scholarly journals 19-Residue Peptide from C-Terminal Tail of DHPR β1A Subunit Potentiates Voltage-Dependent Calcium Release in Adult Skeletal Muscle Fibers

2012 ◽  
Vol 102 (3) ◽  
pp. 362a ◽  
Author(s):  
Rotimi O. Olojo ◽  
Erick O. Hernandez-Ochoa ◽  
Martin F. Schneider
Keyword(s):  
Skeletal Muscle ◽  
Calcium Release ◽  
Muscle Fibers ◽  
Adult Skeletal Muscle ◽  
Skeletal Muscle Fibers ◽  
Voltage Dependent

scholarly journals β1a490–508, a 19-Residue Peptide from C-Terminal Tail of Cav1.1 β1a Subunit, Potentiates Voltage-Dependent Calcium Release in Adult Skeletal Muscle Fibers

2014 ◽  
Vol 106 (3) ◽  
pp. 535-547 ◽  
Author(s):  
Erick O. Hernández-Ochoa ◽  
Rotimi O. Olojo ◽  
Robyn T. Rebbeck ◽  
Angela F. Dulhunty ◽  
Martin F. Schneider
Keyword(s):  
Skeletal Muscle ◽  
Calcium Release ◽  
Muscle Fibers ◽  
Adult Skeletal Muscle ◽  
Skeletal Muscle Fibers ◽  
Voltage Dependent

scholarly journals Growth Associated Protein 43 Is Expressed in Skeletal Muscle Fibers and Is Localized in Proximity of Mitochondria and Calcium Release Units

PLoS ONE ◽  
2013 ◽  
Vol 8 (1) ◽  
pp. e53267 ◽  
Author(s):  
Simone Guarnieri ◽  
Caterina Morabito ◽  
Cecilia Paolini ◽  
Simona Boncompagni ◽  
Raffaele Pilla ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Calcium Release ◽  
Muscle Fibers ◽  
Skeletal Muscle Fibers

scholarly journals Activity-dependent nuclear translocation and intranuclear distribution of NFATc in adult skeletal muscle fibers

2001 ◽  
Vol 155 (1) ◽  
pp. 27-40 ◽  
Author(s):  
Yewei Liu ◽  
Zoltán Cseresnyés ◽  
William R. Randall ◽  
Martin F. Schneider
Keyword(s):  
Skeletal Muscle ◽  
Electrical Stimulation ◽  
Nuclear Translocation ◽  
Fiber Type ◽  
Muscle Fibers ◽  
Adult Skeletal Muscle ◽  
Skeletal Muscle Fibers ◽  
Slow Twitch ◽  
Nuclear Foci ◽  
Fast Twitch

TTranscription factor nuclear factor of activated T cells NFATc (NFATc1, NFAT2) may contribute to slow-twitch skeletal muscle fiber type–specific gene expression. Green fluorescence protein (GFP) or FLAG fusion proteins of either wild-type or constitutively active mutant NFATc [NFATc(S→A)] were expressed in cultured adult mouse skeletal muscle fibers from flexor digitorum brevis (predominantly fast-twitch). Unstimulated fibers expressing NFATc(S→A) exhibited a distinct intranuclear pattern of NFATc foci. In unstimulated fibers expressing NFATc–GFP, fluorescence was localized at the sarcomeric z-lines and absent from nuclei. Electrical stimulation using activity patterns typical of slow-twitch muscle, either continuously at 10 Hz or in 5-s trains at 10 Hz every 50 s, caused cyclosporin A–sensitive appearance of fluorescent foci of NFATc–GFP in all nuclei. Fluorescence of nuclear foci increased during the first hour of stimulation and then remained constant during a second hour of stimulation. Kinase inhibitors and ionomycin caused appearance of nuclear foci of NFATc–GFP without electrical stimulation. Nuclear translocation of NFATc–GFP did not occur with either continuous 1 Hz stimulation or with the fast-twitch fiber activity pattern of 0.1-s trains at 50 Hz every 50 s. The stimulation pattern–dependent nuclear translocation of NFATc demonstrated here could thus contribute to fast-twitch to slow-twitch fiber type transformation.

scholarly journals Anatomical distribution of voltage-dependent membrane capacitance in frog skeletal muscle fibers.

1989 ◽  
Vol 93 (3) ◽  
pp. 565-584 ◽  
Author(s):  
C L Huang ◽  
L D Peachey
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fibers ◽  
Fiber Surface ◽  
Membrane Capacitance ◽  
Hypertonic Solution ◽  
Charge Movement ◽  
Frog Skeletal Muscle ◽  
Transverse Tubule ◽  
Skeletal Muscle Fibers ◽  
Voltage Dependent

Components of nonlinear capacitance, or charge movement, were localized in the membranes of frog skeletal muscle fibers by studying the effect of 'detubulation' resulting from sudden withdrawal of glycerol from a glycerol-hypertonic solution in which the muscles had been immersed. Linear capacitance was evaluated from the integral of the transient current elicited by imposed voltage clamp steps near the holding potential using bathing solutions that minimized tubular voltage attenuation. The dependence of linear membrane capacitance on fiber diameter in intact fibers was consistent with surface and tubular capacitances and a term attributable to the capacitance of the fiber end. A reduction in this dependence in detubulated fibers suggested that sudden glycerol withdrawal isolated between 75 and 100% of the transverse tubules from the fiber surface. Glycerol withdrawal in two stages did not cause appreciable detubulation. Such glycerol-treated but not detubulated fibers were used as controls. Detubulation reduced delayed (q gamma) charging currents to an extent not explicable simply in terms of tubular conduction delays. Nonlinear membrane capacitance measured at different voltages was expressed normalized to accessible linear fiber membrane capacitance. In control fibers it was strongly voltage dependent. Both the magnitude and steepness of the function were markedly reduced by adding tetracaine, which removed a component in agreement with earlier reports for q gamma charge. In contrast, detubulated fibers had nonlinear capacitances resembling those of q beta charge, and were not affected by adding tetracaine. These findings are discussed in terms of a preferential localization of tetracaine-sensitive (q gamma) charge in transverse tubule membrane, in contrast to a more even distribution of the tetracaine-resistant (q beta) charge in both transverse tubule and surface membranes. These results suggest that q beta and q gamma are due to different molecules and that the movement of q gamma in the transverse tubule membrane is the voltage-sensing step in excitation-contraction coupling.

scholarly journals Spontaneous and Voltage-Activated Elementary Calcium Release Events in Intact Skeletal Muscle Fibers Expressing the Embryonic CaV1.1 Splice Variant

2016 ◽  
Vol 110 (3) ◽  
pp. 97a
Author(s):  
Beatrix Dienes ◽  
János Vincze ◽  
Péter Szentesi ◽  
Nasreen Sultana ◽  
Berhnard E. Flucher ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Splice Variant ◽  
Calcium Release ◽  
Muscle Fibers ◽  
Skeletal Muscle Fibers

scholarly journals Activity- and Calcineurin-independent Nuclear Shuttling of NFATc1, but Not NFATc3, in Adult Skeletal Muscle Fibers

2006 ◽  
Vol 17 (4) ◽  
pp. 1570-1582 ◽  
Author(s):  
Tiansheng Shen ◽  
Yewei Liu ◽  
Zoltán Cseresnyés ◽  
Arie Hawkins ◽  
William R. Randall ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Electrical Stimulation ◽  
Nuclear Export ◽  
Muscle Fibers ◽  
Nuclear Accumulation ◽  
Leptomycin B ◽  
Adult Skeletal Muscle ◽  
Casein Kinase 1 ◽  
Nuclear Uptake ◽  
Skeletal Muscle Fibers

The transcription factor NFATc1 may be involved in slow skeletal muscle gene expression. NFATc1 translocates from cytoplasm to nuclei during slow fiber type electrical stimulation of skeletal muscle fibers because of activation of the Ca2+-dependent phosphatase calcineurin, resulting in nuclear factor of activated T-cells (NFAT) dephosphorylation and consequent exposure of its nuclear localization signal. Here, we find that unstimulated adult skeletal muscle fibers exhibit a previously unanticipated nucleocytoplasmic shuttling of NFATc1 without appreciable nuclear accumulation. In resting fibers, the nuclear export inhibitor leptomycin B caused nuclear accumulation of NFATc1 (but not of isoform NFATc3) and formation of NFATc1 intranuclear bodies independent of calcineurin. The rate of nuclear uptake of NFATc1 was 4.6 times lower in resting fibers exposed to leptomycin B than during electrical stimulation. Inhibitors of glycogen synthase kinase and protein kinase A or of casein kinase 1 slowed the decay of nuclear NFATc1 after electrical stimulation, but they did not cause NFATc1 nuclear uptake in unstimulated fibers. We propose that two nuclear translocation pathways, one pathway mediated by calcineurin activation and NFAT dephosphorylation and the other pathway independent of calcineurin and possibly independent of NFAT dephosphorylation, determine the distribution of NFATc1 between cytoplasm and nuclei in adult skeletal muscle.

Calsequestrin targeting to sarcoplasmic reticulum of skeletal muscle fibers

2006 ◽  
Vol 291 (2) ◽  
pp. C245-C253 ◽  
Author(s):  
Alessandra Nori ◽  
Giorgia Valle ◽  
Elena Bortoloso ◽  
Federica Turcato ◽  
Pompeo Volpe
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Calcium Binding ◽  
Calcium Release ◽  
Structural Information ◽  
Muscle Fibers ◽  
Physiological Role ◽  
Homogeneous Distribution ◽  
Skeletal Muscle Fibers ◽  
Domain Iii

Calsequestrin (CS) is the low-affinity, high-capacity calcium binding protein segregated to the lumen of terminal cisternae (TC) of the sarcoplasmic reticulum (SR). The physiological role of CS in controlling calcium release from the SR depends on both its intrinsic properties and its localization. The mechanisms of CS targeting were investigated in skeletal muscle fibers and C2C12 myotubes, a model of SR differentiation, with four deletion mutants of epitope (hemagglutinin, HA)-tagged CS: CS-HAΔ24NH2, CS-HAΔ2D, CS-HAΔ3D, and CS-HAΔHT, a double mutant of the NH2 terminus and domain III. As judged by immunofluorescence of transfected skeletal muscle fibers, only the double CS-HA mutant showed a homogeneous distribution at the sarcomeric I band, i.e., it did not segregate to TC. As shown by subfractionation of microsomes derived from transfected skeletal muscles, CS-HAΔHT was largely associated to longitudinal SR whereas CS-HA was concentrated in TC. In C2C12 myotubes, as judged by immunofluorescence, not only CS-HAΔHT but also CS-HAΔ3D and CS-HAΔ2D were not sorted to developing SR. Condensation competence, a property referable to CS oligomerization, was monitored for the several CS-HA mutants in C2C12 myoblasts, and only CS-HAΔ3D was found able to condense. Together, the results indicate that 1) there are at least two targeting sequences at the NH2 terminus and domain III of CS, 2) SR-specific target and structural information is contained in these sequences, 3) heterologous interactions with junctional SR proteins are relevant for segregation, 4) homologous CS-CS interactions are involved in the overall targeting process, and 5) different targeting mechanisms prevail depending on the stage of SR differentiation.

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