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Modulation of a major 30‐kDa skeletal muscle protein by thyroid hormone
Author(s) -
Gag Jacques,
Ho-Kim My Anh,
Champagne Chantal,
Tremblay Roland R.,
Rogers Peter A.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)81098-x
Subject(s) - medicine , triiodothyronine , endocrinology , skeletal muscle , thyroid , polysome , thyroidectomy , in vitro , hormone , soleus muscle , protein biosynthesis , chemistry , messenger rna , biology , biochemistry , rna , gene , ribosome
Thyroidectomy results in the transformation of type II fibres to type I in rat soleus muscle. In vitro translations containing polyribosomes indicate that the template activity of mRNA coding for a 30‐kDa protein is increased in hypothyroid (6 months) rats. The cellular content of this protein is also increased in hypothyroid rats. The in vitro synthesis of the 30‐kDa protein is not observed in thyroidectomized (10 weeks) rats that have been treated with triiodothyronine. The synthesis and accumulation of this protein are directly related to the proportion of type I fibres in rat skeletal muscle and appear to be modulated by thyroid hormone.