dc.contributor.author | Gerszon, Joanna | |
dc.contributor.author | Rodacka, Aleksandra | |
dc.contributor.author | Serafin, Eligiusz | |
dc.contributor.author | Buczkowski, Adam | |
dc.contributor.author | Michlewska, Sylwia | |
dc.contributor.author | Bielnicki, Antoni | |
dc.contributor.editor | Permyakov, Eugene A. | |
dc.date.accessioned | 2021-10-15T08:09:24Z | |
dc.date.available | 2021-10-15T08:09:24Z | |
dc.date.issued | 2018 | |
dc.identifier.citation | Gerszon J, Serafin E, Buczkowski A, Michlewska S, Bielnicki JA, Rodacka A (2018) Functional consequences of piceatannol binding to glyceraldehyde-3-phosphate dehydrogenase. PLoS ONE 13(1): e0190656. https://doi.org/10.1371/ journal.pone.0190656 | pl_PL |
dc.identifier.issn | 1932-6203 | |
dc.identifier.uri | http://hdl.handle.net/11089/39392 | |
dc.description.abstract | Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is one of the key redox-sensitive proteins whose activity is largely affected by oxidative modifications at its highly reactive cysteine residue in the enzyme’s active site (Cys149). Prolonged exposure to oxidative stress may cause, inter alia, the formation of intermolecular disulfide bonds leading to accumulation of GAPDH aggregates and ultimately to cell death. Recently these anomalies have been linked with the pathogenesis of Alzheimer’s disease. Novel evidences indicate that low molecular compounds may be effective inhibitors potentially preventing the GAPDH translocation to the nucleus, and inhibiting or slowing down its aggregation and oligomerization. Therefore, we decided to establish the ability of naturally occurring compound, piceatannol, to interact with GAPDH and to reveal its effect on functional properties and selected parameters of the dehydrogenase structure. The obtained data revealed that piceatannol binds to GAPDH. The ITC analysis indicated that one molecule of the tetrameric enzyme may bind up to 8 molecules of polyphenol (7.3 ± 0.9). Potential binding sites of piceatannol to the GAPDH molecule were analyzed using the Ligand Fit algorithm. Conducted analysis detected 11 ligand binding positions. We indicated that piceatannol decreases GAPDH activity. Detailed analysis allowed us to presume that this effect is due to piceatannol ability to assemble a covalent binding with nucleophilic cysteine residue (Cys149) which is directly involved in the catalytic reaction. Consequently, our studies strongly indicate that piceatannol would be an exceptional inhibitor thanks to its ability to break the aforementioned pathologic disulfide linkage, and therefore to inhibit GAPDH aggregation. We demonstrated that by binding with GAPDH piceatannol blocks cysteine residue and counteracts its oxidative modifications, that induce oligomerization and GAPDH aggregation. | pl_PL |
dc.description.sponsorship | This work is supported by a grant from the Faculty of Biology and Environmental Protection, University of Lodz (grant number: B1711000001504.02) and by National Science Centre, Poland (grant number 2017/25/N/NZ1/02849) and supported by subsidy for young scientists (Faculty of Biology and Environmental Protection, University of Lodz). Bionanopark Ltd. is a non-profit research institution providing employment for two of the authors [JG, JAB], whose facilities were used for part of the conducted studies. The funder provided support in the form of research materials, but did not have any additional role in the study design, data collection and analysis, decision to publish, or preparation of the manuscript. | pl_PL |
dc.language.iso | en | pl_PL |
dc.publisher | Public Library of Science | pl_PL |
dc.relation.ispartofseries | PLoS ONE;13(1) | |
dc.rights | Uznanie autorstwa 4.0 Międzynarodowe | * |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | * |
dc.subject | enzymes | pl_PL |
dc.subject | binding analysis | pl_PL |
dc.subject | transmission electron microscop | pl_PL |
dc.subject | thiols | pl_PL |
dc.subject | cysteine | pl_PL |
dc.subject | isothermal titration calorimetry | pl_PL |
dc.subject | oxidation | pl_PL |
dc.subject | Alzheimer's disease | pl_PL |
dc.title | Functional consequences of piceatannol binding to glyceraldehyde-3-phosphate dehydrogenase | pl_PL |
dc.type | Article | pl_PL |
dc.page.number | 18 | pl_PL |
dc.contributor.authorAffiliation | Department of Molecular Biophysics, Faculty of Biology and Environmental Protection, University of Lodz, Lodz, Poland | pl_PL |
dc.contributor.authorAffiliation | Department of Molecular Biophysics, Faculty of Biology and Environmental Protection, University of Lodz, Lodz, Poland | pl_PL |
dc.contributor.authorAffiliation | Bionanopark Ltd., Lodz, Poland | pl_PL |
dc.contributor.authorAffiliation | Unit of Biophysical Chemistry, Department of Physical Chemistry, Faculty of Chemistry, University of Lodz, Lodz, Poland | pl_PL |
dc.contributor.authorAffiliation | Laboratory of Computer and Analytical Techniques, Faculty of Biology and Environmental Protection, University of Lodz, Lodz, Poland | pl_PL |
dc.contributor.authorAffiliation | Department of General Biophysics, Faculty of Biology and Environmental Protection, University of Lodz, Lodz, Poland | pl_PL |
dc.contributor.authorAffiliation | Laboratory of Microscopic Imaging and Specialized Biological Techniques, Faculty of Biology and Environmental Protection, University of Lodz, Lodz, Poland | pl_PL |
dc.contributor.authorAffiliation | Bionanopark Ltd., Lodz, Poland | pl_PL |
dc.references | Kadmiri N El, Slassi I, Moutawakil B El, Nadifi S, Tadevosyan A, Hachem A, et al. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and Alzheimer’s disease. Pathol Biol. 2014; 62(6):333–6. pmid:25246025 | pl_PL |
dc.references | Sirover M. Structural analysis of glyceraldehyde-3-phosphate dehydrogenase functional diversity. Int J Biochem Cell Biol. 2014; 1–7. | pl_PL |
dc.references | Butterfield D Allan, Hardas S Sarita, Bader Lange ML. Oxidatively Modified Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) and Alzheimer Disease: Many Pathways to Neurodegeneration. J Alzheimers Dis. 2010; 20(2):369–93. pmid:20164570 | pl_PL |
dc.references | Hildebrandt T, Knuesting J, Berndt C, Morgan B. Cytosolic thiol switches regulating basic cellular functions: GAPDH as an information hub? Biol. Chem. 2015; 396(5):523–37. pmid:25581756 | pl_PL |
dc.references | Tristan C, Shahani N, Sedlak TW, Sawa A. The diverse functions of GAPDH: Views from different subcellular compartments. Cell Signal 2011; 23(2):317–23. pmid:20727968 | pl_PL |
dc.references | Kowalczyk A, Serafin E, Puchała M. Inactivation of chosen dehydrogenases by the products of water radiolysis and secondary albumin and haemoglobin radicals. Int J Radiat Biol. 2008; 1;84(1):15–22. pmid:17852555 | pl_PL |
dc.references | Rahmanto AS, Morgan PE, Hawkins CL, Davies MJ. Cellular effects of peptide and protein hydroperoxides. Free Radic Biol Med. 2010; 48(8):1071–8. pmid:20109544 | pl_PL |
dc.references | Rodacka A, Strumillo J, Serafin E, Puchala M. Analysis of Potential Binding Sites of 3,5,4′-Trihydroxystilbene (Resveratrol) and trans-3,3′,5,5′-Tetrahydroxy-4′-methoxystilbene (THMS) to the GAPDH Molecule Using a Computational Ligand- Docking Method: Structural and Functional Changes in GAPDH Induce. J Phys Chem B. 2015; 119(30): 9592–600. pmid:26112149 | pl_PL |
dc.references | Rodacka A, Gerszon J, Puchala M, Bartosz G. Radiation-induced inactivation of enzymes–Molecular mechanism based on inactivation of dehydrogenases. Radiat Phys Chem. 2016; 128:112–7. | pl_PL |
dc.references | Rodacka A, Serafin E, Puchala M. Efficiency of superoxide anions in the inactivation of selected dehydrogenases. Radiat Phys Chem. 2010; 79(9):960–5. | pl_PL |
dc.references | Nakajima H, Amano W, Fujita A, Fukuhara A, Azuma Y, Hata F, et al. The Active Site Cysteine of the Proapoptotic Protein Glyceraldehyde-3-phosphate Dehydrogenase Is Essential in Oxidative Stress-induced Aggregation and Cell Death. J Biol Chem. 2007; 282(36):26562–74. pmid:17613523 | pl_PL |
dc.references | Nakajima H, Amano W, Kubo T, Fukuhara A, Ihara H, Azuma Y, et al. Glyceraldehyde-3-phosphate Dehydrogenase Aggregate Formation Participates in Oxidative Stress-induced Cell Death. J Biol Chem. 2009; 284(49):34331–41. pmid:19837666 | pl_PL |
dc.references | Itakura M, Nakajima H, Kubo T, Semi Y, Kume S, Higashida S et al. Glyceraldehyde-3-phosphate Dehydrogenase Aggregates Accelerate Amyloid-β Amyloidogenesis in Alzheimer Disease. J Biol Chem. 2015; 290(43):26072–87. pmid:26359500 | pl_PL |
dc.references | Kubo T, Nakajima H, Nakatsuji M, Itakura M, Kaneshige A, Azuma Y, et al. Active site cysteine-null glyceraldehyde-3-phosphate dehydrogenase (GAPDH) rescues nitric oxide-induced cell death. Nitric Oxide. 2016; 53:13–21. pmid:26725192 | pl_PL |
dc.references | Lazarev VF, Nikotina AD, Semenyuk PI, Evstafyeva DB, Mikhaylova ER, Muronetz VI, et al. Small molecules preventing GAPDH aggregation are therapeutically applicable in cell and rat models of oxidative stress. Free Radic Biol ed. 2016; 92:29–38. | pl_PL |
dc.references | Gerszon J, Rodacka A, Puchała M. Antioxidant Properties of Resveratrol and its Protective Effects in Neurodegenerative Diseases. Adv Cell Biol. 2014; 4(2):97–117. | pl_PL |
dc.references | Gerszon J, Walczak A, Rodacka A. Attenuation of H2O2 -induced neuronal cell damage by piceatannol. J Funct Foods. 2017; 35:540–8. | pl_PL |
dc.references | Basli A, Soulet S, Chaher N, Merillon JM, Chibane M, Monti JP, et al. Wine polyphenols: Potential agents in neuroprotection. Oxid Med Cell Longev. 2012; 2012: 805762. pmid:22829964 | pl_PL |
dc.references | Son Y, Byun SJ, Pae HO. Involvement of heme oxygenase-1 expression in neuroprotection by piceatannol, a natural analog and a metabolite of resveratrol, against glutamate-mediated oxidative injury in HT22 neuronal cells. Amino Acids. 2013; 45(2):393–401. pmid:23712764 | pl_PL |
dc.references | Narita K, Hisamoto M, Okuda T, Takeda S, Mykytyn K. Differential Neuroprotective Activity of Two Different Grape Seed Extracts. PLoS One 2011; 6(1): e14575. pmid:21283677 | pl_PL |
dc.references | Cordova-Gomez M, Galano A, Alvarez-Idaboy JR, Perron NR, Brumaghim JL, Aggarwal BB, et al. Piceatannol, a better peroxyl radical scavenger than resveratrol. RSC Adv. 2013; 3(43): 20209–218. | pl_PL |
dc.references | Gertz M, Nguyen GTT, Fischer F, Suenkel B, Schlicker C, Fränzel B, et al. A Molecular Mechanism for Direct Sirtuin Activation by Resveratrol. PLoS One. 2012; 7(11): e49761. pmid:23185430 | pl_PL |
dc.references | Jia Y, Wang N, Liu X. Resveratrol and amyloid-beta: Mechanistic insights. Nutrients. 2017; 9(10):1–13. | pl_PL |
dc.references | Piotrowska H, Kucinska M, Murias M. Biological activity of piceatannol: Leaving the shadow of resveratrol. Mutat. Res. 2012; 750(1):60–82. pmid:22108298 | pl_PL |
dc.references | Gambini J, Inglés M, Olaso G, Abdelaziz KM, Vina J, Borras C. Properties of Resveratrol: In Vitro and In Vivo Studies about Metabolism, Bioavailability, and Biological Effects in Animal Models and Humans. Oxid Med Cell Longev. 2015; 2015:837042. 27. pmid:26221416 | pl_PL |
dc.references | Rhayem Y, Thérond P, Camont L, Couturier M, Beaudeux JL, Legrand A, et al. Chain-breaking activity of resveratrol and piceatannol in a linoleate micellar model. Chem Phys Lipids. 2008; 155(1):48–56. pmid:18590713 | pl_PL |
dc.references | Camont L, Cottart CH, Rhayem Y, Nivet-Antoine V, Djelidi R, Collin F, et al. Simple spectrophotometric assessment of the trans-/cis-resveratrol ratio in aqueous solutions. Anal Chim Acta. 2009; 634(1):121–8. pmid:19154820 | pl_PL |
dc.references | Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, et al. UCSF Chimera—A visualization system for exploratory research and analysis. J Comput Chem. 2004; 25(13):1605–12. pmid:15264254 | pl_PL |
dc.references | Buczkowski A, Urbaniak P, Palecz B. Thermochemical and spectroscopic studies on the supramolecular complex of PAMAM-NH 2 G4 dendrimer and 5-fluorouracil in aqueous solution. Int J Pharm. 2012; 428(1–2):178–82. pmid:22429888 | pl_PL |
dc.references | Pienta NJ. Chemistry: Molecules, Matter, and Change, 4th Edition. J Chem Educ. Division of Chemical Education. 2001; 78(7):883. | pl_PL |
dc.references | Lu Y, Wang AH, Shi P, Zhang H. A theoretical study on the antioxidant activity of piceatannol and isorhapontigenin scavenging nitric oxide and nitrogen dioxide radicals. PLoS One. 2017; 12(1):1–16. | pl_PL |
dc.references | Venkatachalam CM, Jiang X, Oldfield T, Waldman M. LigandFit: A novel method for the shape-directed rapid docking of ligands to protein active sites. J Mol Graph Model. 2003; 21(4):289–307. pmid:12479928 | pl_PL |
dc.references | Wu G, Robertson DH, Brooks CL, Vieth M. Detailed analysis of grid-based molecular docking: A case study of CDOCKER?A CHARMm-based MD docking algorithm. J Comput Chem. 2003; 24(13):1549–62. pmid:12925999 | pl_PL |
dc.references | Talfournier F NC, Mornon J, Guy B. Comparative study of the catalytic domain of phosphorylating glyceraldehyde-3-phosphate dehydrogenases from bacteria and archaea via essential cysteine probes and site-directed mutagenesis. Eur. J. Biochem. 1998; 252, 447–457. pmid:9546660 | pl_PL |
dc.references | Nagradova NK. Study of the Properties of Phosphorylating D Glyceraldehyde 3 phosphate Dehydrogenase. Biochemistry (Mosc). 2001; 66(10):1067–76. | pl_PL |
dc.references | Souza M, Radi R. Glyceraldehyde-3-Phosphate Dehydrogenase Inactivation by Peroxynitrite. Arch Biochem Biophys. 1998; 360(2):187–94. pmid:9851830 | pl_PL |
dc.references | Yang J, Stuart MAC, Kamperman M. Jack of all trades: versatile catechol crosslinking mechanisms. Chem Soc Rev. 2014; 43(2007):8271–98. | pl_PL |
dc.references | Ladiwala ARA, Lin JC, Bale SS, Marcelino-Cruz AM, Bhattacharya M, Dordick JS, et al. Resveratrol selectively remodels soluble oligomers and fibrils of amyloid Aβ into off-pathway conformers. J Biol Chem. 2010; 285(31):24228–37. pmid:20511235 | pl_PL |
dc.references | Hara MR, Agrawal N, Kim SF, Cascio MB, Fujimuro M, Ozeki Y, et al. S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding. Nat Cell Biol. 2005; 7(7):665–74. pmid:15951807 | pl_PL |
dc.references | Bae BI, Hara MR, Cascio MB, Wellington CL, Hayden MR, Ross CA, et al. Mutant Huntingtin: Nuclear translocation and cytotoxicity mediated by GAPDH. Proc Natl Acad Sci. 2006; 103(9):3405–9. pmid:16492755 | pl_PL |
dc.identifier.doi | 10.1371/journal.pone.0190656 | |
dc.discipline | nauki biologiczne | pl_PL |