NDLI: Centruroides toxin, a selective blocker of surface Na+ channels in skeletal muscle: voltage-clamp analysis and biochemical characterization of the receptor.

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Centruroides toxin, a selective blocker of surface Na+ channels in skeletal muscle: voltage-clamp analysis and biochemical characterization of the receptor.

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Centruroides toxin, a selective blocker of surface Na+ channels in skeletal muscle: voltage-clamp analysis and biochemical characterization of the receptor.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Rougier, O. Ildefonse, M. Barhanin, J. Lazdunski, M. Jaimovich, E.
Abstract	This paper describes the effects of a toxin from the scorpion Centruroides suffusus suffusus on frog skeletal muscle. The main findings are the following, (i) Centruroides toxin (CssII) blocks the early phase of the inward sodium current in the muscle that arises from influx via Na+ channels in the surface membrane, but it does not affect the late phase of the inward current that represents flux through Na+ channels in the T-tubule membranes, (ii) CssII, in marked contrast to tetrodotoxin, does not affect contraction of the muscle, (iii) Measurements of the binding of 125I-labeled CssII to a partially purified membrane preparation from the muscle indicate that the Kd of the CssII--receptor complex is approximately 0.4 nM. The half-life for the dissociation of this complex is 3 min at 22 degrees C and 16 min at 2 degrees C. Binding of the radiolabeled toxin varies markedly with pH and becomes insignificant at pH greater than 8.5. Proteolytic digestion of the membrane preparation decreases its ability to bind CssII, suggesting that the receptor is a protein. (iv) The number of binding sites for a radiolabeled derivative of tetrodotoxin on the membrane preparation was similar to that for CssII. However, neither tetrodotoxin nor any of seven other neurotoxins and some local anesthetics that alter the functioning of the Na+ channel have any effect on the binding of CssII to the muscle membrane. These results therefore indicate that CssII belongs to a different class of neurotoxins that has a different receptor on the Na+ channel.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	12
Volume Number	79
Language	English
Publisher	National Academy of Sciences
Publisher Date	1982-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Ion Channels Drug Effects Muscles Neurotoxins Pharmacology Scorpion Venoms Animals Hydrogen-Ion Concentration In Vitro Techniques Muscle Contraction Peptide Hydrolases Metabolism Rana Esculenta Sarcolemma Tetrodotoxin Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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