Neuraminidase reduces the number of super-high-affinity [3H]oxotremorine-M binding sites in lung.
The effects of neuraminidase on the binding of the radioligand agonist [3H]oxotremorine-M ([3H]oxo-M) were investigated in lung membranes. [3H]Oxo-M labelled super-high-affinity binding sites (KD of 1.36 nM), as indicated by the very high affinity displayed by carbachol when tested in competition with 0.5 mM [3H]oxo-M. Neuraminidase reduced the number of [3H]oxo-M binding sites with no change occurring in the KD. These results suggest that the effects of neuraminidase may explain virus-induced airway hyperresponsiveness.
Haddad
E B
EB
Laboratoire de Neuroimmunopharmacologie, Université Louis Pasteur-Strasbourg, Illkirch, France.
Gies
J P
JP
D000818:Animals; D002217:Carbachol / Q000494:pharmacology; D003016:Clostridium perfringens / Q000201:enzymology; D006168:Guinea Pigs; D066298:In Vitro Techniques; D007700:Kinetics; D008168:Lung / Q000187:drug effects / Q000378:metabolism*; D008297:Male; D008566:Membranes / Q000187:drug effects / Q000378:metabolism; D009119:Muscle Contraction / Q000187:drug effects; D009439:Neuraminidase / Q000494:pharmacology*; D010095:Oxotremorine / Q000378:metabolism*; D011976:Receptors, Muscarinic / Q000187:drug effects*
D011976:Receptors, Muscarinic; D010095:Oxotremorine; D002217:Carbachol; D009439:Neuraminidase