[HTML][HTML] The D136A mutation of the V2 vasopressin receptor induces a constitutive activity which permits discrimination between antagonists with partial agonist and …
FEBS letters, 1998•Elsevier
The substitution, in the human V2 vasopressin receptor, of the aspartate at position 136 by
alanine leads to agonist-independent activation of this mutant V2 receptor. Pharmacological
studies of the D136A V2 receptor helped us in characterizing different V2 receptor
antagonists. SR-121463A and OPC-31260, two non-peptide antagonists, behaved as
inverse agonists, while two cyclic peptides d (CH2) 5 [d-Tyr (Et) 2, Val4, Tyr-NH29] AVP and
d (CH2) 5 [d-Ile2, Ile4, Tyr-NH29] AVP known to be V2 antagonists, demonstrated clear …
alanine leads to agonist-independent activation of this mutant V2 receptor. Pharmacological
studies of the D136A V2 receptor helped us in characterizing different V2 receptor
antagonists. SR-121463A and OPC-31260, two non-peptide antagonists, behaved as
inverse agonists, while two cyclic peptides d (CH2) 5 [d-Tyr (Et) 2, Val4, Tyr-NH29] AVP and
d (CH2) 5 [d-Ile2, Ile4, Tyr-NH29] AVP known to be V2 antagonists, demonstrated clear …
The substitution, in the human V2 vasopressin receptor, of the aspartate at position 136 by alanine leads to agonist-independent activation of this mutant V2 receptor. Pharmacological studies of the D136A V2 receptor helped us in characterizing different V2 receptor antagonists. SR-121463A and OPC-31260, two non-peptide antagonists, behaved as inverse agonists, while two cyclic peptides d(CH2)5[d-Tyr(Et)2,Val4,Tyr-NH29]AVP and d(CH2)5[d-Ile2,Ile4,Tyr-NH29]AVP known to be V2 antagonists, demonstrated clear partial agonist properties. The finding of a constitutively activated human V2 receptor represents a useful tool in characterizing V2 receptor antagonist ligands.
Elsevier