PHI — a new brain-gut peptide

Abstract

The detection of the C-terminal amide structure in porcine intestinal extracts has led to the discovery of a 27 amino acid residue peptide designated PHI (PHI-27, peptide HI). The peptide was found to have structural homologies to vasoactive intestinal peptide (VIP) and growth hormone-releasing factor (GRF). Subsequent studies have revealed that PHI exhibits a variety of biological activities which resemble those of VIP. Moreover, it was found that the peptide is able to inhibit the binding of VIP to its receptors, and to stimulate cyclic AMP production. PHI is present in both brain and gut in high concentrations and probably acts as a neurotransmitter or neuromodulator rather than a hormone. A comparison of the amino acid sequences of porcine, human and bovine PHI indicated that human PHI differs from the porcine peptide in two positions (12 and 27), and bovine PHI differs in one position (10). The amino acid sequence (deduced from the cDNA sequence) of the VIP precursor recently obtained from human neuroblastoma cells also contains an identical sequence to the newly-isolated human PHI from human colonic extracts. PHI has thus been shown to be co-synthesized with VIP in the same precursor molecule.