Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1989-11-7
pubmed:abstractText
Treatment of human placental brush-border membrane vesicles with tyrosyl group-specific reagents, N-acetylimidazole, 7-chloro-4-nitrobenzo-2-oxa-1,3,-diazole and tetranitromethane, inhibited NaCl gradient-driven serotonin uptake in these vesicles without affecting vesicle integrity. The concentrations of these reagents causing 50% inhibition of serotonin uptake were 3.75 mM, 10 microM and 5 microM, respectively. The inhibition of N-acetylimidazole was reversible with hydroxylamine and the inhibition by 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole was reversible with 2-mercaptoethanol. Kinetic analysis of serotonin uptake in control and in N-acetylimidazole-treated membrane vesicles revealed that the treatment decreased the maximal velocity of the transport system with virtually no effect on the affinity of the transporter for serotonin. Similarly, the treatment did not change the affinity of the transporter for Na+. Even though serotonin uptake was reduced in treated vesicles compared with control vesicles at all concentrations of Na+, in both cases the dependence of the uptake rate on Na+ concentration was hyperbolic, indicating the involvement of one Na+ per transport of one serotonin molecule. The serotonin transporter could be protected from the N-acetylimidazole-induced inhibition by Na+. It is concluded that tyrosyl residues are essential for optimal transport function of the human placental serotonin transporter and that these critical tyrosyl residues are located at or near the Na+-binding site.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0022-3565
pubmed:author
pubmed:issnType
Print
pubmed:volume
251
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9-15
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Inactivation of the human placental serotonin transporter by tyrosyl group-specific reagents.
pubmed:affiliation
Department of Cell and Molecular Biology, Medical College of Georgia, Augusta.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S.