evidence for a real biological effect. Functional understanding of the effects of NAT2 genetic polymorphisms on metabolism and genotoxicity, tissue-specific expression and the elucidation of the molecular mechanisms responsible are critical for the interpretation of previous and future human molecular epidemiology investigations into the role of NAT2 polymorphism on cancer risk. Although associations have been reported for various cancers, this paper focuses on urinary bladder cancer, a cancer in which a role for NAT2 polymorphism was first proposed and for which evidence is accumulating that the effect is biologically significant with important public health implications.

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Acetyltransferase in Humans: Development and Tissue Distribution

Cited by 109 publications

References 10 publications

Profile of Drug-Metabolizing Enzymes in the Cortex and Medulla of the Human Kidney

Profile of Drug-Metabolizing Enzymes in the Cortex and Medulla of the Human Kidney

Phase II Drug Metabolism

N-acetyltransferase 2 genetic polymorphism: effects of carcinogen and haplotype on urinary bladder cancer risk

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