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G-protein-sensitive guanylyl cyclase activity associated with plasma membranes.
- Source :
-
Archives of biochemistry and biophysics [Arch Biochem Biophys] 1995 Dec 20; Vol. 324 (2), pp. 209-15. - Publication Year :
- 1995
-
Abstract
- A mammalian plasma-membrane-bound guanylyl cyclase is inhibited by NaCl and this inhibition is dependent on GTP concentrations and independent of the chloride salt type. This chloride inhibition is reversed by GTP analogs such as GTP gamma S, suggesting the involvement of G proteins. When the ability of bacterial toxins to affect this chloride-sensitive guanylyl cyclase was examined, pertussis toxin decreased the basal activity and the chloride sensitivity was greatly reduced. Cholera toxin induced a slight activation of the basal activity, without significant changes in the NaCl inhibition. These data indicate that G proteins regulate the chloride sensitivity of this guanylyl cyclase activity. Another property described here is the ability of ATP and analogs to inhibit the basal activity. However, these nucleotides did not modify the chloride sensitivity of the membrane-bound guanylyl cyclase activity.
- Subjects :
- 5'-Nucleotidase metabolism
Adenosine Triphosphate analogs & derivatives
Adenosine Triphosphate pharmacology
Animals
Biomarkers
Cattle
Cell Fractionation
Chlorides pharmacology
Cholera Toxin pharmacology
Dose-Response Relationship, Drug
Guanosine Triphosphate pharmacology
Guanylate Cyclase drug effects
Muscle, Smooth cytology
Muscle, Smooth enzymology
Muscle, Smooth metabolism
Pertussis Toxin
Subcellular Fractions metabolism
Trachea cytology
Trachea enzymology
Trachea metabolism
Virulence Factors, Bordetella pharmacology
Cell Membrane enzymology
GTP-Binding Proteins metabolism
Guanylate Cyclase metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0003-9861
- Volume :
- 324
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Archives of biochemistry and biophysics
- Publication Type :
- Academic Journal
- Accession number :
- 8554311
- Full Text :
- https://doi.org/10.1006/abbi.1995.0032