Panaiyur S. Mohan, Ph.D.
Research Assistant Professor
Department of Psychiatry
New York University School of Medicine
(845)398-5435
mohan@nki.rfmh.org
NYU Profile

Education
  • B.S. Osmania University, India (Chemistry)
  • M.S.Osmania University, India (Biochemistry)
  • Ph.D. Osmania University, India (Biochemistry)

Postdoctoral Training

  • Assistant Research Officer, National Institute of Nutrition, India
  • Research Fellow, Joslin Diabetes Center, Boston, MA

Awards

1967-1973 State Merit Scholarship for Outstanding Scholars

Research Interests

My research aims to understand the role of proteases in the pathogenesis of degenerative diseases. Proteases play an important role in the cascade of events leading to cell death. Abnormal processing of proteins is an early event in several major degenerative disorders. We are particularly interested in characterizing the role of calpains (calcium-activated proteases) in Alzheimer’s disease (AD) and Parkinson’s disease (PD) and in understanding the interplay among the calpain, caspase and cathepsin proteolytic systems in programmed cell death. I use both biochemical and immunochemical techniques to study proteases in postmortem human and animal tissues and in cell culture models. These studies also focus on the regulation of endogenous inhibitors that modulate the activities of the proteases. Based on our discovery of elevated lysosomal hydrolases in CSF of AD patients, we are developing a diagnostic test for Alzheimer’s disease. I am currently developing a sensitive assay for cathepsin D, a lysosomal enzyme especially elevated in AD brain and cerebrospinal fluid (CSF). The assay in conjunction with other available markers in CSF, such as tau protein and amyloid b peptide, will yield a profile with increased detection sensitivity.

Selected Publications

Rao, M.V., Engle, L.J., Mohan, P.S., Yuan, A., Qiu, D., Cataldo, A., Hassinger, L., Jacobsen, S., Lee, V.M., Andreadis, A., Julien, J.P., Bridgman, P.C., Nixon, R.A. Myosin Va binding to neurofilaments is essential for correct myosin Va distribution and transport and neurofilament density. J. Cell Biol. 159:279-90, 2002.

Sanchez, I., Hassinger, L., Sihag, R.K., Cleveland, D., Mohan, P., Nixon, R.A. Local control of neurofilament accumulation during radial growth of myelinating axons in vivo: Selective role of site specific phosphorylation. Journal of Cell Biology. 151: 1013-1024, 2000.

Adamec, E., Mohan, P.S., Cataldo, A.M., Vonsattel, J.P., Nixon, R.A. Up-regulation of the lysosomal system in experimental models of neuronal injury: Implications for Alzheimer’s disease. Neuroscience. 100: 663-675, 2000.

Wang, K.K.W., Postmantur, R.,Nadimpalli, R., Nath, R., Mohan, P., Nixon, R.A., Talanian, R. V.,Keegan, M., Herzog, L., Allen, H. Caspase mediated fragmentation of calpain inhibitor protein calpastatin during apoptosis: Archives of Biochemistry and Biophysics. 356:187-196, 1998.

Grynspan, F., Griffin, W.B., Mohan, P.S., Shea, T.B., and Nixon, R.A: Calpains and Calpastatin in SH-SY5Y Neuroblastoma Cells During Retinoic acid-Induced Differentiation and Neurite outgrowth: Comparison with the Human Brain Calpain System. J. Neurosci. Res. 48:181-191,1997.

Compaine, A.,Schein, J.D.,Tabb, J.S.,Mohan, P.S., and Nixon, R.A.: Limited proteolytic processing of the mature form of Cathepsin D in human and mouse brain: Postmortem stability of enzyme structure. Neurochemistry International. 27:385-396, 1995.

Cressman, C.M., Mohan, P.S., Nixon, R.A., and Shea, T.B. Proteolysis of protein kinase C: mM and
µM calcium requiring calpains have different abilities to generate, and degrade the free catalytic subunit, protein kinase M. FEBS Lett. 367:223-227, 1995.

Schwagerl, A.L.,Mohan, P.S., Cataldo, A.C., Vonsattel, J.P., Kowall, N.W., and Nixon, R.A.: Elevated levels of the endosomal-lysosomal proteinase cathepsin D in cerebrospinal fluid in Alzheimer disease. J. Neurochem. 64:443-446,1995.

Mohan, P.S. and Nixon, R.A.: Purification and properties of high molecular weight calpastatin from bovine brain. J. Neuroc hem. 64: 859-866, 1995.