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MUCOSAL BIOLOGY
Departments of 1Molecular Genetics and Cell Biology, 2Biochemistry and Molecular Biology, and 3Medicine, The University of Chicago, Chicago, Illinois 60637
Submitted 23 October 2002 ; accepted in final form 18 March 2003
Human and pig cDNAs for a novel stomach protein, the product of a gene
expressed at high levels specifically in cells of the antrum mucosa, have been
characterized. The general exon/intron structure of the genomic DNA is
conserved in humans and mice. The predicted protein sequences of the human and
mouse mRNAs contain 185 and 184 amino acids, respectively. The protein
isolated from pig antral extracts has an NH2 terminus consistent
with cleavage of a 20-amino acid signal peptide. Human cDNA was expressed in
E. coli to generate a protein antigen for antibody production. The
antibodies detected polypeptides of
18 kDa in antrum extracts from all
mammalian species tested. Immunocytochemistry located antrum mucosal protein
(AMP)-18 to surface mucosal cells of the mouse antrum and, specifically, to
secretion granules, suggesting that it is cosecreted with mucins. Antrum
extracts and recombinant human AMP-18 exhibit growth-promoting activity on
epithelial cells that can be blocked by the specific antisera. We suggest that
AMP-18 is a "gastrokine" that maintains the integrity of the
gastric mucosal epithelium.
growth factor; stomach; epithelium
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