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PROTEOMICS

蛋白质组学

基本信息

批准号：
8180951
负责人：
Dean P Edwards
金额：
$ 16.63万
依托单位：
BAYLOR COLLEGE OF MEDICINE
依托单位国家：
美国
项目类别：
财政年份：
2010
资助国家：
美国
起止时间：
2010-09-17 至 2015-06-30
项目状态：
已结题

来源：
https://reporter.nih.gov/project-details/8180951
关键词：
Acetylation Affinity Affinity Chromatography Albumins Aliquot Amino Acid Sequence Amino Acids Ammonium Sulfate Antibodies Antibody Affinity Antibody Formation Antigens Apoptosis Applications Grants Area Arts Award Bacteria Baculoviruses Binding Binding Proteins Binding Sites Biological Assay Biological Markers Biometry Bioreactors Biotin Biotinylation Blood capillaries Budgets Buffers C-terminal CD8B1 gene Cancer Biology Cancer Center Cancer Center Support Grant Cattle Cell Culture Techniques Cell Extracts Cell Line Cells Chemistry Chimeric Proteins Chromatography Color Complement component C1s Complementary DNA Complex Computer software Consult Consultations Coomassie blue Coupled Coupling Culture Media Custom Cyclization Cytolysis Data Data Analyses Data Reporting Data Set Databases Denmark Detection Devices Diagnosis Diamond Dimensions Dissociation Dyes Enzyme-Linked Immunosorbent Assay Epitopes Equipment Equipment and supply inventories Eye Faculty Fiber Fingerprint Fluorescence Fractionation Gel Genes Genomics Glycoproteins Goals Gold Grant Growth Factor Height High Pressure Liquid Chromatography Human Resources Hybridomas Hybrids Immune response Immunoblotting Immunoglobulin G Immunohistochemistry Immunoprecipitation In Vitro Inbred BALB C Mice Infection Injection of therapeutic agent Insecta Institution Investments Ion-Exchange Chromatography Procedure Ions Label Laboratories Laboratory culture Lasers Ligands Lipids Liquid substance Logistics Malignant Neoplasms Maps Marker Discovery Mass Spectrum Analysis Measurement Mediating Medicine Membrane Metabolic Marker Methods Methylation Mitogen-Activated Protein Kinases Modeling Modification Molecular Monoclonal Antibodies Multiple Myeloma Mus N-terminal Nature Nitrogen Noise Nuclear Extract Nucleopolyhedrovirus Organization administrative structures Oryctolagus cuniculus Pathway interactions Patients Peptide Hydrolases Peptide Sequence Determination Peptide Synthesis Peptide antibodies Peptide/MHC Complex Peptides Phase Phosphoproteins Phosphorylation Phosphorylation Site Plaque Assay Plasma Plasmids Post-Translational Modification Site Post-Translational Protein Processing Precipitation Preparation Prevention Procedures Process Production Protein Analysis Protein Array Protein Chemistry Protein Databases Protein Sequence Analysis Proteins Proteome Proteomics Proteomics Shared Resource Prowl Quality Control RNA Splicing Recombinant Proteins Recombinants Research Research Personnel Resolution Resource Sharing Resources Robot Running Sampling Scanning Screening procedure Secondary to Sepharose Serum Serum Proteins Services Set protein Shuttle Vectors Signal Pathway Signal Transduction Silver Staining Site Slide Sodium Dodecyl Sulfate-PAGE Solutions Source Specificity Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Spleen Spottings Stable Isotope Labeling Staining method Stains Streptavidin Supervision Suspension Culture System T-Cell Receptor T-Lymphocyte Techniques Technology Testing Time Tissues Training Translational Research Translations Trypsin Tube Two-Dimensional Gel Electrophoresis UV sensitive Universities Validation Vendor Viral Wages Writing amidation base cancer therapy capillary college cooking cost effective cyanine dye 5 cytokine data acquisition detector experience gel electrophoresis genetic regulatory protein homologous recombination immunocytochemistry informatics shared resource instrument instrumentation interest mass spectrometer meetings monoclonal antibody production monomer mouse model myristoylation nano nano-electrospray new technology novel polyvinylidene fluoride pre-clinical pressure protein complex protein expression protein profiling recombinant virus reversed phase chromatography sample collection tool tumor two-dimensional validation studies vector viral DNA

项目摘要

The goal of this shared resource is to provide investigators with cost effective state-of-the-art instrumentation, and specialized expertise for analysis of proteomes with the goal of identifying novel protein biomarkers with applications for prevention, diagnosis and treatment of cancer. Because of the extremely diverse nature of proteins through post-translation modifications (PTMs), secretion, and RNA splicing coupled with their wide dynamic range of expression, no single platform exists for differential analysis of global protein expression. This Shared Resource therefore combines and integrates the instrumentation and expertise of several different faculty co-directors under a single organizational unit directed by Dr. Dean P. Edwards. Through a combined investment by the Institution and the Dan L. Duncan Cancer Center of $1.7M in equipment, start-up salary for new staff and operational support, the Proteomics Shared Resource (PSR) has expanded its technological capabilities and services and has grown tremendously to become one of the heaviest utilized Resources of the Cancer Center. The PSR is currently staffed by four co-directors (Drs Jun Qin, Richard Cook, Shixia Huang, Eastwood Leung) and six highly trained technical staff. New technologies and services developed since the CCSG submission in 2006 include non-mass spectrometry-based protein profiling platforms such as the Luminex fluorescence bead system, two dimensional liquid and gel electrophoresis and antibody/peptide arrays; mass spectrometry identification and PTM analysis of endogenous protein complexes isolated from cells, quantitative mass spectrometry protein profiling by SILAC (stable isotope labeling with heavy amino acids in cells) and enhanced throughput production of monoclonal antibodies (MAbs). These new technologies and services, together with the previously established technologies of protein chemistry, MALDI-TOF identification and PTM analysis of proteins, baculovirus expression of recombinant proteins and conventional hybridoma/MAb production, have created a highly comprehensive Proteomic Shared Resource capable of facilitating both protein biomarker discovery research and translational validation studies through custom antibody production. We will continue to expand and meet the needs of the Cancer Center through shared instrument grant applications and by providing expertise and new leading edge proteomic technologies as the field rapidly evolves.

这一共享资源的目标是为研究人员提供具有成本效益的最先进的仪器和蛋白质组分析的专门知识，目的是识别用于预防、诊断和治疗癌症的新的蛋白质生物标记物。由于蛋白质通过翻译后修饰(PTM)、分泌和RNA剪接的极其多样化的性质，加上它们广泛的动态表达范围，因此没有一个单一的平台可以用于全球蛋白质表达的差异分析。因此，这一共享资源将几个不同教职联合主任的工具和专业知识整合到一个由迪恩·P·爱德华兹博士指导的单一组织单位下。通过该研究所和丹·L·邓肯癌症中心在设备、新员工的启动工资和运营支持方面的170万美元的联合投资，蛋白质组学共享资源(PSR)扩大了其技术能力和服务，并已极大地发展成为癌症中心利用率最高的资源之一。PSR目前由四名联席董事(秦军、理查德·库克、黄诗霞、梁伊斯特伍德)和六名训练有素的技术人员组成。自2006年CCSG提交报告以来，开发的新技术和服务包括基于非质谱学的蛋白质图谱平台，如Luminex荧光珠系统、二维液体和凝胶电泳以及抗体/肽阵列；从细胞中分离的内源性蛋白质复合体的质谱学鉴定和PTM分析，SILAC(细胞中重氨基酸稳定同位素标记)的定量质谱学蛋白质图谱，以及提高产量单抗(MAb)。这些新的技术和服务，与以前建立的蛋白质化学、MALDI-TOF鉴定和蛋白质的PTM分析、重组蛋白质的杆状病毒表达和常规杂交瘤/单抗生产等技术相结合，创建了一个高度综合的蛋白质组共享资源，能够通过定制抗体生产促进蛋白质生物标记物发现研究和翻译验证研究。我们将继续扩大和满足癌症中心的需求，通过共享仪器赠款申请，并提供专业知识和新的前沿蛋白质组技术，以适应该领域的快速发展。