Myofibre hyper-contractility in horses expressing the myosin heavy chain myopathy mutation, myh1e321g

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Standard

Myofibre hyper-contractility in horses expressing the myosin heavy chain myopathy mutation, myh1e321g. / Ochala, Julien; Finno, Carrie J.; Valberg, Stephanie J.

I: Cells, Bind 10, Nr. 12, 3428, 2021.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Ochala, J, Finno, CJ & Valberg, SJ 2021, 'Myofibre hyper-contractility in horses expressing the myosin heavy chain myopathy mutation, myh1e321g', Cells, bind 10, nr. 12, 3428. https://doi.org/10.3390/cells10123428

APA

Ochala, J., Finno, C. J., & Valberg, S. J. (2021). Myofibre hyper-contractility in horses expressing the myosin heavy chain myopathy mutation, myh1e321g. Cells, 10(12), [3428]. https://doi.org/10.3390/cells10123428

Vancouver

Ochala J, Finno CJ, Valberg SJ. Myofibre hyper-contractility in horses expressing the myosin heavy chain myopathy mutation, myh1e321g. Cells. 2021;10(12). 3428. https://doi.org/10.3390/cells10123428

Author

Ochala, Julien ; Finno, Carrie J. ; Valberg, Stephanie J. / Myofibre hyper-contractility in horses expressing the myosin heavy chain myopathy mutation, myh1e321g. I: Cells. 2021 ; Bind 10, Nr. 12.

Bibtex

@article{2e79a297811b456e9f56d6a12d154a32,
title = "Myofibre hyper-contractility in horses expressing the myosin heavy chain myopathy mutation, myh1e321g",
abstract = "Myosinopathies are defined as a group of muscle disorders characterized by mutations in genes encoding myosin heavy chains. Their exact molecular and cellular mechanisms remain unclear. In the present study, we have focused our attention on a MYH1-related E321G amino acid substitution within the head region of the type IIx skeletal myosin heavy chain, associated with clinical signs of atrophy, inflammation and/or profound rhabdomyolysis, known as equine myosin heavy chain myopathy. We performed Mant-ATP chase experiments together with force measurements on isolated IIx myofibres from control horses (MYH1E321G−/− ) and Quarter Horses homozygous (MYH1E321G+/+ ) or heterozygous (MYH1E321G+/− ) for the E321G mutation. The single residue replacement did not affect the relaxed conformations of myosin molecules. Nevertheless, it significantly increased its active behaviour as proven by the higher maximal force production and Ca2+ sensitivity for MYH1E321G+/+ in comparison with MYH1E321G+/− and MYH1E321G−/− horses. Altogether, these findings indicate that, in the presence of the E321G mutation, a molecular and cellular hyper-contractile phenotype occurs which could contribute to the development of the myosin heavy chain myopathy.",
keywords = "Congenital myopathy, Inflammation, Mechanics, Muscle fibre, MYH1, Myosin",
author = "Julien Ochala and Finno, {Carrie J.} and Valberg, {Stephanie J.}",
note = "Publisher Copyright: {\textcopyright} 2021 by the authors. Licensee MDPI, Basel, Switzerland.",
year = "2021",
doi = "10.3390/cells10123428",
language = "English",
volume = "10",
journal = "Cells",
issn = "2073-4409",
publisher = "MDPI AG",
number = "12",

}

RIS

TY - JOUR

T1 - Myofibre hyper-contractility in horses expressing the myosin heavy chain myopathy mutation, myh1e321g

AU - Ochala, Julien

AU - Finno, Carrie J.

AU - Valberg, Stephanie J.

N1 - Publisher Copyright: © 2021 by the authors. Licensee MDPI, Basel, Switzerland.

PY - 2021

Y1 - 2021

N2 - Myosinopathies are defined as a group of muscle disorders characterized by mutations in genes encoding myosin heavy chains. Their exact molecular and cellular mechanisms remain unclear. In the present study, we have focused our attention on a MYH1-related E321G amino acid substitution within the head region of the type IIx skeletal myosin heavy chain, associated with clinical signs of atrophy, inflammation and/or profound rhabdomyolysis, known as equine myosin heavy chain myopathy. We performed Mant-ATP chase experiments together with force measurements on isolated IIx myofibres from control horses (MYH1E321G−/− ) and Quarter Horses homozygous (MYH1E321G+/+ ) or heterozygous (MYH1E321G+/− ) for the E321G mutation. The single residue replacement did not affect the relaxed conformations of myosin molecules. Nevertheless, it significantly increased its active behaviour as proven by the higher maximal force production and Ca2+ sensitivity for MYH1E321G+/+ in comparison with MYH1E321G+/− and MYH1E321G−/− horses. Altogether, these findings indicate that, in the presence of the E321G mutation, a molecular and cellular hyper-contractile phenotype occurs which could contribute to the development of the myosin heavy chain myopathy.

AB - Myosinopathies are defined as a group of muscle disorders characterized by mutations in genes encoding myosin heavy chains. Their exact molecular and cellular mechanisms remain unclear. In the present study, we have focused our attention on a MYH1-related E321G amino acid substitution within the head region of the type IIx skeletal myosin heavy chain, associated with clinical signs of atrophy, inflammation and/or profound rhabdomyolysis, known as equine myosin heavy chain myopathy. We performed Mant-ATP chase experiments together with force measurements on isolated IIx myofibres from control horses (MYH1E321G−/− ) and Quarter Horses homozygous (MYH1E321G+/+ ) or heterozygous (MYH1E321G+/− ) for the E321G mutation. The single residue replacement did not affect the relaxed conformations of myosin molecules. Nevertheless, it significantly increased its active behaviour as proven by the higher maximal force production and Ca2+ sensitivity for MYH1E321G+/+ in comparison with MYH1E321G+/− and MYH1E321G−/− horses. Altogether, these findings indicate that, in the presence of the E321G mutation, a molecular and cellular hyper-contractile phenotype occurs which could contribute to the development of the myosin heavy chain myopathy.

KW - Congenital myopathy

KW - Inflammation

KW - Mechanics

KW - Muscle fibre

KW - MYH1

KW - Myosin

U2 - 10.3390/cells10123428

DO - 10.3390/cells10123428

M3 - Journal article

C2 - 34943936

AN - SCOPUS:85120617984

VL - 10

JO - Cells

JF - Cells

SN - 2073-4409

IS - 12

M1 - 3428

ER -

ID: 288852829