Guanylyl cyclase is a heat-stable enterotoxin receptor

Cell. 1990 Nov 30;63(5):941-8. doi: 10.1016/0092-8674(90)90497-3.

Abstract

Plasma membrane forms of guanylyl cyclase have been shown to function as natriuretic peptide receptors. We describe a new clone (GC-C) encoding a guanylyl cyclase receptor for heat-stable enterotoxin. GC-C encodes a protein containing an extracellular amino acid sequence divergent from that of previously cloned guanylyl cyclases; however, the protein retains the intracellular protein kinase-like and cyclase catalytic domains. Expression of GC-C in COS-7 cells results in high guanylyl cyclase activity. In addition, heat-stable enterotoxin from E. coli, but not natriuretic peptides, causes marked elevations of cyclic GMP and is specifically bound by cells transfected with GC-C. The enterotoxin fails to elevate cyclic GMP in nontransfected cells or in cells transfected with the natriuretic peptide/guanylyl cyclase receptors. These results show that a heat-stable enterotoxin receptor responsible for acute diarrhea is a plasma membrane form of guanylyl cyclase.

Publication types

  • Comparative Study

MeSH terms

  • 1-Methyl-3-isobutylxanthine / pharmacology
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cell Line
  • Cell Membrane / enzymology
  • Cloning, Molecular
  • Enterotoxins / metabolism
  • Guanylate Cyclase / genetics*
  • Guanylate Cyclase / metabolism
  • Kinetics
  • Molecular Sequence Data
  • Oligonucleotide Probes
  • Organ Specificity
  • Receptors, Cell Surface / genetics*
  • Receptors, Cell Surface / metabolism
  • Receptors, Enterotoxin
  • Receptors, Guanylate Cyclase-Coupled
  • Receptors, Peptide*
  • Restriction Mapping
  • Sequence Homology, Nucleic Acid
  • Transfection

Substances

  • Enterotoxins
  • Oligonucleotide Probes
  • Receptors, Cell Surface
  • Receptors, Peptide
  • Guanylate Cyclase
  • Receptors, Enterotoxin
  • Receptors, Guanylate Cyclase-Coupled
  • 1-Methyl-3-isobutylxanthine

Associated data

  • GENBANK/M55636