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Article ; Online: GCN2- and eIF2α-phosphorylation-independent, but ATF4-dependent, induction of CARE-containing genes in methionine-deficient cells.

Mazor, Kevin M / Stipanuk, Martha H

2016 Volume 48, Issue 12, Page(s) 2831–2842

Abstract: Amino-acid deprivation is sensed by the eIF2α kinase GCN2. Under conditions of essential amino-acid limitation, GCN2 phosphorylates eIF2α, inhibiting the formation of a new ternary complex and hence mRNA translation initiation. While decreasing global ... ...

Abstract	Amino-acid deprivation is sensed by the eIF2α kinase GCN2. Under conditions of essential amino-acid limitation, GCN2 phosphorylates eIF2α, inhibiting the formation of a new ternary complex and hence mRNA translation initiation. While decreasing global mRNA translation, eIF2α phosphorylation also increases the translation of the integrated stress response (ISR) transcription factor ATF4, which increases the expression of many stress response genes that contain a C/EBP-ATF response element (CARE), including Atf4, 4Ebp1, Asns, and Chop. Using wild-type as well as Gcn2 knockout and unphosphorylatable eIF2α mutant MEFs, we characterized a novel GCN2/eIF2α phosphorylation-independent, but ATF4-dependent, pathway that upregulates the expression of CARE-containing genes in MEFs lacking GCN2 or phosphorylatable eIF2α when these cells are exposed to methionine-deficient, and to a lesser extent arginine- or histidine-deficient, medium. Thus, we demonstrate a GCN2/eIF2α phosphorylation-independent pathway that converges with the GCN2/eIF2α kinase-dependent pathway at the level of ATF4 and similarly results in the upregulation of CARE-containing genes. We hypothesize that the essential role of methionine-charged initiator tRNA in forming ternary complex is responsible for the robust ability of methionine deficiency to induce ATF4 and the ISR even in the absence of GCN2 or eIF2α kinase activity.
Language	English
Publishing date	2016-12
Publishing country	Austria
Document type	Journal Article
ZDB-ID	1121341-3
ISSN	1438-2199 ; 0939-4451
ISSN (online)	1438-2199
ISSN	0939-4451
DOI	10.1007/s00726-016-2318-9
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Article ; Online: Effects of single amino acid deficiency on mRNA translation are markedly different for methionine versus leucine.

Mazor, Kevin M / Dong, Leiming / Mao, Yuanhui / Swanda, Robert V / Qian, Shu-Bing / Stipanuk, Martha H

Scientific reports

2018 Volume 8, Issue 1, Page(s) 8076

Abstract: Although amino acids are known regulators of translation, the unique contributions of specific amino acids are not well understood. We compared effects of culturing HEK293T cells in medium lacking either leucine, methionine, histidine, or arginine on ... ...

Abstract	Although amino acids are known regulators of translation, the unique contributions of specific amino acids are not well understood. We compared effects of culturing HEK293T cells in medium lacking either leucine, methionine, histidine, or arginine on eIF2 and 4EBP1 phosphorylation and measures of mRNA translation. Methionine starvation caused the most drastic decrease in translation as assessed by polysome formation, ribosome profiling, and a measure of protein synthesis (puromycin-labeled polypeptides) but had no significant effect on eIF2 phosphorylation, 4EBP1 hyperphosphorylation or 4EBP1 binding to eIF4E. Leucine starvation suppressed polysome formation and was the only tested condition that caused a significant decrease in 4EBP1 phosphorylation or increase in 4EBP1 binding to eIF4E, but effects of leucine starvation were not replicated by overexpressing nonphosphorylatable 4EBP1. This suggests the binding of 4EBP1 to eIF4E may not by itself explain the suppression of mRNA translation under conditions of leucine starvation. Ribosome profiling suggested that leucine deprivation may primarily inhibit ribosome loading, whereas methionine deprivation may primarily impair start site recognition. These data underscore our lack of a full understanding of how mRNA translation is regulated and point to a unique regulatory role of methionine status on translation initiation that is not dependent upon eIF2 phosphorylation.
MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Amino Acids/deficiency ; Amino Acids/pharmacology ; Culture Media/chemistry ; Culture Media/pharmacology ; Eukaryotic Initiation Factor-2/metabolism ; Eukaryotic Initiation Factor-4E/metabolism ; HEK293 Cells ; Humans ; Leucine/deficiency ; Leucine/pharmacology ; Methionine/deficiency ; Methionine/pharmacology ; Phosphoproteins/metabolism ; Phosphorylation/drug effects ; Protein Biosynthesis/drug effects ; RNA, Messenger/metabolism ; Ribosomes/drug effects ; Ribosomes/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Amino Acids ; Culture Media ; EIF4EBP1 protein, human ; Eukaryotic Initiation Factor-2 ; Eukaryotic Initiation Factor-4E ; Phosphoproteins ; RNA, Messenger ; Methionine (AE28F7PNPL) ; Leucine (GMW67QNF9C)
Language	English
Publishing date	2018-05-24
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-018-26254-2
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Article: Identification of Taurine-Responsive Genes in Murine Liver Using the Cdo1-Null Mouse Model.

Stipanuk, Martha H / Jurkowska, Halina / Niewiadomski, Julie / Mazor, Kevin M / Roman, Heather B / Hirschberger, Lawrence L

Advances in experimental medicine and biology

2017 Volume 975 Pt 1, Page(s) 475–495

Abstract: The cysteine dioxygenase (Cdo1)-null mouse is unable to synthesize hypotaurine and taurine by the cysteine/cysteine sulfinate pathway and has very low taurine levels in all tissues. The lack of taurine is associated with a lack of taurine conjugation of ... ...

Abstract	The cysteine dioxygenase (Cdo1)-null mouse is unable to synthesize hypotaurine and taurine by the cysteine/cysteine sulfinate pathway and has very low taurine levels in all tissues. The lack of taurine is associated with a lack of taurine conjugation of bile acids, a dramatic increase in the total and unconjugated hepatic bile acid pools, and an increase in betaine and other molecules that serve as organic osmolytes. We used the Cdo1-mouse model to determine the effects of taurine deficiency on expression of proteins involved in sulfur amino acid and bile acid metabolism. We identified cysteine sulfinic acid decarboxylase (Csad), betaine:homocysteine methytransferase (Bhmt), cholesterol 7α-hydroxylase (Cyp7a1), and cytochrome P450 3A11 (Cyp3a11) as genes whose hepatic expression is strongly regulated in response to taurine depletion in the Cdo1-null mouse. Dietary taurine supplementation of Cdo1-null mice restored hepatic levels of these four proteins and their respective mRNAs to wild-type levels, whereas dietary taurine supplementation had no effect on abundance of these proteins or mRNAs in wild-type mice.
MeSH term(s)	Animals ; Cysteine Dioxygenase/deficiency ; Female ; Gene Expression/drug effects ; Gene Expression/physiology ; Liver/drug effects ; Liver/metabolism ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Taurine/metabolism ; Taurine/pharmacology
Chemical Substances	Taurine (1EQV5MLY3D) ; Cysteine Dioxygenase (EC 1.13.11.20)
Language	English
Publishing date	2017-08-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	410187-X
ISSN	0065-2598
ISSN	0065-2598
DOI	10.1007/978-94-024-1079-2_38
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Zs.A 3192: 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)
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Article ; Online: High cysteine diet reduces insulin resistance in SHR-CRP rats.

Krijt, J / Sokolová, J / Šilhavý, J / Mlejnek, P / Kubovčiak, J / Liška, F / Malínská, H / Hüttl, M / Marková, I / Křížková, M / Stipanuk, M H / Křížek, T / Ditroi, T / Nagy, P / Kožich, V / Pravenec, M

Physiological research

2021 Volume 70, Issue 5, Page(s) 687–700

Abstract: Increased plasma total cysteine (tCys) has been associated with obesity and metabolic syndrome in human and some animal studies but the underlying mechanisms remain unclear. In this study, we aimed at evaluating the effects of high cysteine diet ... ...

Abstract	Increased plasma total cysteine (tCys) has been associated with obesity and metabolic syndrome in human and some animal studies but the underlying mechanisms remain unclear. In this study, we aimed at evaluating the effects of high cysteine diet administered to SHR-CRP transgenic rats, a model of metabolic syndrome and inflammation. SHR-CRP rats were fed either standard (3.2 g cystine/kg diet) or high cysteine diet (HCD, enriched with additional 4 g L-cysteine/kg diet). After 4 weeks, urine, plasma and tissue samples were collected and parameters of metabolic syndrome, sulfur metabolites and hepatic gene expression were evaluated. Rats on HCD exhibited similar body weights and weights of fat depots, reduced levels of serum insulin, and reduced oxidative stress in the liver. The HCD did not change concentrations of tCys in tissues and body fluids while taurine in tissues and body fluids, and urinary sulfate were significantly increased. In contrast, betaine levels were significantly reduced possibly compensating for taurine elevation. In summary, increased Cys intake did not induce obesity while it ameliorated insulin resistance in the SHR-CRP rats, possibly due to beneficial effects of accumulating taurine.
MeSH term(s)	Adiposity ; Animals ; Cysteine/metabolism ; Cysteine/pharmacology ; Insulin Resistance ; Lipid Metabolism ; Male ; Rats, Inbred SHR ; Rats, Transgenic ; Rats
Chemical Substances	Cysteine (K848JZ4886)
Language	English
Publishing date	2021-09-10
Publishing country	Czech Republic
Document type	Journal Article
ZDB-ID	1073141-6
ISSN	1802-9973 ; 0369-9463 ; 0862-8408
ISSN (online)	1802-9973
ISSN	0369-9463 ; 0862-8408
DOI	10.33549/physiolres.934736
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Article: Leucine and protein synthesis: mTOR and beyond

Stipanuk, M.H

Nutrition reviews. 2007 Mar., v. 65, no. 3

2007

Abstract: The effects of amino acid intake on protein synthesis in the intact rat appear to be mediated almost entirely by a single amino acid: leucine. The effect of leucine on protein synthesis appears to be closely associated with eIF4G phosphorylation and its ... ...

Abstract	The effects of amino acid intake on protein synthesis in the intact rat appear to be mediated almost entirely by a single amino acid: leucine. The effect of leucine on protein synthesis appears to be closely associated with eIF4G phosphorylation and its association with eIF4E, but whether eIF4G phosphorylation actually mediates the effects of leucine or is merely associated with these events has not been elucidated. Additional research is needed to determine whether leucine effects eIF4G phosphorylation, whether eIF4G phosphorylation is essential for the effect of leucine on protein synthesis, and whether mTOR (mammalian target of rapamycin) or another component of the mTOR complex is somehow involved in leucine-specific signaling.
Keywords	rats ; animal models ; leucine ; protein synthesis ; amino acid requirements ; nutrient intake ; protein phosphorylation ; animal proteins ; biochemical pathways ; signal transduction
Language	English
Dates of publication	2007-03
Size	p. 122-129.
Document type	Article
ZDB-ID	82067-2
ISSN	1753-4887 ; 0029-6643
ISSN (online)	1753-4887
ISSN	0029-6643
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Cysteine dioxygenase is essential for mouse sperm osmoadaptation and male fertility.

Asano, Atsushi / Roman, Heather B / Hirschberger, Lawrence L / Ushiyama, Ai / Nelson, Jacquelyn L / Hinchman, Meleana M / Stipanuk, Martha H / Travis, Alexander J

The FEBS journal

2018 Volume 285, Issue 10, Page(s) 1827–1839

Abstract: Sperm entering the epididymis are immotile and cannot respond to stimuli that will enable them to fertilize. The epididymis is a highly complex organ, with multiple histological zones and cell types that together change the composition and functional ... ...

Abstract	Sperm entering the epididymis are immotile and cannot respond to stimuli that will enable them to fertilize. The epididymis is a highly complex organ, with multiple histological zones and cell types that together change the composition and functional abilities of sperm through poorly understood mechanisms. Sperm take up taurine during epididymal transit, which may play antioxidant or osmoregulatory roles. Cysteine dioxygenase (CDO) is a critical enzyme for taurine synthesis. A previous study reported that male CDO
MeSH term(s)	Acrosome Reaction ; Animals ; Antioxidants/metabolism ; Blotting, Western ; Chromatography, High Pressure Liquid ; Cysteine Dioxygenase/genetics ; Cysteine Dioxygenase/metabolism ; Epididymis/enzymology ; Exocytosis ; Female ; Fertility ; Lipid Peroxidation ; Male ; Mice ; Mice, Knockout ; Osmoregulation ; Phosphorylation ; RNA, Messenger/genetics ; Reverse Transcriptase Polymerase Chain Reaction ; Sperm Maturation ; Spermatozoa/metabolism ; Spermatozoa/physiology ; Taurine/analogs & derivatives ; Taurine/metabolism
Chemical Substances	Antioxidants ; RNA, Messenger ; Taurine (1EQV5MLY3D) ; hypotaurine (5L08GE4332) ; Cysteine Dioxygenase (EC 1.13.11.20)
Language	English
Publishing date	2018-04-16
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.14449
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Article: GCN2- and eIF2Î±-phosphorylation-independent, but ATF4-dependent, induction of CARE-containing genes in methionine-deficient cells

Mazor, Kevin M / Martha H. Stipanuk

Amino acids. 2016 Dec., v. 48, no. 12

2016

Abstract: Amino-acid deprivation is sensed by the eIF2Î± kinase GCN2. Under conditions of essential amino-acid limitation, GCN2 phosphorylates eIF2Î±, inhibiting the formation of a new ternary complex and hence mRNA translation initiation. While decreasing global ... ...

Abstract	Amino-acid deprivation is sensed by the eIF2Î± kinase GCN2. Under conditions of essential amino-acid limitation, GCN2 phosphorylates eIF2Î±, inhibiting the formation of a new ternary complex and hence mRNA translation initiation. While decreasing global mRNA translation, eIF2Î± phosphorylation also increases the translation of the integrated stress response (ISR) transcription factor ATF4, which increases the expression of many stress response genes that contain a C/EBP-ATF response element (CARE), including Atf4, 4Ebp1, Asns, and Chop. Using wild-type as well as Gcn2 knockout and unphosphorylatable eIF2Î± mutant MEFs, we characterized a novel GCN2/eIF2Î± phosphorylation-independent, but ATF4-dependent, pathway that upregulates the expression of CARE-containing genes in MEFs lacking GCN2 or phosphorylatable eIF2Î± when these cells are exposed to methionine-deficient, and to a lesser extent arginine- or histidine-deficient, medium. Thus, we demonstrate a GCN2/eIF2Î± phosphorylation-independent pathway that converges with the GCN2/eIF2Î± kinase-dependent pathway at the level of ATF4 and similarly results in the upregulation of CARE-containing genes. We hypothesize that the essential role of methionine-charged initiator tRNA in forming ternary complex is responsible for the robust ability of methionine deficiency to induce ATF4 and the ISR even in the absence of GCN2 or eIF2Î± kinase activity.
Keywords	gene expression regulation ; genes ; messenger RNA ; methionine ; mutants ; phosphorylation ; stress response ; transcription (genetics) ; transcription factors ; transfer RNA ; translation (genetics)
Language	English
Dates of publication	2016-12
Size	p. 2831-2842.
Publishing place	Springer Vienna
Document type	Article
ZDB-ID	1121341-3
ISSN	1438-2199 ; 0939-4451
ISSN (online)	1438-2199
ISSN	0939-4451
DOI	10.1007/s00726-016-2318-9
Database	NAL-Catalogue (AGRICOLA)

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Zs.A 3490: Show issues

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Article: Sulfur amino acid metabolism: pathways for production and removal of homocysteine and cysteine

Stipanuk, M.H

Annual review of nutrition. 2004, v. 24

2004

Keywords	amino acid metabolism ; methionine ; cysteine ; homocysteine ; adenosylmethionine ; cystathionine beta-synthase ; cystathionine gamma-lyase ; oxygenases ; methyltransferases ; enzyme activity ; gene expression regulation
Language	English
Size	p. 539-577.
Document type	Article
ZDB-ID	406980-8
ISSN	1545-4312 ; 0199-9885
ISSN (online)	1545-4312
ISSN	0199-9885
Database	NAL-Catalogue (AGRICOLA)

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Article: Surprising insights that aren't so surprising in the modeling of sulfur amino acid metabolism.

Stipanuk, M H / Dominy, J E

Amino acids

2006 Volume 30, Issue 3, Page(s) 251–256

Abstract: The modeling of whole organism sulfur amino acid flux control has been aided in recent years by advancements in proteomics and mass spectroscopy-based metabolite analysis. The convergence of these two fields and their respective techniques, as ... ...

Abstract	The modeling of whole organism sulfur amino acid flux control has been aided in recent years by advancements in proteomics and mass spectroscopy-based metabolite analysis. The convergence of these two fields and their respective techniques, as demonstrated by a new study using yeast by Lafaye et al., has shown that researchers seeking to model whole cell/organism metabolism should give careful consideration to the relationships connecting enzyme concentration, enzyme activity, substrate concentration, and metabolic flux. In this paper, we outline some of the fundamental concepts for modeling sulfur amino acid metabolism and how they relate to our current understanding of mammalian sulfur amino acid metabolism.
MeSH term(s)	Amino Acids, Sulfur/metabolism ; Animals ; Humans ; Models, Biological ; Saccharomyces cerevisiae/metabolism
Chemical Substances	Amino Acids, Sulfur
Language	English
Publishing date	2006-05
Publishing country	Austria
Document type	Journal Article ; Review
ZDB-ID	1121341-3
ISSN	1438-2199 ; 0939-4451
ISSN (online)	1438-2199
ISSN	0939-4451
DOI	10.1007/s00726-005-0288-4
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Article ; Online: Sulfur- and seleno-containing amino acids.

Wróbel, Maria / Stipanuk, Martha H / Nagahara, Noriuki

Amino acids

2011 Volume 41, Issue 1, Page(s) 1–2

MeSH term(s)	Amino Acids/chemistry ; Amino Acids/metabolism ; Humans ; Selenium/chemistry ; Selenium/metabolism ; Sulfur/chemistry ; Sulfur/metabolism
Chemical Substances	Amino Acids ; Sulfur (70FD1KFU70) ; Selenium (H6241UJ22B)
Language	English
Publishing date	2011-05-05
Publishing country	Austria
Document type	Editorial ; Introductory Journal Article
ZDB-ID	1121341-3
ISSN	1438-2199 ; 0939-4451
ISSN (online)	1438-2199
ISSN	0939-4451
DOI	10.1007/s00726-011-0930-2
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