|
Ben Cravatt Presents Barnett Lectures on Activity-Based Protein Profiling The Twenty-Sixth Annual Barnett Lectureship
Many enzymes, such as zymogens, have tightly regulated activities. They are produced by the cell in an inactive "proenzyme" form, later activated within the cell, but then inactivated after a short period. Conventional proteomic methods will detect the presence of the protein throughout this entire span of time; however, it is generally only the active form of the protein that has biological significance. Dr. Cravatt has developed chemical probes that target only the active form of many enzymes. Because affinity may in some cases be low, covalent crosslinking tags the active enzyme and survives denaturation and proteolytic cleavage for proteomic analysis.
Dr. Cravatt presented numerous examples from his work. Tabulating enzyme activities which are either elevated or suppressed in tumors or cancer cell lines has detected known and novel cancer-related enzymes.Integrated with analogous metabolomic methods in discovery metabolite profiling (DMP) Dr. Cravatt's work continues to elucidate the signalling networks and the functions of biochemical pathways in cancer pathogenesis. The lectures were followed by a reception and dinner in honor of Dr. Cravatt and his accomplishments. Dr. Cravatt also presented a technical lecture to the Institute the following morning.
|
Dr. Benjamin
Cravatt III, Professor in the Skaggs Institute for
Chemical Biology and Departments of Cell Biology and Chemistry at the Scripps
Research Institute, presented the twenty-sixth annual Barnett Lectureship "Mapping
Biochemical Pathways in Human Disease by Integrated Proteomics and Metabolomics".
Dr. Cravatt has pioneered the field of Activity-Based Protein Profiling (ABPP)
which uses active-site-directed chemical probes to determine the functional
states of large numbers of enzymes in the whole proteome.
 |
|
|
