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Valentin Yakubenko, Ph.D.
Department of Biomedical Sciences
PO Box 70577
Carl A Jones Hall (VA Bldg. 1),
Office 1-31/ lab 130
James H. Quillen College of Medicine
East Tennessee State University
Johnson City, TN 37614
Phone: (423) 439-8511
Education and Professional Background:
Dr. Yakubenko received Ph.D. in biochemistry in the National Academy of Science of Ukraine. He obtained a post-doctoral training in cell and molecular biology in the Lerner Research Institute at the Cleveland Clinic. He was a research faculty in the Cleveland Clinic before joining ETSU in 2015.
My laboratory has been focused on studying the structural and functional properties of leukocyte integrins. Integrins are cell surface signaling receptors, which are involved in cell adhesion and migration during different physiological and pathological conditions. Particularly, we are interested in the mechanism of integrin-mediated recruitment and accumulation of macrophages during chronic inflammatory diseases such as atherosclerosis, diabetes and obesity. There are several major directions in our research:
- To characterize the integrin-ligand interactions and to identify integrin ligand binding motifs.
- To evaluate a mechanism of integrin-mediated cell adhesion and migration.
- To understand the role of integrins in pathophysiological processes, particularly in chronic inflammation during cardiovascular diseases and metabolic dysfunction.
We used different protein chemistry, cell and molecular biology approaches for our
studies, such as molecular cloning and mutagenesis, real time PCR, expression and
analysis of recombinant proteins, adhesion and migration of transfected cell lines
and primary leukocytes, fluorescent microscopy, mouse models of inflammation atherosclerosis,
Current Research Support:
1. National Institute of Health, NIDDK
1R01 DK102020-01 (Yakubenko) 07/01/2014 - 05/01/2018
Role of 2 integrins in macrophage retention and egress during inflammation.
Total cost: $1,299,702
Role: Principal Investigator
The purpose of this proposal is to test the role of leukocyte migratory receptors, integrins M2 and D2, in the retention and egress of macrophages within the site of chronic inflammation during the development of metabolic syndrome.
2. American Heart Association, Grant-in-Aid
14GRNT20410074 (Yakubenko) 07/01/2014 06/30/2016
The contribution of integrin D2 to the macrophage migration and lipid deposition during atherogenesis.
Total cost: $154,000
Role: Principal Investigator
This project is focused on the determination of the impact of integrin D2 on the development of atherosclerosis, focusing on both components of early atherogenesis macrophage accumulation and lipid deposition.
1. Elsori D, YakubenkoVP, Bhattacharjee A, Cathcart MK. Dectin-1 signaling in primary human monocytes is controlled by protein kinase C . J. Leuk. Biol. 2011 Sep; 90(3):599-611.
2. YakubenkoVP, Bhattacharjee A, Pluskota E, Cathcart MK. M2 integrin activation prevents alternative activation of human and murine macrophages and impedes foam cell formation. Circulation Research, 2011, Mar 4;108(5):544-54.
3. Bhattacharjee A, Shukla M, YakubenkoVP, Mulya A, Kundu S, Cathcart MK. IL-4 and IL-13 employ discrete signaling pathways for target gene expression in alternatively activated monocytes/macrophages. Free Radic Biol Med. 2013 Jan;54:1-16.
4. YakubenkoVP, Hsi LC, Cathcart MK, Bhattacharjee A. From macrophage IL-13 receptor to foam cell
formation: mechanisms for
M2 integrin interference. J Biol Chem. 2013 Jan 5;288(4):2778-88.
5. Kundu S, Roome T, Bhattacharjee A, Carnevale KA, YakubenkoVP, Hammock BD and Cathcart MK. Metabolic products of soluble epoxide hydrolase are essential for monocyte chemotaxis to MCP-1 in vitro and in vivo. J Lipid Res. 2013 Feb;54(2):436-47,
6. Thiagarajan PS, YakubenkoVP, Elsori DH, Yadav SP, Willard B, Tan CD, Rodriguez ER, Febbraio M, Cathcart MK. Vimentin is an endogenous ligand for the pattern recognition receptor Dectin-1. Cardiovasc Res. 2013 Aug 1;99(3):494-504.
7. Podolnikova NP, Yakovlev S, YakubenkoVP, Wang X, Gorkun OV, Ugarova TP. The interaction of integrin IIb3 with fibrin occurs through multiple binding sites in the IIb -propeller domain. J Biol Chem. 2014 Jan 24;289(4):2371-83. PMCID: in progress.
8. Liu J, Das M, Yang J, Ithychanda SS, YakubenkoVP, Plow EF, and Qin J. Structural mechanism of integrin inactivation by filamin. Nature Structural and Molecular Biology 2015 May;22(5):383-9.
9. Kim YW, YakubenkoVP, West XZ, Kutralanathan R, Crabb JW, Gao D., Podrez EA, Salomon RG, Byzova TV. Novel Receptor-mediated Mechanism Controlling Tissue Levels of Bioactive Lipid Oxidation Products. Circulation Research. 2015 Jul 31;117(4):321-32.
Complete list of publications in PubMed: http://www.ncbi.nlm.nih.gov/sites/myncbi/valentin.yakubenko.1/bibliography/48660078/public/?sort=date&direction=ascending