Konstantin Kandror

Professor of Biochemistry


Ph.D., Bakh Institute of Biochemistry, Moscow, Russia

General field of research:

Insulin action; Glucose transport

Affiliations other than medicine:

Evans Center for Interdisciplinary Biomedical Research

Contact information:

715 Albany Street, K124
Phone: (617)-638 5049

715 Albany Street, K124
Phone: (617)-638 5308
Fax: (617)-638 5049



Insulin; Glut4; Adipocytes; mTOR; Leptin; Lipolysis

Summary of research interest:

Diabetes mellitus represents one of the major health threats to modern civilization, and its worldwide prevalence is increasing at an alarming rate. In diabetes, insulin cannot stimulate glucose entry into the cell, as it does in normal individuals. As a result, extra glucose stays in the blood and causes multiple health problems. As insulin-regulated glucose transport is the major molecular defect in diabetes, it represents the main focus of our lab. Insulin activates glucose uptake by translocating glucose transporter isoform 4 (Glut4) from its intracellular vesicular storage pool to the plasma membrane. This process, along with exocytosis of synaptic vesicles in neurons, insulin-containing granules in the pancreas, water channel-containing vesicles in the kidney, etc., represents an example of a widely spread type of the biological regulation via regulated exocytosis. Impaired translocation of Glut4-containing vesicles in diabetes may have two explanations. First, the molecular defect may lie in the signal transduction pathway that connects the insulin receptor in the plasma membrane and intracellular Glut4-vesicles. Second, the cell biology (i.e. the protein composition, biogenesis, intracellular trafficking) of Glut4-vesicles may be impaired. Our lab pursues both these directions using the wide arsenal of modern techniques that include molecular biological methods, protein biochemistry, subcellular fractionation, microscopy and in vivo studies.

Recent publications:

Shi, J., Huang, G., and Kandror, K.V.  2008.  Self-assembly of Glut4-storage vesicles in differentiating 3T3-L1 adipocytes.  J.Biol.Chem.; v. 283, #44, 30311-30321.

Chakrabarti, P., Anno, T., Manning B.D., Luo, Z., and Kandror, K.V.  2008.  The mTOR complex 1 regulates leptin biosynthesis in adipocytes at the level of translation.  The role of the 5’-UTR in the expression of leptin mRNA. Mol.Endocrinology; v. 22, #10, 2260-2267.

Li, L.V., Bakirtzi, K., Watson, R., Pessin, J.E., and Kandror, K.V.  2009.  The C-terminus of Glut4 targets the transporter to the perinuclear compartment but not to the insulin-responsive vesicles. Biochem. J.; v.419, #1, 105-112.

Bakirtzi, K., Belfort, G., Lopez-Coviella, I., Kuruppu, D., Cao, L., Abel, E.D., Brownell, A.-D., and Kandror, K.V.  2009.  Cerebellar neurons possess a vesicular compartment structurally and functionally similar to Glut4-storage vesicles from peripheral insulin-sensitive tissues.  J. Neurosci.; v. 29, #16, 5193-5201.

Chakrabarti, P., and Kandror, K.V. 2009.  FoxO1 controls insulin-dependent ATGL expression and lipolysis in adipocytes.  J.Biol.Chem.; v. 284, #20, 13296-13300.

Technologies available for sharing upon request:

Subcellular fractionation; Immunofluorescence microscopy; Protein isolation