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Journal articles on the topic 'Skinned fibres'

Author: Grafiati

Published: 14 March 2023

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1

Galler, S., C. Hutzler, and T. Haller. "Effects of taurine on Ca2(+)-dependent force development of skinned muscle fibre preparations." Journal of Experimental Biology 152, no. 1 (September 1, 1990): 255–64. http://dx.doi.org/10.1242/jeb.152.1.255.

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The effects of the naturally occurring amino acid taurine (2-aminoethanesulphonic acid) on isometric force development were investigated using skinned muscle fibre preparations. In atrial and ventricular pig heart muscles, as well as in fibres of slow abdominal extensor muscle of crayfish, an increase of submaximal isometric force was observed in Ca2(+)-activated skinned fibre preparations at physiological concentrations of taurine. The maximal isometric force remained unaffected in all preparations. It is assumed that taurine increases the Ca2+ sensitivity of the force-generating myofilaments in mammalian hearts and crustacean slow skeletal muscle fibres.

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2

Stienen, G. J. M. "Chronicle of skinned muscle fibres." Journal of Physiology 527, no. 1 (August 2000): 1. http://dx.doi.org/10.1111/j.1469-7793.2000.t01-2-00001.x.

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3

Eddinger, Thomas J., Richard L. Moss, and Robert G. Cassens. "Myosin-ATPase fibre typing of chemically skinned muscle fibres." Histochemical Journal 17, no. 9 (September 1985): 1021–26. http://dx.doi.org/10.1007/bf01417950.

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4

CURTIN, N. A., and R. C. WOLEDGE. "Power Output and Force-Velocity Relationship of Live Fibres from White Myotomal Muscle of the Dogfish, Scyliorhinus Canicula." Journal of Experimental Biology 140, no. 1 (November 1, 1988): 187–97. http://dx.doi.org/10.1242/jeb.140.1.187.

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The relationship between force and velocity of shortening and between power and velocity were examined for myotomal muscle fibre bundles from the dogfish. The maximum velocity of shortening, mean value 4.8 ± 0.2 μms−1 half sarcomere−1 (±S.E.M., N = 13), was determined by the ‘slack step’ method (Edman, 1979) and was found to be independent of fish length. The force-velocity relationship was hyperbolic, except at the high-force end where the observations were below the hyperbola fitted to the rest of the data. The maximum power output was 91 ± 14 W kg−1 wet mass (±S.E.M., N = 7) at a velocity of shortening of 1.3 ± 0.13μms−1 halfsarcomere−1 (±S.E.M., N = 7). This power output is considerably higher than that previously reported for skinned fibres (Bone et al. 1986). Correspondingly the force-velocity relationship is less curved for intact fibres than for skinned fibres. The maximum swimming speed (normalized for fish length) predicted from the observed power output of the muscle fibres decreased with increasing fish size; it ranged from 12.9 to 7.8 fish lengths s−1 for fish 0155–0.645m in length.

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5

ALTRINGHAM, J. D., and I. A. JOHNSTON. "Energy Cost of Contraction in Fast and Slow Muscle Fibres Isolated from an Elasmobranch and an Antarctic Teleost Fish." Journal of Experimental Biology 121, no. 1 (March 1, 1986): 239–50. http://dx.doi.org/10.1242/jeb.121.1.239.

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1. Single fast and small bundles of slow fibres were isolated from the muscles of an elasmobranch (dogfish, Scyliorhinus canicula) and an Antarctic teleost (Notothenia neglecta). A third fibre type present in the dogfish (superficial fibre) was also isolated. Fibres were chemically skinned with a non-ionic detergent. 2. Tension generation and ATPase activity were measured during isometric activations. ATPase activity was estimated by measuring the release of ADP into the experimental solutions using high performance liquid chromatography. 3. In the dogfish fibre types, both tension and ATPase activity increased in the order superficial < slow < fast, even after corrections were made for differences in myofibrillar density. The economy of isometric contraction (tension/ATPase activity) was 50–60% higher in the slow and superficial fibres than in the fast. 4. In the Antarctic species, both tension and ATPase activity of the fast fibres were higher than those of the slow fibres, and the slow fibres were 30% more economical than fast fibres. After correction for differences in myofibrillar density, tensions were very similar. 5. The results are discussed with reference to the energy supply, recruitment pattern and function of the various fibre types.

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6

Jaspers, R. T., H. Degens, P. A. Huijing, and W. J. van der Laarse. "Specific tension of intact and skinned muscle fibres." Journal of Biomechanics 39 (January 2006): S56. http://dx.doi.org/10.1016/s0021-9290(06)83105-2.

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7

FOUCAULT, Georges, Monique VACHER, Tatyana MERKULOVA, Angelica KELLER, and Martine ARRIO-DUPONT. "Presence of enolase in the M-band of skeletal muscle and possible indirect interaction with the cytosolic muscle isoform of creatine kinase." Biochemical Journal 338, no. 1 (February 8, 1999): 115–21. http://dx.doi.org/10.1042/bj3380115.

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Glycerol-skinned skeletal muscle fibres retain the defined sarcomeric structure of the myofibrils. We show here that a small fraction of two enzymes important for energy metabolism, the cytosolic muscle isoform of creatine kinase (EC 2.7.3.2), MM-creatine kinase (MM-CK), and enolase (EC 4.2.1.11), remains bound to skinned fibres. CK is slowly exchangeable, whereas enolase is firmly bound. Two-dimensional gel electrophoresis followed by Western blot analyses demonstrates that both α (ubiquitous) and β (muscle-specific) subunits of enolase are present in these preparations. Enolase and CK were co-localized at the M-band of the sarcomeres, as observed by indirect immunofluorescence and confocal microscopy. Cross-linking experiments were performed on skinned fibres with three bifunctional succinimidyl esters of different lengths and yielded a protein complex of 150 kDa that reacted with antibodies directed against either M-CK or β-enolase. The cross-linking efficiency was greatest for the longest reagent and zero for the shortest one. The length of the cross-linker giving a covalent complex between the two enzymes does not support the notion of a direct interaction between M-CK and enolase. This is the first demonstration of the presence of an enzyme of energy metabolism other than CK at the M-band of myofibres.

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8

De Beer, Evert L., Heather Finkle, Emile E. Voest, Bas G. V. Van Heijst, and Piet Schiereck. "Doxorubicin interacts directly with skinned single skeletal muscle fibres." European Journal of Pharmacology 214, no. 1 (April 1992): 97–100. http://dx.doi.org/10.1016/0014-2999(92)90103-b.

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9

Yates, L. D., R. L. Coby, Z. Luo, and A. M. Gordon. "Filament overlap affects TnC extraction from skinned muscle fibres." Journal of Muscle Research and Cell Motility 14, no. 4 (August 1993): 392–400. http://dx.doi.org/10.1007/bf00121290.

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10

Rees, B. B., and D. G. Stephenson. "Thermal dependence of maximum Ca2+-activated force in skinned muscle fibres of the toad Bufo marinus acclimated at different temperatures." Journal of Experimental Biology 129, no. 1 (May 1, 1987): 309–27. http://dx.doi.org/10.1242/jeb.129.1.309.

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Mechanically skinned muscle fibres from the twitch region of the iliofibularis muscle of cool- (16 +/− 1 degree C) and warm- (32 +/− 1 degree C) acclimated cane toads (Bufo marinus) were activated maximally by Ca2+ in solutions of different pH and at different temperatures (approx. 1–35 degrees C). Acclimation of up to 12 weeks at 16 degrees C and up to 8 weeks at 32 degrees C did not modify the marked thermal dependence of isometric force in the skeletal muscle fibres of the cane toad. The prominent decline of maximum Ca2+-activated force at lower temperatures, a property which is not characteristic of muscles from other anurans, was associated with an obvious decline in fibre stiffness at temperatures below about 20 degrees C, regardless of the temperatures at which the toads were kept prior to experimentation. The results suggest that the decline of isometric force at lower temperatures is due both to a reduction in the number of cross-bridges and to a decrease in the force output per cross-bridge. The maximum Ca2+-activated force response increased when fibres were activated in solutions of increasing pH at all temperatures investigated. This trend is expected to have a compensatory effect on the thermal dependence of the maximum Ca2+-activated force under physiological conditions, because of the elevation of intracellular pH as temperature declines. The isometric force did not depend on the concentration of the zwitterionic species of the pH buffer in solutions. The skinned fibre preparation developed a Ca2+-insensitive residual force following maximal activation. The increment in residual force followed a linear relationship with the duration of activation at a given temperature and a power relationship of activation temperature for a given duration of activation. Fibres from warm-acclimated animals developed less residual force following activations at 15 degrees C than did fibres from cool-acclimated animals, suggesting that thermal acclimation may substantially reduce the magnitude of this phenomenon at temperatures below 20 degrees C.

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11

Mutungi, G., and I. A. Johnston. "The effects of temperature and pH on the contractile properties of skinned muscle fibres from the terrapin, Pseudemys scripta elegans." Journal of Experimental Biology 128, no. 1 (March 1, 1987): 87–105. http://dx.doi.org/10.1242/jeb.128.1.87.

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Fibre types in the iliofibularis muscle of the freshwater terrapin Pseudemys scripta elegans have been characterized on the basis of their histochemical characteristics, nerve endings and contractile properties. Three types of focally innervated fibres are present, corresponding to the fast glycolytic (Fg), fast oxidative glycolytic (FOG) and slow oxidative (SO) fibre types of other vertebrates. Single fibres or small bundles of fibres representing each histochemical type were identified on the basis of their light scattering properties under dark-field illumination. Fibres were detergent-skinned using Brij 58, and their maximum isometric tension (P0) and unloaded contraction velocity (V0) were determined by the slack test method. At 15 degrees C, fast glycolytic fibres generated maximum isometric tensions of 184 +/− 5 kNm-2 and V0 values of 5.5 +/− 0.3 muscle lengths per second (L0s-1). Slow oxidative fibres produced tensions of 70.6 +/− 3 kNm-2 and had V0 values of 1.3 L0s-1. Tensions and V0 values of fast oxidative glycolytic fibres were between those of Fg and SO fibres. The force-velocity (P-V) characteristics of slow oxidative fibres were studied at 5 degrees and 15 degrees C. Points below 0.6 P0 on the curves could be fitted by a linear form of Hill's equation. Maximum contraction velocities (Vmax) extrapolated from the P-V relationship were 0.62 L0s-1 at 5 degrees C and 0.91 L0s-1 at 15 degrees C. The curvature of the P-V relationship was relatively independent of temperature over the range 5 to 15 degrees C. Values for Hill's constant a/P0 were 0.29 and 0.33 at 5 degrees C and 15 degrees C, respectively. The temperature dependence of P0 and contraction velocity at near zero load (Vi) were studied at constant pH, and under conditions designed to simulate the changes in intracellular pH which occur with temperature in vivo (delta pH/delta T = −0.0186). Changes in pH in the range 6.6 to 7.8 had no effect on either tension or Vi at temperatures between 0 degrees and 20 degrees C. However, below and above this pH range, both tension and Vi were depressed. It is concluded that pH changes within the normal physiological range (6.7-7.8) have no effect on the temperature dependence of P0 and Vi.

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12

Duncan, C. J. "Role of calcium in triggering rapid ultrastructural damage in muscle: a study with chemically skinned fibres." Journal of Cell Science 87, no. 4 (May 1, 1987): 581–94. http://dx.doi.org/10.1242/jcs.87.4.581.

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Agents (A23187, caffeine) believed to raise [Ca]i in vertebrate cardiac and skeletal muscles cause rapid and characteristic subcellular damage in vitro and in vivo. By using saponin-skinned amphibian pectoris cutaneous muscle and Ca-EGTA-buffered solutions it is shown that low [Ca] consistently triggers the same rapid (2–20 min), ultrastructural damage. Electron micrographs reveal a close similarity between the damaged intact and skinned preparations, namely loss of myofilament organization, specific Z-line damage, dissolution and hypercontraction bands, characteristic mitochondrial swelling and division. Where both actin and myosin filaments were lost, an underlying cytoskeletal network frequently remained, still attached to the Z-line framework. Ca was effective in skinned preparations from 5 X 10(−7) M to 8 X 10(−6) M, within the concentration range experienced by a contracting muscle. Damage was [Ca]- and time-dependent and it is suggested that it is probably the active movement of Ca ions across key membrane sites that is critical in triggering damage of the myofilament apparatus. Strontium can substitute for Ca at higher concentrations. The action of saponin suggests that the chemically skinned cell is partially activated. Ca-triggering can be bypassed experimentally by membrane-active agents or by sulphydryl agents. Ruthenium Red and trifluoperazine indirectly cause damage in the intact cell by raising [Ca]i. Studies with saponin-skinned cells and protease inhibitors show that changes in pHi, loss of ATP, Ca-activated neutral protease, or release of lysosomal enzymes (cathepsins B, D, L or H), are not involved in characteristic rapid myofilament damage.

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13

Jee, Hyunseok, and Jae-Young Lim. "Discrepancies between Skinned Single Muscle Fibres and Whole Thigh Muscle Function Characteristics in Young and Elderly Human Subjects." BioMed Research International 2016 (2016): 1–8. http://dx.doi.org/10.1155/2016/6206959.

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We aimed to analyse the mechanical properties of skinned single muscle fibres derived from the vastus lateralis (VL) muscle in relation to those of the whole intact thigh muscle and to compare any difference between young and older adults. Sixteen young men (29.25±4.65years), 11 older men (71.45±2.94years), 11 young women (29.64±4.88years), and 7 older women (67.29±1.70years) were recruited. In vivo analyses were performed for mechanical properties such as isokinetic performance, isometric torque, and power. Specific force and maximum shortening velocity (Vo) were measured with single muscle fibres. Sex difference showed greater impact on the functional properties of both the whole muscle (p<0.01) and single muscle fibres than aging (p<0.05). Sex difference, rather than aging, yielded more remarkable differences in gross mechanical properties in the single muscle fibre study in which significant differences between young men and young women were found only in the cross-sectional area and Vo (p<0.05). Age and sex differences reflect the mechanical properties of both single muscle fibres and whole thigh muscle, with the whole muscle yielding more prominent functional properties.

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14

Stienen, G. J., J. L. Kiers, R. Bottinelli, and C. Reggiani. "Myofibrillar ATPase activity in skinned human skeletal muscle fibres: fibre type and temperature dependence." Journal of Physiology 493, no. 2 (June 1, 1996): 299–307. http://dx.doi.org/10.1113/jphysiol.1996.sp021384.

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15

Luo, Ye, Jonathan P. Davis, Lawrence B. Smillie, and Jack A. Rall. "Determinants of relaxation rate in rabbit skinned skeletal muscle fibres." Journal of Physiology 545, no. 3 (December 2002): 887–901. http://dx.doi.org/10.1113/jphysiol.2002.031757.

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16

Jung, D. W. G., T. Blangé, H. de Graaf, and B. W. Treijtel. "Cross-bridge stiffness in Ca2+-activated skinned single muscle fibres." Pflügers Archiv 420, no. 5-6 (April 1992): 434–45. http://dx.doi.org/10.1007/bf00374617.

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17

Izumi, Hidetaka, R. E. Garfield, Fujio Morishita, and Koichi Shirakawa. "Some mechanical properties of skinned fibres of pregnant human myometrium." European Journal of Obstetrics & Gynecology and Reproductive Biology 56, no. 1 (July 1994): 55–62. http://dx.doi.org/10.1016/0028-2243(94)90154-6.

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18

DEGENS, Hans, Mattias SOOP, Peter HÖÖK, Olle LJUNGQVIST, and Lars LARSSON. "Post-operative effects on insulin resistance and specific tension of single human skeletal muscle fibres." Clinical Science 97, no. 4 (August 24, 1999): 449–55. http://dx.doi.org/10.1042/cs0970449.

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Surgery and accidental trauma are associated with a transient period of insulin resistance, substrate catabolism and muscle weakness. In the present study, we evaluated the changes in the force-generating capacity of chemically skinned single muscle fibres following abdominal surgery. Biopsies of the m. vastus lateralis were obtained in three patients 1 day before and 3 or 6 days after surgery. Part of the biopsy was frozen for histochemical analysis of the fibre cross-sectional area (FCSA) and myofibrillar protein content, and another part was used for single-fibre contractile measurements. All patients developed insulin resistance following surgery. The maximum velocity of unloaded shortening of single muscle fibres did not change following surgery. The FCSA did not decrease after surgery, as determined either from histochemical sections or from single fibres measured at a fixed sarcomere length of 2.76±0.09 μm (mean±S.D.). Further, the force-generating capacity of the single fibres, measured as maximal Ca2+-activated force (P0) or as P0 normalized to FCSA (specific tension), remained unchanged, as did the myofibrillar protein content of the muscle. In conclusion, the muscle weakness associated with post-operative insulin resistance is not related to a decreased specific tension or a loss of myofibrillar proteins. Other potential cellular mechanisms underlying post-operative weakness are discussed.

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19

Bershitsky, S. Y., and A. K. Tsaturyan. "Tension responses to joule temperature jump in skinned rabbit muscle fibres." Journal of Physiology 447, no. 1 (February 1, 1992): 425–48. http://dx.doi.org/10.1113/jphysiol.1992.sp019010.

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20

HERZIG, J. "Calcium activation of skinned fibres from cardiomyopathic hamster hearts (BIO 14.6)." Journal of Molecular and Cellular Cardiology 19 (1987): S34. http://dx.doi.org/10.1016/s0022-2828(87)80109-8.

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21

Reyford, H., P. J. Adnet, B. Tavernier, S. Beague, R. Krivosic, and G. Haudecoeur. "HALOTHANE INDUCES CALCIUM RELEASE FROM NORMAL HUMAN SKINNED MASSETER MUSCLE FIBRES." Anesthesiology 89, Supplement (September 1998): 139A. http://dx.doi.org/10.1097/00000542-199809040-00043.

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22

Powers, Krysta, Venus Joumaa, Azim Jinha, Eng Kuan Moo, Ian Curtis Smith, Kiisa Nishikawa, and Walter Herzog. "Titin force enhancement following active stretch of skinned skeletal muscle fibres." Journal of Experimental Biology 220, no. 17 (June 21, 2017): 3110–18. http://dx.doi.org/10.1242/jeb.153502.

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23

Joumaa, Venus, and Walter Herzog. "Does Calcium Sensitivity Increase after Active Stretch in Skinned Muscle Fibres?" Biophysical Journal 106, no. 2 (January 2014): 765a. http://dx.doi.org/10.1016/j.bpj.2013.11.4205.

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24

MILLER, D. "Action of reactive oxygen species on force production in skinned fibres." Journal of Molecular and Cellular Cardiology 24 (July 1992): 28. http://dx.doi.org/10.1016/0022-2828(92)93421-f.

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25

Jaworowski, Åsa, Kurt I. Anderson, Anders Arner, Martin Engström, Mario Gimona, Peter Strasser, and J. Victor Small. "Calponin reduces shortening velocity in skinned taenia coli smooth muscle fibres." FEBS Letters 365, no. 2-3 (May 29, 1995): 167–71. http://dx.doi.org/10.1016/0014-5793(95)00451-e.

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26

Crockford, T., I. Johnston, and B. Mcandrew. "Functionally significant allelic variation in myosin light chain composition in a tropical cichlid." Journal of Experimental Biology 198, no. 12 (December 1, 1995): 2501–8. http://dx.doi.org/10.1242/jeb.198.12.2501.

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Single fast muscle fibres in the tropical fish Oreochromis andersonii were found to contain two myosin light chains (LC1s; LC1f1* or LC1f2*). Breeding experiments confirmed that the different LC1s were of allelic origin and their inheritance patterns conformed to Mendelian expectations (1:2:1). The LC1s differed in apparent relative molecular mass by 800900. No other differences in myosin subunits were found between the LC1 genotypes. The molar ratios of LC3:LC1(total) in the fast muscle of O. andersonii homozygous for LC1f1* or LC1f2* and heterozygous for both alleles were 2.0:1, 2.1:1 and 2.2:1, respectively, as determined by capillary electrophoresis. The maximum contraction velocity (Vmax) of single skinned muscle fibres was determined at 20 °C by the slack-test method. Vmax values (fibre lengths s-1) for fast muscle fibres from O. andersonii which were homozygous for either LC1f2* or LC1f1* were 5.3 and 3.3, respectively, compared with 3.8 when both alleles were present. Crosses between Oreochromis niloticus and O. andersonii produced F1 hybrids which were heterozygous for either LC1n/LC1f1* or LC1n/LC1f2*, where LC1n is the myosin light chain for O. niloticus. The distribution of myosin light chain genotypes in hybrid offspring was not significantly different from the expected Mendelian 1:1 ratio (47 %: 53 %). The Vmax (fibre lengths s-1) of muscle fibres containing LC1f2* from hybrid Oreochromis was 4.3 compared with 3.1 for the LC1f1* genotype. The results are consistent with a functionally significant allelic variation in myosin LC1 in fast muscle fibres from O. andersonii which is also expressed in hybrid genotypes.

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27

Bakker, Anthony J., Ann L. Parkinson, and Stewart I. Head. "Contractile properties of single-skinned skeletal muscle fibres of the extensor digitorum longus muscle of the Australian short-nosed echidna." Australian Journal of Zoology 53, no. 4 (2005): 237. http://dx.doi.org/10.1071/zo05011.

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Eutherian mammal fast-twitch muscle fibres share similar contractile activation properties, suggesting that these properties are highly conserved in mammals. To investigate this hypothesis, we examined the contractile properties of skeletal muscle from the order Monotremata, a mammalian order that separated from eutherians 150 million years ago. The Ca2+- and Sr2+-activation properties of single mechanically skinned skeletal muscle fibres from the extensor digitorum longus (EDL) muscle of the short-nosed echidna were determined. Sigmoidal curves fitted to force response data plotted as a function of pCa (–log[Ca2+]), had a mean slope of 4.32 ± 0.28 and a mean pCa50 and pCa10 value of 6.18 ± 0.01 and 6.41 ± 0.02 respectively (n = 20). The mean pSr50, pSr10 and slope values of curves fitted to the force-response data after activation with Sr2+ were 4.80 ± 0.03, 5.29 ± 0.07 and 2.75 ± 0.18 respectively (n = 20). The mean pCa50–pSr50 value for the echidna EDL fibres was 1.37 ± 0.04. In five of the echidna fibres, exposure to submaximal Ca2+ concentrations produced myofibrillar force oscillations (mean frequency, 0.13 ± 0.01 Hz), a phenomenon found only in eutherian slow and intermediate muscle fibres. These results show that echidna EDL fibres generally have similar contractile properties to eutherian fast-twitch skeletal muscle fibres, such as those found in the EDL of the rat.

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28

West, T. G., C. N. Toepfer, R. C. Woledge, N. A. Curtin, A. Rowlerson, M. Kalakoutis, P. Hudson, and A. M. Wilson. "Power output of skinned skeletal muscle fibres from the cheetah (Acinonyx jubatus)." Journal of Experimental Biology 216, no. 15 (April 11, 2013): 2974–82. http://dx.doi.org/10.1242/jeb.083667.

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29

Asayama, J., Y. Yamahara, T. Tatsumi, H. Miyazaki, M. Inoue, I. Omori, D. Inoue, and M. Nakagawa. "Acute effects of doxorubicin on skinned cardiac muscle fibres of guinea pigs." Cardiovascular Research 26, no. 4 (April 1, 1992): 371–75. http://dx.doi.org/10.1093/cvr/26.4.371.

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30

Kasuga, N., and Y. Umazume. "Deterioration induced by physiological concentration of calcium ions in skinned muscle fibres." Journal of Muscle Research and Cell Motility 11, no. 1 (February 1990): 41–47. http://dx.doi.org/10.1007/bf01833324.

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31

Danieli -Betto, D., R. Betto, and M. Midrio. "Calcium sensitivity and myofibrillar protein isoforms of rat skinned skeletal muscle fibres." Pfl�gers Archiv European Journal of Physiology 417, no. 3 (November 1990): 303–8. http://dx.doi.org/10.1007/bf00370996.

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32

DUNCAN, C. J. "Chemically skinned skeletal muscle fibres and the initiation of rapid cellular damage." Biochemical Society Transactions 15, no. 6 (December 1, 1987): 1165–66. http://dx.doi.org/10.1042/bst0151165.

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33

Savineau, J. P., and R. Marthan. "Activation properties of chemically skinned fibres from human isolated bronchial smooth muscle." Journal of Physiology 474, no. 3 (February 1, 1994): 433–38. http://dx.doi.org/10.1113/jphysiol.1994.sp020034.

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34

Williams, J. H. "Effects of fatigue on depolarization- and caffeine-induced contractures of skinned fibres." Acta Physiologica Scandinavica 180, no. 3 (March 2004): 265–69. http://dx.doi.org/10.1046/j.0001-6772.2003.01243.x.

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35

Gilliver, S. F., H. Degens, J. Rittweger, A. J. Sargeant, and D. A. Jones. "Variation in the determinants of power of chemically skinned human muscle fibres." Experimental Physiology 94, no. 10 (September 15, 2009): 1070–78. http://dx.doi.org/10.1113/expphysiol.2009.048314.

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36

Sperl, W., D. Skladal, N. Lanznaster, R. Schranzhofer, G. Zaunschirm, E. Gnaiger, E. Pl�chl, and F. Gellerich. "Polarographic studies of saponin-skinned muscle fibres in patients with mitochondrial myopathies." Journal of Inherited Metabolic Disease 17, no. 3 (1994): 307–10. http://dx.doi.org/10.1007/bf00711815.

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37

Schiereck, Piet, Evert De Beer, Bas Van Heijst, Paul Janssen, Alexandra Van Andel, Frans Jennekens, Annemiek Sontrop, and Annet Bavinck. "Ca2+ channel antagonists enhance tension in skinned skeletal and heart muscle fibres." European Journal of Pharmacology 249, no. 3 (November 1993): 317–24. http://dx.doi.org/10.1016/0014-2999(93)90528-p.

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38

Morris, Carl A., Larry S. Tobacman, and Earl Homsher. "Thin Filament Activation and Unloaded Shortening Velocity of Rabbit Skinned Muscle Fibres." Journal of Physiology 550, no. 1 (July 2003): 205–15. http://dx.doi.org/10.1113/jphysiol.2003.040899.

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39

Julian, F. J., L. C. Rome, D. G. Stephenson, and S. Striz. "The maximum speed of shortening in living and skinned frog muscle fibres." Journal of Physiology 370, no. 1 (January 1, 1986): 181–99. http://dx.doi.org/10.1113/jphysiol.1986.sp015929.

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40

Goldman, Y. E., and R. M. Simmons. "The stiffness of frog skinned muscle fibres at altered lateral filament spacing." Journal of Physiology 378, no. 1 (September 1, 1986): 175–94. http://dx.doi.org/10.1113/jphysiol.1986.sp016213.

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41

Lewis, Trevor M., Angela F. Dulhunty, Pauline R. Junankar, and Carolyn Stanhope. "Ultrastructure of sarcoballs on the surface of skinned amphibian skeletal muscle fibres." Journal of Muscle Research and Cell Motility 13, no. 6 (December 1992): 640–53. http://dx.doi.org/10.1007/bf01738254.

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Joumaa, Venus, Sadhiq Nazeer, Faruk Ortes, and Walter Herzog. "New Insights into Force After Active Stretch in Damaged Skinned Muscle Fibres." Biophysical Journal 116, no. 3 (February 2019): 405a. http://dx.doi.org/10.1016/j.bpj.2018.11.2187.

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43

Stienen, G. J. M., T. Blang�, and B. W. Treijtel. "Tension development and calcium sensitivity in skinned muscle fibres of the frog." Pfl�gers Archiv European Journal of Physiology 405, no. 1 (September 1985): 19–23. http://dx.doi.org/10.1007/bf00591092.

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Caorsi, Valentina, Dmtry S. Ushakov, Timothy G. West, Niovi Setta-Kaffetzi, and Michael A. Ferenczi. "FRET characterisation for cross-bridge dynamics in single-skinned rigor muscle fibres." European Biophysics Journal 40, no. 1 (September 2, 2010): 13–27. http://dx.doi.org/10.1007/s00249-010-0624-9.

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Lafoux, Aude, Alexandra Divet, Pascal Gervier, and Corinne Huchet-Cadiou. "Diaphragm tension reduced in dystrophic mice by an oxidant, hypochlorous acid." Canadian Journal of Physiology and Pharmacology 88, no. 2 (February 2010): 130–40. http://dx.doi.org/10.1139/y09-117.

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Abstract:

In dystrophin-deficient skeletal muscle cells, in which Ca2+ homeostasis is disrupted and reactive oxygen species production is increased, we hypothesized that hypochlorous acid (HOCl), a strong H2O2-related free radical, damages contractile proteins and the sarcoplasmic reticulum. The aim of the present study was to investigate the effects of exposure to oxidative stress, generated by applying HOCl (100 µmol/L and 1 mmol/L), on the contractile function and sarcoplasmic reticulum properties of dystrophic mice. Experiments were performed on diaphragm muscle, which is severely affected in the mdx mouse, and the results were compared with those obtained in healthy (non-dystrophic) mice. In Triton-skinned fibres from C57BL/10 and mdx mice, 1 mmol/L HOCl increased myofibrillar Ca2+ sensitivity, but decreased maximal Ca2+-activated tension. In the presence of HOCl, higher concentrations of MgATP were required to produce rigor tensions. The interaction between HOCl and the Ca2+ uptake mechanisms was demonstrated using saponin-skinned fibres and sarcoplasmic reticulum vesicles. The results showed that HOCl, at micromolar or millimolar concentrations, can modify sarcoplasmic reticulum Ca2+ uptake and that this effect was more pronounced in diaphragm muscle from mdx mice. We conclude that in dystrophic diaphragm skeletal muscle cells, HOCl activates a cellular pathway that leads to an increase in the intracellular concentration of Ca2+.

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Curtin, N. A., R. A. Diack, T. G. West, A. M. Wilson, and R. C. Woledge. "Skinned fibres produce the same power and force as intact fibre bundles from muscle of wild rabbits." Journal of Experimental Biology 218, no. 18 (July 23, 2015): 2856–63. http://dx.doi.org/10.1242/jeb.121897.

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LYNCH, G. S., M. J. McKENNA, and D. A. WILLIAMS. "Sprint-training effects on some contractile properties of single skinned human muscle fibres." Acta Physiologica Scandinavica 152, no. 3 (November 1994): 295–306. http://dx.doi.org/10.1111/j.1748-1716.1994.tb09809.x.

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Joumaa, Venus, Alex Fitzowich, and Walter Herzog. "Energy cost of isometric force production after active shortening in skinned muscle fibres." Journal of Experimental Biology 220, no. 8 (February 23, 2017): 1509–15. http://dx.doi.org/10.1242/jeb.117622.

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Tavernier, B. "Myofilament calcium sensitivity is decreased in skinned cardiac fibres of endotoxin-treated rabbits." Cardiovascular Research 38, no. 2 (May 1998): 472–79. http://dx.doi.org/10.1016/s0008-6363(98)00028-5.

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ASHLEY, C. "Thin filament activation by photolysis of caged-calcium in skinned muscle fibres*1." Journal of Molecular and Cellular Cardiology 20 (June 1988): 10. http://dx.doi.org/10.1016/0022-2828(88)90242-8.

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