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Yutaka Shimada - One of the best experts on this subject based on the ideXlab platform.
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distribution of Connectin titin nebulin and α actinin at myotendinous junctions of chicken pectoralis muscles an immunofluorescence and immunoelectron microscopic study
Journal of Muscle Research and Cell Motility, 1993Co-Authors: Fujio Atsuta, K. Maruyama, Kenichi Sato, Yutaka ShimadaAbstract:The distribution of Connectin (titin), nebulin and α-actinin in the areas of myotendinous junctions of chicken pectoralis muscles was examined by immunocytochemical methods. Staining with antibodies against Connectin (4C9, SM1 and P1200) and nebulin formed ‘doublets’ flanking nonterminal Z-bands; near the end of muscle fibres ‘singlets’ were seen within the terminal sarcomere on the side adjacent to the terminal Z-bands. The apical regions of muscle processes, where no myosin filaments are present although actin filaments exist, were reactive with anti-nebulin but not with anti-connection. Antibodies against pectoralis (skeletal muscle type) α-actinin stained non terminal Z-bands and that against gizzard (smooth muscle type) the sarcolemma. Terminal Z-bands were unreactive with both of these antibodies. These findings indicate that, although terminal and nonterminal Z-bands differ in their molecular composition, Connectin and nebulin filaments appear to link myosin and actin filaments, respectively, to both Z-band types.
K. Maruyama - One of the best experts on this subject based on the ideXlab platform.
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Biodiversity of the localization of the epitopes to Connectin antibodies in the sarcomeres of lamprey, electric ray, and horse mackerel skeletal muscles.
Tissue & cell, 1994Co-Authors: Yuuki Kawamura, Yukiko Ohtani, K. MaruyamaAbstract:Abstract SDS gel electrophoresis showed the presence of Connectin, ∼3000 kDa, in skeletal muscles of fishes, lamprey, electric ray and horse mackerel. The antibodies to avian or mammalian skeletal muscle Connectin, 3B9 and Pc1200, reacted with all the fish Connectins. However, a monoclonal antibody SM1 recognized electric ray Connectin but did not react with lamprey and horse mackerel Connectins. Immunoelectron microscopy revealed that the epitope to Pc1200 was localized at the periphery of the Z line of all the fish muscle sarcomeres and that to SM1 was located at the N 2 line in the I band of ray muscle. These two localizations are the same as those in rabbit, chicken and frog skeletal muscles. On the other hand, the positions of epitopes to 3B9 were variable in the three classes of fishes, although all of them were localized in the A band. Some of the epitope positions were common to those in chicken skeletal muscle. Thus the present work demonstrates biodiversity of Connectin in fish skeletal muscles, distinct from avian and mammalian skeletal muscles.
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distribution of Connectin titin nebulin and α actinin at myotendinous junctions of chicken pectoralis muscles an immunofluorescence and immunoelectron microscopic study
Journal of Muscle Research and Cell Motility, 1993Co-Authors: Fujio Atsuta, K. Maruyama, Kenichi Sato, Yutaka ShimadaAbstract:The distribution of Connectin (titin), nebulin and α-actinin in the areas of myotendinous junctions of chicken pectoralis muscles was examined by immunocytochemical methods. Staining with antibodies against Connectin (4C9, SM1 and P1200) and nebulin formed ‘doublets’ flanking nonterminal Z-bands; near the end of muscle fibres ‘singlets’ were seen within the terminal sarcomere on the side adjacent to the terminal Z-bands. The apical regions of muscle processes, where no myosin filaments are present although actin filaments exist, were reactive with anti-nebulin but not with anti-connection. Antibodies against pectoralis (skeletal muscle type) α-actinin stained non terminal Z-bands and that against gizzard (smooth muscle type) the sarcolemma. Terminal Z-bands were unreactive with both of these antibodies. These findings indicate that, although terminal and nonterminal Z-bands differ in their molecular composition, Connectin and nebulin filaments appear to link myosin and actin filaments, respectively, to both Z-band types.
Fujio Atsuta - One of the best experts on this subject based on the ideXlab platform.
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distribution of Connectin titin nebulin and α actinin at myotendinous junctions of chicken pectoralis muscles an immunofluorescence and immunoelectron microscopic study
Journal of Muscle Research and Cell Motility, 1993Co-Authors: Fujio Atsuta, K. Maruyama, Kenichi Sato, Yutaka ShimadaAbstract:The distribution of Connectin (titin), nebulin and α-actinin in the areas of myotendinous junctions of chicken pectoralis muscles was examined by immunocytochemical methods. Staining with antibodies against Connectin (4C9, SM1 and P1200) and nebulin formed ‘doublets’ flanking nonterminal Z-bands; near the end of muscle fibres ‘singlets’ were seen within the terminal sarcomere on the side adjacent to the terminal Z-bands. The apical regions of muscle processes, where no myosin filaments are present although actin filaments exist, were reactive with anti-nebulin but not with anti-connection. Antibodies against pectoralis (skeletal muscle type) α-actinin stained non terminal Z-bands and that against gizzard (smooth muscle type) the sarcolemma. Terminal Z-bands were unreactive with both of these antibodies. These findings indicate that, although terminal and nonterminal Z-bands differ in their molecular composition, Connectin and nebulin filaments appear to link myosin and actin filaments, respectively, to both Z-band types.
Si Shangzhuo - One of the best experts on this subject based on the ideXlab platform.
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parking Connecting structure of suspension type monorail vehicle and suspension type monorail vehicle
2017Co-Authors: Lei Zhangwen, Shang Jiangao, Qu Haiyang, Chen Jingjing, Wang Junmin, Li Liang, Si ShangzhuoAbstract:The invention discloses a parking Connecting structure of a suspension type monorail vehicle and the suspension type monorail vehicle. The parking Connecting structure of the suspension type monorail vehicle comprises a Connecting rod, a Connecting seat and a Connecting beam, wherein the Connecting rod is used for transmitting vertical loads, longitudinal traction brake force and transverse swinging force between a suspension type vehicle body and a traveling component, the upper end of the Connecting rod is used for being fixedly connected with the traveling component, the lower end of the Connecting rod is hinged to the Connecting seat, and the Connecting seat is fixedly connected with the Connecting beam. The parking Connecting structure of the suspension type monorail vehicle realizes non-rigid connection between the suspension type monorail vehicle body and a bogie, and internal stress caused by movement of the suspension type monorail vehicle body is solved.
Kenichi Sato - One of the best experts on this subject based on the ideXlab platform.
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distribution of Connectin titin nebulin and α actinin at myotendinous junctions of chicken pectoralis muscles an immunofluorescence and immunoelectron microscopic study
Journal of Muscle Research and Cell Motility, 1993Co-Authors: Fujio Atsuta, K. Maruyama, Kenichi Sato, Yutaka ShimadaAbstract:The distribution of Connectin (titin), nebulin and α-actinin in the areas of myotendinous junctions of chicken pectoralis muscles was examined by immunocytochemical methods. Staining with antibodies against Connectin (4C9, SM1 and P1200) and nebulin formed ‘doublets’ flanking nonterminal Z-bands; near the end of muscle fibres ‘singlets’ were seen within the terminal sarcomere on the side adjacent to the terminal Z-bands. The apical regions of muscle processes, where no myosin filaments are present although actin filaments exist, were reactive with anti-nebulin but not with anti-connection. Antibodies against pectoralis (skeletal muscle type) α-actinin stained non terminal Z-bands and that against gizzard (smooth muscle type) the sarcolemma. Terminal Z-bands were unreactive with both of these antibodies. These findings indicate that, although terminal and nonterminal Z-bands differ in their molecular composition, Connectin and nebulin filaments appear to link myosin and actin filaments, respectively, to both Z-band types.