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      Accelerating effects of blebbistatin on relaxation process of cell membrane permeabilized trachea and taenia cecum from guinea pig

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          Abstract

          Blebbistatin, a potent inhibitor of myosin II, is known to suppress smooth muscle contraction without affecting myosin light chain phosphorylation level. In order to clarify the regulatory mechanisms of blebbistatin on phasic and tonic smooth muscles in detail, we examined the effects of blebbistatin on relaxation process by Ca 2+ removal after Ca 2+-induced contraction of β-escin skinned (cell membrane permeabilized) trachea and taenia cecum preparations from guinea pigs. Blebbistatin significantly suppressed the force during relaxation both in skinned trachea and taenia cecum. The data fitting analysis of the relaxation processes indicates that blebbistatin accelerates slow (latch-like) bridge dissociation.

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          Mechanism of blebbistatin inhibition of myosin II.

          Mihály Kovács, Judit Tóth, Csaba Hetényi … (2004)
          Blebbistatin is a recently discovered small molecule inhibitor showing high affinity and selectivity toward myosin II. Here we report a detailed investigation of its mechanism of inhibition. Blebbistatin does not compete with nucleotide binding to the skeletal muscle myosin subfragment-1. The inhibitor preferentially binds to the ATPase intermediate with ADP and phosphate bound at the active site, and it slows down phosphate release. Blebbistatin interferes neither with binding of myosin to actin nor with ATP-induced actomyosin dissociation. Instead, it blocks the myosin heads in a products complex with low actin affinity. Blind docking molecular simulations indicate that the productive blebbistatin-binding site of the myosin head is within the aqueous cavity between the nucleotide pocket and the cleft of the actin-binding interface. The property that blebbistatin blocks myosin II in an actin-detached state makes the compound useful both in muscle physiology and in exploring the cellular function of cytoplasmic myosin II isoforms, whereas the stabilization of a specific myosin intermediate confers a great potential in structural studies.
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            Specificity of blebbistatin, an inhibitor of myosin II.

            John Limouze, Aaron F. Straight, James R. Sellers … (2003)
            Blebbistatin is a small molecule inhibitor discovered in a screen for inhibitors of nonmuscle myosin IIA. We have examined the specificity and potency of the drug by assaying its effects on the actin-activated MgATPase assay of diverse members of the myosin superfamily. Blebbistatin potently inhibits several striated muscle myosins as well as vertebrate nonmuscle myosin IIA and IIB with IC50 values ranging from 0.5 to 5 microM. Interestingly, smooth muscle which is highly homologous to vertebrate nonmuscle myosin is only poorly inhibited (IC50=80 microM). The drug potently inhibits Dictyostelium myosin II, but poorly inhibits Acanthamoeba myosin II. Blebbistatin did not inhibit representative myosin superfamily members from classes I, V, and X.
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              Myosin phosphorylation and the cross-bridge cycle in arterial smooth muscle.

              P F Dillon, M O Aksoy, S P Driska … (1981)
              Phosphorylation of the 20,000-dalton light chain of myosin is closely correlated with cross-bridge cycling in arterial smooth muscle. Evidence is presented that dephosphorylation can produce an attached, noncycling cross-bridge (latch-bridge) which is responsible for the high economy of force maintenance in this tissue.
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                Author and article information

                Journal
                Journal ID (nlm-ta): J Smooth Muscle Res
                Journal ID (iso-abbrev): J Smooth Muscle Res
                Journal ID (publisher-id): JSMR
                Title: Journal of Smooth Muscle Research
                Publisher: Japan Society of Smooth Muscle Research
                ISSN (Print): 0916-8737
                ISSN (Electronic): 1884-8796
                Publication date (Electronic): 28 April 2020
                Publication date (Print): 2020
                Volume: 56
                Pages: 19-28
                Affiliations
                [1]Department of Frontier Health Sciences, Graduate School of Human Health Sciences, Tokyo Metropolitan University, 7-2-10 Higashiogu, Arakawa-ku, Tokyo 116-8551, Japan
                Author notes
                Corresponding author: Masaru Watanabe, MD, PhD, Department of Frontier Health Sciences, Graduate School of Human Health Sciences, Tokyo Metropolitan University, 7-2-10 Higashiogu, Arakawa-ku, Tokyo 116-8551, JapanE-mail: masaru@ 123456tmu.ac.jp
                Article
                Publisher ID: 0509
                DOI: 10.1540/jsmr.56.19
                PMC ID: 7184228
                PubMed ID: 32350168
                SO-VID: 44d6d55e-ec03-4205-848d-01e1c932ddec
                Copyright © ©2020 The Japan Society of Smooth Muscle Research
                License:

                This is an open-access article distributed under the terms of the Creative Commons Attribution Non-Commercial No Derivatives (by-nc-nd) License. (CC-BY-NC-ND 4.0: http://creativecommons.org/licenses/by-nc-nd/4.0/ ).

                History
                Date received : 15 January 2020
                Date accepted : 12 March 2020
                Categories
                Subject: Original

                Keywords: blebbistatin,skinned preparation,relaxation,latch
                Data availability:
                Keywords: blebbistatin, skinned preparation, relaxation, latch

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