|
Chemistry
James Bruce
Proteomics
Dr.
James Bruce is developing and applying new and existing
technologies for proteomics research at Washington State
University. In addition to directing the WSU Core Proteomics
Laboratory, Dr. Bruce’s own research program is
centered on the development of next- generation proteomics
capabilities, such as the facility for posttranslational
and protein-protein interaction profiling. These capabilities
are being developed with high performance Fourier transform
ion cyclotron resonance mass spectrometry (FTICR-MS).
In addition to his graduate training in FTICR-MS research,
Dr. Bruce has more than 10 years experience in the development
and application of FTICR-MS for biological applications
and proteomics at the national laboratory, industrial,
and academic levels. His expertise ranges from the development
of new technologies for improved protein and peptide
characterization to the application of mass spectrometry
technology to challenging biological problems.
The
central theme of his research program at Washington State
University is the further development and exploitation
of the unique attributes of FTICR-MS for protein and
peptide measurements that will allow characterization
of the proteome at levels unachievable by today’s
technology. This includes the ability to profile proteome
changes at posttranslational levels and the ability to
recognize changes in protein-protein interactions on
a proteome-wide scale. With the number of functional
roles required to support biological organisms now known
to be much greater than the number of gene products for
many organisms, it is clear that the partitioning of
proteins into any one of their many functionalities is
controlled through protein modification and changes in
the make-up of protein complexes or interactions. Therefore,
the ability to profile biological systems and visualize
the changes at these levels is essential to the comprehension
of complex biological organisms on the molecular level.
In addition, this new technology will be used to study
the structures and substrates of many enzymes involved
in diseases, such as Alzheimer’s disease. The identification
of improved substrate sequences has already been shown
to be beneficial for enzyme inhibitor design, however,
technological limitations in those studies resulted in
non-optimal substrate sequences.
Dr.
Bruce’s research program will target the development
of new mass spectrometry-based approaches to identify
fully optimized substrate sequences for enzymes involved
in Alzheimer’s disease, cancer, and many others.
This research will identify intended functional pathways
of enzymes involved in disease, provide new information
relevant to drug development, and indicate potential
side effects of drug intervention. Furthermore, this
research will have a dramatic impact on our fundamental
understanding of normal cellular function, like cell
development, or physiological processes like sleep or
aging, as well as disease states like cancer. These are
targeted areas for collaborative application of this
technology with established WSU scientists in the projects
listed below. Also provided are addresses of Web sites
that describe each collaborator’s research program.
Professor
Nancy Magnuson—Posttranslational modification
profiling relevant to Pim-1 kinase activity in cell
survival.
molecular.biosciences.wsu.edu/faculty/magnuson.html
Professor
James Krueger—Molecular and biochemical
regulation of sleep as visualized by posttranslational
modification profiling of relevant cytokines. www.vetmed.wsu.edu/people-vcapp/krueger.htm
Professor
Raymond Reeves—Deciphering the PTM Code
of Human HMGAI proteins and their involvement in the
cell cycle.
molecular.biosciences.wsu.edu/faculty/reeves.html
Contact
Information
James E. Bruce, Ph.D.
Associate Professor of Chemistry
Washington
State University
PO Box 644630
Pullman, WA 99164-4630
Telephone:
509-335-2116
Fax: 509-335-8867
E-mail: james_bruce@wsu.edu
WSU
Core Proteomics Laboratory www.crb.wsu.edu/2FrontPages/coreProteomics.html/
|
James Bruce
