| Autor: |
Idelfonso-García OG; Laboratory of Liver Diseases, National Institute of Genomic Medicine-INMEGEN, Mexico City 14610, Mexico.; Department of Health Sciences, Metropolitan Autonomous University-Iztapalapa Campus, Mexico City 09340, Mexico., Alarcón-Sánchez BR; Laboratory of Liver Diseases, National Institute of Genomic Medicine-INMEGEN, Mexico City 14610, Mexico.; Department of Cell Biology, Center for Research and Advanced Studies of the National Polytechnic Institute-CINVESTAV-IPN, Mexico City 07360, Mexico., Vásquez-Garzón VR; Laboratory of Fibrosis and Cancer, Faculty of Medicine and Surgery, 'Benito Juárez' Autonomous University of Oaxaca-UABJO, Oaxaca 68020, Mexico.; Directorate of Cátedras, National Council of Science and Technology-CONACYT, Mexico City 03940, Mexico., Baltiérrez-Hoyos R; Laboratory of Fibrosis and Cancer, Faculty of Medicine and Surgery, 'Benito Juárez' Autonomous University of Oaxaca-UABJO, Oaxaca 68020, Mexico.; Directorate of Cátedras, National Council of Science and Technology-CONACYT, Mexico City 03940, Mexico., Villa-Treviño S; Department of Cell Biology, Center for Research and Advanced Studies of the National Polytechnic Institute-CINVESTAV-IPN, Mexico City 07360, Mexico., Muriel P; Laboratory of Experimental Hepatology, Department of Pharmacology, Center for Research and Advanced Studies of the National Polytechnic Institute-CINVESTAV-IPN, Mexico City 07360, Mexico., Serrano H; Department of Health Sciences, Metropolitan Autonomous University-Iztapalapa Campus, Mexico City 09340, Mexico., Pérez-Carreón JI; Laboratory of Liver Diseases, National Institute of Genomic Medicine-INMEGEN, Mexico City 14610, Mexico., Arellanes-Robledo J; Laboratory of Liver Diseases, National Institute of Genomic Medicine-INMEGEN, Mexico City 14610, Mexico.; Directorate of Cátedras, National Council of Science and Technology-CONACYT, Mexico City 03940, Mexico. |
| Abstrakt: |
Nucleoredoxin (NXN), an oxidoreductase enzyme, contributes to cellular redox homeostasis by regulating different signaling pathways in a redox-dependent manner. By interacting with seven proteins so far, namely disheveled (DVL), protein phosphatase 2A (PP2A), phosphofructokinase-1 (PFK1), translocation protein SEC63 homolog (SEC63), myeloid differentiation primary response gene-88 (MYD88), flightless-I (FLII), and calcium/calmodulin-dependent protein kinase II type alpha (CAMK2A), NXN is involved in the regulation of several key cellular processes, including proliferation, organogenesis, cell cycle progression, glycolysis, innate immunity and inflammation, motility, contraction, protein transport into the endoplasmic reticulum, neuronal plasticity, among others; as a result, NXN has been implicated in different pathologies, such as cancer, alcoholic and polycystic liver disease, liver fibrogenesis, obesity, Robinow syndrome, diabetes mellitus, Alzheimer's disease, and retinitis pigmentosa. Together, this evidence places NXN as a strong candidate to be a master redox regulator of cell physiology and as the hub of different redox-sensitive signaling pathways and associated pathologies. This review summarizes and discusses the current insights on NXN-dependent redox regulation and its implication in different pathologies. |
