This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Obesity is associated with numerous medical conditions, the most devastating of which is diabetes (T2DM). Ove 15 million Americans are afflicted with T2DM which represents the leading cause of end-stage renal disease, blindness, and non-traumatic limb amputation. Recent evidence suggests RYGB to be the most effective treatment available for patients with T2DM. Resolution of T2DM is noted in over 80% of obese patients after RYGB. Post-RYGB improvements in T2DM appear to be the result of changes in gut anatomy which influence intestinal metabolism and endocrine function. Despite this important observation, our current understanding of how changes in gut anatomy improve T2DM is limited. We hypothesize that proteomic analyses of pre- and post-RYGB fasting and post-prandial plasma in patients ? T2DM will enhance our understanding of how changes in gut anatomy improve T2DM. Based on our established tissue bank containing longitudinal pre- and post-RYGB tissue samples we are in a unique position to collaborate with PNNL and perform these studies. Furthermore, preliminary proteomic analysis of fasting plasma from pre- and post-RYGB patients support this hypothesis and provide proof of concept. The proposed studies have the potential to dramatically influence our understanding of how RYGB improves T2DM and potentially identify new medical therapies. In addition we anticipate they will identify potential mediators for future study, generate preliminary data for future grant submission and scientific data for publication.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR018522-09
Application #
8365478
Study Section
Special Emphasis Panel (ZRG1-BCMB-H (40))
Project Start
2011-07-01
Project End
2012-06-30
Budget Start
2011-07-01
Budget End
2012-06-30
Support Year
9
Fiscal Year
2011
Total Cost
$57,367
Indirect Cost
Name
Battelle Pacific Northwest Laboratories
Department
Type
DUNS #
032987476
City
Richland
State
WA
Country
United States
Zip Code
99352
Smallwood, Heather S; Duan, Susu; Morfouace, Marie et al. (2017) Targeting Metabolic Reprogramming by Influenza Infection for Therapeutic Intervention. Cell Rep 19:1640-1653
Wang, Hui; Barbieri, Christopher E; He, Jintang et al. (2017) Quantification of mutant SPOP proteins in prostate cancer using mass spectrometry-based targeted proteomics. J Transl Med 15:175
Sigdel, Tara K; Gao, Yuqian; He, Jintang et al. (2016) Mining the human urine proteome for monitoring renal transplant injury. Kidney Int 89:1244-52
Webb-Robertson, Bobbie-Jo M; Wiberg, Holli K; Matzke, Melissa M et al. (2015) Review, evaluation, and discussion of the challenges of missing value imputation for mass spectrometry-based label-free global proteomics. J Proteome Res 14:1993-2001
Ibrahim, Yehia M; Baker, Erin S; Danielson 3rd, William F et al. (2015) Development of a New Ion Mobility (Quadrupole) Time-of-Flight Mass Spectrometer. Int J Mass Spectrom 377:655-662
Ream, Thomas S; Haag, Jeremy R; Pontvianne, Frederic et al. (2015) Subunit compositions of Arabidopsis RNA polymerases I and III reveal Pol I- and Pol III-specific forms of the AC40 subunit and alternative forms of the C53 subunit. Nucleic Acids Res 43:4163-78
Malouli, Daniel; Hansen, Scott G; Nakayasu, Ernesto S et al. (2014) Cytomegalovirus pp65 limits dissemination but is dispensable for persistence. J Clin Invest 124:1928-44
Cox, Jonathan T; Marginean, Ioan; Kelly, Ryan T et al. (2014) Improving the sensitivity of mass spectrometry by using a new sheath flow electrospray emitter array at subambient pressures. J Am Soc Mass Spectrom 25:2028-37
Cao, Li; Toli?, Nikola; Qu, Yi et al. (2014) Characterization of intact N- and O-linked glycopeptides using higher energy collisional dissociation. Anal Biochem 452:96-102
Martin, Jessica L; Yates, Phillip A; Soysa, Radika et al. (2014) Metabolic reprogramming during purine stress in the protozoan pathogen Leishmania donovani. PLoS Pathog 10:e1003938

Showing the most recent 10 out of 350 publications