A subtype of kappa-opioid receptor mediates inhibition of high-affinity GTPase inherent in Gi1 in guinea pig cerebellar membranes.

Abstract:

:The kappa-opioid receptor agonists including U-50,488H and dynorphin A (1-17) in ranges of 0.1-100 nM inhibited the hydrolysis of GTP to GDP (P(i) release) inherent in GTP-binding proteins (G proteins) in guinea pig cerebellar membranes. U-50,488H inhibited only high-affinity GTPase activity, not low-affinity activity. The action of this agonist was found to be biphasic, and there was no inhibition at concentrations > 1 microM. The inhibition was abolished by pretreatment with preactivated pertussis toxin (PTX) at concentrations > 1 micrograms/ml but not with preactivated cholera toxin (30 micrograms/ml). Similar blockade of kappa-receptor-mediated inhibition was also observed when membranes were pretreated with a low concentration (8 microM) of N-ethylmaleimide (NEM) at low temperature (4 degrees C), which alkylates the cysteine residue to be ADP-ribosylated by PTX; but this treatment caused no significant change in kappa-agonist binding. When purified Gi1, but not G(o), was reconstituted into membranes pretreated with NEM, the kappa-receptor-mediated inhibition was recovered. These findings suggest that a subtype of kappa-opioid receptor is coupled to inhibition of intrinsic activity of Gi1.

journal_name

J Neurochem

authors

Ueda H,Misawa H,Fukushima N,Katada T,Ui M,Satoh M

doi

10.1046/j.1471-4159.1996.66020845.x

subject

Has Abstract

pub_date

1996-02-01 00:00:00

pages

845-51

issue

2

eissn

0022-3042

issn

1471-4159

journal_volume

66

pub_type

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