Search results for: John J. Mieyal

Items from 1 to 17 out of 17 results

article

Reply to the Commentary “To Gorelenkova Miller and Mieyal (2015): Sulfhydryl-mediated redox signaling in inflammation: role in neurodegenerative diseases” by M. Kato

Olga Gorelenkova Miller, John J. Mieyal

Archives of Toxicology > 2016 > 90 > 4 > 1019-1020

article

Supplemental Online Pharmacology Modules Increase Recognition and Production Memory in a Hybrid Problem-Based Learning (PBL) Curriculum

Peggy Y. Kim, David W. Allbritton, Ruth A. Keri, John J. Mieyal, more

Medical Science Educator > 2015 > 25 > 3 > 261-269

Introduction Problem-based learning (PBL) presents unique challenges to longitudinal disciplines such as pharmacology. A curricular supplement (PharmWeb) was created to increase pharmacology knowledge, increase surface learning/recognition memory, and increase deeper learning/production memory. Methods First-year medical students (162) were presented 14 brief, optional, self-paced, weekly online...

article

Sulfhydryl-mediated redox signaling in inflammation: role in neurodegenerative diseases

Olga Gorelenkova Miller, John J. Mieyal

Archives of Toxicology > 2015 > 89 > 9 > 1439-1467

Posttranslational modifications of cysteine sulfhydryl (–SH) moieties, e.g., S-nitrosylation, S-glutathionylation, or S-sulfuration, play an important role in cellular response to oxidative stress. Reversible cysteine modifications alter protein function and can play a critical role in redox signal transduction. Perturbation of sulfhydryl homeostasis is a hallmark of many diseases, including neurodegenerative...

article

N-acetyl-l-cysteine sensitizes pancreatic cancers to gemcitabine by targeting the NFκB pathway

Suparna Qanungo, Joachim D. Uys, Yefim Manevich, Anne M. Distler, more

Biomedicine & Pharmacotherapy > 2014 > 68 > 7 > 855-864

First-line therapy for pancreatic cancer is gemcitabine. Although tumors may initially respond to the gemcitabine treatment, soon tumor resistance develops leading to treatment failure. Previously, we demonstrated in human MIA PaCa-2 pancreatic cancer cells that N-acetyl-l-cysteine (NAC), a glutathione (GSH) precursor, prevents NFκB activation via S-glutathionylation of p65-NFκB, thereby blunting...

article

Levodopa Activates Apoptosis Signaling Kinase 1 (ASK1) and Promotes Apoptosis in a Neuronal Model: Implications for the Treatment of Parkinson's Disease

Elizabeth A. Sabens Liedhegner, Kelly M. Steller, John J. Mieyal

Chemical Research in Toxicology > 2011 > 24 > 10 > 1644 - 1652

article

Levodopa Deactivates Enzymes That Regulate Thiol−Disulfide Homeostasis and Promotes Neuronal Cell Death: Implications for Therapy of Parkinson’s Disease

Elizabeth A. Sabens, Anne M. Distler, John J. Mieyal

Biochemistry > 2010 > 49 > 12 > 2715 - 2724

article

Covalent Cross-Linking of Glutathione and Carnosine to Proteins by 4-Oxo-2-nonenal ^†

Xiaochun Zhu, Molly M. Gallogly, John J. Mieyal, Vernon E. Anderson, more

Chemical Research in Toxicology > 2009 > 22 > 6 > 1050 - 1059

chapter

Glutaredoxin and Thioredoxin Enzyme Systems: Catalytic Mechanisms and Physiological Functions

Elizabeth A. Sabens, John J. Mieyal

Glutathione and Sulfur Amino Acids in Human Health and Disease > Antioxidant and Detoxification Activities > 121 - 156

This chapter contains sections titled: Introduction General Characteristics of Glutaredoxins General Characteristics of Thioredoxins Glutaredoxin Mechanism of Action Thioredoxin Mechanism of Action Control of Grx Expression Control of Trx Expression in Mammalian Systems Cellular Functions of Grx Cellular Functions of Trx Reversible Sulfhydryl Oxidation and Disease Conclusions References

article

Kinetic and Mechanistic Characterization and Versatile Catalytic Properties of Mammalian Glutaredoxin 2: Implications for Intracellular Roles ^†

Molly M. Gallogly, David W. Starke, Amanda K. Leonberg, Susan M. English Ospina, more

Biochemistry > 2008 > 47 > 42 > 11144 - 11157

article

Targeted disruption of the glutaredoxin 1 gene does not sensitize adult mice to tissue injury induced by ischemia/reperfusion and hyperoxia

Ye-Shih Ho, Ye Xiong, Dorothy S. Ho, Jinping Gao, more

Free Radical Biology and Medicine > 2007 > 43 > 9 > 1299-1312

To understand the physiological function of glutaredoxin, a thiotransferase catalyzing the reduction of mixed disulfides of protein and glutathione, we generated a line of knockout mice deficient in the cytosolic glutaredoxin 1 (Grx1). To our surprise, mice deficient in Grx1 were not more susceptible to acute oxidative insults in models of heart and lung injury induced by ischemia/reperfusion and...

article

Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress

Molly M Gallogly, John J Mieyal

Current Opinion in Pharmacology > 2007 > 7 > 4 > 381-391

Reversible protein S-glutathionylation (protein-SSG) is an important post-translational modification, providing protection of protein cysteines from irreversible oxidation and serving to transduce redox signals. Analogous to phosphatases, glutaredoxin (GRx) enzymes catalyze deglutathionylation of proteins, regulating diverse intracellular signaling pathways. Recently, other enzymes have been reported...

article

Molecular mechanism of glutathione-mediated protection from oxidized low-density lipoprotein-induced cell injury in human macrophages: Role of glutathione reductase and glutaredoxin

Yanmei Wang, Mu Qiao, John J. Mieyal, Lars M. Asmis, more

Free Radical Biology and Medicine > 2006 > 41 > 5 > 775-785

Macrophage death is a hallmark of advanced atherosclerotic plaque, and oxidized low-density lipoprotein (OxLDL) found in these lesions is believed to contribute to macrophage injury. However, the underlying mechanisms of this phenomenon are only poorly understood. Here we show that in human monocyte-derived macrophages, OxLDL depleted intracellular glutathione (GSH) and inhibited glutathione reductase,...

article

Selective Inactivation of Glutaredoxin by Sporidesmin and Other Epidithiopiperazinediones ^† ^, ^‡

Usha Srinivasan, Aveenash Bala, Shu-chuan Jao, David W. Starke, more

Biochemistry > 2006 > 45 > 29 > 8978 - 8987

article

Computational and Mutational Analysis of Human Glutaredoxin (Thioltransferase): Probing the Molecular Basis of the Low p K _a of Cysteine 22 and Its Role in Catalysis ^† ^, ^‡ ^, ^§

Shu-Chuan Jao, Susan M. English Ospina, Anthony J. Berdis, David W. Starke, more

Biochemistry > 2006 > 45 > 15 > 4785 - 4796

article

Reversible Inactivation of α-Ketoglutarate Dehydrogenase in Response to Alterations in the Mitochondrial Glutathione Status ^†

Amy C. Nulton-Persson, David W. Starke, John J. Mieyal, Luke I. Szweda

Biochemistry > 2003 > 42 > 14 > 4235 - 4242

article

Sensitivity of Protein Sulfhydryl Repair Enzymes to Oxidative Stress

David W Starke, Yuegang Chen, Chandra P Bapna, Edward J Lesnefsky, more

Free Radical Biology and Medicine > 1997 > 23 > 3 > 373-384

According to their demonstrated activities, the thiol-disulfide oxidoreductase (TDOR) enzyme systems [thioltransferase (glutaredoxin) and GSSG reductase; and thioredoxin and thioredoxin reductase] are expected to provide the primary cellular mechanism for protection and repair of sulfhydryl proteins under oxidative stress. Since all four enzymes have active site dithiol moieties, they may be vulnerable...

article

Cloning, expression and characterization of human thioltransferase (glutaredoxin) in E. coli

Carol A. Chrestensen, Christopher B. Eckman, David W. Starke, John J. Mieyal

FEBS Letters > 1995 > 374 > 1 > 25-28

PCR primers were designed from the known amino acid (aa) sequence for human red blood cell thioltransferase (hRBC TTase) and the known cDNA sequence for pig liver TTase (82% homologous) and used to amplify thioltransferase from a pool of human brain cDNAs. The PCR product was inserted into the pKK233-2 expression vector. The DNA sequence of the insert agreed with the aa sequence. High level expression...

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Search results for: John J. Mieyal

Reply to the Commentary “To Gorelenkova Miller and Mieyal (2015): Sulfhydryl-mediated redox signaling in inflammation: role in neurodegenerative diseases” by M. Kato

Supplemental Online Pharmacology Modules Increase Recognition and Production Memory in a Hybrid Problem-Based Learning (PBL) Curriculum

Sulfhydryl-mediated redox signaling in inflammation: role in neurodegenerative diseases

N-acetyl-l-cysteine sensitizes pancreatic cancers to gemcitabine by targeting the NFκB pathway

Levodopa Activates Apoptosis Signaling Kinase 1 (ASK1) and Promotes Apoptosis in a Neuronal Model: Implications for the Treatment of Parkinson's Disease

Levodopa Deactivates Enzymes That Regulate Thiol−Disulfide Homeostasis and Promotes Neuronal Cell Death: Implications for Therapy of Parkinson’s Disease

Covalent Cross-Linking of Glutathione and Carnosine to Proteins by 4-Oxo-2-nonenal ^†

Glutaredoxin and Thioredoxin Enzyme Systems: Catalytic Mechanisms and Physiological Functions

Kinetic and Mechanistic Characterization and Versatile Catalytic Properties of Mammalian Glutaredoxin 2: Implications for Intracellular Roles ^†

Targeted disruption of the glutaredoxin 1 gene does not sensitize adult mice to tissue injury induced by ischemia/reperfusion and hyperoxia

Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress

Molecular mechanism of glutathione-mediated protection from oxidized low-density lipoprotein-induced cell injury in human macrophages: Role of glutathione reductase and glutaredoxin

Selective Inactivation of Glutaredoxin by Sporidesmin and Other Epidithiopiperazinediones ^† ^, ^‡

Computational and Mutational Analysis of Human Glutaredoxin (Thioltransferase): Probing the Molecular Basis of the Low p K _a of Cysteine 22 and Its Role in Catalysis ^† ^, ^‡ ^, ^§

Reversible Inactivation of α-Ketoglutarate Dehydrogenase in Response to Alterations in the Mitochondrial Glutathione Status ^†

Sensitivity of Protein Sulfhydryl Repair Enzymes to Oxidative Stress

Cloning, expression and characterization of human thioltransferase (glutaredoxin) in E. coli

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