A developmental change in the content of parvalbumin in normal and dystrophic mouse (mdx) muscle

Sano, Masaaki; Yokota, Tsukasa; Endo, Toyoshi; Tsukagoshi, Hiroshi

doi:10.1016/0022-510x(90)90224-b

Cited by 20 publications

(12 citation statements)

References 24 publications

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“…3 (and support with pooled data in Table 1) that, under identical experimental conditions, the FDHMs of localized Ca 2ϩ transients recorded at selected sarcomeric sites (T-, Z-and M-) of mdx fibers are significantly longer than their corresponding ones in control fibers. This reveals a limitation in Ca 2ϩ handling by mdx fibers that has not been not previously reported, but which may shed light on potential mechanistic deficiencies linked to the SR Ca 2ϩ pump (26), parvalbumin (27)(28)(29), and calsequestrin (25), previously suggested as potential candidates to explain functional impairments. Curiously, the prolongation in FDHMs demonstrated clearly with the one-to-one comparative analysis of localized transients, is not observed in global transients (see Table 1).…”

Section: Discussionmentioning

confidence: 93%

Dystrophic skeletal muscle fibers display alterations at the level of calcium microdomains

DiFranco

Woods

Capote

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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The spatiotemporal properties of the Ca 2؉ -release process in skeletal muscle fibers from normal and mdx fibers were determined using the confocal-spot detection technique. The Ca 2؉ indicator OGB-5N was used to record action potential-evoked fluorescence signals at consecutive locations separated by 200 nm along multiple sarcomeres of FDB fibers loaded with 10-and 30-mM EGTA. Three-dimensional reconstructions of fluorescence transients demonstrated the existence of microdomains of increased fluorescence around the Ca 2؉ -release sites in both mouse strains. The Ca 2؉ microdomains in mdx fibers were regularly spaced along the fiber axis, displaying a distribution similar to that seen in normal fibers. Nevertheless, both preparations differed in that in 10-mM EGTA Ca 2؉ microdomains had smaller amplitudes and were wider in mdx fibers than in controls. In addition, Ca 2؉ -dependent fluorescence transients recorded at selected locations within the sarcomere of mdx muscle fibers were not only smaller, but also slower than their counterparts in normal fibers. Notably, differences in the spatial features of the Ca 2؉ microdomains recorded in mdx and normal fibers, but not in the amplitude and kinetics of the Ca 2؉ transients, were eliminated in 30-mM EGTA. Our results consistently demonstrate that Ca 2؉ -release flux calculated from release sites in mdx fibers is uniformly impaired with respect to those normal fibers. The Ca 2؉ -release reduction is consistent with that previously measured using global detection techniques.calcium signals ͉ excitation-contraction coupling ͉ muscular dystrophy ͉ muscle physiology ͉ confocal spot detection D uchenne muscular dystrophy (DMD), the most common debilitating genetic disorder affecting boys, is caused by mutations that lead to the improper expression of the protein dystrophin, a major component of the dystrophin glycoprotein complex (DGC) in skeletal muscle (1, 2). A great deal of our understanding of the physiological impact of the absence of dystrophin comes from experimental evidence obtained from studies of the mdx mouse, an animal model of DMD that exhibits a similar alteration of the DGC (for a review see ref.3). Nevertheless, the pathophysiology of DMD is far from being understood.Skeletal muscle fibers from both DMD patients and mdx mice display significantly reduced specific force (4-6), whereas the contractile apparatus seems to be normal (7). By recording global Ca 2ϩ transients in response to both action potential (AP) stimulation (8) and voltage clamp pulses (9), we have recently demonstrated that the ability of the sarcoplasmic reticulum (SR) to release Ca 2ϩ is significantly reduced in mdx muscle fibers compared with that of normal mice. Altogether, our results reporting alterations in the physiology of Ca 2ϩ release in mdx muscle fibers provide a reasonable explanation for muscle weakness in dystrophic fibers.Our observation that the Ca 2ϩ -release flux measured from global detection experiments is reduced in mdx muscle fibers, whereas its voltage dependence ...

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Section: Discussionmentioning

confidence: 93%

Dystrophic skeletal muscle fibers display alterations at the level of calcium microdomains

DiFranco

Woods

Capote

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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“…Indeed, greater rates of relaxation may reflect enhanced expression of Ca 2ϩ -handling proteins such as parvalbumin. Parvalbumin is a Ca 2ϩ -binding protein present in the cytosol, and in fast-twitch muscles such as the TA, the expression of parvalbumin is reduced starting at disease onset in mdx mice (39). Mdx:parvalbumin doubleknockout mice display greater decrements in force-generating capacity of EDL muscles compared with mdx mice, demonstrating further that reductions in Ca 2ϩ -handling proteins can negatively affect muscle function (36).…”

Section: Improved Contractility As a Results Of Repeated Bouts Of Eccementioning

confidence: 99%

Adaptive strength gains in dystrophic muscle exposed to repeated bouts of eccentric contraction

Call¹,

Eckhoff²,

Baltgalvis

et al. 2011

Journal of Applied Physiology

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“…Such differences may in turn modulate the calcium-dependent proteolysis in a muscle type-specific way. Low levels of parvalbumin (Ͻ2.5-fold), a protein that links calcium and a relaxing factor in fast muscles (39), together with the concomitant downregulation of genes encoding ␣ 1 -protease inhibitors type 1, 3, and 5 (Ͻ2.2-fold), could provoke an intensed proteolytic activity within the mdx diaphragm cells and a massive degeneration/disorganization with aging. Relatively low levels of calcium, resulting from higher contents of parvalbumins and of protease inhibitors, apparently prevented the mdx hindlimb cells from such a rapid and dramatic degeneration.…”

Section: Conclusion 2: Dystrophin Deficiency Causes Different Perturbmentioning

confidence: 99%

Global/temporal gene expression in diaphragm and hindlimb muscles of dystrophin-deficient (mdx) mice

Rouger

Cunff

Steenman

et al. 2002

American Journal of Physiology-Cell Physiology

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The mdx mouse is a model for human Duchenne muscular dystrophy (DMD), an X-linked degenerative disease of skeletal muscle tissue characterized by the absence of the dystrophin protein. The mdx mice display a much milder phenotype than DMD patients. After the first week of life when all mdx muscles evolve like muscles of young DMD patients, mdx hindlimb muscles substantially compensate for the lack of dystrophin, whereas mdx diaphragm muscle becomes progressively affected by the disease. We used cDNA microarrays to compare the expression profile of 1,082 genes, previously selected by a subtractive method, in control and mdx hindlimb and diaphragm muscles at 12 time points over the first year of the mouse life. We determined that 1) the dystrophin gene defect induced marked expression remodeling of 112 genes encoding proteins implicated in diverse muscle cell functions and 2) two-thirds of the observed transcriptomal anomalies differed between adult mdx hindlimb and diaphragm muscles. Our results showed that neither mdx diaphram muscle nor mdx hindlimb muscles evolve entirely like the human DMD muscles. This finding should be taken under consideration for the interpretation of future experiments using mdx mice as a model for therapeutic assays.

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A developmental change in the content of parvalbumin in normal and dystrophic mouse (mdx) muscle

Cited by 20 publications

References 24 publications

Dystrophic skeletal muscle fibers display alterations at the level of calcium microdomains

Dystrophic skeletal muscle fibers display alterations at the level of calcium microdomains

Adaptive strength gains in dystrophic muscle exposed to repeated bouts of eccentric contraction

Global/temporal gene expression in diaphragm and hindlimb muscles of dystrophin-deficient (mdx) mice

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