The Proteomics Core enhances the research productivity of KCI members by providing the equipment and trained personnel necessary for analysis of cellular protein composition, protein modification, protein quantitation and protein interaction. Proteome profiling and protein identification services utilize modern mass spectrometer based methods. The primary platform for analysis is the Thermo Finnigan LTQ Linear lon Trap equipped with Electron Transfer Dissociation (ETD). Isolated protein, gel plug and full proteome analysis are supported. Sample preparation is achieved by robotic or manual depletion of high abundance proteins, digestion and solid phase extraction (SPE). Various sorbents including specialized sorbents such as Ti02 for isolation of phosphopeptides are available for SPE. Nanoflow HPLC from a Michrom H4 platform is utilized for most analyses with a Triversa Nanomate robot available as needed. Data analysis is achieved using Mascot, Sequest, XITandem and PEAKS algorithms with secondary data analysis by Scaffold. Results are distributed as hard copy on CD or by deposition on the international Tranche network. The Core enhances research productivity by providing a clear and easily accessible mechanism for protein identification and for relative quantitation of proteins based on isobaric tags. Quantitation technologies supported include cICAT, ITraq, TMT and SILAC and Multiple Reaction Monitoring (MRM). Analysis of isotopically labeled samples is achieved using the Mascot Quantitation package. MRM analysis is achieved using the TSQ Vantage with PinPoint and Skyline software for experimental design and data analysis. The protein identification component of the Proteomics Core provides KCI members access to technology for protein identification, proteomic profiling and biomarker identification. The protein interactions component of the Core provides instrumentation and services for detection of protein binding by Fluorescence Polarization (FP) and Surface Plasmon Resonance (SPR). The instruments in the Core produce sensitive, accurate and real time measurements of protein binding events. Thus, the protein interactions component of the Core supports investigators in asking questions about protein-protein interactions and the effects of those interactions on signaling pathways and cellular function.
Proteomic analysis contributes to our understanding of how cancers arise and is currently being developed for eariy cancer detection as well as therapeutic monitoring. Discovery, validation and hypothesis testing are supported using equipment that is in place and supported by trained personnel. All areas of cancer research are benefiting from proteomic technologies by developing greater understanding of the disease process. Clinically relevant proteomic analysis is expected to deliver unprecedented sensitivity in the detection of cancer and the ability to monitor the effectiveness of treatment.
|Hamel, Lauren M; Penner, Louis A; Albrecht, Terrance L et al. (2016) Barriers to Clinical Trial Enrollment in Racial and Ethnic Minority Patients With Cancer. Cancer Control 23:327-337|
|Xie, Yuran; Kim, Na Hyung; Nadithe, Venkatareddy et al. (2016) Targeted delivery of siRNA to activated T cells via transferrin-polyethylenimine (Tf-PEI) as a potential therapy of asthma. J Control Release 229:120-9|
|Cheriyan, Vino T; Muthu, Magesh; Patel, Ketan et al. (2016) CARP-1 functional mimetics are novel inhibitors of drug-resistant triple negative breast cancers. Oncotarget :|
|Moorman, Patricia G; Alberg, Anthony J; Bandera, Elisa V et al. (2016) Reproductive factors and ovarian cancer risk in African-American women. Ann Epidemiol 26:654-62|
|Najor, Nicole A; Weatherford, Layne; Brush, George S (2016) Prevention of DNA Rereplication Through a Meiotic Recombination Checkpoint Response. G3 (Bethesda) 6:3869-3881|
|Herroon, Mackenzie Katheryn; Diedrich, Jonathan Driscoll; Podgorski, Izabela (2016) New 3D-Culture Approaches to Study Interactions of Bone Marrow Adipocytes with Metastatic Prostate Cancer Cells. Front Endocrinol (Lausanne) 7:84|
|Gimotty, Phyllis A; Shore, Ronald; Lozon, Nancy L et al. (2016) Miscoding of Melanoma Thickness in SEER: Research and Clinical Implications. J Invest Dermatol 136:2168-2172|
|Ekanger, Levi A; Polin, Lisa A; Shen, Yimin et al. (2016) Evaluation of Eu(II) -based positive contrast enhancement after intravenous, intraperitoneal, and subcutaneous injections. Contrast Media Mol Imaging 11:299-303|
|Divi, Vasu; Harris, Jonathan; Harari, Paul M et al. (2016) Establishing quality indicators for neck dissection: Correlating the number of lymph nodes with oncologic outcomes (NRG Oncology RTOG 9501 and RTOG 0234). Cancer :|
|Katz, Matthew H G; Shi, Qian; Ahmad, Syed A et al. (2016) Preoperative Modified FOLFIRINOX Treatment Followed by Capecitabine-Based Chemoradiation for Borderline Resectable Pancreatic Cancer: Alliance for Clinical Trials in Oncology Trial A021101. JAMA Surg 151:e161137|
Showing the most recent 10 out of 634 publications