دورية أكاديمية
The Arylamine N-Acetyltransferases as Therapeutic Targets in Metabolic Diseases Associated with Mitochondrial Dysfunction.
| العنوان: | The Arylamine N-Acetyltransferases as Therapeutic Targets in Metabolic Diseases Associated with Mitochondrial Dysfunction. |
|---|---|
| المؤلفون: | Choudhury C; School of Biomedical Sciences (C.C., M.K.G., C.E.M., N.J.B., F.J.S., R.F.M.) and Australian Institute for Bioengineering and Nanotechnology (S.T.N.), University of Queensland, Brisbane, Australia., Gill MK; School of Biomedical Sciences (C.C., M.K.G., C.E.M., N.J.B., F.J.S., R.F.M.) and Australian Institute for Bioengineering and Nanotechnology (S.T.N.), University of Queensland, Brisbane, Australia., McAleese CE; School of Biomedical Sciences (C.C., M.K.G., C.E.M., N.J.B., F.J.S., R.F.M.) and Australian Institute for Bioengineering and Nanotechnology (S.T.N.), University of Queensland, Brisbane, Australia., Butcher NJ; School of Biomedical Sciences (C.C., M.K.G., C.E.M., N.J.B., F.J.S., R.F.M.) and Australian Institute for Bioengineering and Nanotechnology (S.T.N.), University of Queensland, Brisbane, Australia., Ngo ST; School of Biomedical Sciences (C.C., M.K.G., C.E.M., N.J.B., F.J.S., R.F.M.) and Australian Institute for Bioengineering and Nanotechnology (S.T.N.), University of Queensland, Brisbane, Australia., Steyn FJ; School of Biomedical Sciences (C.C., M.K.G., C.E.M., N.J.B., F.J.S., R.F.M.) and Australian Institute for Bioengineering and Nanotechnology (S.T.N.), University of Queensland, Brisbane, Australia., Minchin RF; School of Biomedical Sciences (C.C., M.K.G., C.E.M., N.J.B., F.J.S., R.F.M.) and Australian Institute for Bioengineering and Nanotechnology (S.T.N.), University of Queensland, Brisbane, Australia. |
| المصدر: | Pharmacological reviews [Pharmacol Rev] 2024 Feb 13; Vol. 76 (2), pp. 300-320. Date of Electronic Publication: 2024 Feb 13. |
| نوع المنشور: | Journal Article; Review |
| اللغة: | English |
| بيانات الدورية: | Publisher: American Society for Pharmacology and Experimental Therapeutics Country of Publication: United States NLM ID: 0421737 Publication Model: Electronic Cited Medium: Internet ISSN: 1521-0081 (Electronic) Linking ISSN: 00316997 NLM ISO Abbreviation: Pharmacol Rev Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Bethesda, Md : American Society for Pharmacology and Experimental Therapeutics Original Publication: Baltimore, Williams & Wilkins. |
| مواضيع طبية MeSH: | Arylamine N-Acetyltransferase*/genetics , Arylamine N-Acetyltransferase*/metabolism , Metabolic Diseases*/drug therapy , Mitochondrial Diseases*/drug therapy, Humans ; Acetyltransferases/genetics ; Acetyltransferases/metabolism ; Substrate Specificity |
| مستخلص: | In humans, there are two arylamine N-acetyltransferase genes that encode functional enzymes ( NAT1 and NAT2 ) as well as one pseudogene, all of which are located together on chromosome 8. Although they were first identified by their role in the acetylation of drugs and other xenobiotics, recent studies have shown strong associations for both enzymes in a variety of diseases, including cancer, cardiovascular disease, and diabetes. There is growing evidence that this association may be causal. Consistently, NAT1 and NAT2 are shown to be required for healthy mitochondria. This review discusses the current literature on the role of both NAT1 and NAT2 in mitochondrial bioenergetics. It will attempt to relate our understanding of the evolution of the two genes with biologic function and then present evidence that several major metabolic diseases are influenced by NAT1 and NAT2. Finally, it will discuss current and future approaches to inhibit or enhance NAT1 and NAT2 activity/expression using small-molecule drugs. SIGNIFICANCE STATEMENT: The arylamine N-acetyltransferases (NATs) NAT1 and NAT2 share common features in their associations with mitochondrial bioenergetics. This review discusses mitochondrial function as it relates to health and disease, and the importance of NAT in mitochondrial function and dysfunction. It also compares NAT1 and NAT2 to highlight their functional similarities and differences. Both NAT1 and NAT2 are potential drug targets for diseases where mitochondrial dysfunction is a hallmark of onset and progression. (Copyright © 2024 by The American Society for Pharmacology and Experimental Therapeutics.) |
| المشرفين على المادة: | EC 2.3.1.5 (Arylamine N-Acetyltransferase) EC 2.3.1.- (Acetyltransferases) EC 2.3.1.5 (NAT2 protein, human) |
| تواريخ الأحداث: | Date Created: 20240213 Date Completed: 20240215 Latest Revision: 20240215 |
| رمز التحديث: | 20240215 |
| DOI: | 10.1124/pharmrev.123.000835 |
| PMID: | 38351074 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 1521-0081 |
|---|---|
| DOI: | 10.1124/pharmrev.123.000835 |