title: Peptide fragments of AMP-18, a novel secreted gastric antrum mucosal protein, are mitogenic and motogenic.
abstract: Antrum mucosal protein (AMP)-18 is a novel 18-kDa protein synthesized by cells of the gastric antrum mucosa. The protein is present in secretion granules of murine gastric antrum epithelial cells and is a component of canine antrum mucus, suggesting that it is secreted into the viscoelastic gel layer on the mucosal surface. Release of the protein appears to be regulated because forskolin decreased the amount of immunoreactive AMP-18 in primary cultures of canine antrum mucosal epithelial cells, and indomethacin gavaged into the stomach of mice reduced AMP-18 content in antrum mucosal tissue before inducing histological injury. A functional domain of the protein was identified by preparing peptides derived from the center of human AMP-18. A 21-mer peptide stimulated growth of gastric and intestinal epithelial cells, but not fibroblasts, and increased restitution of scrape-wounded gastric epithelial monolayers. These functions of AMP-18 suggest that its release onto the apical cell surface is regulated and that the protein and/or peptide fragments may protect the antral mucosa and promote healing by facilitating restitution and proliferation after injury.
authors.affiliation: The Univ. of Chicago, Dept. of Medicine, Chicago, IL 60637, USA. gtoback@medicine.bsd.uchicago.edu
authors.forename: F Gary
authors.initials: FG
authors.lastname: Toback
authors.forename: Margaret M
authors.initials: MM
authors.lastname: Walsh-Reitz
authors.forename: Mark W
authors.initials: MW
authors.lastname: Musch
authors.forename: Eugene B
authors.initials: EB
authors.lastname: Chang
authors.forename: John
authors.initials: J
authors.lastname: Del Valle
authors.forename: Hongyu
authors.initials: H
authors.lastname: Ren
authors.forename: Erick
authors.initials: E
authors.lastname: Huang
authors.forename: Terence E
authors.initials: TE
authors.lastname: Martin
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001667:Binding, Competitive; D002455:Cell Division / Q000187:drug effects; D002478:Cells, Cultured; D005576:Colforsin / Q000494:pharmacology; D016861:Cyclooxygenase Inhibitors / Q000494:pharmacology; D004285:Dogs; D004847:Epithelial Cells / Q000166:cytology / Q000187:drug effects; D005347:Fibroblasts / Q000166:cytology / Q000187:drug effects; D005753:Gastric Mucosa / Q000737:chemistry / Q000187:drug effects / Q000378:metabolism*; D006801:Humans; D007213:Indomethacin / Q000494:pharmacology; D007422:Intestines / Q000166:cytology; D051379:Mice; D008934:Mitogens / Q000032:analysis / Q000378:metabolism / Q000494:pharmacology*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000494:pharmacology*; D036361:Peptide Hormones; D010455:Peptides; D011706:Pyloric Antrum / Q000737:chemistry / Q000187:drug effects / Q000378:metabolism*; D013552:Swine; D014945:Wound Healing
chemical_list: D016861:Cyclooxygenase Inhibitors; C477000:GKN1 protein, human; D008934:Mitogens; D010446:Peptide Fragments; D036361:Peptide Hormones; D010455:Peptides; D005576:Colforsin; D007213:Indomethacin