Linked Life Data

2826992

Source:http://linkedlifedata.com/resource/pubmed/id/2826992

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1988-1-25
pubmed:abstractText
Regulation of the appearance of dihydropyridine-binding sites was studied in primary cultures of chick myotubes. Labeling of surface dihydropyridine-binding sites on intact myotubes at 37 degrees was achieved with (+)-[3H]PN 200-110. The appearance of the sites was prevented in a calcium-free medium using 1.8 mM EGTA, in accordance with the presumed Ca2+ dependency of the appearance of dihydropyridine-binding sites in skeletal muscle cells. Chronic treatment of myotubes with isoproterenol or various other drugs did not modulate either the Bmax or Kd value of the (+)-[3H]PN 200-110 binding to the membrane preparation of treated myotubes (control values were: Kd = 0.16 nm, Bmax = 556 fmol/mg of protein), suggesting a lack of heterologous regulation via beta-adrenergic receptor stimulation. However, depolarization of intact myotubes, either by 47 mM K+ or 10(-5) M veratridine, provoked a 3-fold increase in the Bmax value of (+)-[3H]PN 200-110 binding measured on the intact muscle cells without affecting the Kd value. The effect was reversed upon repolarization of the cells. Depolarizing conditions did not affect the binding on a membrane preparation of the myotubes. Hence, depolarization appeared to specifically trigger the appearance of (+)-[3H]PN 200-110 binding sites on intact myotubes; several hypotheses which could explain the involved mechanism are discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0026-895X
pubmed:author
pubmed:issnType
Print
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
785-91
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Depolarization of chick myotubes triggers the appearance of (+)-[3H]PN 200-110-binding sites.
pubmed:affiliation
Department of Biochemical Pharmacology, Janssen Research Foundation, Beerse, Belgium.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't