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Author Wolfgang, Nörenberg ♦ Hofmann, Fred ♦ Illes, Peter ♦ Klaus, Aktories ♦ Meyer, Dieter K.
Source PubMed Central
Content type Text
File Format PDF
Date Created 2005-01-28
Copyright Year ©1999
Language English
Difficulty Level Medium
Subject Domain (in DDC) Technology ♦ Medicine & health
Subject Keyword Pharmacology
Abstract Actin filament (F-actin) depolymerization leads to the use-dependent rundown of N-methyl-D-aspartate (NMDA) receptor activity in rat hippocampal neurones. Depolymerization is promoted by Ca2+ which enters the cells via NMDA receptor channels. The ras homologue (Rho) GTPases (RhoA, Rac1 and Cdc42) promote actin polymerization and thus control the actin cytoskeleton. We have investigated, by means of the whole-cell patch clamp technique, whether the actin fibres which interact with NMDA receptors are controlled by Rho GTPases. In the presence of intracellular ATP which attenuates rundown, the C3 toxin from Clostridium (C.) botulinum was used to inactivate RhoA. Indeed, it enhanced the use-dependent rundown of NMDA-evoked inward currents to a level similar to that obtained in the absence of ATP. Lethal toxin from Clostridium sordellii which inactivates Rac1 and Cdc42 lacked this effect. We suggest that the function of somatodendritic NMDA receptor channels in rat hippocampal neurones can be modulated by RhoA via its action on F-actin.
ISSN 00071188
Age Range above 22 year
Educational Use Research
Interactivity Type Expositive
Education Level UG and PG
Learning Resource Type Article
Publisher Date 1999-07-01
Journal British Journal of Pharmacology
Volume Number 127
Issue Number 5
Page Count 4
Starting Page 1060
Ending Page 1063

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Source: PubMed Central