{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,10]],"date-time":"2026-10-10T05:11:45Z","timestamp":1791609105895,"version":"4.3.4"},"reference-count":54,"publisher":"IMR Press","issue":"8","license":[{"start":{"date-parts":[[2021,8,30]],"date-time":"2021-08-30T00:00:00Z","timestamp":1630281600000},"content-version":"unspecified","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Front. Biosci. (Landmark Ed)"],"abstract":"<jats:p>Background: Mitochondrial dysfunction plays a crucial role in Parkinson\u2019s disease (PD) pathogenesis. The present study was undertaken to investigate the effects of Telmisartan (TEL), an angiotensin II type 1 receptor (AT1R) blocker, on the mitochondria-specific genes expression in a mouse model of Parkinsonism. Materials and methods: Mice were divided into 5 groups with 6 in each; Group I received 0.5% CMC (control) + saline, Group II received 0.5% CMC + 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) (positive control), Group III &amp; IV received MPTP + TEL 3 and 10 mg\/kg, p.o. respectively, Group V received TEL 10 mg\/kg, p.o. (drug control). MPTP was given 80 mg\/kg intraperitoneal in two divided doses (40 mg\/kg \u00d7 2 at 16 h time interval). Vehicle or TEL was administered 1 h before the MPTP injection. Motor function was assessed 48 h after the first dose of MPTP and animals were euthanized to collect brain. Results: Mice intoxicated with MPTP showed locomotor deficits and significant upregulation of \u03b1-synuclein (\u03b1-syn), downregulation of metastasis-associated protein 1 (MTA1), and Ubiquitin C-terminal hydrolase L1 (UCHL1) in the substantia nigra pars compacta (SNpc) and Striatum (STr) regions of brains. In addition, MPTP intoxication down-regulated mitochondria-specific genes such as DJ-1, PTEN-induced putative kinase 1 (PINK1), Parkin, enriched with leucine repeats kinase 2 (LRRK2) gene expfression. Pre-treatment with TEL restored locomotor functions and upregulated PINK1, Parkin, LRRK2, DJ-1, MTA1 and UCHL1. Conclusion: The present study evidences that TEL has the ability to improve mitochondrial functions in PD.<\/jats:p>","DOI":"10.52586\/4942","type":"journal-article","created":{"date-parts":[[2021,8,26]],"date-time":"2021-08-26T00:58:25Z","timestamp":1629939505000},"source":"Crossref","is-referenced-by-count":10,"title":["Effects of Telmisartan, an AT1 receptor antagonist, on mitochondria-specific genes expression in a mouse MPTP model of Parkinsonism"],"prefix":"10.31083","volume":"26","author":[{"given":"Bipul","family":"Ray","sequence":"first","affiliation":[{"name":"Department of Pharmacology, JSS College of Pharmacy, JSS Academy of Higher Education & Research, 570015 Mysuru, India"},{"name":"Centre for Experimental Pharmacology and Toxicology, Central Animal Facility, JSS Academy of Higher Education & Research, 570015 Mysuru, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Girish","family":"Ramesh","sequence":"first","affiliation":[{"name":"Molecular Biophysics, Saarland University, 66123 Saarland, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sudhir Rama","family":"Verma","sequence":"first","affiliation":[{"name":"Department of Clinical Sciences, College of Dentistry, Ajman University, 346 Ajman, UAE"},{"name":"Center of Medical and Bio-allied Health Sciences Research, Ajman University, 346 Ajman, UAE"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Srinivasan","family":"Ramamurthy","sequence":"first","affiliation":[{"name":"College of Pharmacy & Health Sciences, University of Science and Technology of Fujairah, 2202 Fujairah, UAE"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sunanda","family":"Tuladhar","sequence":"first","affiliation":[{"name":"Department of Pharmacology, JSS College of Pharmacy, JSS Academy of Higher Education & Research, 570015 Mysuru, India"},{"name":"Centre for Experimental Pharmacology and Toxicology, Central Animal Facility, JSS Academy of Higher Education & Research, 570015 Mysuru, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arehally Marappa","family":"Mahalakshmi","sequence":"first","affiliation":[{"name":"Department of Pharmacology, JSS College of Pharmacy, JSS Academy of Higher Education & Research, 570015 Mysuru, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Musthafa Mohamed","family":"Essa","sequence":"first","affiliation":[{"name":"Department of Food Science and Nutrition, CAMS, Sultan Qaboos University, 123 Muscat, Oman"},{"name":"Aging and Dementia Research Group, Sultan Qaboos University, 123 Muscat, Oman"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Saravana Babu","family":"Chidambaram","sequence":"first","affiliation":[{"name":"Department of Pharmacology, JSS College of Pharmacy, JSS Academy of Higher Education & Research, 570015 Mysuru, India"},{"name":"Centre for Experimental Pharmacology and Toxicology, Central Animal Facility, JSS Academy of Higher Education & Research, 570015 Mysuru, India"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"16242","published-online":{"date-parts":[[2021,8,30]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","unstructured":"Chidambaram SB, Bhat A, Ray B, Sugumar M, Muthukumar SP, Manivasagam T, et al. Cocoa beans improve mitochondrial biogenesis via PPAR\u03b3\/PGC1\u03b1 dependent signalling pathway in MPP+ intoxicated human neuroblastoma cells (SH-SY5Y). Nutritional Neuroscience. 2020; 23: 471\u2013480.","DOI":"10.1080\/1028415X.2018.1521088"},{"key":"ref2","doi-asserted-by":"crossref","unstructured":"Martinez-Vicente M. Neuronal mitophagy in neurodegenerative diseases. Frontiers in Molecular Neuroscience. 2017; 10: 64.","DOI":"10.3389\/fnmol.2017.00064"},{"key":"ref3","doi-asserted-by":"crossref","unstructured":"Schapira AHV, Cooper JM, Dexter D, Jenner P, Clark JB, Marsden CD. Mitochondrial complex I deficiency in parkinson\u2019s disease. The Lancet. 1989; 333: 1269.","DOI":"10.1016\/S0140-6736(89)92366-0"},{"key":"ref4","doi-asserted-by":"crossref","unstructured":"Schapira AH, Cooper JM, Dexter D, Clark JB, Jenner P, Marsden CD. Mitochondrial complex I deficiency in Parkinson\u2019s disease. Journal of Neurochemistry. 1990; 54: 823\u2013827.","DOI":"10.1111\/j.1471-4159.1990.tb02325.x"},{"key":"ref5","doi-asserted-by":"crossref","unstructured":"Vives-Bauza C, Tocilescu M, Devries RLA, Alessi DM, Jackson-Lewis V, Przedborski S. Control of mitochondrial integrity in Parkinson\u2019s disease. Progress in Brain Research. 2010; 183: 99\u2013113.","DOI":"10.1016\/S0079-6123(10)83006-7"},{"key":"ref6","doi-asserted-by":"crossref","unstructured":"Parihar MS, Parihar A, Fujita M, Hashimoto M, Ghafourifar P. Mitochondrial association of alpha-synuclein causes oxidative stress. Cellular and Molecular Life Sciences. 2008; 65: 1272\u20131284.","DOI":"10.1007\/s00018-008-7589-1"},{"key":"ref7","doi-asserted-by":"crossref","unstructured":"Parihar MS, Parihar A, Fujita M, Hashimoto M, Ghafourifar P. Alpha-synuclein overexpression and aggregation exacerbates impairment of mitochondrial functions by augmenting oxidative stress in human neuroblastoma cells. 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Frontiers in Neurology. 2020; 11: 572976.","DOI":"10.3389\/fneur.2020.572976"},{"key":"ref11","unstructured":"Venkateshgobi V, Rajasankar S, Johnson WMS, Prabu K, Ramkumar M. Neuroprotective effect of agaricus blazei extract against rotenone-induced motor and nonmotor symptoms in experimental model of parkinson\u2019s disease. The International Journal of Nutrition, Pharmacology, Neurological Diseases. 2018; 8: 59\u201365."},{"key":"ref12","unstructured":"Labandeira-Garcia JL, Rodriguez-Pallares J, Rodr\u00edguez-Perez AI, Garrido-Gil P, Villar-Cheda B, Valenzuela R, et al. Brain angiotensin and dopaminergic degeneration: relevance to Parkinson\u2019s disease. American Journal of Neurodegenerative Disease. 2012; 1: 226\u2013244."},{"key":"ref13","unstructured":"Labandeira-Garcia JL, Rodriguez-Pallares J, Villar-Cheda B, Rodr\u00edguez-Perez AI, Garrido-Gil P, Guerra MJ. Aging, Angiotensin system and dopaminergic degeneration in the substantia nigra. Aging and Disease. 2011; 2: 257\u2013274."},{"key":"ref14","doi-asserted-by":"crossref","unstructured":"Sathiya S, Ranju V, Kalaivani P, Priya RJ, Sumathy H, Sunil AG, et al. Telmisartan attenuates MPTP induced dopaminergic degeneration and motor dysfunction through regulation of \u03b1-synuclein and neurotrophic factors (BDNF and GDNF) expression in C57BL\/6J mice. Neuropharmacology. 2013; 73: 98\u2013110.","DOI":"10.1016\/j.neuropharm.2013.05.025"},{"key":"ref15","doi-asserted-by":"crossref","unstructured":"Sekar S, Mani S, Rajamani B, Manivasagam T, Thenmozhi AJ, Bhat A, et al. Telmisartan ameliorates astroglial and dopaminergic functions in a mouse model of chronic Parkinsonism. Neurotoxicity Research. 2018; 34: 597\u2013612.","DOI":"10.1007\/s12640-018-9921-3"},{"key":"ref16","doi-asserted-by":"crossref","unstructured":"An J, Nakajima T, Kuba K, Kimura A. Losartan inhibits LPS-induced inflammatory signaling through a PPARgamma-dependent mechanism in human THP-1 macrophages. Hypertension Research. 2010; 33: 831\u2013835.","DOI":"10.1038\/hr.2010.79"},{"key":"ref17","doi-asserted-by":"crossref","unstructured":"Grammatopoulos TN, Jones SM, Ahmadi FA, Hoover BR, Snell LD, Skoch J, et al. Angiotensin type 1 receptor antagonist losartan, reduces MPTP-induced degeneration of dopaminergic neurons in substantia nigra. Molecular Neurodegeneration. 2007; 2: 1.","DOI":"10.1186\/1750-1326-2-1"},{"key":"ref18","doi-asserted-by":"crossref","unstructured":"Moradganjeh A, Ziai SA, Roghani M. Losartan pretreatment reduces neurodegeneration and behavioural symptoms in 6-hydroxydopamine induced unilateral rat model of Parkinson\u2019s disease. Pathophysiology. 2013; 20: 243\u2013248.","DOI":"10.1016\/j.pathophys.2013.10.001"},{"key":"ref19","doi-asserted-by":"crossref","unstructured":"Abadir PM, Foster DB, Crow M, Cooke CA, Rucker JJ, Jain A, et al. Identification and characterization of a functional mitochondrial angiotensin system. Proceedings of the National Academy of Sciences. 2011; 108: 14849\u201314854.","DOI":"10.1073\/pnas.1101507108"},{"key":"ref20","doi-asserted-by":"crossref","unstructured":"Liang Y, Huang M, Jiang X, Liu Q, Chang X, Guo Y. The neuroprotective effects of Berberine against amyloid \u03b2-protein-induced apoptosis in primary cultured hippocampal neurons via mitochondria-related caspase pathway. Neuroscience Letters. 2017; 655: 46\u201353.","DOI":"10.1016\/j.neulet.2017.06.048"},{"key":"ref21","doi-asserted-by":"crossref","unstructured":"Qi H, Shen D, Jiang C, Wang H, Chang M. Ursodeoxycholic acid protects dopaminergic neurons from oxidative stress via regulating mitochondrial function, autophagy, and apoptosis in MPTP\/MPP+-induced Parkinson\u2019s disease. Neuroscience Letters. 2021; 741: 135493.","DOI":"10.1016\/j.neulet.2020.135493"},{"key":"ref22","doi-asserted-by":"crossref","unstructured":"Seydi E, Mehrpouya L, Sadeghi H, Rahimi S, Pourahmad J. Luteolin attenuates Fipronil-induced neurotoxicity through reduction of the ROS-mediated oxidative stress in rat brain mitochondria. Pesticide Biochemistry and Physiology. 2021; 173: 104785.","DOI":"10.1016\/j.pestbp.2021.104785"},{"key":"ref23","doi-asserted-by":"crossref","unstructured":"Yang P, Sheng D, Guo Q, Wang P, Xu S, Qian K, et al. Neuronal mitochondria-targeted micelles relieving oxidative stress for delayed progression of Alzheimer\u2019s disease. Biomaterials. 2020; 238: 119844.","DOI":"10.1016\/j.biomaterials.2020.119844"},{"key":"ref24","doi-asserted-by":"crossref","unstructured":"Luchtman DW, Shao D, Song C. Behavior, neurotransmitters and inflammation in three regimens of the MPTP mouse model of Parkinson\u2019s disease. Physiology & Behavior. 2009; 98: 130\u2013138.","DOI":"10.1016\/j.physbeh.2009.04.021"},{"key":"ref25","unstructured":"Paxinos G, Franklin KBJ. Paxinos and Franklin\u2019s the mouse brain in stereotaxic coordinates. Cambridge: Academic Press. 2019."},{"key":"ref26","doi-asserted-by":"crossref","unstructured":"Mani S, Sekar S, Barathidasan R, Manivasagam T, Thenmozhi AJ, Sevanan M, et al. Naringenin decreases \u03b1-Synuclein expression and neuroinflammation in MPTP-induced Parkinson\u2019s disease model in mice. Neurotoxicity Research. 2018; 33: 656\u2013670.","DOI":"10.1007\/s12640-018-9869-3"},{"key":"ref27","doi-asserted-by":"crossref","unstructured":"Kim ST, Son HJ, Choi JH, Ji IJ, Hwang O. Vertical grid test and modified horizontal grid test are sensitive methods for evaluating motor dysfunctions in the MPTP mouse model of Parkinson\u2019s disease. Brain Research. 2010; 1306: 176\u2013183.","DOI":"10.1016\/j.brainres.2009.09.103"},{"key":"ref28","doi-asserted-by":"crossref","unstructured":"Keeney PM, Xie J, Capaldi RA, Bennett JP. Parkinson\u2019s disease brain mitochondrial complex I has oxidatively damaged subunits and is functionally impaired and misassembled. The Journal of Neuroscience. 2006; 26: 5256\u20135264.","DOI":"10.1523\/JNEUROSCI.0984-06.2006"},{"key":"ref29","doi-asserted-by":"crossref","unstructured":"Schapira AH, Mann VM, Cooper JM, Dexter D, Daniel SE, Jenner P, et al. Anatomic and disease specificity of NADH CoQ1 reductase (complex I) deficiency in Parkinson\u2019s disease. Journal of Neurochemistry. 1990; 55: 2142\u20132145.","DOI":"10.1111\/j.1471-4159.1990.tb05809.x"},{"key":"ref30","doi-asserted-by":"crossref","unstructured":"Valenzuela R, Costa-Besada MA, Iglesias-Gonzalez J, Perez-Costas E, Villar-Cheda B, Garrido-Gil P, et al. Mitochondrial angiotensin receptors in dopaminergic neurons. Role in cell protection and aging-related vulnerability to neurodegeneration. Cell Death & Disease. 2016; 7: e2427.","DOI":"10.1038\/cddis.2016.327"},{"key":"ref31","doi-asserted-by":"crossref","unstructured":"Rodriguez-Pallares J, Rey P, Parga JA, Mu\u00f1oz A, Guerra MJ, Labandeira-Garcia JL. Brain angiotensin enhances dopaminergic cell death via microglial activation and NADPH-derived ROS. Neurobiology of Disease. 2008; 31: 58\u201373.","DOI":"10.1016\/j.nbd.2008.03.003"},{"key":"ref32","unstructured":"Sathiya S, Babu CS. Telmisartan alleviates nitrosative stress in turn dopaminergic degeneration in mice MPTP model of parkinsonism\u2014biochemical and histopathological evidences. International Journal of Pharmacy and Pharmaceutical Sciences. 2015; 7: 97\u2013101."},{"key":"ref33","doi-asserted-by":"crossref","unstructured":"Charan RA, LaVoie MJ. Pathologic and therapeutic implications for the cell biology of parkin. Molecular and Cellular Neurosciences. 2015; 66: 62\u201371.","DOI":"10.1016\/j.mcn.2015.02.008"},{"key":"ref34","doi-asserted-by":"crossref","unstructured":"Dave KD, De Silva S, Sheth NP, Ramboz S, Beck MJ, Quang C, et al. Phenotypic characterization of recessive gene knockout rat models of Parkinson\u2019s disease. Neurobiology of Disease. 2014; 70: 190\u2013203.","DOI":"10.1016\/j.nbd.2014.06.009"},{"key":"ref35","doi-asserted-by":"crossref","unstructured":"Villeneuve LM, Purnell PR, Boska MD, Fox HS. Early expression of Parkinson\u2019s disease-related mitochondrial abnormalities in PINK1 knockout rats. Molecular Neurobiology. 2016; 53: 171\u2013186.","DOI":"10.1007\/s12035-014-8927-y"},{"key":"ref36","doi-asserted-by":"crossref","unstructured":"Narendra D, Tanaka A, Suen D, Youle RJ. Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. The Journal of Cell Biology. 2008; 183: 795\u2013803.","DOI":"10.1083\/jcb.200809125"},{"key":"ref37","doi-asserted-by":"crossref","unstructured":"Wood-Kaczmar A, Gandhi S, Yao Z, Abramov AY, Abramov ASY, Miljan EA, et al. PINK1 is necessary for long term survival and mitochondrial function in human dopaminergic neurons. PLoS ONE. 2008; 3: e2455.","DOI":"10.1371\/journal.pone.0002455"},{"key":"ref38","doi-asserted-by":"crossref","unstructured":"Yu W, Sun Y, Guo S, Lu B. The PINK1\/Parkin pathway regulates mitochondrial dynamics and function in mammalian hippocampal and dopaminergic neurons. Human Molecular Genetics. 2011; 20: 3227\u20133240.","DOI":"10.1093\/hmg\/ddr235"},{"key":"ref39","doi-asserted-by":"crossref","unstructured":"S\u00e1nchez-Dan\u00e9s A, Richaud-Patin Y, Carballo-Carbajal I, Jim\u00e9nez-Delgado S, Caig C, Mora S, et al. Disease-specific phenotypes in dopamine neurons from human iPS-based models of genetic and sporadic Parkinson\u2019s disease. EMBO Molecular Medicine. 2012; 4: 380\u2013395.","DOI":"10.1002\/emmm.201200215"},{"key":"ref40","doi-asserted-by":"crossref","unstructured":"Reinhardt P, Schmid B, Burbulla LF, Sch\u00f6ndorf DC, Wagner L, Glatza M, et al. Genetic correction of a LRRK2 mutation in human iPSCs links parkinsonian neurodegeneration to ERK-dependent changes in gene expression. Cell Stem Cell. 2013; 12: 354\u2013367.","DOI":"10.1016\/j.stem.2013.01.008"},{"key":"ref41","doi-asserted-by":"crossref","unstructured":"Ludtmann MHR, Kostic M, Horne A, Gandhi S, Sekler I, Abramov AY. LRRK2 deficiency induced mitochondrial Ca2+ efflux inhibition can be rescued by Na+\/Ca2+\/Li+ exchanger upregulation. Cell Death & Disease. 2019; 10: 265.","DOI":"10.1038\/s41419-019-1469-5"},{"key":"ref42","doi-asserted-by":"crossref","unstructured":"Toyofuku T, Okamoto Y, Ishikawa T, Sasawatari S, Kumanogoh A. LRRK2 regulates endoplasmic reticulum\u2013mitochondrial tethering through the PERK-mediated ubiquitination pathway. The EMBO Journal. 2020; 39: e100875.","DOI":"10.15252\/embj.2020105826"},{"key":"ref43","doi-asserted-by":"crossref","unstructured":"Agliardi C, Meloni M, Guerini FR, Zanzottera M, Bolognesi E, Baglio F, et al. Oligomeric \u03b1-syn and SNARE complex proteins in peripheral extracellular vesicles of neural origin are biomarkers for Parkinson\u2019s disease. Neurobiology of Disease. 2021; 148: 105185.","DOI":"10.1016\/j.nbd.2020.105185"},{"key":"ref44","doi-asserted-by":"crossref","unstructured":"Volpicelli-Daley LA, Luk KC, Patel TP, Tanik SA, Riddle DM, Stieber A, et al. Exogenous \u03b1-synuclein fibrils induce Lewy body pathology leading to synaptic dysfunction and neuron death. Neuron. 2011; 72: 57\u201371.","DOI":"10.1016\/j.neuron.2011.08.033"},{"key":"ref45","doi-asserted-by":"crossref","unstructured":"Zhang L, Shimoji M, Thomas B, Moore DJ, Yu S, Marupudi NI, et al. Mitochondrial localization of the Parkinson\u2019s disease related protein DJ-1: implications for pathogenesis. Human Molecular Genetics. 2005; 14: 2063\u20132073.","DOI":"10.1093\/hmg\/ddi211"},{"key":"ref46","doi-asserted-by":"crossref","unstructured":"Mitsumoto A, Nakagawa Y. DJ-1 is an indicator for endogenous reactive oxygen species elicited by endotoxin. Free Radical Research. 2002; 35: 885\u2013893.","DOI":"10.1080\/10715760100301381"},{"key":"ref47","doi-asserted-by":"crossref","unstructured":"Shendelman S, Jonason A, Martinat C, Leete T, Abeliovich A. DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-synuclein aggregate formation. PLoS Biology. 2004; 2: e362.","DOI":"10.1371\/journal.pbio.0020362"},{"key":"ref48","doi-asserted-by":"crossref","unstructured":"Xu C, Kang W, Chen Y, Jiang T, Zhang J, Zhang L, et al. DJ-1 Inhibits \u03b1-Synuclein aggregation by regulating chaperone-mediated autophagy. Frontiers in Aging Neuroscience. 2017; 9: 308.","DOI":"10.3389\/fnagi.2017.00308"},{"key":"ref49","doi-asserted-by":"crossref","unstructured":"Cartier AE, Ubhi K, Spencer B, Vazquez-Roque RA, Kosberg KA, Fourgeaud L, et al. Differential effects of UCHL1 modulation on alpha-synuclein in PD-like models of alpha-synucleinopathy. 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Journal of Biological Chemistry. 2016; 291: 12310\u201312321.","DOI":"10.1074\/jbc.M115.707224"},{"key":"ref53","doi-asserted-by":"crossref","unstructured":"Lev N, Barhum Y, Pilosof NS, Ickowicz D, Cohen HY, Melamed E, et al. DJ-1 protects against dopamine toxicity: implications for Parkinson\u2019s disease and aging. The Journals of Gerontology: Series A, Biological Sciences and Medical Sciences. 2013; 68: 215\u2013225.","DOI":"10.1093\/gerona\/gls147"},{"key":"ref54","doi-asserted-by":"crossref","unstructured":"Mita Y, Kataoka Y, Saito Y, Kashi T, Hayashi K, Iwasaki A, et al. Distribution of oxidized DJ-1 in Parkinson\u2019s disease-related sites in the brain and in the peripheral tissues: effects of aging and a neurotoxin. 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