Linked Life Data

8025534

Source:http://linkedlifedata.com/resource/pubmed/id/8025534

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1994-8-10
pubmed:abstractText
We have examined the ability of divalent cations to inhibit 3H-GR 65630 binding to 5-HT3 receptor recognition sites in rat brain cortical membranes. Among the divalent metal cations tested, Cd2+, Zn2+ and Cu2+ inhibited the specific 3H-GR 65630 binding activity to 5-HT3 receptors at a concentration of 0.1-1 mM. The other divalent metal cations tested (i.e. Co2+, Ni2+, Ba2+, Ca2+, Mg2+ and Mn2+) produced no inhibition of the specific 3H-GR 65630 binding. Cd2+, Zn2+ and Cu2+ did not change the Bmax value of the binding activity, but significantly increased the Kd value. It was suggested that these cations inhibited the binding activity by reducing affinity of the 5-HT3 receptor for the antagonist, resulting in apparent inhibition of the binding activity. As to the binding association rate, Cd2+, Cu2+ and Zn2+ were found to have an inhibitory effect. The binding dissociation rate, however, was shown to be decreased by Cu2+ but not by Cd2+ and Zn2+. Furthermore, the Zn(2+)-induced inhibition of 3H-GR 65630 binding was suggested to be antagonized by both concanavalin A and wheatgerm agglutinin. The Cu(2+)-induced inhibition, however, was not influenced by these lectins, indicating that Cu2+ has a different lectin sensitivity for its inhibitory effect. The different mechanism of action between Cu2+ and Zn2+ was suggested in their inhibitory effect on the specific 3H-GR 65630 binding activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0197-0186
pubmed:author
pubmed:issnType
Print
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
259-66
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Differential effects of divalent cations on specific 3H-GR 65630 binding to 5-HT3 receptors in rat cortical membranes.
pubmed:affiliation
Department of Pharmacology, Hiroshima University School of Medicine, Japan.
pubmed:publicationType
Journal Article