LIVIVO - Search results -

Search results

Result 1 - 10 of total 56

Search options

Article ; Online: Profiling microbial community structures and functions in bioremediation strategies for treating 1,4-dioxane-contaminated groundwater.

Miao, Yu / Heintz, Monica B / Bell, Caitlin H / Johnson, Nicholas W / Polasko, Alexandra LaPat / Favero, David / Mahendra, Shaily

Journal of hazardous materials

2020 Volume 408, Page(s) 124457

Abstract: Microbial community compositions and functional profiles were analyzed in microcosms established using aquifer materials from a former automobile factory site, where 1,4-dioxane was identified as the primary contaminant of concern. Propane or oxygen ... ...

Abstract	Microbial community compositions and functional profiles were analyzed in microcosms established using aquifer materials from a former automobile factory site, where 1,4-dioxane was identified as the primary contaminant of concern. Propane or oxygen biostimulation resulted in limited 1,4-dioxane degradation, which was markedly enhanced with the addition of nutrients, resulting in abundant Mycobacterium and Methyloversatilis taxa and high expressions of propane monooxygenase gene, prmA. In bioaugmented treatments, Pseudonocardia dioxanivorans CB1190 or Rhodococcus ruber ENV425 strains dominated immediately after augmentation and degraded 1,4-dioxane rapidly which was consistent with increased representation of xenobiotic and lipid metabolism-related functions. Although the bioaugmented microbes decreased due to insufficient growth substrates and microbial competition, they did continue to degrade 1,4-dioxane, presumably by indigenous propanotrophic and heterotrophic bacteria, inducing similar community structures across bioaugmentation conditions. In various treatments, functional redundancy acted as buffer capacity to ensure a stable microbiome, drove the restoration of the structure and microbial functions to original levels, and induced the decoupling between basic metabolic functions and taxonomy. The results of this study provided valuable information for design and decision-making for ex-situ bioreactors and in-situ bioremediation applications. A metagenomics-based understanding of the treatment process will enable efficient and accurate adjustments when encountering unexpected issues in bioremediation.
MeSH term(s)	Biodegradation, Environmental ; Dioxanes ; Groundwater ; Microbiota ; Rhodococcus ; Water Pollutants, Chemical
Chemical Substances	Dioxanes ; Water Pollutants, Chemical ; 1,4-dioxane (J8A3S10O7S)
Language	English
Publishing date	2020-11-02
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1491302-1
ISSN	1873-3336 ; 0304-3894
ISSN (online)	1873-3336
ISSN	0304-3894
DOI	10.1016/j.jhazmat.2020.124457
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Book: Transcription factors and DNA replication

Pederson, David S. / Heintz, Nicholas H.

(Molecular biology intelligence unit)

1994

Author's details	David S. Pederson ; Nicholas H. Heintz
Series title	Molecular biology intelligence unit
Keywords	DNA Replication ; Transcription Factors
Language	English
Size	113 S. : Ill.
Publisher	Landes
Publishing place	Austin
Publishing country	United States
Document type	Book
HBZ-ID	HT006740287
ISBN	1-57059-069-9 ; 978-1-57059-069-6
Database	Catalogue ZB MED Medicine, Health

In stock of ZB MED Cologne/Königswinter

Shelf mark	Loan status	Location
1995 A 4186	order for loan	Magazin

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: The cell cycle is a redox cycle: linking phase-specific targets to cell fate.

Burhans, William C / Heintz, Nicholas H

Free radical biology & medicine

2009 Volume 47, Issue 9, Page(s) 1282–1293

Abstract: Reactive oxygen species (ROS) regulate the strength and duration of signaling through redox-dependent signal transduction pathways via the cyclic oxidation/reduction of cysteine residues in kinases, phosphatases, and other regulatory factors. Signaling ... ...

Abstract	Reactive oxygen species (ROS) regulate the strength and duration of signaling through redox-dependent signal transduction pathways via the cyclic oxidation/reduction of cysteine residues in kinases, phosphatases, and other regulatory factors. Signaling circuits may be segregated in organelles or other subcellular domains with distinct redox states, permitting them to respond independently to changes in the oxidation state of two major thiol reductants, glutathione and thioredoxin. Studies in yeast, and in complex eukaryotes, show that oscillations in oxygen consumption, energy metabolism, and redox state are intimately integrated with cell cycle progression. Because signaling pathways play specific roles in different phases of the cell cycle and the hierarchy of redox-dependent regulatory checkpoints changes during cell cycle progression, the effects of ROS on cell fate vary during the cell cycle. In G1, ROS stimulate mitogenic pathways that control the activity of cyclin-dependent kinases (CDKs) and phosphorylation of the retinoblastoma protein (pRB), thereby regulating S-phase entry. In response to oxidative stress, Nrf2 and Foxo3a promote cell survival by inducing the expression of antioxidant enzymes and factors involved in cell cycle withdrawal, such as the cyclin-dependent kinase inhibitor (CKI) p27. In S phase, ROS induce S-phase arrest via PP2A-dependent dephosphorylation of pRB. In precancerous cells, unconstrained mitogenic signaling by activated oncogenes induces replication stress in S phase, which activates the DNA-damage response and induces cell senescence. A number of studies suggest that interactions of ROS with the G1 CDK/CKI network play a fundamental role in senescence, which is considered a barrier to tumorigenesis. Adaptive responses and loss of checkpoint proteins such as p53 and p16(INK4a) allow tumor cells to tolerate constitutive mitogenic signaling and enhanced production of ROS, leading to altered redox status in many fully transformed cells. Alterations in oxidant and energy metabolism of cancer cells have emerged as fertile ground for new therapeutic targets. The present challenge is to identify redox-dependent targets relevant to each cell cycle phase, to understand how these targets control fate decisions, and to describe the mechanisms that link metabolism to cell cycle progression.
MeSH term(s)	Animals ; Cell Cycle/physiology ; Cell Cycle Proteins/metabolism ; Humans ; Oxidation-Reduction ; Reactive Oxygen Species/metabolism ; Signal Transduction/physiology
Chemical Substances	Cell Cycle Proteins ; Reactive Oxygen Species
Language	English
Publishing date	2009-05-29
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	807032-5
ISSN	1873-4596 ; 0891-5849
ISSN (online)	1873-4596
ISSN	0891-5849
DOI	10.1016/j.freeradbiomed.2009.05.026
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 2109: 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)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: AMPK activity regulates trafficking of mitochondria to the leading edge during cell migration and matrix invasion.

Cunniff, Brian / McKenzie, Andrew J / Heintz, Nicholas H / Howe, Alan K

Molecular biology of the cell

2016 Volume 27, Issue 17, Page(s) 2662–2674

Abstract: Cell migration is a complex behavior involving many energy-expensive biochemical events that iteratively alter cell shape and location. Mitochondria, the principal producers of cellular ATP, are dynamic organelles that fuse, divide, and relocate to ... ...

Abstract	Cell migration is a complex behavior involving many energy-expensive biochemical events that iteratively alter cell shape and location. Mitochondria, the principal producers of cellular ATP, are dynamic organelles that fuse, divide, and relocate to respond to cellular metabolic demands. Using ovarian cancer cells as a model, we show that mitochondria actively infiltrate leading edge lamellipodia, thereby increasing local mitochondrial mass and relative ATP concentration and supporting a localized reversal of the Warburg shift toward aerobic glycolysis. This correlates with increased pseudopodial activity of the AMP-activated protein kinase (AMPK), a critically important cellular energy sensor and metabolic regulator. Furthermore, localized pharmacological activation of AMPK increases leading edge mitochondrial flux, ATP content, and cytoskeletal dynamics, whereas optogenetic inhibition of AMPK halts mitochondrial trafficking during both migration and the invasion of three-dimensional extracellular matrix. These observations indicate that AMPK couples local energy demands to subcellular targeting of mitochondria during cell migration and invasion.
MeSH term(s)	AMP-Activated Protein Kinases/metabolism ; Adenosine Triphosphate/metabolism ; Cell Line, Tumor ; Cell Movement/physiology ; Cytoskeleton/metabolism ; Energy Metabolism ; Female ; Glycolysis ; Humans ; Mitochondria/metabolism ; Mitochondria/physiology ; Ovarian Neoplasms ; Phosphorylation ; Protein Transport ; Pseudopodia/metabolism ; Pseudopodia/physiology
Chemical Substances	Adenosine Triphosphate (8L70Q75FXE) ; AMP-Activated Protein Kinases (EC 2.7.11.31)
Language	English
Publishing date	2016-09-01
Publishing country	United States
Document type	Journal Article
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E16-05-0286
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 2853: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 410: Show issues

Order via subito

Details ▾

Article: Resolution of oxidative stress by thioredoxin reductase: Cysteine versus selenocysteine.

Cunniff, Brian / Snider, Gregg W / Fredette, Nicholas / Stumpff, Jason / Hondal, Robert J / Heintz, Nicholas H

Redox biology

2014 Volume 2, Page(s) 475–484

Abstract: Thioredoxin reductase (TR) catalyzes the reduction of thioredoxin (TRX), which in turn reduces mammalian typical 2-Cys peroxiredoxins (PRXs 1-4), thiol peroxidases implicated in redox homeostasis and cell signaling. Typical 2-Cys PRXs are inactivated by ... ...

Abstract	Thioredoxin reductase (TR) catalyzes the reduction of thioredoxin (TRX), which in turn reduces mammalian typical 2-Cys peroxiredoxins (PRXs 1-4), thiol peroxidases implicated in redox homeostasis and cell signaling. Typical 2-Cys PRXs are inactivated by hyperoxidation of the peroxidatic cysteine to cysteine-sulfinic acid, and regenerated in a two-step process involving retro-reduction by sulfiredoxin (SRX) and reduction by TRX. Here transient exposure to menadione and glucose oxidase was used to examine the dynamics of oxidative inactivation and reactivation of PRXs in mouse C10 cells expressing various isoforms of TR, including wild type cytoplasmic TR1 (Sec-TR1) and mitochondrial TR2 (Sec-TR2) that encode selenocysteine, as well as mutants of TR1 and TR2 in which the selenocysteine codon was changed to encode cysteine (Cys-TR1 or Cys-TR2). In C10 cells endogenous TR activity was insensitive to levels of hydrogen peroxide that hyperoxidize PRXs. Expression of Sec-TR1 increased TR activity, reduced the basal cytoplasmic redox state, and increased the rate of reduction of a redox-responsive cytoplasmic GFP probe (roGFP), but did not influence either the rate of inactivation or the rate of retro-reduction of PRXs. In comparison to roGFP, which was reduced within minutes once oxidants were removed reduction of 2-Cys PRXs occurred over many hours. Expression of wild type Sec-TR1 or Sec-TR2, but not Cys-TR1 or TR2, increased the rate of reduction of PRXs and improved cell survival after menadione exposure. These results indicate that expression levels of TR do not reduce the severity of initial oxidative insults, but rather govern the rate of reduction of cellular factors required for cell viability. Because Sec-TR is completely insensitive to cytotoxic levels of hydrogen peroxide, we suggest TR functions at the top of a redox pyramid that governs the oxidation state of peroxiredoxins and other protein factors, thereby dictating a hierarchy of phenotypic responses to oxidative insults.
MeSH term(s)	Animals ; Cell Survival ; Cysteine/analogs & derivatives ; Cysteine/metabolism ; Epithelial Cells/enzymology ; Glucose Oxidase/metabolism ; Humans ; Hydrogen Peroxide/pharmacology ; Lung/cytology ; Lung/enzymology ; Mice ; Oxidative Stress ; Peroxiredoxins/metabolism ; Selenocysteine/metabolism ; Thioredoxin Reductase 1/genetics ; Thioredoxin Reductase 1/metabolism ; Thioredoxin Reductase 2/genetics ; Thioredoxin Reductase 2/metabolism ; Vitamin K 3/pharmacology
Chemical Substances	Selenocysteine (0CH9049VIS) ; Vitamin K 3 (723JX6CXY5) ; Hydrogen Peroxide (BBX060AN9V) ; Glucose Oxidase (EC 1.1.3.4) ; Peroxiredoxins (EC 1.11.1.15) ; Thioredoxin Reductase 1 (EC 1.8.1.9) ; Thioredoxin Reductase 2 (EC 1.8.1.9) ; Cysteine (K848JZ4886)
Language	English
Publishing date	2014-02-19
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2701011-9
ISSN	2213-2317
ISSN	2213-2317
DOI	10.1016/j.redox.2014.01.021
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: A direct and continuous assay for the determination of thioredoxin reductase activity in cell lysates.

Cunniff, Brian / Snider, Gregg W / Fredette, Nicholas / Hondal, Robert J / Heintz, Nicholas H

Analytical biochemistry

2013 Volume 443, Issue 1, Page(s) 34–40

Abstract: Thioredoxin reductase (TR) is an oxidoreductase responsible for maintaining thioredoxin in the reduced state, thereby contributing to proper cellular redox homeostasis. The C-terminal active site of mammalian TR contains the rare amino acid ... ...

Abstract	Thioredoxin reductase (TR) is an oxidoreductase responsible for maintaining thioredoxin in the reduced state, thereby contributing to proper cellular redox homeostasis. The C-terminal active site of mammalian TR contains the rare amino acid selenocysteine, which is essential to its activity. Alterations in TR activity due to changes in cellular redox homeostasis are found in clinical conditions such as cancer, viral infection, and various inflammatory processes; therefore, quantification of thioredoxin activity can be a valuable indicator of clinical conditions. Here we describe a new direct assay, termed the SC-TR assay, to determine the activity of TR based on the reduction of selenocystine, a diselenide-bridged amino acid. Rather than being an end-point assay as in older methods, the SC-TR assay directly monitors the continuous consumption of NADPH at 340 nm by TR as it reduces selenocystine. The SC-TR assay can be used in a cuvette using traditional spectrophotometry or as a 96-well plate-based format using a plate reader. In addition, the SC-TR assay is compatible with the use of nonionic detergents, making it more versatile than other methods using cell lysates.
MeSH term(s)	Animals ; Cell Line ; Cystine/analogs & derivatives ; Cystine/chemistry ; Enzyme Assays ; Epithelial Cells/chemistry ; Epithelial Cells/enzymology ; Mice ; NADP/chemistry ; Organoselenium Compounds/chemistry ; Oxidation-Reduction ; Respiratory Mucosa/chemistry ; Respiratory Mucosa/enzymology ; Selenocysteine/chemistry ; Sensitivity and Specificity ; Spectrophotometry ; Thioredoxin-Disulfide Reductase/analysis
Chemical Substances	Organoselenium Compounds ; Selenocysteine (0CH9049VIS) ; selenocystine (1464-43-3) ; Cystine (48TCX9A1VT) ; NADP (53-59-8) ; Thioredoxin-Disulfide Reductase (EC 1.8.1.9)
Language	English
Publishing date	2013-08-21
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1110-1
ISSN	1096-0309 ; 0003-2697
ISSN (online)	1096-0309
ISSN	0003-2697
DOI	10.1016/j.ab.2013.08.013
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 389: 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)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Peroxiredoxins and Beyond; Redox Systems Regulating Lung Physiology and Disease.

Elko, Evan A / Cunniff, Brian / Seward, David J / Chia, Shi Biao / Aboushousha, Reem / van de Wetering, Cheryl / van der Velden, Jos / Manuel, Allison / Shukla, Arti / Heintz, Nicholas H / Anathy, Vikas / van der Vliet, Albert / Janssen-Heininger, Yvonne M W

Antioxidants & redox signaling

2019 Volume 31, Issue 14, Page(s) 1070–1091

Abstract: Significance: ...

Abstract	Significance:
MeSH term(s)	Animals ; Humans ; Lung/metabolism ; Lung Diseases/metabolism ; Oxidation-Reduction ; Peroxiredoxins/metabolism
Chemical Substances	Peroxiredoxins (EC 1.11.1.15)
Language	English
Publishing date	2019-04-05
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1483836-9
ISSN	1557-7716 ; 1523-0864
ISSN (online)	1557-7716
ISSN	1523-0864
DOI	10.1089/ars.2019.7752
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 5488: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: S-phase arrest by reactive nitrogen species is bypassed by okadaic acid, an inhibitor of protein phosphatases PP1/PP2A.

Ranjan, Priya / Heintz, Nicholas H

Free radical biology & medicine

2006 Volume 40, Issue 2, Page(s) 247–259

Abstract: In mammalian cells DNA damage activates a checkpoint that halts progression through S phase. To determine the ability of nitrating agents to induce S-phase arrest, mouse C10 cells synchronized in S phase were treated with nitrogen dioxide (NO(2)) or SIN- ... ...

Abstract	In mammalian cells DNA damage activates a checkpoint that halts progression through S phase. To determine the ability of nitrating agents to induce S-phase arrest, mouse C10 cells synchronized in S phase were treated with nitrogen dioxide (NO(2)) or SIN-1, a generator of reactive nitrogen species (RNS). SIN-1 or NO(2) induced S-phase arrest in a dose- and time-dependent manner. As for the positive controls adozelesin and cisplatin, arrest was accompanied by phosphorylation of ATM kinase; dephosphorylation of pRB; decreases in RF-C, cyclin D1, Cdc25A, and Cdc6; and increases in p21. Comet assays indicated that RNS induce minimal DNA damage. Moreover, in a cell-free replication system, nuclei from cells treated with RNS were able to support control levels of DNA synthesis when incubated in cytosolic extracts from untreated cells, whereas nuclei from cells treated with cisplatin were not. Induction of phosphatase activity may represent one mechanism of RNS-induced arrest, for the PP1/PP2A phosphatase inhibitor okadaic acid inhibited dephosphorylation of pRB; prevented decreases in the levels of RF-C, cyclin D1, Cdc6, and Cdc25A; and bypassed arrest by SIN-1 or NO(2), but not cisplatin or adozelesin. Our studies suggest that RNS may induce S-phase arrest through mechanisms that differ from those elicited by classical DNA-damaging agents.
MeSH term(s)	Animals ; Ataxia Telangiectasia Mutated Proteins ; Cell Cycle/drug effects ; Cell Cycle Proteins/drug effects ; Cell Cycle Proteins/metabolism ; Cell Line ; Cells, Cultured ; Cisplatin/pharmacology ; Cyclin D1/drug effects ; Cyclin D1/metabolism ; DNA/biosynthesis ; DNA/drug effects ; DNA Damage/drug effects ; DNA-Binding Proteins/drug effects ; DNA-Binding Proteins/metabolism ; Dose-Response Relationship, Drug ; In Vitro Techniques ; Mice ; Molsidomine/analogs & derivatives ; Molsidomine/pharmacology ; Nitrogen Dioxide/pharmacology ; Nuclear Proteins/drug effects ; Nuclear Proteins/metabolism ; Okadaic Acid/pharmacology ; Phosphoprotein Phosphatases/antagonists & inhibitors ; Phosphorylation ; Protein-Serine-Threonine Kinases/drug effects ; Protein-Serine-Threonine Kinases/metabolism ; Reactive Nitrogen Species/antagonists & inhibitors ; Reactive Nitrogen Species/metabolism ; Reactive Nitrogen Species/pharmacology ; Replication Protein C/drug effects ; Replication Protein C/metabolism ; Retinoblastoma Protein/drug effects ; Retinoblastoma Protein/metabolism ; S Phase/drug effects ; Time Factors ; Tumor Suppressor Proteins/drug effects ; Tumor Suppressor Proteins/metabolism ; cdc25 Phosphatases/drug effects ; cdc25 Phosphatases/metabolism
Chemical Substances	CDC6 protein, mouse ; Cell Cycle Proteins ; DNA-Binding Proteins ; Nuclear Proteins ; Reactive Nitrogen Species ; Retinoblastoma Protein ; Tumor Suppressor Proteins ; Cyclin D1 (136601-57-5) ; Okadaic Acid (1W21G5Q4N2) ; linsidomine (5O5U71P6VQ) ; DNA (9007-49-2) ; Molsidomine (D46583G77X) ; Ataxia Telangiectasia Mutated Proteins (EC 2.7.11.1) ; Atm protein, mouse (EC 2.7.11.1) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; Phosphoprotein Phosphatases (EC 3.1.3.16) ; Cdc25a protein, mouse (EC 3.1.3.48) ; cdc25 Phosphatases (EC 3.1.3.48) ; Replication Protein C (EC 3.6.4.-) ; Cisplatin (Q20Q21Q62J) ; Nitrogen Dioxide (S7G510RUBH)
Language	English
Publishing date	2006-01-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	807032-5
ISSN	1873-4596 ; 0891-5849
ISSN (online)	1873-4596
ISSN	0891-5849
DOI	10.1016/j.freeradbiomed.2005.08.049
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 2109: 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)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Redox regulation of cell-cycle re-entry: cyclin D1 as a primary target for the mitogenic effects of reactive oxygen and nitrogen species.

Burch, Peter M / Heintz, Nicholas H

Antioxidants & redox signaling

2005 Volume 7, Issue 5-6, Page(s) 741–751

Abstract: Reactive oxygen and nitrogen species inhibit or promote cell proliferation by modulating the cell signaling pathways that dictate decisions between cell survival, proliferation, and death. In the growth factor-dependent pathways that regulate mitogenesis, ...

Abstract	Reactive oxygen and nitrogen species inhibit or promote cell proliferation by modulating the cell signaling pathways that dictate decisions between cell survival, proliferation, and death. In the growth factor-dependent pathways that regulate mitogenesis, numerous positive and negative effectors of signaling are influenced by physiological fluctuations of oxidants, including receptor tyrosine kinases, small GTPases, mitogen-activated protein kinases, protein phosphatases, and transcription factors. The same mitogenic pathways that are sensitive to oxidant levels also directly regulate the expression of cyclin D1, a labile factor required for progression through the G1 phase on the cell cycle. Because the transition from G0 to G1 is the only phase of the cell cycle that is not regulated by cyclin-dependent kinases, but rather by redox-dependent signaling pathways, expression of cyclin D1 represents a primary regulatory node for the dose-dependent effects of oxidants on the induction of cell growth. We suggest that expression of cyclin D1 represents a useful marker for assessing the integration of proliferative and growth inhibitory effects of oxidants on the redox-dependent signaling events that control reentry into the cell cycle.
MeSH term(s)	Animals ; Cell Cycle ; Cyclin D1/metabolism ; Humans ; Mitogens/metabolism ; Reactive Nitrogen Species/metabolism ; Reactive Oxygen Species/metabolism ; Signal Transduction
Chemical Substances	Mitogens ; Reactive Nitrogen Species ; Reactive Oxygen Species ; Cyclin D1 (136601-57-5)
Language	English
Publishing date	2005-05
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.2005.7.741
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 5488: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Peroxiredoxin 3 levels regulate a mitochondrial redox setpoint in malignant mesothelioma cells.

Cunniff, Brian / Wozniak, Alexandra N / Sweeney, Patrick / DeCosta, Kendra / Heintz, Nicholas H

Redox biology

2014 Volume 3, Page(s) 79–87

Abstract: Peroxiredoxin 3 (PRX3), a typical 2-Cys peroxiredoxin located exclusively in the mitochondrial matrix, is the principal peroxidase responsible for metabolizing mitochondrial hydrogen peroxide, a byproduct of cellular respiration originating from the ... ...

Abstract	Peroxiredoxin 3 (PRX3), a typical 2-Cys peroxiredoxin located exclusively in the mitochondrial matrix, is the principal peroxidase responsible for metabolizing mitochondrial hydrogen peroxide, a byproduct of cellular respiration originating from the mitochondrial electron transport chain. Mitochondrial oxidants are produced in excess in cancer cells due to oncogenic transformation and metabolic reorganization, and signals through FOXM1 and other redox-responsive factors to support a hyper-proliferative state. Over-expression of PRX3 in cancer cells has been shown to counteract oncogene-induced senescence and support tumor cell growth and survival making PRX3 a credible therapeutic target. Using malignant mesothelioma (MM) cells stably expressing shRNAs to PRX3 we show that decreased expression of PRX3 alters mitochondrial structure, function and cell cycle kinetics. As compared to control cells, knockdown of PRX3 expression increased mitochondrial membrane potential, basal ATP production, oxygen consumption and extracellular acidification rates. shPRX3 MM cells failed to progress through the cell cycle compared to wild type controls, with increased numbers of cells in G2/M phase. Diminished PRX3 expression also induced mitochondrial hyperfusion similar to the DRP1 inhibitor mdivi-1. Cell cycle progression and changes in mitochondrial networking were rescued by transient expression of either catalase or mitochondrial-targeted catalase, indicating high levels of hydrogen peroxide contribute to perturbations in mitochondrial structure and function in shPRX3 MM cells. Our results indicate that PRX3 levels establish a redox set point that permits MM cells to thrive in response to increased levels of mROS, and that perturbing the redox status governed by PRX3 impairs proliferation by altering cell cycle-dependent dynamics between mitochondrial networking and energy metabolism.
MeSH term(s)	Catalase/genetics ; Catalase/metabolism ; Cell Cycle Checkpoints/genetics ; Cell Line, Tumor ; Gene Expression ; Gene Knockdown Techniques ; Humans ; Lung Neoplasms/genetics ; Lung Neoplasms/metabolism ; Mesothelioma/genetics ; Mesothelioma/metabolism ; Mesothelioma, Malignant ; Metabolome ; Metabolomics ; Mitochondria/metabolism ; Mitochondrial Dynamics/genetics ; Oxidants/metabolism ; Oxidation-Reduction ; Peroxiredoxin III/genetics ; Peroxiredoxin III/metabolism
Chemical Substances	Oxidants ; Peroxiredoxin III (EC 1.11.1.15) ; Catalase (EC 1.11.1.6)
Language	English
Publishing date	2014-11-18
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2701011-9
ISSN	2213-2317 ; 2213-2317
ISSN (online)	2213-2317
ISSN	2213-2317
DOI	10.1016/j.redox.2014.11.003
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

To top

More links

Kategorien

Order via subito

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito