We request a Thermo Scientific Orbitrap Elite mass spectrometer with an electron transfer dissociation source to be placed at the Oregon Health &Science University in the Proteomics Shared Resource. Due to its high resolution, sensitivity and fast scan rates, this instrument will be used to increase the productivity of proteomics research across the entire OHSU campus. The major users of the instrument utilize it to study the cause and treatment of several diseases including: cataracts, hearing loss, leukemia, parasitic disease, alcoholism, and methamphetamine addiction. Complex mixtures of proteins will be analyzed by digesting them with trypsin, separating the resulting peptides by chromatography and generation of tandem MS data. Quantification of relative changes in protein abundance between samples will be determined using both stable isotope tagging strategies and label free quantification. Modifications in proteins will be detected with the aid o the requested electron transfer dissociation source. The high resolution of the instrument will also be used to measure hydrogen/deuterium exchange rates in proteins to probe the structure of protein complexes. The introduction of this instrument will fulfill the growing needs of the researchers at the Oregon Health &Sciences University to incorporate state-of-the-art tools in proteomics into their research. This will speed their progress of discovery to improve the detection and treatment of human disease.

Public Health Relevance

We request funding for a Thermo Scientific Orbitrap Elite high-resolution mass spectrometer. The instrument will be used to identify and determine the relative abundance of proteins to support research on diseases including cancer, cataracts, hearing loss, parasitic infection, and drug addiction. The instrument will be maximally utilized by placement in the Oregon Health &Science University's Proteomics Shared Research where its introduction will increase research productivity across the entire campus.

Agency
National Institute of Health (NIH)
Institute
Office of The Director, National Institutes of Health (OD)
Type
Biomedical Research Support Shared Instrumentation Grants (S10)
Project #
1S10OD012246-01A1
Application #
8333650
Study Section
Special Emphasis Panel (ZRG1-BCMB-D (30))
Program Officer
Levy, Abraham
Project Start
2012-08-01
Project End
2014-07-31
Budget Start
2012-08-01
Budget End
2014-07-31
Support Year
1
Fiscal Year
2012
Total Cost
$853,719
Indirect Cost
Name
Oregon Health and Science University
Department
Biochemistry
Type
Schools of Medicine
DUNS #
096997515
City
Portland
State
OR
Country
United States
Zip Code
97239
De Maria, Alicia; Wilmarth, Phillip A; David, Larry L et al. (2017) Proteomic Analysis of the Bovine and Human Ciliary Zonule. Invest Ophthalmol Vis Sci 58:573-585
Danelishvili, Lia; Chinison, Jessica J J; Pham, Tuan et al. (2017) The Voltage-Dependent Anion Channels (VDAC) of Mycobacterium avium phagosome are associated with bacterial survival and lipid export in macrophages. Sci Rep 7:7007
Avenarius, Matthew R; Krey, Jocelyn F; Dumont, Rachel A et al. (2017) Heterodimeric capping protein is required for stereocilia length and width regulation. J Cell Biol 216:3861-3881
Midgett, Madeline; López, Claudia S; David, Larry et al. (2017) Increased Hemodynamic Load in Early Embryonic Stages Alters Endocardial to Mesenchymal Transition. Front Physiol 8:56
Krey, J F; Wilmarth, P A; David, L L et al. (2017) Analysis of the Proteome of Hair-Cell Stereocilia by Mass Spectrometry. Methods Enzymol 585:329-354
Whitson, Jeremy A; Wilmarth, Phillip A; Klimek, John et al. (2017) Proteomic analysis of the glutathione-deficient LEGSKO mouse lens reveals activation of EMT signaling, loss of lens specific markers, and changes in stress response proteins. Free Radic Biol Med 113:84-96
Plubell, Deanna L; Wilmarth, Phillip A; Zhao, Yuqi et al. (2017) Extended Multiplexing of Tandem Mass Tags (TMT) Labeling Reveals Age and High Fat Diet Specific Proteome Changes in Mouse Epididymal Adipose Tissue. Mol Cell Proteomics 16:873-890
Midgett, Madeline; López, Claudia S; David, Larry et al. (2017) Increased Hemodynamic Load in Early Embryonic Stages Alters Myofibril and Mitochondrial Organization in the Myocardium. Front Physiol 8:631
Carter-O'Connell, Ian; Jin, Haihong; Morgan, Rory K et al. (2016) Identifying Family-Member-Specific Targets of Mono-ARTDs by Using a Chemical Genetics Approach. Cell Rep 14:621-631
Gross, Sean M; Lehman, Steven L (2016) Functional phosphorylation sites in cardiac myofilament proteins are evolutionarily conserved in skeletal myofilament proteins. Physiol Genomics 48:377-87

Showing the most recent 10 out of 23 publications