Expression of Preprosomatostatin Genes in Heterologous Cells
The biosynthesis, intracellular transport and posttranslational processing of peptide hormone precursors is a very useful model for investigating cellular and molecular aspects of the secretory pathway. Since the discovery of proinsulin, it is evident that most polypeptide hormones are synthesized as larger precursors. DNA sequencing has established the sequence of numerous hormone and neuropeptide precursors (Douglass et al., 1984), many of which contain the sequences of several bioactive peptides. To generate a biologically active peptide from its precursor, the pro hormone must be proteolytically cleaved and in addition, may undergo several post-translational modifications including glycosylation, sulfation, phosphorylation, amidation and acetylation (Mains, et al., 1983). These reactions occur sequentially as the precursor is transported from the ER to the Golgi apparatus and secretory granules prior to secretion. A major goal of our laboratory is to identify sorting and processing sequences in the precursor to the peptide hormone somatostatin.
KeywordsHigh Performance Liquid Chromatography Microsomal Membrane Polypeptide Hormone Heterologous Cell Secretory Apparatus
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