Premium
Thrombin‐induced inhibition of myoblast differentiation is mediated by Gβγ
Author(s) -
Nagao Motoshi,
Kaziro Yoshito,
Itoh Hiroshi
Publication year - 2000
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/s0014-5793(00)01458-7
Subject(s) - thrombin , myogenesis , heterotrimeric g protein , c2c12 , skeletal muscle , myocyte , chemistry , thrombin receptor , microbiology and biotechnology , biochemistry , receptor , biology , g protein , endocrinology , platelet , immunology
Thrombin has been shown to inhibit skeletal muscle differentiation. However, the mechanisms by which thrombin represses myogenesis remain unknown. Since the thrombin receptor couples to G i , G q/11 and G 12 , we examined which subunits of heterotrimeric guanine nucleotide‐binding regulatory proteins (Gα i , Gα q/11 , Gα 12 or Gβγ) participate in the thrombin‐induced inhibition of C2C12 myoblast differentiation. Gα i2 and Gα 11 had no inhibitory effect on the myogenic differentiation. Gα 12 prevented only myoblast fusion, whereas Gβγ inhibited both the induction of skeletal muscle‐specific markers and the myotube formation. In addition, the thrombin‐induced reduction of creatine kinase activity was blocked by the C‐terminal peptide of β‐adrenergic receptor kinase, which is known to sequester free Gβγ. These results suggest that the thrombin‐induced inhibition of muscle differentiation is mainly mediated by Gβγ.