Homocysteine-Thiolactone Modulates Gating of Mitochondrial Voltage-Dependent Anion Channel (VDAC) and Protects It from Induced Oxidative Stress.

Animals Homocysteine / analogs & derivatives Hydrogen Peroxide / metabolism Mitochondria / metabolism Oxidative Stress Rats Voltage-Dependent Anion Channels / chemistry
Bilayer electrophysiology Homocysteine-thiolactone (HTL) Hydrogen peroxide (H2O2) Oxidative stress Voltage-dependent anion channel (VDAC)

Journal

The Journal of membrane biology
ISSN: 1432-1424
Titre abrégé: J Membr Biol
Pays: United States
ID NLM: 0211301

Informations de publication

Date de publication:
02 2022
Historique:
received: 07 10 2021
accepted: 10 01 2022
pubmed: 2 2 2022
medline: 10 5 2022
entrez: 1 2 2022
Statut: ppublish

Résumé

The gating of the Voltage-Dependent Anion Channel (VDAC) is linked to oxidative stress through increased generation of mitochondrial ROS with increasing mitochondrial membrane potential (ΔΨ

Identifiants

DOI: 10.1007/s00232-022-00215-3 PMID: 35103807
pubmed: 35103807
doi: 10.1007/s00232-022-00215-3
pii: 10.1007/s00232-022-00215-3
doi:

Substances chimiques

Voltage-Dependent Anion Channels 0
Homocysteine 0LVT1QZ0BA
Hydrogen Peroxide BBX060AN9V
homocysteine thiolactone D5H88XF24X

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

79-97

Informations de copyright

© 2022. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.

Références

Álvarez-Maqueda M, El Bekay R, Monteseirín J et al (2004) Homocysteine enhances superoxide anion release and NADPH oxidase assembly by human neutrophils: effects on MAPK activation and neutrophil migration. Atherosclerosis 172:229–238. https://doi.org/10.1016/j.atherosclerosis.2003.11.005
doi: 10.1016/j.atherosclerosis.2003.11.005 pubmed: 15019532
Attie AD, Raines RT (1995) Analysis of receptor-ligand interactions. J Chem Educ 72:119–124. https://doi.org/10.1021/ed072p119
doi: 10.1021/ed072p119 pubmed: 28736457 pmcid: 5521016
Austin RC, Sood SK, Dorward AM et al (1998) Homocysteine-dependent alterations in mitochondrial gene expression, function and structure: homocysteine and H
doi: 10.1074/jbc.273.46.30808 pubmed: 9804859
Avdonin PV, Nadeev AD, Mironova GY et al (2019) Enhancement by hydrogen peroxide of calcium signals in endothelial cells induced by 5-HT1B and 5-HT2B receptor agonists. Oxid Med Cell Longev. https://doi.org/10.1155/2019/1701478
doi: 10.1155/2019/1701478 pubmed: 30886671 pmcid: 6388333
Aykin-Burns N, Ahmad IM, Zhu Y et al (2009) Increased levels of superoxide and H2O2 mediate the differential susceptibility of cancer cells versus normal cells to glucose deprivation. Biochem J 418:29–37. https://doi.org/10.1042/BJ20081258
doi: 10.1042/BJ20081258 pubmed: 18937644
Azoulay-Zohar H, Israelson A, Abu-Hamad S, Shoshan-Barmatz V (2004) In self-defence: hexokinase promotes voltage-dependent anion channel closure and prevents mitochondria-mediated apoptotic cell death. Biochem J 377:347–355. https://doi.org/10.1042/BJ20031465
doi: 10.1042/BJ20031465 pubmed: 14561215 pmcid: 1223882
Banerjee J, Ghosh S (2006) Phosphorylation of rat brain mitochondrial voltage-dependent anion as a potential tool to control leakage of cytochrome c. J Neurochem 98:670–676. https://doi.org/10.1111/j.1471-4159.2006.03853.x
doi: 10.1111/j.1471-4159.2006.03853.x pubmed: 16787424
Banerjee J, Ghosh S (2004) Interaction of mitochondrial voltage-dependent anion channel from rat brain with plasminogen protein leads to partial closure of the channel. Biochim Biophys Acta - Biomembr 1663:6–8. https://doi.org/10.1016/j.bbamem.2004.02.005
doi: 10.1016/j.bbamem.2004.02.005
Báthori G, Csordás G, Garcia-Perez C et al (2006) Ca2+-dependent control of the permeability properties of the mitochondrial outer membrane and voltage-dependent anion-selective channel (VDAC). J Biol Chem 281:17347–17358. https://doi.org/10.1074/jbc.M600906200
doi: 10.1074/jbc.M600906200 pubmed: 16597621
Bayrhuber M, Meins T, Habeck M et al (2008) Structure of the human voltage-dependent anion channel. Proc Natl Acad Sci USA 105:15370–15375. https://doi.org/10.1073/pnas.0808115105
doi: 10.1073/pnas.0808115105 pubmed: 18832158 pmcid: 2557026
Bedard K, Krause KH (2007) The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol Rev 87:245–313
doi: 10.1152/physrev.00044.2005
Bejarano I, Espino J, González-Flores D et al (2009) Role of calcium signals on hydrogen peroxide-induced apoptosis in human myeloid HL-60 cells. Int J Biomed Sci 5:246–256
pubmed: 23675144 pmcid: 3614781
Ben-Hail D, Shoshan-Barmatz V (2014) Purification of VDAC1 from rat liver mitochondria. Cold Spring Harb Protoc 2014:94–99. https://doi.org/10.1101/pdb.prot073130
doi: 10.1101/pdb.prot073130 pubmed: 24371315
Bera AK, Ghosh S (2001) Dual mode of gating of voltage-dependent anion channel as revealed by phosphorylation. J Struct Biol 135:67–72. https://doi.org/10.1006/jsbi.2001.4399
doi: 10.1006/jsbi.2001.4399 pubmed: 11562167
Bharathselvi M, Biswas J, Selvi R et al (2013) Increased homocysteine, homocysteine-thiolactone, protein homocysteinylation and oxidative stress in the circulation of patients with Eales’ disease. Ann Clin Biochem 50:330–338. https://doi.org/10.1177/0004563213492146
doi: 10.1177/0004563213492146 pubmed: 23761385
Brand MD (2016) Mitochondrial generation of superoxide and hydrogen peroxide as the source of mitochondrial redox signaling. Free Radic Biol Med 100:14–31
doi: 10.1016/j.freeradbiomed.2016.04.001
Cankurtaran M, Yesil Y, Kuyumcu ME et al (2013) Altered levels of homocysteine and serum natural antioxidants links oxidative damage to Alzheimer’s disease. J Alzheimer’s Dis 33:1051–1058. https://doi.org/10.3233/JAD-2012-121630
doi: 10.3233/JAD-2012-121630
Castro J, Bittner CX, Humeres A et al (2004) A cytosolic source of calcium unveiled by hydrogen peroxide with relevance for epithelial cell death. Cell Death Differ 11:468–478
doi: 10.1038/sj.cdd.4401372
Checchetto V, Reina S, Magrì A et al (2014) Recombinant human voltage dependent anion selective channel isoform 3 (hVDAC3) forms pores with a very small conductance. Cell Physiol Biochem 34:842–853. https://doi.org/10.1159/000363047
doi: 10.1159/000363047 pubmed: 25171321
Chen WT, Kuo YY, Lin GB et al (2020) Thermal cycling protects SH-SY5Y cells against hydrogen peroxide and β-amyloid-induced cell injury through stress response mechanisms involving Akt pathway. PLoS ONE. https://doi.org/10.1371/journal.pone.0240022
doi: 10.1371/journal.pone.0240022 pubmed: 33382842 pmcid: 7775088
Chwatko G, Boers GHJ, Strauss KA et al (2007) Mutations in methylenetetrahydrofolate reductase or cystathionine β-syntase gene, or a high-methionine diet, increase homocysteine thiolactone levels in humans and mice. FASEB J 21:1707–1713. https://doi.org/10.1096/fj.06-7435com
doi: 10.1096/fj.06-7435com pubmed: 17327360
Clarke R, Smith AD, Jobst KA et al (1998) Folate, vitamin B12, and serum total homocysteine levels in confirmed Alzheimer disease. Arch Neurol 55:1449–1455. https://doi.org/10.1001/archneur.55.11.1449
doi: 10.1001/archneur.55.11.1449 pubmed: 9823829
Colombini M (1979) A candidate for the permeability pathway of the outer mitochondrial membrane [19]. Nature 279:643–645
doi: 10.1038/279643a0
de Pinto V, Prezioso G, Palmieri F (1987) A simple and rapid method for the purification of the mitochondrial porin from mammalian tissues. BBA Biomembr 905:499–502. https://doi.org/10.1016/0005-2736(87)90480-9
doi: 10.1016/0005-2736(87)90480-9
De Pinto V, Reina S, Guarino F, Messina A (2008) Structure of the voltage dependent anion channel: state of the art. J Bioenerg Biomembr 40:139–147. https://doi.org/10.1007/s10863-008-9140-3
doi: 10.1007/s10863-008-9140-3 pubmed: 18668358
De Stefani D, Bononi A, Romagnoli A et al (2012) VDAC1 selectively transfers apoptotic Ca 2 signals to mitochondria. Cell Death Differ 19:267–273. https://doi.org/10.1038/cdd.2011.92
doi: 10.1038/cdd.2011.92 pubmed: 21720385
DeHart DN, Fang D, Heslop K et al (2018) Opening of voltage dependent anion channels promotes reactive oxygen species generation, mitochondrial dysfunction and cell death in cancer cells. Biochem Pharmacol 148:155–162. https://doi.org/10.1016/j.bcp.2017.12.022
doi: 10.1016/j.bcp.2017.12.022 pubmed: 29289511
Del Río LA, López-Huertas E (2016) ROS generation in peroxisomes and its role in cell signaling. Plant Cell Physiol 57:1364–1376
pubmed: 27081099
Dröge W (2002) Free radicals in the physiological control of cell function. Physiol Rev 82:47–95
doi: 10.1152/physrev.00018.2001
Dubey AK, Godbole A, Mathew MK (2016) Regulation of VDAC trafficking modulates cell death. Cell Death Discov. https://doi.org/10.1038/cddiscovery.2016.85
doi: 10.1038/cddiscovery.2016.85 pubmed: 28028442 pmcid: 5149589
Eskes R, Desagher S, Antonsson B, Martinou J-C (2000) Bid Induces the oligomerization and insertion of bax into the outer mitochondrial membrane. Mol Cell Biol 20:929–935. https://doi.org/10.1128/mcb.20.3.929-935.2000
doi: 10.1128/mcb.20.3.929-935.2000 pubmed: 10629050 pmcid: 85210
Fiek C, Benz R, Roos N, Brdiczka D (1982) Evidence for identity between the hexokinase-binding protein and the mitochondrial porin in the outer membrane of rat liver mitochondria. BBA - Biomembr 688:429–440. https://doi.org/10.1016/0005-2736(82)90354-6
doi: 10.1016/0005-2736(82)90354-6
Forman HJ, Bernardo A, Davies KJA (2016) What is the concentration of hydrogen peroxide in blood and plasma? Arch Biochem Biophys 603:48–53
doi: 10.1016/j.abb.2016.05.005
Gandhi S, Abramov AY (2012) Mechanism of oxidative stress in neurodegeneration. Oxid. Med. Cell. Longev.
Gesztelyi R, Zsuga J, Kemeny-Beke A et al (2012) The Hill equation and the origin of quantitative pharmacology. Arch Hist Exact Sci 66:427–438
doi: 10.1007/s00407-012-0098-5
Gincel D, Shoshan-Barmatz V (2004) Glutamate interacts with VDAC and modulates opening of the mitochondrial permeability transition pore. J Bioenerg Biomembr 36:179–186. https://doi.org/10.1023/B:JOBB.0000023621.72873.9e
doi: 10.1023/B:JOBB.0000023621.72873.9e pubmed: 15224967
Gincel D, Zaid H, SHOSHAN-BARMATZ V, (2001) Calcium binding and translocation by the voltage-dependent anion channel: a possible regulatory mechanism in mitochondrial function. Biochem J 358:147–155. https://doi.org/10.1042/bj3580147
doi: 10.1042/bj3580147 pubmed: 11485562 pmcid: 1222042
Gonz A, Granados P, Pariente A (2005) H
doi: 10.1007/s11010-005-3457-6
Gupta R, Ghosh S (2017a) JNK3 phosphorylates Bax protein and induces ability to form pore on bilayer lipid membrane. Biochim Open 4:41–46. https://doi.org/10.1016/j.biopen.2017.02.001
doi: 10.1016/j.biopen.2017.02.001 pubmed: 29450140 pmcid: 5801821
Gupta R, Ghosh S (2017b) Phosphorylation of purified mitochondrial Voltage-Dependent Anion Channel by c-Jun N-terminal Kinase-3 modifies channel voltage-dependence. Biochim Open 4:78–87. https://doi.org/10.1016/j.biopen.2017.03.002
doi: 10.1016/j.biopen.2017.03.002 pubmed: 29450145 pmcid: 5802065
Gupta R, Ghosh S (2015) Phosphorylation of voltage-dependent anion channel by c-Jun N-terminal Kinase-3 leads to closure of the channel. Biochem Biophys Res Commun 459:100–106. https://doi.org/10.1016/j.bbrc.2015.02.077
doi: 10.1016/j.bbrc.2015.02.077 pubmed: 25721670
Gurda D, Handschuh L, Kotkowiak W, Jakubowski H (2015) Homocysteine thiolactone and N-homocysteinylated protein induce pro-atherogenic changes in gene expression in human vascular endothelial cells. Amino Acids 47:1319–1339. https://doi.org/10.1007/s00726-015-1956-7
doi: 10.1007/s00726-015-1956-7 pubmed: 25802182 pmcid: 4458266
Heslop KA, Rovini A, Hunt EG et al (2020) JNK activation and translocation to mitochondria mediates mitochondrial dysfunction and cell death induced by VDAC opening and sorafenib in hepatocarcinoma cells. Biochem Pharmacol. https://doi.org/10.1016/j.bcp.2019.113728
doi: 10.1016/j.bcp.2019.113728 pubmed: 31759978
Hodge T, Colombini M (1997) Regulation of metabolite flux through voltage-gating of VDAC channels. J Membr Biol 157:271–279. https://doi.org/10.1007/s002329900235
doi: 10.1007/s002329900235 pubmed: 9178614
Holmström KM, Finkel T (2014) Cellular mechanisms and physiological consequences of redox-dependent signalling. Nat Rev Mol Cell Biol 15:411–421
doi: 10.1038/nrm3801
Hu Q, Corda S, Zweier JL et al (1998) Hydrogen peroxide induces intracellular calcium oscillations in human aortic endothelial cells. Circulation 97:268–275. https://doi.org/10.1161/01.CIR.97.3.268
doi: 10.1161/01.CIR.97.3.268 pubmed: 9462529
Hu T, Chen K, Hu L et al (2016) H
doi: 10.1038/srep36396 pubmed: 28442790 pmcid: 5180223
Huang RFS, Huang SM, Lin BS et al (2001) Homocysteine thiolactone induces apoptotic DNA damage mediated by increased intracellular hydrogen peroxide and caspase 3 activation in HL-60 cells. Life Sci 68:2799–2811. https://doi.org/10.1016/S0024-3205(01)01066-9
doi: 10.1016/S0024-3205(01)01066-9 pubmed: 11432446
Jakubowski H (1997) Metabolism of homocysteine thiolactone in human cell cultures: possible mechanism for pathological consequences of elevated homocysteine levels. J Biol Chem 272:1935–1942
doi: 10.1016/S0021-9258(19)67504-6
Jakubowski H (2019) Homocysteine modification in protein structure/function and human disease. Physiol Rev 99:555–604. https://doi.org/10.1152/physrev.00003.2018
doi: 10.1152/physrev.00003.2018 pubmed: 30427275
Jakubowski H (2002) The determination of homocysteine-thiolactone in biological samples. Anal Biochem 308:112–119. https://doi.org/10.1016/S0003-2697(02)00224-5
doi: 10.1016/S0003-2697(02)00224-5 pubmed: 12234471
Jakubowski H, Boers GHJ, Strauss KA (2008) Mutations in cystathionine β-synthase or methylenetetrahydrofolate reductase gene increase N -homocysteinylated protein levels in humans. FASEB J 22:4071–4076. https://doi.org/10.1096/fj.08-112086
doi: 10.1096/fj.08-112086 pubmed: 18708589
Kardaras F, Kardara DF (1995) Hyperhomocysteinemia An Independent Risk Factor for Vascular Disease _ Enhanced Reader. Hell J Cardiol 36:275–279
Keinan N, Pahima H, Ben-Hail D, Shoshan-Barmatz V (2013) The role of calcium in VDAC1 oligomerization and mitochondria-mediated apoptosis. Biochim Biophys Acta Mol Cell Res 1833:1745–1754. https://doi.org/10.1016/j.bbamcr.2013.03.017
doi: 10.1016/j.bbamcr.2013.03.017
Keinan N, Tyomkin D, Shoshan-Barmatz V (2010) Oligomerization of the mitochondrial protein voltage-dependent anion channel is coupled to the induction of apoptosis. Mol Cell Biol 30:5698–5709. https://doi.org/10.1128/mcb.00165-10
doi: 10.1128/mcb.00165-10 pubmed: 20937774 pmcid: 3004265
Kl T, N Q, T S, et al (2005) High homocysteine and low B vitamins predict cognitive decline in. Veterans Aff Norm Aging Study Am J Clin Nutr 82:627–635
Korshunov SS, Skulachev VP, Starkov AA (1997) High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria. FEBS Lett 416:15–18. https://doi.org/10.1016/S0014-5793(97)01159-9
doi: 10.1016/S0014-5793(97)01159-9 pubmed: 9369223
Krammer EM, Vu GT, Homblé F, Prévost M (2015) Dual mechanism of ion permeation through VDAC revealed with inorganic phosphate ions and phosphate metabolites. PLoS ONE. https://doi.org/10.1371/journal.pone.0121746
doi: 10.1371/journal.pone.0121746 pubmed: 25951191 pmcid: 4423960
Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685. https://doi.org/10.1038/227680a0
doi: 10.1038/227680a0 pubmed: 5432063
Laskowski RA, Swindells MB (2011) LigPlot+: Multiple ligand-protein interaction diagrams for drug discovery. J Chem Inf Model 51:2778–2786. https://doi.org/10.1021/ci200227u
doi: 10.1021/ci200227u pubmed: 21919503
Lassègue B, San Martín A, Griendling KK (2012) Biochemistry, physiology, and pathophysiology of NADPH oxidases in the cardiovascular system. Circ Res 110:1364–1390
doi: 10.1161/CIRCRESAHA.111.243972
Lee AC, Xu X, Blachly-Dyson E et al (1998a) The role of yeast VDAC genes on the permeability of the mitochondrial outer membrane. J Membr Biol 161:173–181. https://doi.org/10.1007/s002329900324
doi: 10.1007/s002329900324 pubmed: 9435273
Lee S, Tak E, Lee J et al (2011) Mitochondrial H
doi: 10.1038/cr.2011.55 pubmed: 21445095 pmcid: 3203677
Lee SR, Kwont KS, Kim SR, Rhee SG (1998b) Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor. J Biol Chem 273:15366–15372. https://doi.org/10.1074/jbc.273.25.15366
doi: 10.1074/jbc.273.25.15366 pubmed: 9624118
Lehmann M, Gottfries CG, Regland B (1999) Identification of cognitive impairment in the elderly: Homocysteine is an early marker. Dement Geriatr Cogn Disord 10:12–20. https://doi.org/10.1159/000017092
doi: 10.1159/000017092 pubmed: 9844033
Lemasters JJ (2017) Evolution of voltage-dependent anion channel function: From molecular sieve to governator to actuator of ferroptosis. Front Oncol. https://doi.org/10.3389/fonc.2017.00303
doi: 10.3389/fonc.2017.00303 pubmed: 29312890 pmcid: 5743667
Li Q, Duan MJ, Li SS et al (2016) Recognition and binding of voltage-dependent anion channel-1 with ATP and NADH by spectroscopic analysis and molecular docking. RSC Adv 6:13407–13417. https://doi.org/10.1039/c5ra27694b
doi: 10.1039/c5ra27694b
Liou G-Y, Storz P (2010) Reactive oxygen species in cancer. Free Radic Res 44:479–496. https://doi.org/10.3109/10715761003667554
doi: 10.3109/10715761003667554 pubmed: 20370557
Lipper CH, Stofleth JT, Bai F et al (2019) Redox-dependent gating of VDAC by mitoNEET. Proc Natl Acad Sci USA 116:19924–19929. https://doi.org/10.1073/pnas.1908271116
doi: 10.1073/pnas.1908271116 pubmed: 31527235 pmcid: 6778226
Liu HH, Shih TS, Huang HR et al (2013) Plasma homocysteine is associated with increased oxidative stress and antioxidant enzyme activity in welders. Sci World J. https://doi.org/10.1155/2013/370487
doi: 10.1155/2013/370487
Liu N, Li Y, Nan W et al (2020) Interaction of TPPP3 with VDAC1 promotes endothelial injury through activation of reactive oxygen species. Oxid Med Cell Longev. https://doi.org/10.1155/2020/5950195
doi: 10.1155/2020/5950195 pubmed: 33959213 pmcid: 7791970
Lominadze D, Roberts AM, Tyagi N et al (2006) Homocysteine causes cerebrovascular leakage in mice. Am J Physiol - Hear Circ Physiol 290:1206–1213. https://doi.org/10.1152/ajpheart.00376.2005
doi: 10.1152/ajpheart.00376.2005
Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265–275. https://doi.org/10.1016/s0021-9258(19)52451-6
doi: 10.1016/s0021-9258(19)52451-6 pubmed: 14907713
Lu L, Zhang C, Cai Q et al (2013) Voltage-dependent anion channel involved in the -synuclein-induced dopaminergic neuron toxicity in rats. Acta Biochim Biophys Sin (shanghai) 45:170–178. https://doi.org/10.1093/abbs/gms114
doi: 10.1093/abbs/gms114
Ludwig O, De Pinto V, Palmieri F, Benz R (1986) Pore formation by the mitochondrial porin of rat brain in lipid bilayer membranes. BBA - Biomembr 860:268–276. https://doi.org/10.1016/0005-2736(86)90523-7
doi: 10.1016/0005-2736(86)90523-7
Madesh M, Hajnóczky G (2001) VDAC-dependent permeabilization of the outer mitochondrial membrane by superoxide induces rapid and massive cytochrome c release. J Cell Biol 155:1003–1015. https://doi.org/10.1083/jcb.200105057
doi: 10.1083/jcb.200105057 pubmed: 11739410 pmcid: 2150912
Mailloux RJ (2015) Teaching the fundamentals of electron transfer reactions in mitochondria and the production and detection of reactive oxygen species. Redox Biol 4:381–398
doi: 10.1016/j.redox.2015.02.001
Majewski N, Nogueira V, Bhaskar P et al (2004) Hexokinase-mitochondria interaction mediated by Akt is required to inhibit apoptosis in the presence or absence of Bax and Bak. Mol Cell 16:819–830. https://doi.org/10.1016/j.molcel.2004.11.014
doi: 10.1016/j.molcel.2004.11.014 pubmed: 15574336
Maldonado EN (2017) VDAC-tubulin, an anti-Warburg pro-oxidant switch. Front. Oncol. 7
Malik C, Ghosh S (2020a) Regulation of single-channel conductance of voltage-dependent anion channel by mercuric chloride in a planar lipid bilayer. J Membr Biol 253:357–371. https://doi.org/10.1007/s00232-020-00134-1
doi: 10.1007/s00232-020-00134-1 pubmed: 32748041
Malik C, Ghosh S (2020b) Modulation of the mitochondrial voltage-dependent anion channel (VDAC) by hydrogen peroxide and its recovery by curcumin. Eur Biophys J 49:661–672. https://doi.org/10.1007/s00249-020-01469-2
doi: 10.1007/s00249-020-01469-2 pubmed: 33098437
Malik C, Ghosh S (2020) Quinidine partially blocks mitochondrial voltage-dependent anion channel (VDAC). Eur Biophys J 49:193–205. https://doi.org/10.1007/s00249-020-01426-z
doi: 10.1007/s00249-020-01426-z pubmed: 32152682
Malik C, Siddiqui SI, Ghosh S (2021) Extracellular Signal-Regulated Kinase1 (ERK1)-Mediated Phosphorylation of Voltage-Dependent Anion Channel (VDAC) Suppresses its Conductance. J Membr Biol. https://doi.org/10.1007/s00232-021-00205-x
doi: 10.1007/s00232-021-00205-x pubmed: 34731249
Markwell MAK, Haas SM, Tolbert NE, Bieber LL (1981) Protein determination in membrane and lipoprotein samples: manual and automated procedures. Methods in Enzymology. Academic Press, London, pp 296–303
McCaddon A, Davies G, Hudson P et al (1998) Total serum homocysteine in senile dementia of Alzheimer type. Int J Geriatr Psychiatry 13:235–239. https://doi.org/10.1002/(SICI)1099-1166(199804)13:4%3c235::AID-GPS761%3e3.0.CO;2-8
doi: 10.1002/(SICI)1099-1166(199804)13:4<235::AID-GPS761>3.0.CO;2-8 pubmed: 9646150
Menzel VA, Cassará MC, Benz R et al (2009) Molecular and functional characterization of VDAC2 purified from mammal spermatozoa. Biosci Rep 29:351–362. https://doi.org/10.1042/BSR20080123
doi: 10.1042/BSR20080123 pubmed: 18976238
Mercié P, Garnier O, Lascoste L et al (2000) Homocysteine-thiolactone induces caspase-independent vascular endothelial cell death with apoptotic features. Apoptosis 5:403–411. https://doi.org/10.1023/A:1009652011466
doi: 10.1023/A:1009652011466 pubmed: 11256881
Messina A, Reina S, Guarino F, De Pinto V (2012) VDAC isoforms in mammals. Biochim Biophys Acta - Biomembr 1818:1466–1476. https://doi.org/10.1016/j.bbamem.2011.10.005
doi: 10.1016/j.bbamem.2011.10.005
Milton NGN (2008) Homocysteine inhibits hydrogen peroxide breakdown by catalase. Open Enzym Inhib J 1:34–41. https://doi.org/10.2174/1874940200801010034
doi: 10.2174/1874940200801010034
Morris GM, Ruth H, Lindstrom W et al (2009) Software news and updates AutoDock4 and AutoDockTools4: automated docking with selective receptor flexibility. J Comput Chem 30:2785–2791. https://doi.org/10.1002/jcc.21256
doi: 10.1002/jcc.21256 pubmed: 19399780 pmcid: 2760638
Motulsky HJ, Neubig RR (2010) Analyzing binding data. Curr Protoc Neurosci. https://doi.org/10.1002/0471142301.ns0705s52
doi: 10.1002/0471142301.ns0705s52 pubmed: 20578035
Murphy MP (2009) How mitochondria produce reactive oxygen species. Biochem J 417:1–13
doi: 10.1042/BJ20081386
Nulton-Persson AC, Szweda LI (2001) Modulation of mitochondrial function by hydrogen peroxide. J Biol Chem 276:23357–23361. https://doi.org/10.1074/jbc.M100320200
doi: 10.1074/jbc.M100320200 pubmed: 11283020
Park E, Lee GJ, Choi S et al (2010) The role of glutamate release on voltage-dependent anion channels (VDAC)-mediated apoptosis in an eleven vessel occlusion model in rats. PLoS ONE. https://doi.org/10.1371/journal.pone.0015192
doi: 10.1371/journal.pone.0015192 pubmed: 21209831 pmcid: 3013133
Pervin S, Singh R, Rosenfeld ME et al (1998) Estradiol suppresses MCP-1 expression in vivo: Implications for atherosclerosis. Arterioscler Thromb Vasc Biol 18:1575–1582. https://doi.org/10.1161/01.ATV.18.10.1575
doi: 10.1161/01.ATV.18.10.1575 pubmed: 9763529
Peskin AV, Pace PE, Behring JB et al (2016) Glutathionylation of the active site cysteines of peroxiredoxin 2 and recycling by glutaredoxin. J Biol Chem 291:3053–3062. https://doi.org/10.1074/jbc.M115.692798
doi: 10.1074/jbc.M115.692798 pubmed: 26601956
Queralt-Martín M, Bergdoll L, Teijido O et al (2020) A lower affinity to cytosolic proteins reveals VDAC3 isoform-specific role in mitochondrial biology. J Gen Physiol. https://doi.org/10.1085/JGP.201912501
doi: 10.1085/JGP.201912501 pubmed: 31935282 pmcid: 7062508
Raghavan A, Sheiko T, Graham BH, Craigen WJ (2012) Voltage-dependant anion channels: Novel insights into isoform function through genetic models. Biochim Biophys Acta - Biomembr 1818:1477–1485. https://doi.org/10.1016/j.bbamem.2011.10.019
doi: 10.1016/j.bbamem.2011.10.019
Rašić-Marković A, Stanojlović O, Hrnčić D et al (2009) The activity of erythrocyte and brain Na+/K+ and Mg
doi: 10.1007/s11010-009-0040-6 pubmed: 19224340
Reina S, Palermo V, Guarnera A et al (2010) Swapping of the N-terminus of VDAC1 with VDAC3 restores full activity of the channel and confers anti-aging features to the cell. FEBS Lett 584:2837–2844. https://doi.org/10.1016/j.febslet.2010.04.066
doi: 10.1016/j.febslet.2010.04.066 pubmed: 20434446
Reina S, Pittalà MGG, Guarino F et al (2020) Cysteine Oxidations in Mitochondrial Membrane Proteins: The Case of VDAC Isoforms in Mammals. Front Cell Dev Biol 8:1–15. https://doi.org/10.3389/fcell.2020.00397
doi: 10.3389/fcell.2020.00397
Roos N, Benz R, Brdiczka D (1982) Identification and characterization of the pore-forming protein in the outer membrane of rat liver mitochondria
Rosenquist TH, Ratashak SA, Selhub J (1996) Homocysteine induces congenital defects of the heart and neural tube: Effect of folic acid. Proc Natl Acad Sci USA 93:15227–15232. https://doi.org/10.1073/pnas.93.26.15227
doi: 10.1073/pnas.93.26.15227 pubmed: 8986792 pmcid: 26385
Rostovtseva T, Colombini M (1997) Vdac channels mediate and gate the flow of ATP: implications for the regulation of mitochondrial function. Biophys J 72:1954–1962. https://doi.org/10.1016/S0006-3495(97)78841-6
doi: 10.1016/S0006-3495(97)78841-6 pubmed: 9129800 pmcid: 1184392
Roybal CN, Yang S, Sun CW et al (2004) Homocysteine increases the expression of vascular endothelial growth factor by a mechanism involving endoplasmic reticulum stress and transcription factor ATF4. J Biol Chem 279:14844–14852. https://doi.org/10.1074/jbc.M312948200
doi: 10.1074/jbc.M312948200 pubmed: 14747470
Saletti R, Reina S, Pittalà MGG et al (2018) Post-translational modifications of VDAC1 and VDAC2 cysteines from rat liver mitochondria. Biochim Biophys Acta - Bioenergy 1859:806–816. https://doi.org/10.1016/j.bbabio.2018.06.007
doi: 10.1016/j.bbabio.2018.06.007
Schein SJ, Colombini M, Finkelstein A (1976) Reconstitution in planar lipid bilayers of a voltage-dependent anion-selective channel obtained from paramecium mitochondria. J Membr Biol 30:99–120. https://doi.org/10.1007/BF01869662
doi: 10.1007/BF01869662 pubmed: 1011248
Sen U, Basu P, Abe OA et al (2009) Hydrogen sulfide ameliorates hyperhomocysteinemia-associated chronic renal failure. Am J Physiol - Ren Physiol 297:410–419. https://doi.org/10.1152/ajprenal.00145.2009
doi: 10.1152/ajprenal.00145.2009
Shoshan-Barmatz V, De S, Meir A (2017) The mitochondrial voltage-dependent anion channel 1, Ca2+ transport, apoptosis, and their regulation. Front Oncol. https://doi.org/10.3389/fonc.2017.00060
doi: 10.3389/fonc.2017.00060 pubmed: 29312890 pmcid: 5743667
Shrivastava R, Ghosh S (2021) Collective dynamics of ion channels on bilayer lipid membranes. ACS Omega 6:7544–7557. https://doi.org/10.1021/acsomega.°C06061
doi: 10.1021/acsomega.°C06061 pubmed: 33778266 pmcid: 7992176
Sies H (2017) Hydrogen peroxide as a central redox signaling molecule in physiological oxidative stress: oxidative eustress. Redox Biol 11:613–619
doi: 10.1016/j.redox.2016.12.035
Sindrewicz P, Li X, Yates EA et al (2019) Intrinsic tryptophan fluorescence spectroscopy reliably determines galectin-ligand interactions. Sci Rep. https://doi.org/10.1038/s41598-019-47658-8
doi: 10.1038/s41598-019-47658-8 pubmed: 31413267 pmcid: 6694196
Srejovic I, Jakovljevic V, Zivkovic V et al (2015) The effects of the modulation of NMDA receptors by homocysteine thiolactone and dizocilpine on cardiodynamics and oxidative stress in isolated rat heart. Mol Cell Biochem 401:97–105. https://doi.org/10.1007/s11010-014-2296-8
doi: 10.1007/s11010-014-2296-8 pubmed: 25467376
Sun L, Shukair S, Naik TJ et al (2008) Glucose phosphorylation and mitochondrial binding are required for the protective effects of hexokinases I and II. Mol Cell Biol 28:1007–1017. https://doi.org/10.1128/mcb.00224-07
doi: 10.1128/mcb.00224-07 pubmed: 18039843
Tan W, Colombini M (2007) VDAC closure increases calcium ion flux. Biochim Biophys Acta - Biomembr 1768:2510–2515. https://doi.org/10.1016/j.bbamem.2007.06.002
doi: 10.1016/j.bbamem.2007.06.002
Trott O, Olson AJ (2009) AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J Comput Chem NA-NA. https://doi.org/10.1002/jcc.21334
doi: 10.1002/jcc.21334
Tsai MY, Hanson NQ, Bignell MK, Schwichtenberg KA (1996) Simultaneous detection and screening of T833C and G919A mutations of the cystathionine β-synthase gene by single-strand conformational polymorphism. Clin Biochem 29:473–477. https://doi.org/10.1016/0009-9120(96)00045-8
doi: 10.1016/0009-9120(96)00045-8 pubmed: 8884070
Ujwal R, Cascio D, Colletier JP et al (2008) The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating. Proc Natl Acad Sci USA 105:17742–17747. https://doi.org/10.1073/pnas.0809634105
doi: 10.1073/pnas.0809634105 pubmed: 18988731 pmcid: 2584669
Villinger S, Giller K, Bayrhuber M et al (2014) Nucleotide interactions of the human voltage-dependent anion channel. J Biol Chem 289:13397–13406. https://doi.org/10.1074/jbc.M113.524173
doi: 10.1074/jbc.M113.524173 pubmed: 24668813 pmcid: 4036348
Wang L, Jhee KH, Hua X et al (2004) Modulation of cystathionine β-synthase level regulates total serum homocysteine in mice. Circ Res 94:1318–1324. https://doi.org/10.1161/01.RES.0000129182.46440.4a
doi: 10.1161/01.RES.0000129182.46440.4a pubmed: 15105297
Xu X, Decker W, Sampson MJ et al (1999) Mouse VDAC isoforms expressed in yeast: channel properties and their roles in mitochondrial outer membrane permeability. J Membr Biol 170:89–102. https://doi.org/10.1007/s002329900540
doi: 10.1007/s002329900540 pubmed: 10430654
Yamamoto T, Yamada A, Watanabe M et al (2006) VDAC1, having a shorter N-terminus than VDAC2 but showing the same migration in an SDS-polyacrylamide gel, is the predominant form expressed in mitochondria of various tissues. J Proteome Res 5:3336–3344. https://doi.org/10.1021/pr060291w
doi: 10.1021/pr060291w pubmed: 17137335
Yehezkel G, Hadad N, Zaid H et al (2006) Nucleotide-binding sites in the voltage-dependent anion channel: characterization and localization. J Biol Chem 281:5938–5946. https://doi.org/10.1074/jbc.M510104200
doi: 10.1074/jbc.M510104200 pubmed: 16354668
Zhuo J-M, Portugal SG, Kruger DW et al (2010) Diet-induced hyperhomocysteinemia increases amyloid-β formation and deposition in a mouse model of Alzheimers disease. Curr Alzheimer Res 7:140–149
doi: 10.2174/156720510790691326
Zivkovic V, Jakovljevic V, Pechanova O et al (2013) Effects of DL-homocysteine thiolactone on cardiac contractility, coronary flow, and oxidative stress markers in the isolated rat heart: The role of different gasotransmitters. Biomed Res Int. https://doi.org/10.1155/2013/318471
doi: 10.1155/2013/318471 pubmed: 24350259 pmcid: 3857920
Zizi M, Forte M, Blachly-Dyson E, Colombini M (1994) NADH regulates the gating of VDAC, the mitochondrial outer membrane channel. J Biol Chem 269:1614–1616. https://doi.org/10.1016/s0021-9258(17)42070-9
doi: 10.1016/s0021-9258(17)42070-9 pubmed: 7507479

Auteurs

T Daniel Tuikhang Koren (TDT)

Department of Biophysics, University of Delhi South Campus, New Delhi, 110021, India.
ORCID: 0000-0002-8579-4502

Subhendu Ghosh (S)

Department of Biophysics, University of Delhi South Campus, New Delhi, 110021, India. subho@south.du.ac.in.
ORCID: 0000-0002-2070-8634

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Classifications MeSH

questionsmedicales.fr › Eucaryotes › Animaux › Homocysteine-Thiolactone Modulates Gating of...
questionsmedicales.fr › Acides aminés, peptides et protéines › Acides aminés › Acides aminés soufrés › Homocystéine › Homocysteine-Thiolactone Modulates Gating of...
questionsmedicales.fr › Composés chimiques organiques › Radicaux libres › Peroxydes › Peroxyde d'hydrogène › Homocysteine-Thiolactone Modulates Gating of...
questionsmedicales.fr › Cellules › Structures cellulaires › Fractions subcellulaires › Mitochondries › Homocysteine-Thiolactone Modulates Gating of...
questionsmedicales.fr › Phénomènes physiologiques › Stress physiologique › Stress oxydatif › Homocysteine-Thiolactone Modulates Gating of...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Rodentia › Muridae › Murinae › Rats › Homocysteine-Thiolactone Modulates Gating of...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines membranaires › Protéines de transport membranaire › Canaux ioniques › Porines › Canaux anioniques voltage-dépendants › Homocysteine-Thiolactone Modulates Gating of...