Gastrotropin: not an enterooxyntin but a member of a family of cytoplasmic hydrophobic ligand binding proteins.
作者： I Gantz , S.F. Nothwehr , M Lucey , J.C. Sacchettini , J DelValle
DOI: 10.1016/S0021-9258(19)47054-3
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摘要: Abstract Gastrotropin, a peptide initially isolated from porcine intestinal extracts, has been proposed to be an enterooxyntin. We have full length gastrotropin cDNA hog small lambda gt11 library. No evidence of co-translational translocation or processing the encoded 127-residue protein could demonstrated using in vitro transcription/translation/microsomal assay. Comparative sequence analyses indicate that is new member family cytoplasmic hydrophobic ligand proteins. Analysis distribution nine adult Sprague-Dawley rat tissues revealed gene expressed intestine but not stomach, liver, heart, skeletal muscle, lung, kidney, adrenals, brain. Bioactivity studies neither nor carboxyl-terminally amidated tridecapeptide fragment deduced influence acid secretory activity rats with gastric fistulas canine parietal cells. Together these data suggest likely secreted as hormone function Moreover, it appears represents one several members binding proteins are intestine.
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