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Connectin filaments link thick filaments and Z lines in frog skeletal muscle as revealed by immunoelectron microscopy

In an earlier study connectin, an elastic protein of striated muscle, was found to be associated with "gap filaments" originating from the thick filaments in the myofibril, but it was not clear whether it extends to Z lines or not (Maruyama, K., H. Sawada, S. Kimura, K. Ohashi, H. Higuchi,...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1985
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114010/
https://www.ncbi.nlm.nih.gov/pubmed/3905821
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description In an earlier study connectin, an elastic protein of striated muscle, was found to be associated with "gap filaments" originating from the thick filaments in the myofibril, but it was not clear whether it extends to Z lines or not (Maruyama, K., H. Sawada, S. Kimura, K. Ohashi, H. Higuchi, and Y. Umazume, 1984, J. Cell Biol., 99:1391-1397). In the present immunoelectron microscopic study using polyclonal antibodies against native connectin, we have concluded that the connectin structures are directly linked to Z lines from the thick (myosin) filaments in myofibrils of skinned fibers of frog skeletal muscle. There were five distinct antibody-binding stripes in each half of the A band and two stripes in the A-I junction region. Deposits of antibodies were recognized in I bands and Z lines. We suggest that connectin filaments run alongside the thick filaments, starting from a region approximately 0.15 micron from the center of the A band.
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spelling pubmed-21140102008-05-01 Connectin filaments link thick filaments and Z lines in frog skeletal muscle as revealed by immunoelectron microscopy J Cell Biol Articles In an earlier study connectin, an elastic protein of striated muscle, was found to be associated with "gap filaments" originating from the thick filaments in the myofibril, but it was not clear whether it extends to Z lines or not (Maruyama, K., H. Sawada, S. Kimura, K. Ohashi, H. Higuchi, and Y. Umazume, 1984, J. Cell Biol., 99:1391-1397). In the present immunoelectron microscopic study using polyclonal antibodies against native connectin, we have concluded that the connectin structures are directly linked to Z lines from the thick (myosin) filaments in myofibrils of skinned fibers of frog skeletal muscle. There were five distinct antibody-binding stripes in each half of the A band and two stripes in the A-I junction region. Deposits of antibodies were recognized in I bands and Z lines. We suggest that connectin filaments run alongside the thick filaments, starting from a region approximately 0.15 micron from the center of the A band. The Rockefeller University Press 1985-12-01 /pmc/articles/PMC2114010/ /pubmed/3905821 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Connectin filaments link thick filaments and Z lines in frog skeletal muscle as revealed by immunoelectron microscopy
title Connectin filaments link thick filaments and Z lines in frog skeletal muscle as revealed by immunoelectron microscopy
title_full Connectin filaments link thick filaments and Z lines in frog skeletal muscle as revealed by immunoelectron microscopy
title_fullStr Connectin filaments link thick filaments and Z lines in frog skeletal muscle as revealed by immunoelectron microscopy
title_full_unstemmed Connectin filaments link thick filaments and Z lines in frog skeletal muscle as revealed by immunoelectron microscopy
title_short Connectin filaments link thick filaments and Z lines in frog skeletal muscle as revealed by immunoelectron microscopy
title_sort connectin filaments link thick filaments and z lines in frog skeletal muscle as revealed by immunoelectron microscopy
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114010/
https://www.ncbi.nlm.nih.gov/pubmed/3905821