Evidence map›Paper›PMID 24918754›Full record

ArticlePloS one2014

Definite differences between in vitro actin-myosin sliding and muscle contraction as revealed using antibodies to myosin head.

Haruo Sugi, Shigeru Chaen, Takakazu Kobayashi, Takahiro Abe, Kazushige Kimura, Yasutake Saeki, Yoshiki Ohnuki, Takuya Miyakawa, Masaru Tanokura, Seiryo Sugiura

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.2field-weighted citation impact, top 20% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

5 citing papers in PubMed, 13 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 5 institutions in 1 country.

Haruo SugiDepartment of Physiology, School of Medicine, Teikyo University, Tokyo, Japan.
Shigeru ChaenDepartment of Integrated Sciences in Physics and Biology, College of Humanities and Sciences, Nihon University, Tokyo, Japan.
Takakazu KobayashiDepartment of Electronic Engineering, Shibaura Institute of Technology, Tokyo, Japan.
Takahiro AbeDepartment of Electronic Engineering, Shibaura Institute of Technology, Tokyo, Japan.
Kazushige KimuraDepartment of Electronic Engineering, Shibaura Institute of Technology, Tokyo, Japan.
Yasutake SaekiDepartment of Physiology, School of Dentistry, Tsurumi University, Yokohama, Japan.
Yoshiki OhnukiDepartment of Physiology, School of Dentistry, Tsurumi University, Yokohama, Japan.
Takuya MiyakawaDepartment of Applied Biochemistry, Graduate School of Agriculture and Life Sciences, University of Tokyo, Tokyo, Japan.
Masaru TanokuraDepartment of Applied Biochemistry, Graduate School of Agriculture and Life Sciences, University of Tokyo, Tokyo, Japan.
Seiryo SugiuraGraduate School of Frontier Sciences, University of Tokyo, Tokyo, Japan.
Shibaura Institute of Technology · JPThe University of Tokyo · JPTsurumi University · JPNihon University · JPTeikyo University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Muscle contraction results from attachment-detachment cycles between myosin heads extending from myosin filaments and actin filaments. It is generally believed that a myosin head first attaches to actin, undergoes conformational changes to produce force and motion in muscle, and then detaches from actin. Despite extensive studies, the molecular mechanism of myosin head conformational changes still remains to be a matter for debate and speculation. The myosin head consists of catalytic (CAD), converter (CVD) and lever arm (LD) domains. To give information about the role of these domains in the myosin head performance, we have examined the effect of three site-directed antibodies to the myosin head on in vitro ATP-dependent actin-myosin sliding and Ca2+-activated contraction of muscle fibers. Antibody 1, attaching to junctional peptide between 50K and 20K heavy chain segments in the CAD, exhibited appreciable effects neither on in vitro actin-myosin sliding nor muscle fiber contraction. Since antibody 1 covers actin-binding sites of the CAD, one interpretation of this result is that rigor actin-myosin linkage is absent or at most a transient intermediate in physiological actin-myosin cycling. Antibody 2, attaching to reactive lysine residue in the CVD, showed a marked inhibitory effect on in vitro actin-myosin sliding without changing actin-activated myosin head (S1) ATPase activity, while it showed no appreciable effect on muscle contraction. Antibody 3, attaching to two peptides of regulatory light chains in the LD, had no significant effect on in vitro actin-myosin sliding, while it reduced force development in muscle fibers without changing MgATPase activity. The above definite differences in the effect of antibodies 2 and 3 between in vitro actin-myosin sliding and muscle contraction can be explained by difference in experimental conditions; in the former, myosin heads are randomly oriented on a glass surface, while in the latter myosin heads are regularly arranged within filament-lattice structures.

Indexed as

Muscle ContractionActin CytoskeletonActinsAdenosine TriphosphatasesAdenosine TriphosphateAnimalsAntibodies, MonoclonalBinding SitesCalciumMagnesiumMotionMuscle Fibers, SkeletalMyosinsProtein Structure, TertiaryRabbitsActinsAdenosine TriphosphatasesAdenosine TriphosphateAntibodies, MonoclonalCalciumMagnesiumMyosins

Identifiers

PMID24918754
PMCPMC4053314
OpenAlexW2005169356

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.