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Differences in metabolite genotoxicity test results of rat liver S9 microsomes treated with various microsomal enzyme inducers.
Toxicol Mech Methods
January 2025
Drug Safety Research and Evaluation, Research, Takeda Pharmaceutical Company Limited, Fujisawa, Japan.
The rat S9 microsome fraction is commonly used to assess compound metabolite formation during genotoxicity assessments. However, methods using S9 have not been standardized for genotoxicity studies, and different experimental methods are used at various facilities. Therefore, this study investigated whether the differences between the two experimental conditions (1) S9 inducers, phenobarbital + beta-naphthoflavones vs.
View Article and Find Full Text PDFConstruction of a pumpless gravity-driven vascularized Skin-on-a-Chip for the study of hepatocytotoxicity in percutaneous exposure to exogenous chemicals.
Biomed Microdevices
September 2024
Department of Health Toxicology, College of Naval Medicine, Naval Medical University, Shanghai, 200433, China.
Article Synopsis
- Existing Skin-on-a-Chip (SoC) technology faces limitations due to complex structures and the need for multiple devices, hindering the assessment of harmful chemicals that impact liver health after skin contact.
- A new gravity-driven SoC was developed, featuring three layers of cell chambers (human skin, blood vessel cells, and liver cells) that allows for effective study of liver toxicity from exogenous chemicals, with validation through specific parameters.
- This SoC accurately mimics the way chemicals are absorbed through the skin, processed in the bloodstream, and affect the liver, offering a potential substitute for animal testing in evaluating the safety of skin-penetrating chemicals.
Urinary Amino-PAHs in relation to diesel engine emissions and urinary mutagenicity.
Int J Hyg Environ Health
August 2023
Division of Cancer Epidemiology and Genetics, National Cancer Institute, Bethesda, MD, USA.
Diesel exhaust has long been of health concern due to established toxicity including carcinogenicity in humans. However, the precise components of diesel engine emissions that drive carcinogenesis are still unclear. Limited work has suggested that nitrated polycyclic aromatic hydrocarbons (NPAHs) such as 1-nitropyrene and 2-nitrofluorene may be more abundant in diesel exhaust.
View Article and Find Full Text PDFMolecular and Functional Characterization of -Acetyltransferases in Common Marmosets and Pigs.
Drug Metab Dispos
November 2022
Joint Faculty of Veterinary Medicine, Kagoshima University, Kagoshima, Japan (Y.U., M.I., A.A., M.S.); Laboratory of Drug Metabolism and Pharmacokinetics, Showa Pharmaceutical University, Tokyo, Japan(S.U., K.B., N.M., H.Y.); and School of Veterinary Medicine, Kitasato University, Aomori, Japan (H.K.)
Arylamine -acetyltransferases (NATs) are drug-metabolizing enzymes that are essential for the metabolism of endogenous substrates and xenobiotics. The molecular characteristics of NATs have been extensively investigated in humans but remain to be investigated in common marmosets and pigs, animal species that are often used in drug metabolism studies. In this study, marmoset NAT1 and pig NAT1 cDNAs were isolated from liver samples and were characterized by molecular analyses and drug-metabolism assays.
View Article and Find Full Text PDFHuman -Acetyltransferase 1 and 2 Differ in Affinity Towards Acetyl-Coenzyme A Cofactor and -Hydroxy-Arylamine Carcinogens.
Front Pharmacol
February 2022
Department of Pharmacology and Toxicology, University of Louisville School of Medicine, Louisville, KY, United States.
Arylamine N-acetyltransferases catalyze the transfer of acetyl groups from the endogenous cofactor acetyl coenzyme A (AcCoA) to arylamine (-acetylation) and -hydroxy-arylamine (-acetylation) acceptors. Humans express two arylamine -acetyltransferase isozymes (NAT1 and NAT2) which catalyze both - and -acetylation but differ in genetic regulation, substrate selectivity, and expression in human tissues. We investigated recombinant human and expressed in an JM105 and expression systems as well as in Chinese hamster ovary (CHO) cells to assess the relative affinity of AcCoA for human NAT1 and NAT2.
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