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Your search keyword '"Butler-Browne, G.S."' showing total 45 results
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45 results on '"Butler-Browne, G.S."'

1. Slow myosin heavy chain expression in the absence of muscle activity

Author

Agbulut, O., Vignaud, A., Hourde, C., Mouisel, E., Fougerousse, F., Butler-Browne, G.S., and Ferry, A.

Subjects
Atrophy -- Research, Myosin -- Physiological aspects, Muscles -- Physiological aspects, Biological sciences
Abstract

Innervation has been generally accepted to be a major factor involved in both triggering and maintaining the expression of slow myosin heavy chain (MHC-1) in skeletal muscle. However, previous findings from our laboratory have suggested that, in the mouse, this is not always the case (30). Based on these results, we hypothesized that neurotomy would not markedly reduced the expression of MHC-1 protein in the mouse soleus muscles. In addition, other cellular, biochemical, and functional parameters were also studied in these denervated soleus muscles to complete our study. Our results show that denervation reduced neither the relative amount of MHC-1 protein, nor the percentage of muscle fibers expressing MHC-1 protein (P > 0.05). The fact that MHC-1 protein did not respond to muscle inactivity was confirmed in three different mouse strains (129/SV, C57BL/6, and CD1). In contrast, all of the other histological, biochemical, and functional muscle parameters were markedly altered by denervation. Cross-sectional area (CSA) of muscle fibers, maximal tetanic isometric force, maximal velocity of shortening, maximal power, and citrate synthase activity were all reduced in denervated muscles compared with innervated muscles (P < 0.05). Contraction and one-half relaxation times of the twitch were also increased by denervation (P < 0.05). Addition of tenotomy to denervation had no further effect on the relative expression of MHC-1 protein (P > 0.05), despite a greater reduction in CSA and citrate synthase activity (P < 0.05). In conclusion, a deficit in neural input leads to marked atrophy and reduction in performance in mouse soleus muscles. However, the maintenance of the relative expression of slow MHC protein is independent of neuromuscular activity in mice. skeletal muscle; tenotomy; force; slow myosin heavy chain; power; velocity of shortening; oxidative capacity; atrophy

Published
2009

5. Clones of human satellite cells can express in vitro both fast and slow myosin heavy chains

Author

Edom, F., Mouly, V., Barbet, J.P., Fiszman, M.Y., and Butler-Browne, G.S.

Subjects
Myosin -- Research, Muscle cells -- Research, Gene expression -- Analysis, Biological sciences
Abstract

Human satellite cells derived from quadriceps and masseter muscles do not express fast and slow myosin heavy chains (MHCs). However, fused muscle cell cultures express matured fast and slow MHCs along with fetal and embryonic isoforms. The fast and slow MHCs are coexpressed in the same myotubes with the slow MHCs limited to the nuclear region.

Published
1994

8. Generation of Isogenic D4Z4 Contracted and Noncontracted Immortal Muscle Cell Clones from a Mosaic Patient A Cellular Model for FSHD

Author

Krom, Y.D., Dumonceaux, J., Mamchaoui, K., Hamer, B. den, Mariot, V., Negroni, E., Geng, L.N., Martin, N., Tawil, R., Tapscott, S.J., Engelen, B.G.M. van, Mouly, V., Butler-Browne, G.S., and Maarel, S.M. van der

Subjects
musculoskeletal diseases, congenital, hereditary, and neonatal diseases and abnormalities, Human Movement & Fatigue [DCN MP - Plasticity and memory NCEBP 10]
Abstract

Item does not contain fulltext In most cases facioscapulohumeral muscular dystrophy (FSHD) is caused by contraction of the D4Z4 repeat in the 4q subtelomere. This contraction is associated with local chromatin decondensation and derepression of the DUX4 retrogene. Its complex genetic and epigenetic cause and high clinical variability in disease severity complicate investigations on the pathogenic mechanism underlying FSHD. A validated cellular model bypassing the considerable heterogeneity would facilitate mechanistic and therapeutic studies of FSHD. Taking advantage of the high incidence of somatic mosaicism for D4Z4 repeat contraction in de novo FSHD, we have established a clonal myogenic cell model from a mosaic patient. Individual clones are genetically identical except for the size of the D4Z4 repeat array, being either normal or FSHD sized. These clones retain their myogenic characteristics, and D4Z4 contracted clones differ from the noncontracted clones by the bursts of expression of DUX4 in sporadic nuclei, showing that this burst-like phenomenon is a locus-intrinsic feature. Consequently, downstream effects of DUX4 expression can be observed in D4Z4 contracted clones, like differential expression of DUX4 target genes. We also show their participation to in vivo regeneration with immunodeficient mice, further expanding the potential of these clones for mechanistic and therapeutic studies. These cell lines will facilitate pairwise comparisons to identify FSHD-specific differences and are expected to create new opportunities for high-throughput drug screens.

Published
2012
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17. Skeletal muscle regeneration and the mitotic clock

Author

Renault, V, primary, Piron-Hamelin, G, additional, Forestier, C, additional, DiDonna, S, additional, Decary, S, additional, Hentati, F, additional, Saillant, G, additional, Butler-Browne, G.S, additional, and Mouly, V, additional

Published
2000
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19. Reversible Immortalization of Human Myogenic Cells by Site-Specific Excision of a Retrovirally Transferred Oncogene

Author

Berghella, L., primary, Angelis, L. De, additional, Coletta, M., additional, Berarducci, B., additional, Sonnino, C., additional, Salvatori, G., additional, Anthonissen, C., additional, Cooper, R., additional, Butler-Browne, G.S., additional, Mouly, V., additional, Ferrari, G., additional, Mavilio, F., additional, and Cossu, G., additional

Published
1999
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36. Human Muscle Precursor Cell Regeneration in the Mouse Host Is Enhanced by Growth Factors

Author

Brimah, K., Ehrhardt, J., Mouly, V., Butler-Browne, G.S., Partridge, T.A., and Morgan, J.E.

Abstract

The aim of this study was to optimize human muscle formation in vivo from implanted human muscle precursor cells. We transplanted donor muscle precursor cells (MPCs) prepared from postnatal or fetal human muscle into immunodeficient host mice and showed that irradiation of host muscle significantly enhanced muscle formation by donor cells. The amount of donor muscle formed in cryodamaged host muscle was increased by exposure of donor cells to growth factors before their implantation into injured host muscle. Insulin-like growth factor type I (IGF-I) significantly increased the amount of muscle formed by postnatal human muscle cells, but not by fetal human MPCs. However, treatment of fetal muscle cells with IGF-I, in combination with basic fibroblast growth factor and plasmin, significantly increased the amount of donor muscle formed. In vivo, human MPCs formed mosaic human–mouse muscle fibers, in which each human myonucleus was associated with a zone of human sarcolemmal protein spectrin.

Published
2004
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37. Extended Amplification In Vitro and Replicative Senescence: Key Factors Implicated in the Success of Human Myoblast Transplantation

Author

Cooper, R.N., Thiesson, D., Furling, D., Di Santo, J.P., Butler-Browne, G.S., and Mouly, V.

Abstract

The limited success of human myoblast transplantation has been related to immune rejection, poor survival, and limited spread of injected myoblasts after transplantation. An important issue that has received little attention, but is nevertheless of fundamental importance in myoblast transplantation protocols, is the proliferative capacity of human satellite cells. Previous studies from our laboratory have demonstrated that the maximum number of divisions that a population of satellite cells can make decreases with age during the first two decades of life then stabilizes in adulthood. These observations indicate that when satellite cells are used as vectors in myoblast transplantation protocols it is important to consider donor age and the number of divisions that the cells have made prior to transplantation as limiting factors in obtaining an optimal number of donor derived muscle fibers. In this study, myoblasts derived from donors of different ages (newborn, 17 years old, and 71 years old) were isolated and amplified in culture. Their potential to participate in in vivo muscle regeneration in RAG2-/-/γc/C5 triple immunodeficient hosts after implantation was evaluated at 4 and 8 weeks postimplantation. Our results demonstrate that prolonged amplification in culture and the approach to replicative senescence are both important factors that may condition the success of myoblast transplantation protocols.

Published
2003
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38. Clones of Human Satellite Cells Can Express in Vitroboth Fast and Slow Myosin Heavy Chains

Author

Edom, F., Mouly, V., Barbet, J.P., Fiszman, M.Y., and Butler-Browne, G.S.

Abstract

In order to test the diversification among satellite cells in man, satellite cells were isolated from human quadriceps and masseter muscles. The growth kinetics and morphological features of these cells were determined in vitroand the expression of the different myosin heavy (embryonic, fetal, fast, and slow) and light chain isoforms was analyzed. In all satellite cell cultures, only the four fast-type light chains (MLClemb, MLC1F, MLC2F, and MLC3F) were synthesized and no slow myosin light chains were ever detected. However, we found that fused cultures of human satellite cells express both adult fast and slow myosin heavy chains (MHCs), in addition to embryonic and fetal isoforms. In order to determine if distinct fast and slow cell lineages could be detected among the satellite cells, a clonal analysis was carried out on both cell populations. This analysis was first carried out on clonal populations and was confirmed by the analysis of isolated clones. Double-labeling experiments confirmed that all myogenic clones which expressed fast MHC also coexpressed slow MHC. Therefore, we found no evidence for the existence of different fast and slow satellite cell lineages in human postnatal skeletal muscle.

Published
1994
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