scholarly journals Chicken Insulin-Like Growth Factor-I Stimulates Protein Synthesis of Chicken Embryo Myoblasts Cultured in Serum-Free Medium

2001 ◽  
Vol 14 (1) ◽  
pp. 17-20 ◽  
Author(s):  
K. Kita ◽  
J. Okumura
Keyword(s):  
Protein Synthesis ◽  
Growth Factor ◽  
Chicken Embryo ◽  
Insulin Like Growth Factor ◽  
Serum Free Medium ◽  
Free Medium ◽  
Serum Free ◽  
Factor I ◽  
Growth Factor I

scholarly journals Effect of a null mutation of the insulin-like growth factor I receptor gene on growth and transformation of mouse embryo fibroblasts.

1994 ◽  
Vol 14 (6) ◽  
pp. 3604-3612 ◽  
Author(s):  
C Sell ◽  
G Dumenil ◽  
C Deveaud ◽  
M Miura ◽  
D Coppola ◽  
...  
Keyword(s):  
Growth Factors ◽  
Growth Factor ◽  
Soft Agar ◽  
T Antigen ◽  
Insulin Like Growth Factor ◽  
Serum Free Medium ◽  
Free Medium ◽  
Serum Free ◽  
Factor I ◽  
Growth Factor I

Fibroblast cell lines, designated R- and W cells, were generated, respectively, from mouse embryos homozygous for a targeted disruption of the Igf1r gene, encoding the type 1 insulin-like growth factor receptor, and from their wild-type littermates. W cells grow normally in serum-free medium supplemented with various combinations of purified growth factors, while pre- and postcrisis R- cells cannot grow, as they are arrested before entering the S phase. R- cells are able to grow in 10% serum, albeit more slowly than W cells, and with all phases of the cell cycle being elongated. An activated Ha-ras expressed from a stably transfected plasmid is unable to overcome the inability of R- cells to grow in serum-free medium supplemented with purified clones. Nevertheless, even in the presence of serum, R- cells stably transfected with Ha-ras, alone or in combination with simian virus 40 large T antigen, fail to form colonies in soft agar. Reintroduction into R- cells (or their derivatives) of a plasmid expressing the human insulin-like growth factor I receptor RNA and protein restores their ability to grow with purified growth factors or in soft agar. The signaling pathways participating in cell growth and transformation are discussed on the basis of these results.

Effect of a null mutation of the insulin-like growth factor I receptor gene on growth and transformation of mouse embryo fibroblasts

1994 ◽  
Vol 14 (6) ◽  
pp. 3604-3612
Author(s):  
C Sell ◽  
G Dumenil ◽  
C Deveaud ◽  
M Miura ◽  
D Coppola ◽  
...  
Keyword(s):  
Growth Factors ◽  
Growth Factor ◽  
Soft Agar ◽  
T Antigen ◽  
Insulin Like Growth Factor ◽  
Serum Free Medium ◽  
Free Medium ◽  
Serum Free ◽  
Factor I ◽  
Growth Factor I

Fibroblast cell lines, designated R- and W cells, were generated, respectively, from mouse embryos homozygous for a targeted disruption of the Igf1r gene, encoding the type 1 insulin-like growth factor receptor, and from their wild-type littermates. W cells grow normally in serum-free medium supplemented with various combinations of purified growth factors, while pre- and postcrisis R- cells cannot grow, as they are arrested before entering the S phase. R- cells are able to grow in 10% serum, albeit more slowly than W cells, and with all phases of the cell cycle being elongated. An activated Ha-ras expressed from a stably transfected plasmid is unable to overcome the inability of R- cells to grow in serum-free medium supplemented with purified clones. Nevertheless, even in the presence of serum, R- cells stably transfected with Ha-ras, alone or in combination with simian virus 40 large T antigen, fail to form colonies in soft agar. Reintroduction into R- cells (or their derivatives) of a plasmid expressing the human insulin-like growth factor I receptor RNA and protein restores their ability to grow with purified growth factors or in soft agar. The signaling pathways participating in cell growth and transformation are discussed on the basis of these results.

Lanreotide Reduces Serum Free and Total Insulin-Like Growth Factor-I After Angioplasty

Circulation ◽  
1996 ◽  
Vol 94 (10) ◽  
pp. 2465-2471 ◽  
Author(s):  
Jan Frystyk ◽  
Christian Skjærbæk ◽  
Niels Alexander ◽  
Håkan Emanuelsson ◽  
Harry Suryapranata ◽  
...  
Keyword(s):  
Growth Factor ◽  
Insulin Like Growth Factor ◽  
Serum Free ◽  
Factor I ◽  
Growth Factor I

Insulin-like growth factor I accelerates protein synthesis in skeletal muscle during sepsis

1995 ◽  
Vol 269 (5) ◽  
pp. E977-E981 ◽  
Author(s):  
C. V. Jurasinski ◽  
T. C. Vary
Keyword(s):  
Protein Synthesis ◽  
Growth Factor ◽  
Peptide Chain ◽  
Translational Efficiency ◽  
Insulin Like Growth Factor ◽  
Recombinant Human Insulin ◽  
Chain Initiation ◽  
Factor I ◽  
Igf I ◽  
Growth Factor I

Sepsis causes an inhibition of protein synthesis in gastrocnemius that is resistant to the anabolic effects of insulin. The purpose of the present studies was to investigate the effect of recombinant human insulin-like growth factor I (IGF-I) on protein synthesis during a 30-min perfusion of the isolated rat hindlimb from septic rats. Inclusion of IGF-I (1 or 10 nM) in the perfusate stimulated protein synthesis in gastrocnemius of septic rats 2.5-fold and restored rates of protein synthesis to those observed in control rats. The stimulation of protein synthesis did not result from an increase in the RNA content but was correlated with a 2.5-fold increase in the translational efficiency. The enhanced translational efficiency was accompanied by a 33 and 55% decrease in the abundance of free 40S and 60S ribosomal subunits, respectively, indicating that IGF-I accelerated peptide-chain initiation relative to elongation/termination. These studies provide evidence that IGF-I can accelerate protein synthesis in gastrocnemius during chronic sepsis by reversing the sepsis-induced inhibition of peptide-chain initiation.

Changes in protein metabolism of ovine primary muscle cultures on treatment with growth hormone, insulin, insulin-like growth factor I or epidermal growth factor

1987 ◽  
Vol 112 (1) ◽  
pp. 87-96 ◽  
Author(s):  
J. M. M. Harper ◽  
J. B. Soar ◽  
P. J. Buttery
Keyword(s):  
Growth Hormone ◽  
Protein Synthesis ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Insulin Like Growth Factor ◽  
Factor I ◽  
Muscle Cultures ◽  
Epidermal Growth ◽  
Growth Factor I ◽  
High Concentrations

ABSTRACT Methods for the primary culture of muscle cells from fetal sheep were developed which gave high yields of cells. Myoblasts were grown in vitro, and allowed to fuse to form contractile multinucleate myotubes; these could be maintained in a good condition for at least 2 weeks. Protein turnover in these differentiated cultures was examined for sensitivity to each of four potentially anabolic peptide hormones and growth factors: insulin, insulin-like growth factor I (somatomedin C), epidermal growth factor and growth hormone. Insulin was found to have no effect except at high concentrations (1 μmol/l), compatible with its role as a somatomedin analogue. Insulin-like growth factor I was active at lower levels (1 nmol/l) but the cultures were not as responsive to it as were primary rat muscle cultures or differentiated L6 cells, which were tested in similar experiments. The maximum stimulation of protein synthesis observed with the ruminant system was only 16%. Epidermal growth factor was highly anabolic for primary cultures from sheep muscle, and the cells were very sensitive to it, half-maximal stimulation of protein synthesis being seen with concentrations as low as 20 pmol/l. No effects of bovine growth hormone were seen in the ovine system. However, an inhibition of protein breakdown was found with high concentrations (0·1 μmol/l) in the L6 rat myoblast cell line. It was found that the culture conditions used could affect the observed responses of protein synthesis and degradation, despite withdrawal of serum from the incubation media 22 h before testing. J. Endocr. (1987) 112, 87–96

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