Assistant Professor, Neurobiology & Anatomy
Andrey Tsvetkov, PhD, is an assistant professor in the department of Neurobiology and Anatomy at McGovern Medical School, the University of Texas Health Science Center at Houston. Dr. Tsvetkov joined the department in 2013 after completing his postdoctoral training with Dr. Steven Finkbeiner at the University of California, the Gladstone Institute of Neurological Disease. He earned a PhD in physiology and biophysics from the University of Illinois at Chicago. Born in the Central Asia, the Republic of Kazakhstan, Dr. Tsvetkov received his master’s in molecular biology from Moscow State University, the Russian Federation. He is a recipient of two awards from the Hereditary Disease Foundation for Huntington disease research. His laboratory and the department of Neurobiology and Anatomy provide a vibrant research environment for interdisciplinary interactions with colleagues at the University of Texas Health Science Center, M.D. Anderson Cancer Center, and other University of Texas institutions.
Molecular Mechanisms of Brain Aging and Neurodegeneration
Areas of Research
Understanding the mechanisms of aging is a problem of paramount importance, both scientifically and socially. Aging is a complex phenomenon, and its mechanisms are poorly understood. Andrey’s laboratory explores different aspects of brain aging and neurodegeneration. We are particularly interested in the molecular mechanisms of successful and unsuccessful brain aging, and in age-associated neurodegenerative Huntington disease. Our long-term goals are to understand how the brain changes during successful and unsuccessful aging and whether these changes can be halted to slow aging and blunt neurodegeneration.
Molecular mechanisms of neuronal autophagy
Transcriptional dysregulation in unsuccessful brain aging
Chemotherapy- and virus-induced brain damage and aging
Development of new microscopy techniques to study neurodegeneration
Left panel: neurons expressing a morphology marker mApple2 (red) and the first exon of mutant huntingtin fused to EGFP (green). The yellow fluorescence labels inclusion bodies formed by mutant huntingtin, and reflects the overlap between red mApple2 and green EGFP. Middle panel: Electron micrograph of striatal neurons undergoing autophagy. Note the two mitochondria engulfed by an autophagosome. Right panel: cultured striatal neurons stained with antibodies against MAP2 (red), DARPP-32 (green), and a nuclear Hoechst stain (blue).
Moruno Manchon JF, Uzor N-E, Dabaghian Y, Furr-Stimming EE, Finkbeiner S, Tsvetkov AS. (2015) Cytoplasmic sphingosine-1-phosphate pathway modulates neuronal autophagy. Sci Rep. 5, 15213; doi: 10.1038/srep15213.
- Barmada SJ, Serio A, Arjun A, Bilican B, Daub A, Ando DM, Tsvetkov A, Pleiss M, Li X, Peisach D, Shaw C, Chandran S, Finkbeiner S. (2014) Autophagy induction enhances TDP43 turnover and survival in neuronal ALS models. Nat Chem Biol. 10(8):677-85.
- Tsvetkov AS, Arrasate M, Barmada S, Ando DM, Sharma P, Shaby BA, Finkbeiner S. (2013) Proteostasis of polyglutamine varies among neurons and predicts neurodegeneration. Nat Chem Biol. 9(9):586-92.
- Tsvetkov AS, Ando DM, Finkbeiner S. (2013) Longitudinal imaging of neurons expressing polyQ-expanded proteins. Methods Mol Biol. 1017:1-20.
- Aron R, Tsvetkov A, Finkbeiner S. (2013) NUB1 snubs huntingtin toxicity. Nat Neurosci. 16(5):523-5.
- Tsvetkov AS, Miller J, Arrasate M, Wong JS, Pleiss MA, Finkbeiner S. (2010) A small-molecule scaffold induces autophagy in primary neurons and protects against toxicity in a Huntington disease model. Proc Natl Acad Sci USA. 107(39):16982-7.
- Mitra S, Tsvetkov AS, Finkbeiner S. (2009) Protein turnover and inclusion body formation. Autophagy.5: 1037–1038.
- Montie H, Cho M, Holder L, Tsvetkov AS, Finkbeiner S, Merry DE. (2009) Cytoplasmic retention of polyglutamine-expanded androgen receptor ameliorates disease via autophagy in a mouse model of spinal and bulbar muscular atrophy. Hum Mol Genet. 18(11):1937-50.
- Mitra S, Tsvetkov AS, Finkbeiner S. (2009) Single-neuron ubiquitin-proteasome dynamics accompanying inclusion body formation in Huntington’s disease. J Biol Chem. 284(7):4398-403.