Disruption of the actin cytoskeleton abolishes high affinity 3H-glibenclamide binding in rat aortic rings

Naunyn-Schmiedeberg's Archives of Pharmacology

Volumn 357, Issue 2, 1998, Pages 183-185

  Löffler Walz, Cornelia ^a   Quast, Ulrich ^a  

^a UNIVERSITY OF TÜBINGEN   (Germany)

Author keywords

Actin filaments; Cytochalasin D; Cytoskeleton; Glibenclamide binding; Latrunculin B; P1075 binding; Phalloidin; Vascular sulphonylurea receptor

Indexed keywords

2 CYANO 1 (1,1 DIMETHYLPROPYL) 3 (3 PYRIDYL)GUANIDINE; ACTIN; CYTOCHALASIN D; GLIBENCLAMIDE; PHALLOIDIN; POTASSIUM CHANNEL; RADIOPHARMACEUTICAL AGENT; SULFONYLUREA DERIVATIVE;

ACTIN FILAMENT; ANIMAL TISSUE; AORTA; ARTICLE; BINDING AFFINITY; CYTOSKELETON; DRUG BINDING; NONHUMAN; RAT;

ACTINS; ADENOSINE TRIPHOSPHATE; ANIMALS; AORTA, THORACIC; BICYCLO COMPOUNDS, HETEROCYCLIC; CYTOCHALASIN D; CYTOSKELETON; GLYBURIDE; GUANIDINES; MALE; MUSCLE, SMOOTH, VASCULAR; NUCLEIC ACID SYNTHESIS INHIBITORS; PHALLOIDINE; POTASSIUM CHANNEL BLOCKERS; POTASSIUM CHANNELS; PYRIDINES; RATS; THIAZOLES; THIAZOLIDINES; VASODILATOR AGENTS;

EID: 0031931992     PISSN: 00281298     EISSN: None     Source Type: Journal    
DOI: 10.1007/PL00005153     Document Type: Article

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