DNA · 1985 · 120 citations · 33 references
Life SciencesMolecular BiologyMolecular GeneticsGene ExpressionMolecular NeurobiologySignal TransductionGastrointestinal PhysiologyProtein Synthesis3' Untranslated Region AnalysisAmino Acid Sequence-structure RelationshipsAmino Acid-derived Hormone StructureBioactive Peptide FormationBioactive Peptide MaturationPropeptide ProcessingVasoactive Intestinal Peptide Signaling
Vasoactive intestinal polypeptide (VIP) is a 28-amino-acid hormone produced primarily by neural tissues. The amino acid sequence of VIP is similar to that of a number of gastrointestinal hormones, including glucagon and secretin. VIP is synthesized as part of a polyprotein, pre-proVIP, which generates, in addition to VIP, an additional bioactive peptide known as PHM. As a first step toward understanding the molecular basis of pre-proVIP gene expression, we have isolated the pre-proVIP gene and have determined its structure. The gene is approximately 9 kb long and is interrupted by six introns which appear to divide the gene into functional domains. One of the introns occurs within the 3'-untranslated region of the gene.
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