血浆蛋白探索会议 - Day2

概要 | 短期研讨会 | Day 1 | Day 2 | Day 3

议程 (PDF : English)

Tuesday, January 8

7:00am - 6:00pm Registration Open

7:30 - 8:15 Breakfast Workshop

8:15 Chairperson乫s Remarks

KEYNOTE PRESENTATION

8:20 Sifting Wheat from Chaff: The Critical Role of Biomarker Verification in Expanding the Clinical Diagnostics Portfolio N. Leigh Anderson, Ph.D., Founder & CEO, Plasma Proteome Institute The striking shortfall in new protein diagnostics emerging from proteomics research now appears more likely to reflect a lack of critical biomarker verification capacity than a failure in biomarker 乬discovery乭, in which large numbers of candidates are routinely uncovered. The core problem is that >95% of these candidates fail as reliable disease-specific indicators in the general population, where biological noise often overpowers the weak biomarker signal. Addressing this roadblock requires inverting the current biomarker paradigm, and placing primary emphasis on development of technology and collection of sample sets specifically tailored to support statistically definitive tests of large panels of biomarker candidates. In the limiting case, high-throughput verification may rival de novo 乬discovery乭 as the source of future biomarkers.

8:50 Cyclic Abundant Protein Immunodepletion (CAPI) of Human Plasma Proteins
Mark Baker, Ph.D., Professor of Proteomics, Chemistry & Biomolecular Sciences Department, Macquarie University and Chief Executive Officer, Australian Proteome Analysis Facility Ltd.
Briefly, we discuss the use of a novel method of protein pre-fractionation using a multidimensional chromatography approach prior to analysis by gel electrophoresis, LC-ESI and LC-MALDI. In addition, we highlight the use of a novel immuno-depletion strategy for the depletion of these high abundant proteins using chicken IgY antibodies. We will also present data showing the advantages of using this depletion strategy on state-of-the-art proteomic techniques including Differential Gel Electrophoresis (DIGE) and MRM乫s.

9:20 SELDI, PF2D & LC/MS/MS: The Power of Three for Medium Throughput Proteome Mining
Gary Coulton, Ph.D., Director, Medical Biomics Centre, St. George乫s, University of London
Integration of automated SELDI-TOF/MS, PF2D and LC/MS/MS gives a novel medium throughput system for discovery, statistical validation and identification of protein biomarkers. High throughput SELDI (1500 samples per run) on gold arrays generates statistically valid biomarkers rapidly. SELDI also gives 乬protein mass maps乭 of the 1152 fractions generated by PF2D. Only fractions containing mass matches with SELDI markers are analysed by LC/MS/MS to give a panel of candidate biomarker identities. Subsequent analysis by SELDI of samples immunodepleted by antibodies to candidate biomarkers locks the original SELDI biomarker to its protein identity. This approach places the burden of statistical validation upfront reducing the number of potential targets to be validated downstream by immuno-based assays.

9:50 Coffee Break in the Exhibit Hall

10:45 N-Terminal Cofradic^TM Proteomic Analysis of Serum Facilitates Identification of Low Abundance Serum Proteins
Koen Kas, Ph.D., Chief Scientific Officer, Pronota nv
Protein biomarker discovery in serum is challenging due to the vast dynamic range and high number of proteins circulating in serum. Complexity reduction of the proteome can be achieved through the sub-selection of particular peptides or proteins using a range of different procedures. In the N-teromics Cofradic technology every free N-terminal tryptic peptide of a protein or protein fragment is tagged. Diagonal chromatographic steps select and separate only these N-terminal fragments, whereas all non terminal fragments -generated by the tryptic digest- are removed from the peptide mixture thereby significantly reducing the complexity in comparison with standard proteomics technologies. This N-terminal selection strategy demonstrates an unprecedented power to discover low abundant serum proteins and reveals that serum proteins are subject to extensive cleavage by endogenous proteases.

11:15 SELDI-TOF in Quantitative Detection of Therapeutic Proteins and in the Identification of Protein Interactions
Bruno Antonsson, Ph.D. Senior Scientist, Protein Biochemistry, Geneva Research Center, Merck Serono International
The use of SELDI-TOF in the quantification of therapeutic proteins in plasma will be presented. The method allows for the detection of modifications of the protein in vivo. Furthermore, a method for the identification of interacting proteins from plasma samples will be presented and discussed.

Featured Presentation

11:45 New Technology for the Plasma Proteome and Its Application to Clinical Proteomics William S. Hancock, Ph.D., Bradstreet Chair & Professor, Chemistry & Chemical Biology, Northeastern University  We have developed the multi-lectin affinity chromatography (M-LAC) approach to study the plasma glycoproteome. This approach allows one to focus on the set of proteins that are more likely to be secreted. Furthermore, glycosylation has been shown to be altered in disease and thus study of the glycoproteome can facilitate the study of disease related changes in the blood proteome. This approach has been used in the study of breast and colon cancer with the goal of discovering markers associated with the early detection. We have also studied a mouse xenograft in which an implant of MCF-7 was treated with estrogen. Although a technical challenge, the characterization of human proteins in mouse plasma allows one to determine which proteins are secreted specifically from the tumor tissue. These results will be compared with the plasma proteome from patients suffering from diabetes and autoimmune disease, namely psoriasis and rheumatoid arthritis (RA).

12:15 Close of Morning Session

12:30 Luncheon Workshop 
or Lunch on Your Own 

2:00 Chairperson乫s Remarks

2:05 Identity of Assay Interfering Proteins
Michel Awwad, Ph.D., Associate Director, Bioanalytical Research and Development, Wyeth
Biological matrices, particularly plasma, often contain substance(s) (mainly proteins) that affect either positively or negatively the signal generated in an assay. I will be describing our attempts to identify these interfering substances as a first step in an effort to eliminate their effect.

2:35 Title to Be Announced
Title to Be Announced

3:05 From Discovery to Commercialization: Regulatory Strategies 
B. Melina Cimler, Ph.D., Vice President, Regulatory Affairs, Beckman Coulter
The complexity of validation of biomarkers for early disease detection and therapeutic selection and monitoring has contributed to the slow progress of personalized medicine. Regulatory requirements worldwide are being harmonized and heightened to ensure patient safety. Understanding the regulatory pathways available for moving biomarkers through the pipeline in an efficient manner is key to successful rapid commercialization.

3:35 Talk Title to Be Announced	Sponsored by
John Quinn, Ph.D., Chief Science Officer, ICx Nomadics Bioinstrumentation

3:50 Refreshment Break in the Exhibit Hall

4:30 BuzZ Sessions - Small Group Moderated Discussions Have a topic idea?

5:30 Close of Day