PMID: 8592160Feb 1, 1996Paper

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

Journal of Neurochemistry
H UedaM Satoh

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.

Citations

May 28, 2010·Journal of Cellular Physiology·Cristina M Velázquez-MarreroJosé R Lemos
May 21, 1999·Biochemical and Biophysical Research Communications·A Yoshida, H Ueda
May 1, 1997·Cellular Signalling·K M Standifer, G W Pasternak
Jul 15, 1998·Peptides·N FukushimaH Ueda
Feb 6, 2003·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·Igor M Prudnikov, Vladimir N Tsyvkin

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