Abstract
We report here the detection of a high molecular weight (greater than 400,000) cytoskeletal protein in the myogenic and neural tube derived structures of the chick embryo using a monoclonal antibody, F51H2. Immunohistological analysis reveals that this protein is concentrated in the myotome part of the somites, in the heart primordium, and in the neural tube at the end of the 2nd day of incubation. In cultured fibroblasts, the antibody appeared to decorate a filamentous network, although immunoreactivity was not detected on mesenchymal cells in situ. This network was also observed in cultured myoblasts where it has been demonstrated to be coincident to that of desmin. In colchicine-treated cells the immunoreactivity coincided with the perinuclear cap formed by the collapse of intermediate filaments (IFs). Immunoblot experiments confirmed the early distribution of F51H2 antigen in muscle and nerve tissues and its concentration in a salt-resistant IF-rich fraction of muscle tissues. In addition, there is a progressive loss of immunoreactivity during development. The immunoreactive band on sodium dodecyl sulfate gels was faint in tissues from newly hatched chickens and absent in adult tissues. It is suggested that the monoclonal antibody observed herein reacts with an embryo specific high molecular weight protein that is associated with IFs.
Published Version
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