Histochemical and immunohistochemical properties of skeletal muscle fibres fromRana andXenopus

Rowlerson, A; Spurway, Neil

doi:10.1007/bf01002746

Cited by 45 publications

(74 citation statements)

References 31 publications

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“…According to these findings relative electrophoretic mobility of individual protein bands within a species was diagnostic and SDS-PAGE could be a useful tool for understanding of systematic relations. This is in accordance with the suggestion of a previous study (Rowlerson & Spurway 1988) showing that the different fiber types in Rana and Xenopus limb muscle contained different MHC isoforms.…”

Section: Discussionsupporting

confidence: 93%

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Interspecific differences in molecular weights of skeletal myosin, actin, troponin C and tropomyosin in the frogs Hyla japonica and Xenopus tropicalis

Bülbül

Kutrup

2007

Biologia

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Molecular weights of the skeletal muscle myosin, actin, troponin C and tropomyosin were compared in two frog species, Hyla japonica and Xenopus tropicalis, by SDS-PAGE and Western blot. Polyclonal antibody was produced using H. japonica skeletal muscle as the antigen. Polyclonal antibodies to nematode (Caenorhabditis elegans), mold slime (Physarum polycephalum), crab (Pagurus japonicus) and chicken skeletal muscle were also used. In H. japonica, the molecular weights of skeletal myosin, actin, troponin C and tropomyosin were 230, 42, 19 and 38 kDa, respectively, by using anti-C. elegans paramyosin, anti-P. polycephalum actin, anti-crab troponin C and anti-chicken gizzard tropomyosin antibodies. Molecular weights of the same proteins in X. tropicalis detected by the same antibodies were 230, 43, 20 and 40 kDa, respectively. In total, 29 protein bands were detected in H. japonica skeletal muscle and 24 bands in X. tropicalis by SDS-PAGE. The results revealed interspecific differences in molecular weights of selected skeletal muscle proteins and in the total skeletal muscle protein profiles between the two frog species.

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Section: Discussionsupporting

confidence: 93%

“…A detailed and systematic study of skeletal fiber types in Rana and Xenopus limb muscle, using myosin isoform-based criteria, was performed by Rowlerson & Spurway (1988). Limb muscle differences were also studied in Xenopus laevis (Daudin, 1802) (Lannergren 1979).…”

Section: Introductionmentioning

confidence: 99%

Interspecific differences in molecular weights of skeletal myosin, actin, troponin C and tropomyosin in the frogs Hyla japonica and Xenopus tropicalis

Bülbül

Kutrup

2007

Biologia

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“…Fiber types were classified after mechanics analysis on the basis of native isomyosin bands and limited analysis of MHC and MLC isoforms with SDS-PAGE (19). Five major fiber types and several subtypes were identified in X. laevis and appeared to contain as many as five MHC isoforms (20,22,41,43). However, a one-to-one correspondence between fiber type and MHC isoform is not yet certain.…”

Section: Discussionmentioning

confidence: 99%

Influence of myosin isoforms on contractile properties of intact muscle fibers from Rana pipiens

Lutz

Sirsi

Shapard-Palmer

et al. 2002

American Journal of Physiology-Cell Physiology

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The myosin heavy chain (MHC) and myosin light chain (MLC) isoforms in skeletal muscle of Rana pipiens have been well characterized. We measured the force-velocity (F-V) properties of single intact fast-twitch fibers from R. pipiens that contained MHC types 1 or 2 (MHC1 or MHC2) or coexpressed MHC1 and MHC2 isoforms. Velocities were measured between two surface markers that spanned most of the fiber length. MHC and MLC isoform content was quantified after mechanics analysis by SDS-PAGE. Maximal shortening velocity (V max) and velocity at half-maximal tension (VP 50) increased with percentage of MHC1 (%MHC1). Maximal specific tension (Po/CSA, where Po is isometric tension and CSA is fiber cross-sectional area) and maximal mechanical power (Wmax) also increased with %MHC1. MHC concentration was not significantly correlated with %MHC1, indicating that the influence of %MHC1 on Po/CSA and Wmax was due to intrinsic differences between MHC isoforms and not to concentration. The MLC3-to-MLC1 ratio was not significantly correlated with Vmax, VP 50, Po/CSA, or Wmax. These data demonstrate the powerful relationship between MHC isoforms and F-V properties of the two most common R. pipiens fiber types. mechanics; maximal shortening velocity; fiber type; maximal power; specific tension EXPRESSION OF A HETEROGENEOUS population of muscle cells, with a wide range of contractile properties, is a hallmark of vertebrate skeletal muscle. The differences in force-velocity (F-V) properties among muscle fiber types permit muscles to perform a wide range of mechanical tasks. Functional differences among fiber types have been correlated with myosin heavy chain (MHC) and myosin light chain (MLC) isoforms. Thus differential expression of MHC and MLC isoforms is an important determinant of functional diversity in muscular systems and is matched to the specific motor requirements of an organism.The greatest emphasis in single-fiber mechanical studies has been on determining the influence of MHC and MLC isoforms on maximal shortening velocity (V max ). Mechanical studies of single skinned fibers (sarcolemma permeabilized or removed) have demonstrated a correlation between MHC isoforms and V max (2,3,16,24,39,40,44; for reviews see Refs. 5 and 42). With the use of the in vitro motility assay, where the potential influences of thin-filament regulatory proteins and muscle activation are avoided, the correlation between speed and MHC isoforms has been corroborated (6, 18).The influence of MLC isoforms on V max is more controversial and may be variable among vertebrates. Several studies have established a significant effect of the molar ratio of essential (alkali) light chains [MLC3-to-MLC1 ratio (MLC3/MLC1)] on V max (2, 14, 25, 37, 44; for reviews see Refs. 5, 36, and 42). Independent support for the role of MLC3/MLC1 in regulating myosin kinetics has been documented in a genetic model of fish (7) and with the in vitro motility assay (26). However, in human skinned fast-twitch fibers, MLC3/ MLC1 had no influence on V max (23,24,46). In any cas...

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“…Nitro blue tetrazolium, adjusted to pH·7.6 with NaOH (Rowlerson and Spurway, 1988). Sections were incubated in the staining medium in air-tight, light-proof containers for at least 90·min.…”

Section: Histochemistrymentioning

confidence: 99%

Getting the jump on skeletal muscle disuse atrophy: preservation of contractile performance in aestivatingCyclorana alboguttata(Günther 1867)

Symonds

James

Franklin

2007

Journal of Experimental Biology

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SUMMARY Prolonged immobilisation or unloading of skeletal muscle causes muscle disuse atrophy, which is characterised by a reduction in muscle cross-sectional area and compromised locomotory function. Animals that enter seasonal dormancy, such as hibernators and aestivators, provide an interesting model for investigating atrophy associated with disuse. Previous research on the amphibian aestivator Cyclorana alboguttata (Günther 1867)demonstrated an absence of muscle disuse atrophy after 3 months of aestivation, as measured by gastrocnemius muscle contractile properties and locomotor performance. In this study, we aimed to investigate the effect of aestivation on iliofibularis and sartorius muscle morphology and contractile function of C. alboguttata over a longer, more ecologically relevant time-frame of 9 months. We found that whole muscle mass, muscle cross-sectional area, fibre number and proportions of fibre types remained unchanged after prolonged disuse. There was a significant reduction in iliofibularis fibre cross-sectional area (declined by 36% for oxidative fibre area and 39% for glycolytic fibre area) and sartorius fibre density (declined by 44%). Prolonged aestivation had little effect on the isometric properties of the skeletal muscle of C. alboguttata. There was a significant reduction in the isometric contraction times of the relatively slow-twitch iliofibularis muscle, suggesting that the muscle was becoming slower after 9 months of aestivation (time to peak twitch increased by 25%, time from peak twitch to half relaxation increased by 34% and time from last stimulus to half tetanus relation increased by 20%). However, the results of the work-loop analysis clearly demonstrate that, despite changes to muscle morphology and isometric kinetics, the overall contractile performance and power output levels of muscles from 9-month aestivating C. alboguttata are maintained at control levels.

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Histochemical and immunohistochemical properties of skeletal muscle fibres fromRana andXenopus

Cited by 45 publications

References 31 publications

Interspecific differences in molecular weights of skeletal myosin, actin, troponin C and tropomyosin in the frogs Hyla japonica and Xenopus tropicalis

Interspecific differences in molecular weights of skeletal myosin, actin, troponin C and tropomyosin in the frogs Hyla japonica and Xenopus tropicalis

Influence of myosin isoforms on contractile properties of intact muscle fibers from Rana pipiens

Getting the jump on skeletal muscle disuse atrophy: preservation of contractile performance in aestivatingCyclorana alboguttata(Günther 1867)

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