Myosin Heavy Chain

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Sam J Mathew - One of the best experts on this subject based on the ideXlab platform.

  • Myosin Heavy Chain embryonic regulates skeletal muscle differentiation during mammalian development
    Development, 2020
    Co-Authors: Megha Agarwal, Akashi Sharma, Anushree Bharadwaj, Masum Saini, Sam J Mathew, Gabrielle Kardon, Pankaj Kumar, Amit Kumar
    Abstract:

    Myosin Heavy Chain-embryonic (MyHC-emb) is a skeletal muscle-specific contractile protein expressed during muscle development. Mutations in MYH3, the gene encoding MyHC-emb, lead to Freeman-Sheldon and Sheldon-Hall congenital contracture syndromes. Here, we characterize the role of MyHC-emb during mammalian development using targeted mouse alleles. Germline loss of MyHC-emb leads to neonatal and postnatal alterations in muscle fiber size, fiber number, fiber type and misregulation of genes involved in muscle differentiation. Deletion of Myh3 during embryonic myogenesis leads to the depletion of the myogenic progenitor cell pool and an increase in the myoblast pool, whereas fetal myogenesis-specific deletion of Myh3 causes the depletion of both myogenic progenitor and myoblast pools. We reveal that the non-cell-autonomous effect of MyHC-emb on myogenic progenitors and myoblasts is mediated by the fibroblast growth factor (FGF) signaling pathway, and exogenous FGF rescues the myogenic differentiation defects upon loss of MyHC-emb function in vitro Adult Myh3 null mice exhibit scoliosis, a characteristic phenotype exhibited by individuals with Freeman-Sheldon and Sheldon-Hall congenital contracture syndrome. Thus, we have identified MyHC-emb as a crucial myogenic regulator during development, performing dual cell-autonomous and non-cell-autonomous functions.This article has an associated 'The people behind the papers' interview.

  • Myosin Heavy Chain embryonic regulates skeletal muscle differentiation during mammalian development
    Development, 2020
    Co-Authors: Megha Agarwal, Akashi Sharma, Anushree Bharadwaj, Masum Saini, Sam J Mathew, Gabrielle Kardon, Pankaj Kumar, Amit Kumar
    Abstract:

    Myosin Heavy Chain-embryonic (MyHC-emb) is a skeletal muscle specific contractile protein expressed during muscle development. Mutations in MYH3, the gene encoding MyHC-emb leads to Freeman-Sheldon and Sheldon-Hall congenital contracture syndromes. Here, we characterize the role of MyHC-emb during mammalian development using targeted mouse alleles. Germline loss-of MyHC-emb leads to neonatal and postnatal alterations in muscle fiber size, fiber number, fiber type and mis-regulation of genes involved in muscle differentiation. Deletion of Myh3 during embryonic myogenesis leads to depletion of the myogenic progenitor cell pool and increase in the myoblast pool while fetal myogenesis-specific deletion of Myh3 causes depletion of both myogenic progenitor and myoblast pools. We uncover that the non-cell autonomous effect of MyHC-emb on myogenic progenitors and myoblasts are mediated by the fibroblast growth factor (FGF) signaling pathway and exogenous FGF rescues the myogenic differentiation defects upon loss of MyHC-emb function in vitro. Adult Myh3 null mice exhibit scoliosis, a characteristic phenotype exhibited by Freeman-Sheldon and Sheldon-Hall congenital contracture syndrome patients. Thus, we have identified MyHC-emb as a crucial myogenic regulator during development, performing dual cell autonomous and non-cell autonomous functions.

Robert J. Talmadge - One of the best experts on this subject based on the ideXlab platform.

  • enhanced protein electrophoresis technique for separating human skeletal muscle Myosin Heavy Chain isoforms
    Electrophoresis, 1999
    Co-Authors: Marcas M Bamman, Robert J. Talmadge, Mark S F Clarke, Daniel L Feeback
    Abstract:

    Talmadge and Roy (J. Appl. Physiol. 1993, 75, 2337-2340) previously established a sodium dodecyl sulfate - polyacrylamide gel electrophoresis (SDS-PAGE) protocol for separating all four rat skeletal muscle Myosin Heavy Chain (MHC) isoforms (MHC I, IIa, IIx, IIb); however, when applied to human muscle, the type II MHC isoforms (Ila, IIx) are not clearly distinguished. In this brief paper we describe a modification of the SDS-PAGE protocol which yields distinct and consistent separation of all three adult human MHC isoforms (MHC I, IIa, IIx) in a minigel system. MHC specificity of each band was confirmed by Western blot using three monoclonal IgG antibodies (mAbs) immunoreactive against MHCI (mAb MHCs, Novacastra Laboratories), MHCI+IIa (mAb BF-35), and MHCIIa+IIx (mAb SC-71). Results provide a valuable SDS-PAGE minigel technique for separating MHC isoforms in human muscle without the difficult task of casting gradient gels.

  • electrophoretic separation of rat skeletal muscle Myosin Heavy Chain isoforms
    Journal of Applied Physiology, 1993
    Co-Authors: Robert J. Talmadge
    Abstract:

    A new technique for the sodium dodecyl sulfate-polyacrylamide gel electrophoretic separation of rat skeletal muscle Myosin Heavy-Chain (MHC) isoforms is presented. This technique allows for the sep...

  • electrophoretic separation of rat skeletal muscle Myosin Heavy Chain isoforms
    Journal of Applied Physiology, 1993
    Co-Authors: Robert J. Talmadge, Roland R Roy
    Abstract:

    A new technique for the sodium dodecyl sulfate-polyacrylamide gel electrophoretic separation of rat skeletal muscle Myosin Heavy-Chain (MHC) isoforms is presented. This technique allows for the separation of the four identified MHC isoforms known to be present in adult rat skeletal muscle. These types of MHC are commonly called I, IIa, IIx or IId, and IIb. The procedure can be performed using minigel electrophoresis systems and does not involve preparation of gradient-separating gels or the use of special cooling devices. The procedure accommodates both silver and Coomasie Blue staining. Thus the procedure is simple to perform and highly repeatable, providing high-resolution separation of MHC protein isoforms. The percent composition of the four adult MHCs in rat soleus, medial gastrocnemius, diaphragm, and levator ani muscles by use of this procedure and Coomasie Blue staining is similar to that previously reported. This new technique provides a novel and easy-to-perform method for the separation of rat skeletal muscle MHC isoforms.

Larseric Thornell - One of the best experts on this subject based on the ideXlab platform.

  • Pedrosa-Domellof F. Myosin Heavy Chain isoforms in human extraocular muscles. Invest Ophthalmol Vis Sci
    2013
    Co-Authors: Daniel Kjellgren, Larseric Thornell, Jesper Andersen, Fatima Pedrosa-domellöf
    Abstract:

    PURPOSE. To investigate the Myosin Heavy Chain (MyHC) composition of human extraocular (EOM) and levator palpebrae (LP) muscle fibers. METHODS. Adult human EOMs and LP were studied with SDS-PAGE, immunoblots, and immunocytochemistry, with antibodies against six MyHC isoforms. Myofibrillar adenosine triphosphatase (mATPase) and reduced nicotinamide adenine dinucleotide (NADH)-TR activity and fiber area were also determined. RESULTS. Most of the fibers in both layers stained strongly with anti-MyHCIIa. Approximately 14 % of the fibers in the global layer and 16 % in the orbital layer were labeled with anti-MyHCI. The remaining 24 % of the fibers in the global layer and 3 % in the orbital layer were not stained with either of these two antibodies, but were reactive to anti-MyHCeom (MyHCeom pos /MyHCIIa neg fibers). The fibers stained with anti

  • fiber content and Myosin Heavy Chain composition of muscle spindles in aged human biceps brachii
    Journal of Histochemistry and Cytochemistry, 2005
    Co-Authors: Jingxia Liu, Perolof Eriksson, Larseric Thornell, Fatima Pedrosadomellof
    Abstract:

    The present study investigated potential age-related changes in human muscle spindles with respect to the intrafusal fiber-type content and Myosin Heavy Chain (MyHC) composition in biceps brachii m ...

  • Myosin Heavy Chain iia gene mutation e706k is pathogenic and its expression increases with age
    Neurology, 2002
    Co-Authors: Homa Tajsharghi, Larseric Thornell, Niklas Darin, Tommy Martinsson, Marten Kyllerman, J Wahlstrom, Anders Oldfors
    Abstract:

    BACKGROUND: The authors recently described a new autosomal dominant myopathy (OMIM 605637 inclusion body myopathy 3) associated with a missense mutation in the Myosin Heavy Chain (MyHC) IIa gene (M ...

  • Myosin Heavy Chain composition of muscle spindles in human biceps brachii
    Journal of Histochemistry and Cytochemistry, 2002
    Co-Authors: Jingxia Liu, Perolof Eriksson, Larseric Thornell, Fatima Pedrosadomellof
    Abstract:

    Data on the Myosin Heavy Chain (MyHC) composition of human muscle spindles are scarce in spite of the well-known correlation between MyHC composition and functional properties of skeletal muscle fibers. The MyHC composition of intrafusal fibers from 36 spindles of human biceps brachii muscle was studied in detail by immunocytochemistry with a large battery of antibodies. The MyHC content of isolated muscle spindles was assessed with SDS-PAGE and immunoblots. Four major MyHC isoforms (MyHCI, IIa, embryonic, and intrafusal) were detected with SDS-PAGE. Immunocytochemistry revealed very complex staining patterns for each intrafusal fiber type. The bag(1) fibers contained slow tonic MyHC along their entire fiber length and MyHCI, alpha-cardiac, embryonic, and fetal isoforms along a variable part of their length. The bag(2) fibers contained MyHC slow tonic, I, alpha-cardiac, embryonic, and fetal isoforms with regional variations. Chain fibers contained MyHCIIa, embryonic, and fetal isoforms throughout the fiber, and MyHCIIx at least in the juxtaequatorial region. Virtually each muscle spindle had a different allotment of numbers of bag(1), bag(2) and Chain fibers. Taken together, the complexity in intrafusal fiber content and MyHC composition observed indicate that each muscle spindle in the human biceps has a unique identity.

  • Myosin Heavy Chain composition of muscle spindles in human biceps brachii
    Histochemistry and Cell Biology, 2002
    Co-Authors: Jingxia Liu, Perolof Eriksson, Larseric Thornell, Fatima Pedrosadomellof
    Abstract:

    Data on the Myosin Heavy Chain (MyHC) composition of human muscle spindles are scarce in spite of the well-known correlation between MyHC composition and functional properties of skeletal muscle fi ...

Roland R Roy - One of the best experts on this subject based on the ideXlab platform.

  • myonuclear number and Myosin Heavy Chain expression in rat soleus single muscle fibers after spaceflight
    Journal of Applied Physiology, 1996
    Co-Authors: David L Allen, Roland R Roy, W Yasui, T Tanaka, Yoshinobu Ohira, Shunji Nagaoka, Chiharu Sekiguchi, W E Hinds, V R Edgerton
    Abstract:

    The effects of 14 days of spaceflight on myonuclear number, fiber size, and Myosin Heavy Chain (MHC) expression in isolated rat soleus muscle fiber segments were studied. Single soleus muscle fiber...

  • electrophoretic separation of rat skeletal muscle Myosin Heavy Chain isoforms
    Journal of Applied Physiology, 1993
    Co-Authors: Robert J. Talmadge, Roland R Roy
    Abstract:

    A new technique for the sodium dodecyl sulfate-polyacrylamide gel electrophoretic separation of rat skeletal muscle Myosin Heavy-Chain (MHC) isoforms is presented. This technique allows for the separation of the four identified MHC isoforms known to be present in adult rat skeletal muscle. These types of MHC are commonly called I, IIa, IIx or IId, and IIb. The procedure can be performed using minigel electrophoresis systems and does not involve preparation of gradient-separating gels or the use of special cooling devices. The procedure accommodates both silver and Coomasie Blue staining. Thus the procedure is simple to perform and highly repeatable, providing high-resolution separation of MHC protein isoforms. The percent composition of the four adult MHCs in rat soleus, medial gastrocnemius, diaphragm, and levator ani muscles by use of this procedure and Coomasie Blue staining is similar to that previously reported. This new technique provides a novel and easy-to-perform method for the separation of rat skeletal muscle MHC isoforms.

Fatima Pedrosadomellof - One of the best experts on this subject based on the ideXlab platform.

  • fiber content and Myosin Heavy Chain composition of muscle spindles in aged human biceps brachii
    Journal of Histochemistry and Cytochemistry, 2005
    Co-Authors: Jingxia Liu, Perolof Eriksson, Larseric Thornell, Fatima Pedrosadomellof
    Abstract:

    The present study investigated potential age-related changes in human muscle spindles with respect to the intrafusal fiber-type content and Myosin Heavy Chain (MyHC) composition in biceps brachii m ...

  • Myosin Heavy Chain composition of muscle spindles in human biceps brachii
    Journal of Histochemistry and Cytochemistry, 2002
    Co-Authors: Jingxia Liu, Perolof Eriksson, Larseric Thornell, Fatima Pedrosadomellof
    Abstract:

    Data on the Myosin Heavy Chain (MyHC) composition of human muscle spindles are scarce in spite of the well-known correlation between MyHC composition and functional properties of skeletal muscle fibers. The MyHC composition of intrafusal fibers from 36 spindles of human biceps brachii muscle was studied in detail by immunocytochemistry with a large battery of antibodies. The MyHC content of isolated muscle spindles was assessed with SDS-PAGE and immunoblots. Four major MyHC isoforms (MyHCI, IIa, embryonic, and intrafusal) were detected with SDS-PAGE. Immunocytochemistry revealed very complex staining patterns for each intrafusal fiber type. The bag(1) fibers contained slow tonic MyHC along their entire fiber length and MyHCI, alpha-cardiac, embryonic, and fetal isoforms along a variable part of their length. The bag(2) fibers contained MyHC slow tonic, I, alpha-cardiac, embryonic, and fetal isoforms with regional variations. Chain fibers contained MyHCIIa, embryonic, and fetal isoforms throughout the fiber, and MyHCIIx at least in the juxtaequatorial region. Virtually each muscle spindle had a different allotment of numbers of bag(1), bag(2) and Chain fibers. Taken together, the complexity in intrafusal fiber content and MyHC composition observed indicate that each muscle spindle in the human biceps has a unique identity.

  • Myosin Heavy Chain composition of muscle spindles in human biceps brachii
    Histochemistry and Cell Biology, 2002
    Co-Authors: Jingxia Liu, Perolof Eriksson, Larseric Thornell, Fatima Pedrosadomellof
    Abstract:

    Data on the Myosin Heavy Chain (MyHC) composition of human muscle spindles are scarce in spite of the well-known correlation between MyHC composition and functional properties of skeletal muscle fi ...

  • human extraocular muscles unique pattern of Myosin Heavy Chain expression during myotube formation
    Investigative Ophthalmology & Visual Science, 2000
    Co-Authors: Fatima Pedrosadomellof, C. A. Lucas, Ylva Holmgren, Larseric Thornell
    Abstract:

    PURPOSE: To study the Myosin Heavy Chain composition of the human extraocular muscles (EOMs) during development.METHODS: EOMs from human fetuses of 8 to 22 weeks of gestation were studied with immu ...

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