A small-molecule inhibitor of skeletal muscle myosin II View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2002-01

AUTHORS

A Cheung, J A Dantzig, S Hollingworth, S M Baylor, Y E Goldman, T J Mitchison, A F Straight

ABSTRACT

We screened a small-molecule library for inhibitors of rabbit muscle myosin II subfragment 1 (S1) actin-stimulated ATPase activity. The best inhibitor, N-benzyl-p-toluene sulphonamide (BTS), an aryl sulphonamide, inhibited the Ca2+-stimulated S1 ATPase, and reversibly blocked gliding motility. Although BTS does not compete for the nucleotide-binding site of myosin, it weakens myosin's interaction with F-actin. BTS reversibly suppressed force production in skinned skeletal muscle fibres from rabbit and frog skin at micromolar concentrations. BTS suppressed twitch production of intact frog fibres with minimum alteration of Ca2+ metabolism. BTS is remarkably specific, as it was much less effective in suppressing contraction in rat myocardial or rabbit slow-twitch muscle, and did not inhibit platelet myosin II. The isolation of BTS and the recently discovered Eg5 kinesin inhibitor, monastrol, suggests that motor proteins may be potential targets for therapeutic applications. More... »

PAGES

83-88

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ncb734

DOI

http://dx.doi.org/10.1038/ncb734

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1020039813

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/11744924


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