Effect of hydrogen sulfide on glycolysis‐based energy production in mouse erythrocytes
Hydrogen sulfide (H2S) is a gasotransmitter that regulates both physiological and pathophysiological processes in mammalian cells. Recent studies have demonstrated that H2S promotes aerobic energy production in the mitochondria in response to hypoxia, but its effect on anaerobic energy production ha...
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Published in | Journal of cellular physiology Vol. 237; no. 1; pp. 763 - 773 |
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Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
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01.01.2022
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Abstract | Hydrogen sulfide (H2S) is a gasotransmitter that regulates both physiological and pathophysiological processes in mammalian cells. Recent studies have demonstrated that H2S promotes aerobic energy production in the mitochondria in response to hypoxia, but its effect on anaerobic energy production has yet to be established. Glycolysis is the anaerobic process by which ATP is produced through the metabolism of glucose. Mammalian red blood cells (RBCs) extrude mitochondria and nucleus during erythropoiesis. These cells would serve as a unique model to observe the effect of H2S on glycolysis‐mediated energy production. The purpose of this study was to determine the effect of H2S on glycolysis‐mediated energy production in mitochondria‐free mouse RBCs. Western blot analysis showed that the only H2S‐generating enzyme expressed in mouse RBCs is 3‐mercaptopyruvate sulfurtransferase (MST). Supplement of the substrate for MST stimulated, but the inhibition of the same suppressed, the endogenous production of H2S. Both exogenously administered H2S salt and MST‐derived endogenous H2S stimulated glycolysis‐mediated ATP production. The effect of NaHS on ATP levels was not affected by oxygenation status. On the contrary, hypoxia increased intracellular H2S levels and MST activity in mouse RBCs. The mitochondria‐targeted H2S donor, AP39, did not affect ATP levels of mouse RBCs. NaHS at low concentrations (3–100 μM) increased ATP levels and decreased cell viability after 3 days of incubation in vitro. Higher NaHS concentrations (300–1000 μM) lowered ATP levels, but prolonged cell viability. H2S may offer a cytoprotective effect in mammalian RBCs to maintain oxygen‐independent energy production.
The effect of H2S on glycolysis‐mediated energy production has not been studied in depth. Here, we report that mouse red blood cells (RBCs), which rely solely on glycolysis for energy production, have the capacity to endogenously produce H2S and that H2S stimulates glycolysis. Moreover, exposure of RBCs to H2S salt significantly prolonged the lifespan of mouse RBCs ex vivo, indicating that H2S may have a functional impact on RBC survival. |
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AbstractList | Hydrogen sulfide (H2S) is a gasotransmitter that regulates both physiological and pathophysiological processes in mammalian cells. Recent studies have demonstrated that H2S promotes aerobic energy production in the mitochondria in response to hypoxia, but its effect on anaerobic energy production has yet to be established. Glycolysis is the anaerobic process by which ATP is produced through the metabolism of glucose. Mammalian red blood cells (RBCs) extrude mitochondria and nucleus during erythropoiesis. These cells would serve as a unique model to observe the effect of H2S on glycolysis‐mediated energy production. The purpose of this study was to determine the effect of H2S on glycolysis‐mediated energy production in mitochondria‐free mouse RBCs. Western blot analysis showed that the only H2S‐generating enzyme expressed in mouse RBCs is 3‐mercaptopyruvate sulfurtransferase (MST). Supplement of the substrate for MST stimulated, but the inhibition of the same suppressed, the endogenous production of H2S. Both exogenously administered H2S salt and MST‐derived endogenous H2S stimulated glycolysis‐mediated ATP production. The effect of NaHS on ATP levels was not affected by oxygenation status. On the contrary, hypoxia increased intracellular H2S levels and MST activity in mouse RBCs. The mitochondria‐targeted H2S donor, AP39, did not affect ATP levels of mouse RBCs. NaHS at low concentrations (3–100 μM) increased ATP levels and decreased cell viability after 3 days of incubation in vitro. Higher NaHS concentrations (300–1000 μM) lowered ATP levels, but prolonged cell viability. H2S may offer a cytoprotective effect in mammalian RBCs to maintain oxygen‐independent energy production.
The effect of H2S on glycolysis‐mediated energy production has not been studied in depth. Here, we report that mouse red blood cells (RBCs), which rely solely on glycolysis for energy production, have the capacity to endogenously produce H2S and that H2S stimulates glycolysis. Moreover, exposure of RBCs to H2S salt significantly prolonged the lifespan of mouse RBCs ex vivo, indicating that H2S may have a functional impact on RBC survival. Hydrogen sulfide (H S) is a gasotransmitter that regulates both physiological and pathophysiological processes in mammalian cells. Recent studies have demonstrated that H S promotes aerobic energy production in the mitochondria in response to hypoxia, but its effect on anaerobic energy production has yet to be established. Glycolysis is the anaerobic process by which ATP is produced through the metabolism of glucose. Mammalian red blood cells (RBCs) extrude mitochondria and nucleus during erythropoiesis. These cells would serve as a unique model to observe the effect of H S on glycolysis-mediated energy production. The purpose of this study was to determine the effect of H S on glycolysis-mediated energy production in mitochondria-free mouse RBCs. Western blot analysis showed that the only H S-generating enzyme expressed in mouse RBCs is 3-mercaptopyruvate sulfurtransferase (MST). Supplement of the substrate for MST stimulated, but the inhibition of the same suppressed, the endogenous production of H S. Both exogenously administered H S salt and MST-derived endogenous H S stimulated glycolysis-mediated ATP production. The effect of NaHS on ATP levels was not affected by oxygenation status. On the contrary, hypoxia increased intracellular H S levels and MST activity in mouse RBCs. The mitochondria-targeted H S donor, AP39, did not affect ATP levels of mouse RBCs. NaHS at low concentrations (3-100 μM) increased ATP levels and decreased cell viability after 3 days of incubation in vitro. Higher NaHS concentrations (300-1000 μM) lowered ATP levels, but prolonged cell viability. H S may offer a cytoprotective effect in mammalian RBCs to maintain oxygen-independent energy production. Hydrogen sulfide (H2S) is a gasotransmitter that regulates both physiological and pathophysiological processes in mammalian cells. Recent studies have demonstrated that H2S promotes aerobic energy production in the mitochondria in response to hypoxia, but its effect on anaerobic energy production has yet to be established. Glycolysis is the anaerobic process by which ATP is produced through the metabolism of glucose. Mammalian red blood cells (RBCs) extrude mitochondria and nucleus during erythropoiesis. These cells would serve as a unique model to observe the effect of H2S on glycolysis‐mediated energy production. The purpose of this study was to determine the effect of H2S on glycolysis‐mediated energy production in mitochondria‐free mouse RBCs. Western blot analysis showed that the only H2S‐generating enzyme expressed in mouse RBCs is 3‐mercaptopyruvate sulfurtransferase (MST). Supplement of the substrate for MST stimulated, but the inhibition of the same suppressed, the endogenous production of H2S. Both exogenously administered H2S salt and MST‐derived endogenous H2S stimulated glycolysis‐mediated ATP production. The effect of NaHS on ATP levels was not affected by oxygenation status. On the contrary, hypoxia increased intracellular H2S levels and MST activity in mouse RBCs. The mitochondria‐targeted H2S donor, AP39, did not affect ATP levels of mouse RBCs. NaHS at low concentrations (3–100 μM) increased ATP levels and decreased cell viability after 3 days of incubation in vitro. Higher NaHS concentrations (300–1000 μM) lowered ATP levels, but prolonged cell viability. H2S may offer a cytoprotective effect in mammalian RBCs to maintain oxygen‐independent energy production. Abstract Hydrogen sulfide (H 2 S) is a gasotransmitter that regulates both physiological and pathophysiological processes in mammalian cells. Recent studies have demonstrated that H 2 S promotes aerobic energy production in the mitochondria in response to hypoxia, but its effect on anaerobic energy production has yet to be established. Glycolysis is the anaerobic process by which ATP is produced through the metabolism of glucose. Mammalian red blood cells (RBCs) extrude mitochondria and nucleus during erythropoiesis. These cells would serve as a unique model to observe the effect of H 2 S on glycolysis‐mediated energy production. The purpose of this study was to determine the effect of H 2 S on glycolysis‐mediated energy production in mitochondria‐free mouse RBCs. Western blot analysis showed that the only H 2 S‐generating enzyme expressed in mouse RBCs is 3‐mercaptopyruvate sulfurtransferase (MST). Supplement of the substrate for MST stimulated, but the inhibition of the same suppressed, the endogenous production of H 2 S. Both exogenously administered H 2 S salt and MST‐derived endogenous H 2 S stimulated glycolysis‐mediated ATP production. The effect of NaHS on ATP levels was not affected by oxygenation status. On the contrary, hypoxia increased intracellular H 2 S levels and MST activity in mouse RBCs. The mitochondria‐targeted H 2 S donor, AP39, did not affect ATP levels of mouse RBCs. NaHS at low concentrations (3–100 μM) increased ATP levels and decreased cell viability after 3 days of incubation in vitro. Higher NaHS concentrations (300–1000 μM) lowered ATP levels, but prolonged cell viability. H 2 S may offer a cytoprotective effect in mammalian RBCs to maintain oxygen‐independent energy production. |
Author | Wondimu, Eden T. Fu, Ming Torregrossa, Roberta Jin, Zhuping Whiteman, Matthew Wu, Lingyun Zhang, Quanxi Yang, Guangdong Wang, Rui |
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CitedBy_id | crossref_primary_10_3390_cells13050371 crossref_primary_10_1089_ars_2022_0067 crossref_primary_10_1021_acsbiomedchemau_3c00028 crossref_primary_10_1016_j_phymed_2024_155785 crossref_primary_10_1016_j_redox_2022_102331 |
Cites_doi | 10.1096/fj.12-216507 10.1182/blood.v99.9.3439 10.1016/j.niox.2014.04.008 10.1182/blood-2008-05-159269 10.1080/15384101.2019.1618125 10.1016/j.tibs.2014.03.003 10.1073/pnas.1115634109 10.1096/fj.06-7407com 10.1073/pnas.1101315108 10.2337/db07-1820 10.1021/acs.jproteome.6b00733 10.1016/B978-0-12-416618-9.00005-4 10.1074/jbc.M115.639831 10.1371/journal.pone.0067322 10.1016/j.cell.2018.03.001 10.1016/j.bcmd.2004.01.015 10.1186/s13550-017-0266-3 10.1177/2041731411432365 10.1111/bph.12773 10.1186/1742-9994-10-33 10.1089/ars.2016.6954 10.1038/scientificamerican0310-66 10.3389/fphys.2017.01110 10.1152/ajpregu.00348.2019 10.1126/science.1162667 10.1053/tmrv.2002.35212 10.1016/j.ejphar.2005.12.037 10.2119/molmed.2015.00035 10.1182/blood-2005-04-1622 10.1016/j.bcp.2017.03.025 10.1111/trf.12804 10.1039/C3MD00323J 10.1096/fj.02-0211hyp 10.4274/tjh.2016.0251 10.1089/ars.2014.5930 10.1073/pnas.1308487110 10.1016/j.bbamem.2018.07.009 10.1080/10715762.2018.1431626 10.1016/j.bcp.2018.01.045 10.1152/ajprenal.00174.2010 10.1111/j.1537-2995.2008.01734.x |
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Keywords | hypoxia ATP production 3-mercaptopyruvate sulfur transferase glycolysis red blood cell |
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References | 2002; 16 2017; 7 2014; 116 2017; 8 2011; 2 2013; 27 2017; 26 2018; 149 2010; 302 2015; 55 2002; 99 2019; 18 2008; 57 2014; 171 2008; 322 2014; 41 2013; 8 2016; 15 2017; 136 2019; 1861 2006; 532 2012; 109 2004; 32 2014; 5 2011; 108 2015; 290 2018; 173 2013; 10 2020 2010; 299 2015; 22 2015; 21 2017; 34 2005; 106 2008; 48 2018; 52 2014 2013; 110 2014; 39 2008; 112 2007; 21 2020; 319 2014; 542 e_1_2_9_30_1 e_1_2_9_31_1 e_1_2_9_11_1 e_1_2_9_34_1 e_1_2_9_10_1 e_1_2_9_35_1 e_1_2_9_13_1 e_1_2_9_32_1 e_1_2_9_12_1 e_1_2_9_33_1 Baynes J. W. (e_1_2_9_3_1) 2014 e_1_2_9_15_1 e_1_2_9_14_1 e_1_2_9_39_1 e_1_2_9_17_1 e_1_2_9_36_1 e_1_2_9_16_1 e_1_2_9_37_1 e_1_2_9_19_1 e_1_2_9_18_1 e_1_2_9_41_1 e_1_2_9_42_1 e_1_2_9_20_1 e_1_2_9_40_1 e_1_2_9_22_1 e_1_2_9_45_1 e_1_2_9_21_1 e_1_2_9_24_1 e_1_2_9_43_1 e_1_2_9_23_1 e_1_2_9_44_1 e_1_2_9_8_1 e_1_2_9_7_1 e_1_2_9_6_1 e_1_2_9_5_1 e_1_2_9_4_1 e_1_2_9_2_1 e_1_2_9_9_1 Vrhovac I. (e_1_2_9_38_1) 2014; 116 e_1_2_9_26_1 e_1_2_9_25_1 e_1_2_9_28_1 e_1_2_9_27_1 e_1_2_9_29_1 |
References_xml | – volume: 8 year: 2017 article-title: Effects of hypoxia on erythrocyte membrane properties—Implications for intravascular hemolysis and purinergic control of blood flow publication-title: Frontiers in Physiology – volume: 99 start-page: 3439 issue: 9 year: 2002 end-page: 3448 article-title: Erythrocyte survival is promoted by plasma and suppressed by a Bak‐derived BH3 peptide that interacts with membrane‐associated Bcl‐X(L) publication-title: Blood – volume: 10 issue: 1 year: 2013 article-title: Avian erythrocytes have functional mitochondria, opening novel perspectives for birds as animal models in the study of ageing publication-title: Frontiers in Zoology – volume: 18 start-page: 1316 issue: 12 year: 2019 end-page: 1334 article-title: Proliferating tumor cells mimick glucose metabolism of mature human erythrocytes publication-title: Cell Cycle – volume: 55 start-page: 205 issue: 1 year: 2015 end-page: 219 article-title: An update on red blood cell storage lesions, as gleaned through biochemistry and omics technologies publication-title: Transfusion – volume: 109 start-page: 2943 issue: 8 year: 2012 end-page: 2948 article-title: Hydrogen sulfide (H S) metabolism in mitochondria and its regulatory role in energy production publication-title: Proceedings of the National Academy of Sciences of the United States of America – volume: 302 start-page: 66 issue: 3 year: 2010 end-page: 71 article-title: Toxic gas, lifesaver publication-title: Scientific American – volume: 149 start-page: 163 year: 2018 end-page: 173 article-title: Investigations on the role of hemoglobin in sulfide metabolism by intact human red blood cells publication-title: Biochemical Pharmacology – volume: 532 start-page: 11 issue: 1–2 year: 2006 end-page: 17 article-title: Stimulation of erythrocyte phosphatidylserine exposure by chlorpromazine publication-title: European Journal of Pharmacology – volume: 108 start-page: 10986 issue: 27 year: 2011 end-page: 10991 article-title: Multiscale approach to link red blood cell dynamics, shear viscosity, and ATP release publication-title: Proceedings of the National Academy of Sciences of the United States of America – volume: 542 start-page: 91 year: 2014 end-page: 114 article-title: Techniques to monitor glycolysis publication-title: Methods in Enzymology – volume: 171 start-page: 4322 issue: 18 year: 2014 end-page: 4336 article-title: Utilizing hydrogen sulfide as a novel anti‐cancer agent by targeting cancer glycolysis and pH imbalance publication-title: British Journal of Pharmacology – volume: 26 start-page: 718 issue: 13 year: 2017 end-page: 742 article-title: Red blood cell function and dysfunction: Redox regulation, nitric oxide metabolism, anemia publication-title: Antioxidants & Redox Signaling – volume: 52 start-page: 288 issue: 2 year: 2018 end-page: 303 article-title: Hydrogen sulfide increases glutathione biosynthesis, and glucose uptake and utilisation in C C mouse myotubes publication-title: Free Radical Research – volume: 319 start-page: R69 issue: 1 year: 2020 end-page: R78 article-title: H S‐stimulated bioenergetics in chicken erythrocytes and the underlying mechanism publication-title: American Journal of Physiology: Regulatory, Integrative and Comparative Physiology – volume: 8 issue: 6 year: 2013 article-title: Brain 3‐mercaptopyruvate sulfurtransferase (3MST): Cellular localization and downregulation after acute stroke publication-title: PLOS One – year: 2014 – volume: 15 start-page: 3883 issue: 10 year: 2016 end-page: 3895 article-title: AltitudeOmics: Red blood cell metabolic adaptation to high altitude hypoxia publication-title: Journal of Proteome Research – volume: 16 start-page: 283 issue: 4 year: 2002 end-page: 295 article-title: Storage of red blood cells: New approaches publication-title: Transfusion Medicine Reviews – volume: 27 start-page: 601 issue: 2 year: 2013 end-page: 611 article-title: Intramitochondrial hydrogen sulfide production by 3‐mercaptopyruvate sulfurtransferase maintains mitochondrial electron flow and supports cellular bioenergetics publication-title: FASEB Journal – volume: 112 start-page: 4729 issue: 12 year: 2008 end-page: 4738 article-title: The Glut1 and Glut4 glucose transporters are differentially expressed during perinatal and postnatal erythropoiesis publication-title: Blood – volume: 2 start-page: 204173141143 2365 issue: 1 year: 2011 article-title: Evolution of oxygen utilization in multicellular organisms and implications for cell signalling in tissue engineering publication-title: Journal of Tissue Engineering – volume: 57 start-page: 2445 issue: 9 year: 2008 end-page: 2452 article-title: Evidence for interindividual heterogeneity in the glucose gradient across the human red blood cell membrane and its relationship to hemoglobin glycation publication-title: Diabetes – volume: 21 start-page: 1 issue: 1 year: 2015 end-page: 14 article-title: Regulation of vascular tone, angiogenesis and cellular bioenergetics by the 3‐mercaptopyruvate sulfurtransferase/H S pathway: Functional impairment by hyperglycemia and restoration by DL‐α‐lipoic acid publication-title: Molecular Medicine – volume: 7 start-page: 19 issue: 1 year: 2017 article-title: F‐FDG‐labeled red blood cell PET for blood‐pool imaging: Preclinical evaluation in rats publication-title: EJNMMI Research – volume: 16 start-page: 1792 issue: 13 year: 2002 end-page: 1798 article-title: Two's company, three's a crowd: Can H S be the third endogenous gaseous transmitter? publication-title: FASEB Journal – volume: 21 start-page: 1699 issue: 8 year: 2007 end-page: 1706 article-title: Sulfide, the first inorganic substrate for human cells publication-title: FASEB Journal – volume: 110 start-page: 12679 issue: 31 year: 2013 end-page: 12684 article-title: Oxygen‐sensitive mitochondrial accumulation of cystathionine β‐synthase mediated by Lon protease publication-title: Proceedings of the National Academy of Sciences of the United States of America – volume: 32 start-page: 401 issue: 3 year: 2004 end-page: 407 article-title: Conventional transport assays underestimate sugar transport rates in human red cells publication-title: Blood Cells, Molecules, & Diseases – volume: 5 start-page: 728 year: 2014 end-page: 736 article-title: The synthesis and functional evaluation of a mitochondria‐targeted hydrogen sulfide donor, (10‐oxo‐10‐(4‐(3‐thioxo‐3H‐1,2‐dithiol‐5‐yl)phenoxy)decyl)triphenylphosphonium bromide (AP39) publication-title: MedChemComm – volume: 173 start-page: 117 issue: 1 year: 2018 end-page: 129 article-title: Amino acid restriction triggers angiogenesis via GCN2/ATF4 regulation of VEGF and H S production publication-title: Cell – volume: 290 start-page: 8310 issue: 13 year: 2015 end-page: 8320 article-title: Sulfide oxidation by a noncanonical pathway in red blood cells generates thiosulfate and polysulfides publication-title: The Journal of Biological Chemistry – year: 2020 – volume: 136 start-page: 86 year: 2017 end-page: 98 article-title: H S‐induced S‐sulfhydration of lactate dehydrogenase a (LDHA) stimulates cellular bioenergetics in HCT116 colon cancer cells publication-title: Biochemical Pharmacology – volume: 299 start-page: F1 issue: 1 year: 2010 end-page: F13 article-title: Hypoxic regulation of erythropoiesis and iron metabolism publication-title: American Journal of Physiology–Renal Physiology – volume: 106 start-page: 4034 issue: 13 year: 2005 end-page: 4042 article-title: The energy‐less red blood cell is lost: Erythrocyte enzyme abnormalities of glycolysis publication-title: Blood – volume: 1861 start-page: 236 issue: 1 year: 2019 end-page: 244 article-title: Morphological changes induced in erythrocyte by amyloid beta peptide and glucose depletion: A combined atomic force microscopy and biochemical study publication-title: Biochimica et Biophysica Acta, Biomembranes – volume: 322 start-page: 587 issue: 5901 year: 2008 end-page: 590 article-title: H S as a physiologic vasorelaxant: Hypertension in mice with deletion of cystathionine gamma‐lyase publication-title: Science – volume: 48 start-page: 1478 issue: 7 year: 2008 end-page: 1485 article-title: Survival of red blood cells after transfusion: A comparison between red cells concentrates of different storage periods publication-title: Transfusion – volume: 41 start-page: 120 year: 2014 end-page: 130 article-title: AP39, a novel mitochondria‐targeted hydrogen sulfide donor, stimulates cellular bioenergetics, exerts cytoprotective effects and protects against the loss of mitochondrial DNA integrity in oxidatively stressed endothelial cells in vitro publication-title: Nitric Oxide: Biology and Chemistry – volume: 22 start-page: 377 issue: 5 year: 2015 end-page: 397 article-title: Hydrogen sulfide as an oxygen sensor publication-title: Antioxidants & Redox Signaling – volume: 34 start-page: 111 issue: 1 year: 2017 end-page: 113 article-title: Posttranslational modifications of red blood cell ghost proteins as “signatures” for distinguishing between low‐ and high‐risk myelodysplastic syndrome patients publication-title: Turkish Journal of Haematology – volume: 39 start-page: 227 issue: 5 year: 2014 end-page: 232 article-title: Gasotransmitters: Growing pains and joys publication-title: Trends in Biochemical Sciences – volume: 116 start-page: 131 issue: 2 year: 2014 end-page: 138 article-title: Glucose transporter in the mammalian blood cells publication-title: Periodicum Biologorum – ident: e_1_2_9_26_1 doi: 10.1096/fj.12-216507 – volume-title: Medical biochemistry year: 2014 ident: e_1_2_9_3_1 contributor: fullname: Baynes J. W. – ident: e_1_2_9_39_1 doi: 10.1182/blood.v99.9.3439 – ident: e_1_2_9_33_1 doi: 10.1016/j.niox.2014.04.008 – ident: e_1_2_9_27_1 doi: 10.1182/blood-2008-05-159269 – ident: e_1_2_9_13_1 doi: 10.1080/15384101.2019.1618125 – ident: e_1_2_9_42_1 doi: 10.1016/j.tibs.2014.03.003 – ident: e_1_2_9_12_1 doi: 10.1073/pnas.1115634109 – ident: e_1_2_9_7_1 – ident: e_1_2_9_14_1 doi: 10.1096/fj.06-7407com – ident: e_1_2_9_11_1 doi: 10.1073/pnas.1101315108 – ident: e_1_2_9_19_1 doi: 10.2337/db07-1820 – ident: e_1_2_9_10_1 doi: 10.1021/acs.jproteome.6b00733 – ident: e_1_2_9_35_1 doi: 10.1016/B978-0-12-416618-9.00005-4 – ident: e_1_2_9_37_1 doi: 10.1074/jbc.M115.639831 – ident: e_1_2_9_45_1 doi: 10.1371/journal.pone.0067322 – ident: e_1_2_9_23_1 doi: 10.1016/j.cell.2018.03.001 – ident: e_1_2_9_5_1 doi: 10.1016/j.bcmd.2004.01.015 – ident: e_1_2_9_25_1 doi: 10.1186/s13550-017-0266-3 – ident: e_1_2_9_31_1 doi: 10.1177/2041731411432365 – ident: e_1_2_9_22_1 doi: 10.1111/bph.12773 – ident: e_1_2_9_32_1 doi: 10.1186/1742-9994-10-33 – ident: e_1_2_9_20_1 doi: 10.1089/ars.2016.6954 – ident: e_1_2_9_41_1 doi: 10.1038/scientificamerican0310-66 – ident: e_1_2_9_15_1 doi: 10.3389/fphys.2017.01110 – ident: e_1_2_9_18_1 doi: 10.1152/ajpregu.00348.2019 – ident: e_1_2_9_44_1 doi: 10.1126/science.1162667 – ident: e_1_2_9_17_1 doi: 10.1053/tmrv.2002.35212 – volume: 116 start-page: 131 issue: 2 year: 2014 ident: e_1_2_9_38_1 article-title: Glucose transporter in the mammalian blood cells publication-title: Periodicum Biologorum contributor: fullname: Vrhovac I. – ident: e_1_2_9_2_1 doi: 10.1016/j.ejphar.2005.12.037 – ident: e_1_2_9_8_1 doi: 10.2119/molmed.2015.00035 – ident: e_1_2_9_43_1 doi: 10.1182/blood-2005-04-1622 – ident: e_1_2_9_36_1 doi: 10.1016/j.bcp.2017.03.025 – ident: e_1_2_9_9_1 doi: 10.1111/trf.12804 – ident: e_1_2_9_21_1 doi: 10.1039/C3MD00323J – ident: e_1_2_9_40_1 doi: 10.1096/fj.02-0211hyp – ident: e_1_2_9_30_1 doi: 10.4274/tjh.2016.0251 – ident: e_1_2_9_28_1 doi: 10.1089/ars.2014.5930 – ident: e_1_2_9_34_1 doi: 10.1073/pnas.1308487110 – ident: e_1_2_9_6_1 doi: 10.1016/j.bbamem.2018.07.009 – ident: e_1_2_9_29_1 doi: 10.1080/10715762.2018.1431626 – ident: e_1_2_9_4_1 doi: 10.1016/j.bcp.2018.01.045 – ident: e_1_2_9_16_1 doi: 10.1152/ajprenal.00174.2010 – ident: e_1_2_9_24_1 doi: 10.1111/j.1537-2995.2008.01734.x |
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Snippet | Hydrogen sulfide (H2S) is a gasotransmitter that regulates both physiological and pathophysiological processes in mammalian cells. Recent studies have... Hydrogen sulfide (H S) is a gasotransmitter that regulates both physiological and pathophysiological processes in mammalian cells. Recent studies have... Abstract Hydrogen sulfide (H 2 S) is a gasotransmitter that regulates both physiological and pathophysiological processes in mammalian cells. Recent studies... |
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SubjectTerms | 3‐mercaptopyruvate sulfur transferase Adenosine Triphosphate - metabolism Anaerobic processes Animals ATP ATP production Cell viability Energy Erythrocytes Erythrocytes - metabolism Erythropoiesis Glucose metabolism Glycolysis Hydrogen sulfide Hydrogen Sulfide - metabolism Hydrogen Sulfide - pharmacology Hypoxia Incubation Low concentrations Mammalian cells Mammals Mammals - metabolism Mice Mitochondria Oxygenation red blood cell Substrate inhibition Sulfurtransferase |
Title | Effect of hydrogen sulfide on glycolysis‐based energy production in mouse erythrocytes |
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