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Article ; Online: Differential Receptor Tyrosine Kinase Phosphorylation in the Uterus of Rats Following Developmental Exposure to Tetrabromobisphenol A.

Castro, Lysandra / Liu, Jingli / Yu, Linda / Burwell, Alanna D / Saddler, Trey O / Santiago, Lindsay A / Xue, William / Foley, Julie F / Staup, Michael / Flagler, Norris D / Shi, Min / Birnbaum, Linda S / Darlene, Dixon

Toxicology research and application

2021 Volume 5

Abstract: Tetrabromobisphenol A (TBBPA) is a brominated flame retardant that induces endometrial adenocarcinoma and other uterine tumors in Wistar Han rats; however, early molecular events or biomarkers of TBBPA exposure remain unknown. We investigated the effects ...

Abstract	Tetrabromobisphenol A (TBBPA) is a brominated flame retardant that induces endometrial adenocarcinoma and other uterine tumors in Wistar Han rats; however, early molecular events or biomarkers of TBBPA exposure remain unknown. We investigated the effects of TBBPA on growth factor receptor activation (phospho-RTK) in uteri of rats following early-life exposures. Pregnant Wistar Han rats were exposed to TBBPA (0, 0.1, 25, 250 mg/kg/day) via oral gavage on gestation day 6 through weaning of pups (PND 21). Pups were exposed
Language	English
Publishing date	2021-11-18
Publishing country	England
Document type	Journal Article
ISSN	2397-8473
ISSN (online)	2397-8473
DOI	10.1177/23978473211047164
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Article: Mitochondria as a target for the cardioprotective effects of nitric oxide in ischemia-reperfusion injury.

Burwell, Lindsay S / Brookes, Paul S

Antioxidants & redox signaling

2008 Volume 10, Issue 3, Page(s) 579–599

Abstract: During cardiac ischemia-reperfusion (IR) injury, excessive generation of reactive oxygen species (ROS) and overload of Ca(2+) at the mitochondrial level both lead to opening of the mitochondrial permeability transition (PT) pore on reperfusion. This can ... ...

Abstract	During cardiac ischemia-reperfusion (IR) injury, excessive generation of reactive oxygen species (ROS) and overload of Ca(2+) at the mitochondrial level both lead to opening of the mitochondrial permeability transition (PT) pore on reperfusion. This can result in the depletion of ATP, irreversible oxidation of proteins, lipids, and DNA within the cardiomyocyte, and can trigger cell-death pathways. In contrast, mitochondria are also implicated in the cardioprotective signaling processes of ischemic preconditioning (IPC), to prevent IR-related pathology. Nitric oxide (NO) has emerged as a potent effector molecule for a variety of cardioprotective strategies, including IPC. Whereas NO is most noted for its activation of the "classic" soluble guanylate cyclase (sGC) signaling pathway, emerging evidence indicates that NO can directly act on mitochondria, independent of the sGC pathway, affording acute cardioprotection against IR injury. These direct effects of NO* on mitochondria are the focus of this review.
MeSH term(s)	Animals ; Cardiotonic Agents/pharmacology ; Humans ; Mitochondria, Heart/drug effects ; Nitric Oxide/pharmacology ; Reperfusion Injury/prevention & control
Chemical Substances	Cardiotonic Agents ; Nitric Oxide (31C4KY9ESH)
Language	English
Publishing date	2008-03
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	1483836-9
ISSN	1557-7716 ; 1523-0864
ISSN (online)	1557-7716
ISSN	1523-0864
DOI	10.1089/ars.2007.1845
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Zs.A 5488: Show issues

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Article ; Online: Erythritol is a pentose-phosphate pathway metabolite and associated with adiposity gain in young adults.

Hootman, Katie C / Trezzi, Jean-Pierre / Kraemer, Lisa / Burwell, Lindsay S / Dong, Xiangyi / Guertin, Kristin A / Jaeger, Christian / Stover, Patrick J / Hiller, Karsten / Cassano, Patricia A

Proceedings of the National Academy of Sciences of the United States of America

2017 Volume 114, Issue 21, Page(s) E4233–E4240

Abstract: Metabolomic markers associated with incident central adiposity gain were investigated in young adults. In a 9-mo prospective study of university freshmen ( ...

Abstract	Metabolomic markers associated with incident central adiposity gain were investigated in young adults. In a 9-mo prospective study of university freshmen (
Language	English
Publishing date	2017-05-23
Publishing country	United States
Document type	Journal Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1620079114
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Zs.A 1148: Show issues

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Article ; Online: Cardioprotection by metabolic shut-down and gradual wake-up.

Burwell, Lindsay S / Nadtochiy, Sergiy M / Brookes, Paul S

Journal of molecular and cellular cardiology

2009 Volume 46, Issue 6, Page(s) 804–810

Abstract: Mitochondria play a critical role in cardiac function, and are also increasingly recognized as end effectors for various cardioprotective signaling pathways. Mitochondria use oxygen as a substrate, so by default their respiration is inhibited during ... ...

Abstract	Mitochondria play a critical role in cardiac function, and are also increasingly recognized as end effectors for various cardioprotective signaling pathways. Mitochondria use oxygen as a substrate, so by default their respiration is inhibited during hypoxia/ischemia. However, at reperfusion a surge of oxygen and metabolic substrates into the cell is thought to lead to rapid reestablishment of respiration, a burst of reactive oxygen species (ROS) generation and mitochondrial Ca(2+) overload. Subsequently these events precipitate opening of the mitochondrial permeability transition (PT) pore, which leads to myocardial cell death and dysfunction. Given that mitochondrial respiration is already inhibited during hypoxia/ischemia, it is somewhat surprising that many respiratory inhibitors can improve recovery from ischemia-reperfusion (IR) injury. In addition ischemic preconditioning (IPC), in which short non-lethal cycles of IR can protect against subsequent prolonged IR injury, is known to lead to endogenous inhibition of several respiratory complexes and glycolysis. This has led to a hypothesis that the wash-out of inhibitors or reversal of endogenous inhibition at reperfusion may afford protection by facilitating a more gradual wake-up of mitochondrial function, thereby avoiding a burst of ROS and Ca(2+) overload. This paper will review the evidence in support of this hypothesis, with a focus on inhibition of each of the mitochondrial respiratory complexes.
MeSH term(s)	Electron Transport Complex I/metabolism ; Electron Transport Complex I/physiology ; Electron Transport Complex II/metabolism ; Electron Transport Complex II/physiology ; Electron Transport Complex III/metabolism ; Electron Transport Complex III/physiology ; Electron Transport Complex IV/metabolism ; Electron Transport Complex IV/physiology ; Glycolysis/physiology ; Ischemic Preconditioning, Myocardial ; Mitochondria/metabolism ; Mitochondria/physiology ; Models, Biological ; Myocardial Reperfusion Injury/metabolism ; Myocardial Reperfusion Injury/physiopathology ; Myocardial Reperfusion Injury/prevention & control ; Nitric Oxide/metabolism ; Nitric Oxide/physiology
Chemical Substances	Nitric Oxide (31C4KY9ESH) ; Electron Transport Complex II (EC 1.3.5.1) ; Electron Transport Complex IV (EC 1.9.3.1) ; Electron Transport Complex I (EC 7.1.1.2) ; Electron Transport Complex III (EC 7.1.1.8)
Language	English
Publishing date	2009-03-10
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	80157-4
ISSN	1095-8584 ; 0022-2828
ISSN (online)	1095-8584
ISSN	0022-2828
DOI	10.1016/j.yjmcc.2009.02.026
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Zs.A 426: Show issues

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Article: Cardioprotection and mitochondrial S-nitrosation: effects of S-nitroso-2-mercaptopropionyl glycine (SNO-MPG) in cardiac ischemia-reperfusion injury.

Nadtochiy, Sergiy M / Burwell, Lindsay S / Brookes, Paul S

Journal of molecular and cellular cardiology

2007 Volume 42, Issue 4, Page(s) 812–825

Abstract: ... that mitochondrial protein S-nitrosation may be a cardioprotective mechanism. The reagent S-nitroso-2-mercaptopropionyl ... glycine (SNO-MPG) was therefore developed to enhance mitochondrial S-nitrosation and elicit ... cardioprotection. Within cardiomyocytes, mitochondrial proteins were effectively S-nitrosated by SNO-MPG ...

Abstract	Mitochondrial dysfunction is a key pathologic event in cardiac ischemia-reperfusion (IR) injury, and protection of mitochondrial function is a potential mechanism underlying ischemic preconditioning (IPC). Acknowledging the role of nitric oxide (NO()) in IPC, it was hypothesized that mitochondrial protein S-nitrosation may be a cardioprotective mechanism. The reagent S-nitroso-2-mercaptopropionyl-glycine (SNO-MPG) was therefore developed to enhance mitochondrial S-nitrosation and elicit cardioprotection. Within cardiomyocytes, mitochondrial proteins were effectively S-nitrosated by SNO-MPG. Consistent with the recent discovery of mitochondrial complex I as an S-nitrosation target, SNO-MPG inhibited complex I activity and cardiomyocyte respiration. The latter effect was insensitive to the NO() scavenger c-PTIO, indicating no role for NO()-mediated complex IV inhibition. A cardioprotective role for reversible complex I inhibition has been proposed, and consistent with this SNO-MPG protected cardiomyocytes from simulated IR injury. Further supporting a cardioprotective role for endogenous mitochondrial S-nitrosothiols, patterns of protein S-nitrosation were similar in mitochondria isolated from Langendorff perfused hearts subjected to IPC, and mitochondria or cells treated with SNO-MPG. The functional recovery of perfused hearts from IR injury was also improved under conditions which stabilized endogenous S-nitrosothiols (i.e. dark), or by pre-ischemic administration of SNO-MPG. Mitochondria isolated from SNO-MPG-treated hearts at the end of ischemia exhibited improved Ca(2+) handling and lower ROS generation. Overall these data suggest that mitochondrial S-nitrosation and complex I inhibition constitute a protective signaling pathway that is amenable to pharmacologic augmentation.
MeSH term(s)	Animals ; Calcium/metabolism ; Cardiotonic Agents/pharmacology ; Male ; Membrane Potentials/drug effects ; Mitochondria, Heart/drug effects ; Mitochondria, Heart/physiology ; Myocardial Reperfusion Injury/metabolism ; Myocardial Reperfusion Injury/physiopathology ; Myocardial Reperfusion Injury/prevention & control ; Myocardium/metabolism ; Nitrosation ; Rats ; Rats, Sprague-Dawley ; Reactive Oxygen Species/metabolism ; Tiopronin/chemistry ; Tiopronin/pharmacology
Chemical Substances	Cardiotonic Agents ; Reactive Oxygen Species ; Tiopronin (C5W04GO61S) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2007-04
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	80157-4
ISSN	1095-8584 ; 0022-2828
ISSN (online)	1095-8584
ISSN	0022-2828
DOI	10.1016/j.yjmcc.2007.01.010
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Zs.A 426: Show issues

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Article ; Online: The C. elegans mitochondrial K+(ATP) channel: a potential target for preconditioning.

Wojtovich, Andrew P / Burwell, Lindsay S / Sherman, Teresa A / Nehrke, Keith W / Brookes, Paul S

Biochemical and biophysical research communications

2008 Volume 376, Issue 3, Page(s) 625–628

Abstract: Ischemic preconditioning (IPC) is an evolutionarily conserved endogenous mechanism whereby short periods of non-lethal exposure to hypoxia alleviate damage caused by subsequent ischemia reperfusion (IR). Pharmacologic targeting has suggested that the ... ...

Abstract	Ischemic preconditioning (IPC) is an evolutionarily conserved endogenous mechanism whereby short periods of non-lethal exposure to hypoxia alleviate damage caused by subsequent ischemia reperfusion (IR). Pharmacologic targeting has suggested that the mitochondrial ATP-sensitive potassium channel (mK(ATP)) is central to IPC signaling, despite its lack of molecular identity. Here, we report that isolated Caenorhabditis elegans mitochondria have a K(ATP) channel with the same physiologic and pharmacologic characteristics as the vertebrate channel. Since C. elegans also exhibit IPC, our observations provide a framework to study the role of mK(ATP) in IR injury in a genetic model organism.
MeSH term(s)	Animals ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/metabolism ; Ischemic Preconditioning ; Mitochondria/metabolism ; Models, Animal ; Potassium Channels/agonists ; Potassium Channels/drug effects ; Potassium Channels/metabolism ; Reperfusion Injury/metabolism
Chemical Substances	Caenorhabditis elegans Proteins ; Potassium Channels ; mitochondrial K(ATP) channel
Language	English
Publishing date	2008-11-21
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2008.09.043
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Zs.A 116: Show issues

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Article: Regulation of mitochondrial fission and apoptosis by the mitochondrial outer membrane protein hFis1.

Yu, Tianzheng / Fox, Randall J / Burwell, Lindsay S / Yoon, Yisang

Journal of cell science

2005 Volume 118, Issue Pt 18, Page(s) 4141–4151

Abstract: Mitochondrial fission is a highly regulated process mediated by a defined set of protein factors and is involved in the early stage of apoptosis. In mammals, at least two proteins, the dynamin-like protein DLP1/Drp1 and the mitochondrial outer membrane ... ...

Abstract	Mitochondrial fission is a highly regulated process mediated by a defined set of protein factors and is involved in the early stage of apoptosis. In mammals, at least two proteins, the dynamin-like protein DLP1/Drp1 and the mitochondrial outer membrane protein hFis1, participate in mitochondrial fission. The cytosolic domain of hFis1 contains six alpha-helices that form two tetratricopeptide repeat (TPR) motifs. Overexpression of hFis1 induces DLP1-mediated fragmentation of mitochondria, suggesting that hFis1 is a limiting factor in mitochondrial fission by recruiting cytosolic DLP1. In the present study, we identified two regions of hFis1 that are necessary for correct fission of mitochondria. We found that the TPR region of hFis1 participates in the interaction with DLP1 or DLP1-containing complex and that the first helix (alpha1) of hFis1 is required for mitochondrial fission presumably by regulating DLP1-hFis1 interaction. Misregulated interaction between DLP1 and hFis1 by alpha1 deletion induced mitochondrial swelling, in part by the mitochondrial permeability transition, but significantly delayed cell death. Our data suggest that hFis1 is a main regulator of mitochondrial fission, controlling the recruitment and assembly of DLP1 during both normal and apoptotic fission processes.
MeSH term(s)	Amino Acid Motifs ; Animals ; Apoptosis/physiology ; Cell Line ; Cell Membrane Permeability ; GTP Phosphohydrolases/metabolism ; Humans ; Intracellular Membranes/metabolism ; Membrane Proteins ; Microtubule-Associated Proteins/metabolism ; Mitochondria/metabolism ; Mitochondrial Proteins/biosynthesis ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Transfection
Chemical Substances	FIS1 protein, human ; Membrane Proteins ; Microtubule-Associated Proteins ; Mitochondrial Proteins ; GTP Phosphohydrolases (EC 3.6.1.-) ; DNM1L protein, human (EC 3.6.5.5)
Language	English
Publishing date	2005-09-15
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.02537
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Zs.A 1200: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 14: Show issues

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Article ; Online: Direct evidence for S-nitrosation of mitochondrial complex I.

Burwell, Lindsay S / Nadtochiy, Sergiy M / Tompkins, Andrew J / Young, Sara / Brookes, Paul S

The Biochemical journal

2006 Volume 394, Issue Pt 3, Page(s) 627–634

Abstract: ... that complex I can be inhibited by S-nitrosation of a cysteine. However, direct molecular evidence for this is ... gel electrophoresis, Superose 6 column chromatography) with sensitive detection methods for S-nitrosothiols ... chemiluminescence, biotin-switch assay), to show that the 75 kDa subunit of complex I is S-nitrosated ...

Abstract	NO* (nitric oxide) is a pleiotropic signalling molecule, with many of its effects on cell function being elicited at the level of the mitochondrion. In addition to the well-characterized binding of NO* to the Cu(B)/haem-a3 site in mitochondrial complex IV, it has been proposed by several laboratories that complex I can be inhibited by S-nitrosation of a cysteine. However, direct molecular evidence for this is lacking. In this investigation we have combined separation techniques for complex I (blue-native gel electrophoresis, Superose 6 column chromatography) with sensitive detection methods for S-nitrosothiols (chemiluminescence, biotin-switch assay), to show that the 75 kDa subunit of complex I is S-nitrosated in mitochondria treated with S-nitrosoglutathione (10 microM-1 mM). The stoichiometry of S-nitrosation was 7:1 (i.e. 7 mol of S-nitrosothiols per mol of complex I) and this resulted in significant inhibition of the complex. Furthermore, S-nitrosothiols were detected in mitochondria isolated from hearts subjected to ischaemic preconditioning. The implications of these results for the physiological regulation of respiration, for reactive oxygen species generation and for a potential role of S-nitrosation in cardioprotection are discussed.
MeSH term(s)	Animals ; Electron Transport Complex I/metabolism ; Ischemic Preconditioning, Myocardial ; Male ; Mitochondria/chemistry ; Mitochondria/metabolism ; Myocardium/metabolism ; Nitrates/metabolism ; Nitrosation ; Rats ; Rats, Sprague-Dawley ; S-Nitrosothiols/metabolism ; Sensitivity and Specificity
Chemical Substances	Nitrates ; S-Nitrosothiols ; Electron Transport Complex I (EC 1.6.5.3)
Language	English
Publishing date	2006-03-15
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2969-5
ISSN	1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
ISSN (online)	1470-8728
ISSN	0006-2936 ; 0306-3275 ; 0264-6021
DOI	10.1042/BJ20051435
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Article ; Online: Erythritol is a pentose-phosphate pathway metabolite and associated with adiposity gain in young adults.

Hootman, Katie C / Trezzi, Jean-Pierre / Kraemer, Lisa / Burwell, Lindsay S / Dong, Xiangyi / Guertin, Kristin A / Jaeger, Christian / Stover, Patrick J / Hiller, Karsten / Cassano, Patricia A

2017

Abstract: Metabolomic markers associated with incident central adiposity gain were investigated in young adults. In a 9-mo prospective study of university freshmen (n = 264). Blood samples and anthropometry measurements were collected in the first 3 d on campus ... ...

Abstract	Metabolomic markers associated with incident central adiposity gain were investigated in young adults. In a 9-mo prospective study of university freshmen (n = 264). Blood samples and anthropometry measurements were collected in the first 3 d on campus and at the end of the year. Plasma from individuals was pooled by phenotype [incident central adiposity, stable adiposity, baseline hemoglobin A1c (HbA1c) > 5.05%, HbA1c < 4.92%] and assayed using GC-MS, chromatograms were analyzed using MetaboliteDetector software, and normalized metabolite levels were compared using Welch's t test. Assays were repeated using freshly prepared pools, and statistically significant metabolites were quantified in a targeted GC-MS approach. Isotope tracer studies were performed to determine if the potential marker was an endogenous human metabolite in men and in whole blood. Participants with incident central adiposity gain had statistically significantly higher blood erythritol [P < 0.001, false discovery rate (FDR) = 0.0435], and the targeted assay revealed 15-fold [95% confidence interval (CI): 13.27, 16.25] higher blood erythritol compared with participants with stable adiposity. Participants with baseline HbA1c > 5.05% had 21-fold (95% CI: 19.84, 21.41) higher blood erythritol compared with participants with lower HbA1c (P < 0.001, FDR = 0.00016). Erythritol was shown to be synthesized endogenously from glucose via the pentose-phosphate pathway (PPP) in stable isotope-assisted ex vivo blood incubation experiments and through in vivo conversion of erythritol to erythronate in stable isotope-assisted dried blood spot experiments. Therefore, endogenous production of erythritol from glucose may contribute to the association between erythritol and obesity observed in young adults.
Subject code	610 ; 500
Language	English
Publishing date	2017-05-23
Publishing country	de
Document type	Article ; Online
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Article ; Online: Erythritol is a pentose-phosphate pathway metabolite and associated with adiposity gain in young adults.

Hootman, Katie C / Trezzi, Jean-Pierre / Kraemer, Lisa / Burwell, Lindsay S / Dong, Xiangyi / Guertin, Kristin A / Jaeger, Christian / Stover, Patrick J / Hiller, Karsten / Cassano, Patricia A

2017

Abstract	Metabolomic markers associated with incident central adiposity gain were investigated in young adults. In a 9-mo prospective study of university freshmen (n = 264). Blood samples and anthropometry measurements were collected in the first 3 d on campus and at the end of the year. Plasma from individuals was pooled by phenotype [incident central adiposity, stable adiposity, baseline hemoglobin A1c (HbA1c) > 5.05%, HbA1c < 4.92%] and assayed using GC-MS, chromatograms were analyzed using MetaboliteDetector software, and normalized metabolite levels were compared using Welch's t test. Assays were repeated using freshly prepared pools, and statistically significant metabolites were quantified in a targeted GC-MS approach. Isotope tracer studies were performed to determine if the potential marker was an endogenous human metabolite in men and in whole blood. Participants with incident central adiposity gain had statistically significantly higher blood erythritol [P < 0.001, false discovery rate (FDR) = 0.0435], and the targeted assay revealed 15-fold [95% confidence interval (CI): 13.27, 16.25] higher blood erythritol compared with participants with stable adiposity. Participants with baseline HbA1c > 5.05% had 21-fold (95% CI: 19.84, 21.41) higher blood erythritol compared with participants with lower HbA1c (P < 0.001, FDR = 0.00016). Erythritol was shown to be synthesized endogenously from glucose via the pentose-phosphate pathway (PPP) in stable isotope-assisted ex vivo blood incubation experiments and through in vivo conversion of erythritol to erythronate in stable isotope-assisted dried blood spot experiments. Therefore, endogenous production of erythritol from glucose may contribute to the association between erythritol and obesity observed in young adults.
Subject code	610 ; 500
Language	English
Publishing date	2017-05-23
Publishing country	de
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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