Abstract
Heat-stable enterotoxin (STa) is an important causative agent of diarrheal disease throughout the world. STa is known to bind specifically to receptors in the intestine, provoking intense intestinal secretion. Binding of STa, or of the mammalian endogenous ligands guanylin and uroguanylin, activates the guanylyl cyclase C receptor (GC-C); the resulting elevation of cGMP levels stimulates chloride secretion via CFTR. We have generated knockout mice which completely lack the GC-C receptor. These mice are viable and show no obvious alteration in intestinal fluidity. However, GC-C null mice are refractory to the secretory action of STa, proving that the GC-C receptor is necessary for the diarrheal response induced by STa.
Copyright 1997 Academic Press.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Bacterial Toxins / pharmacology*
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Biological Assay
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Blotting, Northern
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Cells, Cultured
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Drug Resistance
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Enterotoxins / pharmacology*
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Escherichia coli Proteins
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Guanylate Cyclase / deficiency
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Guanylate Cyclase / genetics
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Guanylate Cyclase / metabolism*
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Intestinal Mucosa / drug effects
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Intestinal Mucosa / enzymology
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Intestinal Mucosa / metabolism*
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Mice
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Mice, Inbred Strains
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Mice, Knockout
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Molecular Sequence Data
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RNA, Messenger / genetics
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Receptors, Cell Surface / deficiency*
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Receptors, Cell Surface / genetics
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Receptors, Enterotoxin
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Receptors, Guanylate Cyclase-Coupled
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Receptors, Peptide / deficiency
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Receptors, Peptide / genetics
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Receptors, Peptide / metabolism*
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Stem Cells
Substances
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Bacterial Toxins
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Enterotoxins
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Escherichia coli Proteins
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RNA, Messenger
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Receptors, Cell Surface
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Receptors, Peptide
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heat stable toxin (E coli)
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Guanylate Cyclase
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Receptors, Enterotoxin
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Receptors, Guanylate Cyclase-Coupled