Robert B. Petersen, Ph.D.

Associate Professor

Mailing Address:
2103 Cornell Rd.
WRB 5126
Cleveland, OH 44106-7288

phone: (216) 368-6709
fax: (216) 368-0494
email: Robert.Petersen@Case.edu

Biography
Dr. Petersen received his Ph.D. in Cell and Developmental Biology from the University of Minnesota in 1985. After spending one year in the Institute of Human Genetics at the University of Minnesota as a research associate he moved to the University of Chicago as an NIH postdoctoral fellow in the laboratory of Dr. Susan Lindquist. There he studied posttranscriptional regulation of the heat shock response in the fruit fly, Drosophila melanogaster. At the University of Chicago he attained parenthetical rank as an instructor. He became an Assistant Professor at Case Western Reserve University in the Department of Pathology in 1991 and became an Associate Professor in 1998.

Research
The prion protein, a normal cellular protein, is suspected to be a major, if not the only component of the agent that causes the spongiform encephalopathies. During the course of these diseases, the prion protein is "converted" to a protease-resistant form. It is this protease-resistant form that has been attributed with pathogenic potential. Two of these diseases, Creutzfeldt-Jakob disease (CJD) and the recently described fatal familial insomnia (FFI), are propagated as inherited or sporadic forms. The inherited form of FFI shares a mutation of codon 178 of the protein gene with one type of inherited CJD. We have shown that the genetic basis for these two diseases arising from a single mutation lies in a common polymorphism in the prion protein gene. The polymorphism apparently affects the topography of the lesions produced in the two diseases. Since the conformation of the prion protein seems to be at the heart of the pathogenic process, our group is trying to characterize the effect of known mutations in the prion protein gene on the synthesis and metabolism of the protein which result in a variety of distinct neurodegenerative conditions in both cell and animal models. We are also investigating the disease process at a cellular level.

Publications
Capellari S, Zaidi SIA, Long AC, Kwon EE, Petersen RB (2000). The Thr183Ala mutation, not the loss of the first glycosylation site, alters the physical properties of the prion protein. J Alzheimer's Disease 2:27-35.

Capellari S, Parchi P, Russo CM, Sanford J, Sy M-S, Gambetti P, Petersen RB (2000). Effect of the E200K mutation on prion protein metabolism: Comparative study of a cell model and human brain. Am J Pathol 157, 613-622.

Syed I.A. Zaidi, Sandra L. Richardson, Sabina Capellari, Li Song, Bernardino Ghetti, Man-Sun Sy, Pierluigi Gambetti, and Robert B. Petersen. Characterization of the F198S Prion Protein Mutation: Enhanced Glycosylation and Defective Refolding. J. Alz. Dis. 159-171, 2005.

Petersen RB , Siedlak SL, Lee HG, Kim YS, Nunomura A, Tagliavini F, Ghetti B, Cras P, Moreira PI, Castellani RJ, Guentchev M, Budka H, Ironside JW, Gambetti P, Smith MA, Perry G. Redox metals and oxidative abnormalities in human prion diseases. Acta Neuropathol (Berl). 2005 Aug 11; [Epub ahead of print].