Publication
Title
-mediated binding of serotonin and dopamine to skeletal muscle actin: resemblance to "serotonin binding proteins"
Author
Abstract
Fe2+ stimulates the binding of [H-3]serotonin and [H-3]dopamine to rabbit skeletal muscle actin. This binding is inhibited by reducing agents (sodium ascorbate, vitamin E), by superoxide dismutase and by sulfhydryl group-modifying reagents (N-ethylmaleimide, 2,2'-dinitro-5,5'-dithiobenzoic acid). The effect of Fe2+ is mimicked by oxidants (sodium periodate, potassium nitroso-disulfonate) and by superoxide radicals. Once formed, the binding cannot be decreased by a large excess of monoamine. It is proposed that Fe2+ catalyses the autoxidation of the monoamines by generating oxygen free radicals, and the oxidation products are likely to bind covalently to exposed cysteine residues of actin. Digestion of [H-3]dopamine-labelled actin by cyanogen bromide and then by V8 protease(EC3.4.21.19) yields two labelled peptides whose apparent molecular weights (4.1 and 1.2 kDa) are compatible with the labelling of cysteine-10 and -374. Fe2+ also inactivates some of the binding sites of actin. This inactivation, and the covalent nature of the binding precludes the interpretation of monoamine saturation and competition binding data in terms of reversible bimolecular interactions.
Language
English
Source (journal)
European journal of pharmacology: molecular pharmacology section. - Amsterdam
Publication
Amsterdam : 1995
ISSN
0922-4106
Volume/pages
288:2(1995), p. 209-218
ISI
A1995QC87800011
Full text (Publisher's DOI)
Full text (publisher's version - intranet only)
UAntwerpen
Faculty/Department
Research group
Publication type
Subject
Affiliation
Publications with a UAntwerp address
External links
Web of Science
Record
Identification
Creation 08.10.2008
Last edited 09.08.2017
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