
Khatuna Gagnidze, Ph.D.
Postdoctoral Fellow, Department of Pharmacology and Systems Therapeutics
E-mail: khatuna.gagnidze@mssm.edu
Tel: (212) 241-6545
Ph.D. (2007) Mount Sinai School of Biological Sciences
M.S. (1996) Tbilisi State University, Tbilisi, Republic of Georgia
B.S. Tbilisi State University, Tbilisi, Republic of Georgia
Endothelin-converting enzyme-2 (ECE-2) is a zinc metallopeptidase that catalyzes the cleavage of peptide bond on the amino-terminus of aromatic and aliphatic residues, however to date no endogenous substrates of this peptidase have been identified. Restricted neuroendocrine distribution and acidic pH optimum of ECE-2 leads us to believe that it may be involved in the neuropeptide processing/degradation along the secretory pathway. By using ECE-2 knockout mouse as a model system and employing multidisciplinary approach such as behavioral characterization, quantitative peptidomics, and structural and biochemical analysis we are trying to identify endogenous substrates of ECE-2 and delineate its physiological functions.
K. Gagnidze, G. Pollonini, C.M. Alberini. MuSK is expressed and co-localized with agrin in hippocampal neurons. Abstract. Society for Neuroscience Annual Meeting. New Orleans, LA, 2003.
D. Platano, K. Gagnidze, G. Pollonini, C.M. Alberini. Dendritic expression of C/EBPβ and C/EBPδ. Abstract. Society for Neuroscience Annual Meeting. New Orleans, LA, 2003.
K. Gagnidze, O. Tkalych,, LD Fricker. and LA Devi. Studies To Characterize Non-Classical Processing Of Neuropeptides: Quantitative Peptidomic Analysis Of Peptides From Animals Lacking Endothelin-Convering Enzyme-2. Abstract. Society for Neuroscience Annual Meeting. San Diego, CA, 2007.