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Effect of inhibitors of signal transduction on IGF‐1‐induced protein synthesis associated with hypertrophy in cultured neonatal rat ventricular myocytes
Author(s) -
Lavandero Sergio,
Foncea Rocı́o,
Pérez Viviana,
Sapag-Hagar Mario
Publication year - 1998
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(98)00008-8
Subject(s) - wortmannin , genistein , myocyte , medicine , autophosphorylation , staurosporine , mapk/erk pathway , endocrinology , signal transduction , muscle hypertrophy , cardiac myocyte , protein kinase a , biology , protein kinase c , chemistry , pi3k/akt/mtor pathway , microbiology and biotechnology , kinase
IGF‐1 increased 2‐fold protein synthesis in cardiac myocytes. Genistein, whether added during preincubation or with IGF‐1 at the start of incubation, significantly inhibited the IGF‐1‐induced stimulation of protein synthesis, autophosphorylation of the β‐subunit of IGF‐1 receptor and inhibition of ERK. When added 1 or 6 h after IGF‐1, however, genistein was without effect. IGF‐1‐stimulated protein synthesis was also significantly inhibited by PD‐098059, staurosporine, and rapamycin, but not by wortmannin, in cardiac myocytes. Some inhibitors produced a reduction in cell size. Activation of the ERK cascade by IGF‐1 may be responsible for some of the features associated with cardiac myocyte hypertrophy.