Involvement of GTP-regulatory protein in brain prostaglandin E2 receptor and separation of the two components.
The specific binding protein for prostaglandin (PG) E2 solubilized from porcine brain was sensitive to guanine nucleotides. GTP inhibited the association and enhanced the dissociation of the specific [3H]PGE2 binding. Scatchard analyses showed that GTP (10 microM) decreased the binding affinity more than 3-fold without major change in the number of binding site. Gel filtration separated the binding site from GTP-regulatory component (N). The separated binding protein had a reduced affinity to PGE2 and lost its sensitivity to GTP. The addition of the separated N restored its responsiveness to GTP, and also increased the binding affinity to the original level. These results provide direct evidence for the molecular interaction between the PGE2 binding protein and N in the brain.
Yumoto
N
N
Hatanaka
M
M
Watanabe
Y
Y
Hayaishi
O
O
D000818:Animals; D001921:Brain / Q000378:metabolism*; D002793:Cholic Acids; D019204:GTP-Binding Proteins / Q000378:metabolism*; D006160:Guanosine Triphosphate / Q000494:pharmacology; D007700:Kinetics; D046911:Macromolecular Substances; D011485:Protein Binding / Q000187:drug effects; D011956:Receptors, Cell Surface / Q000378:metabolism*; D011982:Receptors, Prostaglandin / Q000302:isolation & purification / Q000378:metabolism*; D018078:Receptors, Prostaglandin E; D013552:Swine
D002793:Cholic Acids; D046911:Macromolecular Substances; D011956:Receptors, Cell Surface; D011982:Receptors, Prostaglandin; D018078:Receptors, Prostaglandin E; D006160:Guanosine Triphosphate; D019204:GTP-Binding Proteins; C028213:3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate