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Article ; Online: Amyloid and the macrophage: it's all about local production of IL-1β.

Broniowska, Katarzyna A / Corbett, John A

2014 Volume 63, Issue 5, Page(s) 1448–1450

MeSH term(s)	Animals ; Diabetes Mellitus, Type 2/metabolism ; Insulin-Secreting Cells/metabolism ; Interleukin-1beta/biosynthesis ; Islet Amyloid Polypeptide/pharmacology ; Islets of Langerhans/metabolism ; Macrophages/metabolism
Chemical Substances	Interleukin-1beta ; Islet Amyloid Polypeptide
Language	English
Publishing date	2014-04-21
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	80085-5
ISSN	1939-327X ; 0012-1797
ISSN (online)	1939-327X
ISSN	0012-1797
DOI	10.2337/db14-0003
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Article ; Online: Peroxiredoxin 1 plays a primary role in protecting pancreatic β-cells from hydrogen peroxide and peroxynitrite.

Stancill, Jennifer S / Happ, John T / Broniowska, Katarzyna A / Hogg, Neil / Corbett, John A

American journal of physiology. Regulatory, integrative and comparative physiology

2020 Volume 318, Issue 5, Page(s) R1004–R1013

Abstract: Both reactive nitrogen and oxygen species (RNS and ROS), such as nitric oxide, peroxynitrite, and hydrogen peroxide, have been implicated as mediators of pancreatic β-cell damage during the pathogenesis of autoimmune diabetes. While β-cells are thought ... ...

Abstract	Both reactive nitrogen and oxygen species (RNS and ROS), such as nitric oxide, peroxynitrite, and hydrogen peroxide, have been implicated as mediators of pancreatic β-cell damage during the pathogenesis of autoimmune diabetes. While β-cells are thought to be vulnerable to oxidative damage due to reportedly low levels of antioxidant enzymes, such as catalase and glutathione peroxidase, we have shown that they use thioredoxin reductase to detoxify hydrogen peroxide. Thioredoxin reductase is an enzyme that participates in the peroxiredoxin antioxidant cycle. Peroxiredoxins are expressed in β-cells and, when overexpressed, protect against oxidative stress, but the endogenous roles of peroxiredoxins in the protection of β-cells from oxidative damage are unclear. Here, using either glucose oxidase or menadione to continuously deliver hydrogen peroxide, or the combination of dipropylenetriamine NONOate and menadione to continuously deliver peroxynitrite, we tested the hypothesis that β-cells use peroxiredoxins to detoxify both of these reactive species. Either pharmacological peroxiredoxin inhibition with conoidin A or specific depletion of cytoplasmic peroxiredoxin 1 (
MeSH term(s)	Animals ; Cell Death ; Cell Line, Tumor ; Cytoplasm/enzymology ; Cytoprotection ; DNA Damage ; Enzyme Inhibitors/pharmacology ; Hydrogen Peroxide/toxicity ; Insulin-Secreting Cells/drug effects ; Insulin-Secreting Cells/enzymology ; Insulin-Secreting Cells/pathology ; Male ; Oxidative Stress/drug effects ; Peroxiredoxins/antagonists & inhibitors ; Peroxiredoxins/genetics ; Peroxiredoxins/metabolism ; Peroxynitrous Acid/toxicity ; Quinoxalines/pharmacology ; RNA Interference ; RNA, Small Interfering/genetics ; RNA, Small Interfering/metabolism ; Rats, Sprague-Dawley ; Signal Transduction ; Thioredoxin Reductase 1/metabolism
Chemical Substances	Enzyme Inhibitors ; Quinoxalines ; RNA, Small Interfering ; conoidin A ; Peroxynitrous Acid (14691-52-2) ; Hydrogen Peroxide (BBX060AN9V) ; Prdx1 protein, rat (EC 1.11.1.14) ; Peroxiredoxins (EC 1.11.1.15) ; Thioredoxin Reductase 1 (EC 1.8.1.9) ; Txnrd1 protein, rat (EC 1.8.1.9)
Language	English
Publishing date	2020-04-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	603839-6
ISSN	1522-1490 ; 0363-6119
ISSN (online)	1522-1490
ISSN	0363-6119
DOI	10.1152/ajpregu.00011.2020
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Article ; Online: Pancreatic β-cells detoxify H

Stancill, Jennifer S / Broniowska, Katarzyna A / Oleson, Bryndon J / Naatz, Aaron / Corbett, John A

The Journal of biological chemistry

2019 Volume 294, Issue 13, Page(s) 4843–4853

Abstract: Oxidative stress is thought to promote pancreatic β-cell dysfunction and contribute to both type 1 and type 2 diabetes. Reactive oxygen species (ROS), such as superoxide and hydrogen peroxide, are mediators of oxidative stress that arise largely from ... ...

Abstract	Oxidative stress is thought to promote pancreatic β-cell dysfunction and contribute to both type 1 and type 2 diabetes. Reactive oxygen species (ROS), such as superoxide and hydrogen peroxide, are mediators of oxidative stress that arise largely from electron leakage during oxidative phosphorylation. Reports that β-cells express low levels of antioxidant enzymes, including catalase and GSH peroxidases, have supported a model in which β-cells are ill-equipped to detoxify ROS. This hypothesis seems at odds with the essential role of β-cells in the control of metabolic homeostasis and organismal survival through exquisite coupling of oxidative phosphorylation, a prominent ROS-producing pathway, to insulin secretion. Using glucose oxidase to deliver H
MeSH term(s)	Animals ; Cell Survival ; DNA Damage ; Hydrogen Peroxide/metabolism ; Insulin Secretion ; Insulin-Secreting Cells/metabolism ; Male ; Oxidation-Reduction ; Peroxiredoxins/metabolism ; Rats ; Rats, Sprague-Dawley ; Thioredoxin-Disulfide Reductase/metabolism ; Thioredoxins/metabolism
Chemical Substances	Thioredoxins (52500-60-4) ; Hydrogen Peroxide (BBX060AN9V) ; Peroxiredoxins (EC 1.11.1.15) ; Thioredoxin-Disulfide Reductase (EC 1.8.1.9)
Language	English
Publishing date	2019-01-18
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA118.006219
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Article ; Online: The chemical biology of S-nitrosothiols.

Broniowska, Katarzyna A / Hogg, Neil

Antioxidants & redox signaling

2012 Volume 17, Issue 7, Page(s) 969–980

Abstract: Significance: S-nitrosothiol formation and protein S-nitrosation is an important nitric oxide (NO)-dependent signaling paradigm that is relevant to almost all aspects of cell biology, from proliferation, to homeostasis, to programmed cell death. However, ...

Abstract	Significance: S-nitrosothiol formation and protein S-nitrosation is an important nitric oxide (NO)-dependent signaling paradigm that is relevant to almost all aspects of cell biology, from proliferation, to homeostasis, to programmed cell death. However, the mechanisms by which S-nitrosothiols are formed are still largely unknown, and there are gaps of understanding between the known chemical biology of S-nitrosothiols and their reported functions. Recent advances: This review attempts to describe the biological chemistry of S-nitrosation and to point out where the challenges lie in matching the known chemical biology of these compounds with their reported functions. The review will detail new discoveries concerning the mechanisms of the formation of S-nitrosothiols in biological systems. Critical issues: Although S-nitrosothiols may be formed with some degree of specificity on particular protein thiols, through un-catalyzed chemistry, and mechanisms for their degradation and redistribution are present, these processes are not sufficient to explain the vast array of specific and targeted responses of NO that have been attributed to S-nitrosation. Elements of catalysis have been discovered in the formation, distribution, and metabolism of S-nitrosothiols, but it is less clear whether these represent a specific network for targeted NO-dependent signaling. Future directions: Much recent work has uncovered new targets for S-nitrosation through either targeted or proteome-wide approaches There is a need to understand which of these modifications represent concerted and targeted signaling processes and which is an inevitable consequence of living with NO. There is still much to be learned about how NO transduces signals in cells and the role played by protein S-nitrosation.
MeSH term(s)	Animals ; Humans ; Nitric Oxide/metabolism ; Nitrosation/physiology ; S-Nitrosothiols/chemistry ; S-Nitrosothiols/metabolism
Chemical Substances	S-Nitrosothiols ; Nitric Oxide (31C4KY9ESH)
Language	English
Publishing date	2012-06-07
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	1483836-9
ISSN	1557-7716 ; 1523-0864
ISSN (online)	1557-7716
ISSN	1523-0864
DOI	10.1089/ars.2012.4590
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Article ; Online: Reply to Gurgul-Convey and Lenzen: Cytokines, nitric oxide, and β-cells.

Broniowska, Katarzyna A / Mathews, Clayton E / Corbett, John A

The Journal of biological chemistry

2015 Volume 290, Issue 16, Page(s) 10571

MeSH term(s)	Animals ; Islets of Langerhans/metabolism ; Nitric Oxide/metabolism ; Superoxides/metabolism
Chemical Substances	Superoxides (11062-77-4) ; Nitric Oxide (31C4KY9ESH)
Language	English
Publishing date	2015-06-10
Publishing country	United States
Document type	Letter ; Comment
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.l115.648600
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Article: β-Cell responses to nitric oxide.

Broniowska, Katarzyna A / Oleson, Bryndon J / Corbett, John A

Vitamins and hormones

2014 Volume 95, Page(s) 299–322

Abstract: Autoimmune diabetes is characterized by the selective destruction of insulin-secreting β-cells that occurs during an inflammatory reaction in and around pancreatic islets of Langerhans. Cytokines such as interleukin-1, released by activated immune cells, ...

Abstract	Autoimmune diabetes is characterized by the selective destruction of insulin-secreting β-cells that occurs during an inflammatory reaction in and around pancreatic islets of Langerhans. Cytokines such as interleukin-1, released by activated immune cells, have been shown to inhibit insulin secretion from pancreatic β-cells and cause islet destruction. In response to cytokines, β-cells express inducible nitric oxide synthase and produce micromolar levels of the free radical nitric oxide. Nitric oxide inhibits the mitochondrial oxidation of glucose resulting in an impairment of insulin secretion. Nitric oxide is also responsible for cytokine-mediated DNA damage in β-cells. While nitric oxide mediates the inhibitory and toxic effects of cytokines, it also activates protective pathways that allow β-cells to recover from this damage. This review will focus on the dual role of nitric oxide as a mediator of cytokine-induced damage and the activator of repair mechanisms that protect β-cells from cytokine-mediated injury.
MeSH term(s)	Animals ; Apoptosis ; Cytokines/metabolism ; Diabetes Mellitus, Type 1/immunology ; Diabetes Mellitus, Type 1/metabolism ; Diabetes Mellitus, Type 1/pathology ; Endoplasmic Reticulum Stress ; Humans ; Insulin/metabolism ; Insulin Secretion ; Insulin-Secreting Cells/immunology ; Insulin-Secreting Cells/metabolism ; Insulin-Secreting Cells/pathology ; Models, Biological ; Necrosis ; Nitric Oxide/metabolism ; Nitric Oxide Synthase Type II/metabolism
Chemical Substances	Cytokines ; Insulin ; Nitric Oxide (31C4KY9ESH) ; NOS2 protein, human (EC 1.14.13.39) ; Nitric Oxide Synthase Type II (EC 1.14.13.39)
Language	English
Publishing date	2014-01-09
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	201161-x
ISSN	2162-2620 ; 0083-6729
ISSN (online)	2162-2620
ISSN	0083-6729
DOI	10.1016/B978-0-12-800174-5.00012-0
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Article ; Online: Differential mechanisms of inhibition of glyceraldehyde-3-phosphate dehydrogenase by S-nitrosothiols and NO in cellular and cell-free conditions.

Broniowska, Katarzyna A / Hogg, Neil

American journal of physiology. Heart and circulatory physiology

2010 Volume 299, Issue 4, Page(s) H1212–9

Abstract: S-nitrosothiols are nitric oxide (NO)-derived molecules found in biological systems. They have been variously discussed as both NO reservoirs and as major actors in NO-dependent, but cGMP-independent, signal transduction. Although S-nitrosation of ... ...

Abstract	S-nitrosothiols are nitric oxide (NO)-derived molecules found in biological systems. They have been variously discussed as both NO reservoirs and as major actors in NO-dependent, but cGMP-independent, signal transduction. Although S-nitrosation of specific cysteine residues has been suggested to represent a novel redox-based signaling mechanism, the exact mechanisms of S-nitrosothiol formation under (patho)physiological conditions and the determinants of signaling specificity have not yet been established. Here we examined the sensitivity of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) to inhibition by S-nitrosocysteine (CysNO) and NO both intracellularly and in isolation. Bovine aortic endothelial cells (BAECs) and purified GAPDH preparations were treated with CysNO or NO, and enzymatic activity was monitored. Intracellular GAPDH was irreversibly inhibited upon CysNO administration, whereas treatment with NO resulted in a DTT-reversible inhibition of the enzyme. Purified GAPDH was inhibited by both CysNO and NO, but the inhibition pattern was diametrically opposite to that observed in the cells; CysNO-dependent inhibition was reversed with DTT, whereas NO-dependent inhibition was not. In the presence of GSH, NO inhibited purified GAPDH in a DTT-reversible way. Our data suggest that in response to CysNO treatment, cellular GAPDH undergoes S-nitrosation, which results in an irreversible inhibition of the enzyme under turnover conditions. In contrast, NO inhibits the enzyme via oxidative mechanisms that do not involve S-nitrosation and are reversible. In summary, our data show that GAPDH is a target for CysNO- and NO-dependent inhibition; however, these two agents inhibit the enzyme via different mechanisms both inside the cell and in isolation. Additionally, the differences observed between the cellular system and purified protein strongly imply that the intracellular environment dictates the mechanism of inhibition.
MeSH term(s)	Animals ; Aorta/cytology ; Aorta/drug effects ; Aorta/enzymology ; Cattle ; Cells, Cultured ; Cysteine/analogs & derivatives ; Cysteine/pharmacology ; Endothelium, Vascular/cytology ; Endothelium, Vascular/drug effects ; Endothelium, Vascular/enzymology ; Glyceraldehyde-3-Phosphate Dehydrogenases/antagonists & inhibitors ; Models, Animal ; Nitric Oxide/pharmacology ; S-Nitrosothiols/pharmacology ; Signal Transduction
Chemical Substances	S-Nitrosothiols ; Nitric Oxide (31C4KY9ESH) ; S-nitrosocysteine (926P2322P4) ; Glyceraldehyde-3-Phosphate Dehydrogenases (EC 1.2.1.-) ; Cysteine (K848JZ4886)
Language	English
Publishing date	2010-07-30
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	603838-4
ISSN	1522-1539 ; 0363-6135
ISSN (online)	1522-1539
ISSN	0363-6135
DOI	10.1152/ajpheart.00472.2010
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Article: Cardiomyocyte Differentiation Promotes Cell Survival During Nicotinamide Phosphoribosyltransferase Inhibition Through Increased Maintenance of Cellular Energy Stores.

Kropp, Erin M / Broniowska, Katarzyna A / Waas, Matthew / Nycz, Alyssa / Corbett, John A / Gundry, Rebekah L

Stem cells translational medicine

2017 Volume 6, Issue 4, Page(s) 1191–1201

Abstract: To address concerns regarding the tumorigenic potential of undifferentiated human pluripotent stem cells (hPSC) that may remain after in vitro differentiation and ultimately limit the broad use of hPSC-derivatives for therapeutics, we recently described ... ...

Abstract	To address concerns regarding the tumorigenic potential of undifferentiated human pluripotent stem cells (hPSC) that may remain after in vitro differentiation and ultimately limit the broad use of hPSC-derivatives for therapeutics, we recently described a method to selectively eliminate tumorigenic hPSC from their progeny by inhibiting nicotinamide phosphoribosyltransferase (NAMPT). Limited exposure to NAMPT inhibitors selectively removes hPSC from hPSC-derived cardiomyocytes (hPSC-CM) and spares a wide range of differentiated cell types; yet, it remains unclear when and how cells acquire resistance to NAMPT inhibition during differentiation. In this study, we examined the effects of NAMPT inhibition among multiple time points of cardiomyocyte differentiation. Overall, these studies show that in vitro cardiomyogenic commitment and continued culturing provides resistance to NAMPT inhibition and cell survival is associated with the ability to maintain cellular ATP pools despite depletion of NAD levels. Unlike cells at earlier stages of differentiation, day 28 hPSC-CM can survive longer periods of NAMPT inhibition and maintain ATP generation by glycolysis and/or mitochondrial respiration. This is distinct from terminally differentiated fibroblasts, which maintain mitochondrial respiration during NAMPT inhibition. Overall, these results provide new mechanistic insight into how regulation of cellular NAD and energy pools change with hPSC-CM differentiation and further inform how NAMPT inhibition strategies could be implemented within the context of cardiomyocyte differentiation. Stem Cells Translational Medicine 2017;6:1191-1201.
MeSH term(s)	Acrylamides/pharmacology ; Cell Differentiation/drug effects ; Cell Survival/drug effects ; Cells, Cultured ; Enzyme Inhibitors/pharmacology ; Humans ; Myocytes, Cardiac/cytology ; Myocytes, Cardiac/drug effects ; Myocytes, Cardiac/metabolism ; Nicotinamide Phosphoribosyltransferase/antagonists & inhibitors ; Nicotinamide Phosphoribosyltransferase/metabolism ; Piperidines/pharmacology ; Pluripotent Stem Cells/cytology ; Pluripotent Stem Cells/drug effects ; Pluripotent Stem Cells/metabolism
Chemical Substances	Acrylamides ; Enzyme Inhibitors ; N-(4-(1-benzoylpiperidin-4-yl)butyl)-3-(pyridin-3-yl)acrylamide ; Piperidines ; Nicotinamide Phosphoribosyltransferase (EC 2.4.2.12)
Language	English
Publishing date	2017-02-22
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2642270-0
ISSN	2157-6580 ; 2157-6564
ISSN (online)	2157-6580
ISSN	2157-6564
DOI	10.1002/sctm.16-0151
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Article ; Online: Nitrosative stress and redox-cycling agents synergize to cause mitochondrial dysfunction and cell death in endothelial cells.

Diers, Anne R / Broniowska, Katarzyna A / Hogg, Neil

Redox biology

2013 Volume 1, Page(s) 1–7

Abstract: Nitric oxide production by the endothelium is required for normal vascular homeostasis; however, in conditions of oxidative stress, interactions of nitric oxide with reactive oxygen species (ROS) are thought to underlie endothelial dysfunction. Beyond ... ...

Abstract	Nitric oxide production by the endothelium is required for normal vascular homeostasis; however, in conditions of oxidative stress, interactions of nitric oxide with reactive oxygen species (ROS) are thought to underlie endothelial dysfunction. Beyond canonical nitric oxide signaling pathways, nitric oxide production results in the post-translational modification of protein thiols, termed S-nitrosation. The potential interplay between S-nitrosation and ROS remains poorly understood and is the focus of the current study. The effects of the S-nitrosating agent S-nitrosocysteine (CysNO) in combination with redox-cycling agents was examined in bovine aortic endothelial cells (BAEC). CysNO significantly impairs mitochondrial function and depletes the NADH/NAD(+) pool; however, these changes do not result in cell death. When faced with the additional stressor of a redox-cycling agent used to generate ROS, further loss of NAD(+) occurs, and cellular ATP pools are depleted. Cellular S-nitrosothiols also accumulate, and cell death is triggered. These data demonstrate that CysNO sensitizes endothelial cells to redox-cycling agent-dependent mitochondrial dysfunction and cell death and identify attenuated degradation of S-nitrosothiols as one potential mechanism for the enhanced cytotoxicity.
MeSH term(s)	Animals ; Aorta/cytology ; Aorta/drug effects ; Cattle ; Cell Death ; Cells, Cultured ; Cysteine/analogs & derivatives ; Cysteine/pharmacology ; Drug Synergism ; Endothelial Cells/drug effects ; Endothelial Cells/pathology ; Mitochondria/drug effects ; Mitochondria/physiology ; Naphthoquinones/pharmacology ; Nitrosation ; Reactive Oxygen Species ; S-Nitrosothiols/pharmacology
Chemical Substances	Naphthoquinones ; Reactive Oxygen Species ; S-Nitrosothiols ; 2,3-dimethoxy-1,4-naphthoquinone (6956-96-3) ; S-nitrosocysteine (926P2322P4) ; Cysteine (K848JZ4886)
Language	English
Publishing date	2013-01-11
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2701011-9
ISSN	2213-2317 ; 2213-2317
ISSN (online)	2213-2317
ISSN	2213-2317
DOI	10.1016/j.redox.2012.11.003
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Article ; Online: The Role of Metabolic Flexibility in the Regulation of the DNA Damage Response by Nitric Oxide.

Oleson, Bryndon J / Broniowska, Katarzyna A / Yeo, Chay Teng / Flancher, Michael / Naatz, Aaron / Hogg, Neil / Tarakanova, Vera L / Corbett, John A

Molecular and cellular biology

2019 Volume 39, Issue 18

Abstract: In this report, we show that nitric oxide suppresses DNA damage response (DDR) signaling in the pancreatic β-cell line INS 832/13 and rat islets by inhibiting intermediary metabolism. Nitric oxide is known to inhibit complex IV of the electron transport ... ...

Abstract	In this report, we show that nitric oxide suppresses DNA damage response (DDR) signaling in the pancreatic β-cell line INS 832/13 and rat islets by inhibiting intermediary metabolism. Nitric oxide is known to inhibit complex IV of the electron transport chain and aconitase of the Krebs cycle. Non-β cells compensate by increasing glycolytic metabolism to maintain ATP levels; however, β cells lack this metabolic flexibility, resulting in a nitric oxide-dependent decrease in ATP and NAD
MeSH term(s)	Adenosine Triphosphate/metabolism ; Animals ; Cell Line ; Cell Respiration/drug effects ; Cell Survival/drug effects ; DNA Damage ; DNA Repair/drug effects ; Glycolysis/drug effects ; Hep G2 Cells ; Humans ; Insulin-Secreting Cells/cytology ; Insulin-Secreting Cells/drug effects ; Insulin-Secreting Cells/metabolism ; Male ; Mice ; Mitochondria/drug effects ; Mitochondria/metabolism ; NAD/metabolism ; Nitric Oxide/pharmacology ; Rats ; Rats, Sprague-Dawley
Chemical Substances	NAD (0U46U6E8UK) ; Nitric Oxide (31C4KY9ESH) ; Adenosine Triphosphate (8L70Q75FXE)
Language	English
Publishing date	2019-08-27
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	779397-2
ISSN	1098-5549 ; 0270-7306
ISSN (online)	1098-5549
ISSN	0270-7306
DOI	10.1128/MCB.00153-19
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