Abstract |
125I-[Tyr2] scyllatoxin allowed to label a single class of high-affinity receptors in membranes from the human neuroblastoma cell line NB-OK 1. The Kd of these receptors was 60 pM for scyllatoxin ( Leiurotoxin I) and 20 pM for apamin and the Bmax was low (3.8 fmol/mg membrane protein). K+ increased toxin binding at low concentrations but exerted opposite effects at high concentrations. Ca2+, guanidinium and Na+ exerted only inhibitory effects on binding. Scyllatoxin binding sites were overexpressed 2.5-fold after a 24-h cell pretreatment with 2 mM butyrate. This effect was suppressed by cycloheximide.
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Authors | D Gossen, J C Gesquière, M Tastenoy, P De Neef, M Waelbroeck, J Christophe |
Journal | FEBS letters
(FEBS Lett)
Vol. 285
Issue 2
Pg. 271-4
(Jul 22 1991)
ISSN: 0014-5793 [Print] England |
PMID | 1855593
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Butyrates
- Guanidines
- Potassium Channels
- Receptors, Cholinergic
- Scorpion Venoms
- scyllatoxin receptor
- Butyric Acid
- leiurotoxin I
- Apamin
- Cycloheximide
- Sodium
- Guanidine
- Potassium
- Calcium
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Topics |
- Amino Acid Sequence
- Apamin
(antagonists & inhibitors, metabolism)
- Butyrates
(pharmacology)
- Butyric Acid
- Calcium
(metabolism)
- Cell Membrane
(metabolism)
- Cycloheximide
(pharmacology)
- Gene Expression Regulation
(drug effects)
- Guanidine
- Guanidines
(metabolism)
- Humans
- Kinetics
- Molecular Sequence Data
- Neuroblastoma
- Potassium
(metabolism)
- Potassium Channels
- Radioligand Assay
- Receptors, Cholinergic
(drug effects, metabolism)
- Scorpion Venoms
(metabolism)
- Sodium
(metabolism)
- Tumor Cells, Cultured
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