NSF Award
9874851
9874851<br/>Wiese<br/><br/>Glycosylation of proteins represents the most complex post-translational modification of proteins known to occur. It is becoming increasingly accepted that the oligosaccharide moieties of glycoproteins have an important role in protein stability, function and turnover, and one of the moieties shown to have an influence on these roles is fucose. A large number of studies have reported that glycoprotein metabolism in general is altered in cancer and other diseases. Understanding fucose metabolism in greater depth may allow manipulation of the fucosylation state of proteins, thereby manipulating protein half-lives. The research objectives of the proposal are: <br/>1. to characterize fucosylated proteins secreted by rat hepatoma cells, in terms of protein properties and glycosylation patterns, under different inductive conditions; <br/>2. to examine the effect of fucosylation on protein turnover, a. in terms of receptor-mediated endocytosis; and b. in terms of degradation, both in vitro and in vivo.<br/>As part of the CAREER grant, the P.I. will redesign several courses in biochemistry, including developing online biochemistry materials; and will develop his research program as a series of experiments to be carried out by undergraduates, and by a high school student and teacher.
