Linked Life Data

3121365

Source:http://linkedlifedata.com/resource/pubmed/id/3121365

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1988-2-2
pubmed:abstractText
The kinetic and pharmacological profiles of the potent and selective D-2 dopamine agonist 2-(N-propyl-N-2-thienylethylamino)-5-hydroxytetralin ([3H]N-0437) have recently been described. This report concerns the effects of chemical lesions and metal ions on the radioreceptor binding of [3H]N-0437. Kainic acid lesions reduced the maximum number of binding sites (Bmax) in the rat striatum by 50%. The affinity of [3H]N-0437 for dopamine receptors was reduced by half. 6-Hydroxydopamine lesions had no measurable effect on the Bmax or on the KD. Of the physiological metal ions tested only Na+ had a significant effect on the binding. Sodium ions reduced the affinity of [3H]N-0437 for striatal receptors from 5.0 +/- 1.1 nM to 8.4 +/- 0.3 nM. In addition GTP lowered the Bmax from 1121 +/- 44 to 868 +/- 84 fmol/mg protein. The trace ions Li+ and Mn2+ had no effect at a concentration of 3.0 mM, while the exogenous ion Hg2+ at the same concentration prevented the specific binding of [3H]N-0437. Together, the results suggest that [3H]N-0437 labels both pre- and postsynaptic receptors, although postsynaptic receptors are labelled preferentially. Moreover, there is an indication that GTP shifts the affinity state of the D-2 receptor from high to low, while Na+ seems to be an allosteric inhibitor.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0014-2999
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
143
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
101-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
The effects of kainic acid and 6-hydroxydopamine lesions, metal ions and GTP on in vitro binding of the D-2 dopamine agonist, [3H]N-0437, to striatal membranes.
pubmed:affiliation
Department of Medicinal Chemistry, State University of Groningen, The Netherlands.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't