Masaru Miyagi, Ph.D.
Case Western Reserve University
Center for Proteomics
10900 Euclid Ave., BRB 928
Cleveland, OH 44106-4988
Phone: (216) 368-5917
Fax: (216) 368-6846
Email: masaru.miyagi@case.edu
Faculty Appointments
Case Center for Proteomics (Assistant Professor)
Department of Pharmacology (secondary)
Department of Ophthalmology (secondary)
Academic History
| 1997 | Ph.D., Biochemistry, Osaka University |
| 1998-2000 | Post-doctoral Fellow, Biochemistry, Cleveland Clinic Foundation |
Positions and Honors
| 1993-1997 | Manager, Mass Spectrometry Laboratory, Biotechnology Research Laboratories, Takara Shuzo Co., Ltd., Kusatsu, Japan |
| 2000-2002 | Project Scientist, Department of Ophthalmic Research, Cole Eye Institute, Cleveland Clinic Foundation, Cleveland, Ohio |
| 2002-2006 | Director, Proteomics/Mass Spectrometry Core Facility, University of North Dakota School of Medicine and Health Sciences, Grand Forks, North Dakota |
| 2002-2006 | Assistant Professor, Department of Biochemistry and Molecular Biology, University of North Dakota School of Medicine and Health Sciences, Grand Forks, North Dakota |
| 2006- | Co-Director, Proteomics Module, Visual Science Research Center, Case Western Reserve University, Cleveland, Ohio |
| 2006- | Assistant Professor, Center for Proteomics, Departments of Pharmacology and Ophthalmology, Case Western Reserve University, Cleveland, Ohio |
Current Graduate Students
Vikram Palamalai (Biochemistry, University of North Dakota)
Dagmar Hajkova (Pharmacology, Case)
Research
My laboratory has two major research interests: 1) molecular mechanisms of retinal light damage and 2) development of proteomic methods.
Molecular Mechanisms of Light-induced Photoreceptor Cell Degeneration in Experimental Animals
Acute light-induced photoreceptor cell degeneration in experimental animals has been studied for more than 40 years as a model for visual cell loss arising from human retinal degenerative diseases such as age-related macular degeneration (AMD). The exact cause of AMD is unknown, but the photoreceptor cell degeneration, whether in AMD or a result of experimental light exposure, is generally characterized by apoptosis of photoreceptor cells. Oxidative stress has been indicated to be involved in the photoreceptor cell death in both AMD and the experimental model, because certain doses of antioxidants such as vitamin C appear to help control the advance of late AMD and to prevent the experimental light-induced damage. Therefore, elucidating the molecular mechanisms that trigger intense light-induced apoptosis might help to identify similar mechanisms in human diseases and lead to therapies that prevent AMD and other retinal degenerative diseases.
We use proteomic and biochemical approaches to study molecular mechanisms of light-induced photoreceptor cell degeneration. It has been demonstrated that light-induced photoreceptor degeneration is circadian dependent; greater damage in rats exposed to light during the nighttime period than during the daytime period, suggesting that the expression profile of photoreceptor rod outer segments (ROS) proteins at the onset of light exposure appears to be important in determining light damage susceptibility. Therefore, we hypothesize that there are proteins expressed in ROS during the daytime period that protect photoreceptor cells from light damage. Our research effort has been focused on identifying such protective proteins against light damage.
Development of Proteomic Methods
The completion of the genome sequencing of humans and other species and the emergence of new technologies in mass spectrometry have together fostered unprecedented opportunities for studying proteins on a large scale. Although mass spectrometry is the pre-eminent technology in proteomics studies, currently available methods on the front end of the mass spectrometer are not satisfied for the maximum use of mass spectrometry technology. Therefore, development of new proteomics methods on the front end of the mass spectrometer is of critical importance towards the advancement of proteomics studies.
We are currently developing two proteomics methods. One is a proteolytic 18O labeling method for quantitative proteomics and the other is a method for selectively enriching nitrotyrosine containing peptides for determining the sites of nitration.
Recent Publications
- Rao, K. C. S., Carruth R. T., Miyagi, M. (2005) Proteolytic 18O labeling by peptidyl-Lys metalloendopeptidase for comparative proteomics. J. Proteome Res. 4, 507-514.
- Rao, K. C. S., Palamalai, V, Dunlevy, J. R. and Miyagi, M. (2005) Peptidyl-Lys Metalloendopeptidase Catalyzed 18O Labeling for Comparative Proteomics: Application to Cytokines/LPS Treated Human Retinal Pigment Epithelium Cell Line. Mol. Cell. Proteomics, 4. 1550-1557.
- Hajkova, D., K. C. Rao, K. C. S., and Miyagi, M. (2006) The pH Dependency of the Carboxyl Oxygen Exchange Reaction Catalyzed by Lysyl Endopeptidase and Trypsin. J. Proteome Res. 5, 1667-1673.
- Palamalai, V., Darrow, R. M., Organisciak, D. T. and Miyagi, M. (2006) Light-Induced Changes of Protein Nitration in Photoreceptor Rod Outer Segments. Mol Vis. (in press).
- Miyagi, M. and Rao, K. C. S. (2006) Proteolytic 18O Labeling Strategy for Quantitative Proteomics. Mass Rev. (in press).