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Human guanylin: cDNA isolation, structure, and activity.

R C Wiegand·J Kato·M D Huang·K F Fok·J F Kachur·M G Currie
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Abstract

Guanylin is a mammalian peptide homologue of heat-stable enterotoxins that acts on intestinal guanylate cyclase to elicit an increase in cyclic GMP. We have isolated a cDNA encoding an apparent precursor of guanylin from a human intestinal cDNA library. The mRNA is expressed at high levels in human ileum and colon. Human guanylin stimulated increases in T84 cell cyclic GMP levels, displaced 125I-labelled heat-stable enterotoxin (STa) binding to this cell line, and stimulated increases in short-circuit current (Isc) of isolated rat proximal colonic mucosa. This peptide may play a role in regulating fluid and electrolyte absorption in human intestines.

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Amino Acid SequenceAnimalsBacterial ToxinsBase SequenceCell LineChloridesColonCyclic GMPDNAElectric ConductivityEnterotoxinsEscherichia coli ProteinsGastrointestinal HormonesHumansIleumMolecular Sequence DataNatriuretic PeptidesPeptide BiosynthesisPeptidesRatsJournal Article

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R C Wiegand, J Kato, M D Huang, K F Fok, J F Kachur, M G Currie. 1992-10-19. Human guanylin: cDNA isolation, structure, and activity.. https://doi.org/10.1016/0014-5793(92)81387-2

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