Human plasma posttranslational modification database and its potential clinical application

Yeou-Guang Tsay, M.D., Ph.D.
Proteomics Research Center and Institute of Biochemistry & Molecular Biology, National Yang-Ming University

Inasmuch as the number of protein species is limited in human plasma, it becomes more and more difficult for biomedical scientists to deduce novel protein targets for development of diagnostic methodologies. In order to discover new structural targets, my laboratory has been undertaking a different approach. We have been testing the hypothesis that posttranslational modifications in plasma proteome may serve as the good clinical markers. We have employed a new comprehensive mapping strategy for simultaneous characterization of multiple types of protein modifications. Thus far, we have successfully identified a variety of new modifications on plasma proteins, including serine phosphorylation, proline hydroxylation, tryptophan hydroxylation, serine glycosylation and so on. We believe that the database comprising protein modification information should provide a solid basis for the systemic survey of posttranslational modification statuses in the plasma proteome. This will help us define the roles of protein modification analyses in development of new diagnostic methods.
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