Insulin-Like Growth Factor-I and Transferrin Mediate Growth and Survival of Chinese Hamster Ovary Cells

2000 ◽  
Vol 16 (5) ◽  
pp. 698-702 ◽  
Author(s):  
N.-A.S. Sunstrom ◽  
R.D. Gay ◽  
D.C. Wong ◽  
N.A. Kitchen ◽  
L. DeBoer ◽  
...  
Keyword(s):  
Growth Factor ◽  
Chinese Hamster Ovary ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Insulin Like Growth Factor ◽  
Ovary Cells ◽  
Growth And Survival ◽  
Factor I ◽  
Growth Factor I

scholarly journals Glycosylation defects alter insulin but not insulin-like growth factor I binding to Chinese hamster ovary cells.

1986 ◽  
Vol 261 (30) ◽  
pp. 14076-14081
Author(s):  
J M Podskalny ◽  
D G Rouiller ◽  
G Grunberger ◽  
R C Baxter ◽  
A McElduff ◽  
...  
Keyword(s):  
Growth Factor ◽  
Chinese Hamster Ovary ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Insulin Like Growth Factor ◽  
Ovary Cells ◽  
Factor I ◽  
Growth Factor I

scholarly journals Differential phosphorylation of IRS-1 by insulin and insulin-like growth factor I receptors in Chinese hamster ovary cells

2001 ◽  
Vol 171 (1) ◽  
pp. 153-162 ◽  
Author(s):  
M Amoui ◽  
BP Craddock ◽  
WT Miller
Keyword(s):  
Growth Factor ◽  
Insulin Receptor ◽  
Chinese Hamster Ovary ◽  
Chinese Hamster Ovary Cells ◽  
Tyrosine Phosphatase ◽  
Chinese Hamster ◽  
Insulin Like Growth Factor ◽  
Factor I ◽  
Growth Factor I ◽  
Differential Phosphorylation

Insulin receptor (IR) and insulin-like growth factor I receptor (IGF-IR) are closely related receptor tyrosine kinases. Despite their high degree of homology, recent evidence suggests that the two receptors have distinct biological roles. In several recent studies, the cytoplasmic tyrosine kinase domains of the two receptors have been shown to possess different signalling specificities. In this study, we examine the hypothesis that differential phosphorylation of insulin receptor substrate 1 (IRS-1) may contribute to these differences in signalling between the two receptors. Using Chinese hamster ovary (CHO) cells stably expressing human IR or IGF-IR and activated by their respective ligands, we show that there are differences between the two receptors with regard to the complement of SH2-containing proteins recruited to IRS-1. In particular, IGF-IR appears to couple IRS-1 preferentially to Grb2 whereas, in contrast, IR appears to couple IRS-1 preferentially to the p85 subunit of phosphatidyl inositol 3-kinase (PI3-kinase) and to Nck. The two receptors couple IRS-1 equally to the tyrosine phosphatase SHP2. We have also generated phosphospecific antibodies to three important tyrosine phosphorylation sites on IRS-1 (pY608, pY895 and pY1172). We used these antibodies to probe the phosphorylation status of these sites in intact CHO/IR and CHO/IGF-IR cells. In the case of pY608, these results also show evidence for differential phosphorylation of IRS-1 by the two receptors. Taken together, the results presented here support the notion that the cytoplasmic domains of IR and IGF-IR have differences in their intrinsic signalling potentials.

Expression, purification and characterization of secreted recombinant human insulin-like growth factor-I (IGF-I) and the potent variant des(1–3)IGF-I in Chinese hamster ovary cells

1991 ◽  
Vol 6 (3) ◽  
pp. 231-239 ◽  
Author(s):  
P. McKinnon ◽  
M. Ross ◽  
J. R. E. Wells ◽  
F. J. Ballard ◽  
G. L. Francis
Keyword(s):  
Growth Factor ◽  
Human Insulin ◽  
Chinese Hamster Ovary ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Recombinant Human Insulin ◽  
Ovary Cells ◽  
Factor I ◽  
Igf I ◽  
Recombinant Peptides

ABSTRACT Recombinant human insulin-like growth factor-I (hIGF-I) and a biologically potent variant lacking the N-terminal tripeptide (des(1–3)IGF-I) were produced from transfected Chinese hamster ovary cells. The constructs encoding the signal peptide, sequence of the mature peptide and a C-terminal extension peptide were expressed under the control of a Rous sarcoma virus promoter. Successfully transfected clones secreting correctly processed recombinant hIGF-I or des(1–3)IGF-I were selected by their secretion of IGF-I-like activity into the culture medium. The recombinant peptides were purified to homogeneity as assessed by high-performance liquid chromatography and N-terminal sequence analysis. The purified recombinant peptides exhibited biological potencies equivalent to authentic IGF-I and des(1–3)IGF-I respectively.

Expression of secreted recombinant human insulin-like growth factor-II (IGF-II) in Chinese hamster ovary cells

1994 ◽  
Vol 36 (1) ◽  
pp. 75-83
Author(s):  
Hicham Bekkari ◽  
Driss Sekkat ◽  
Jean Straczek ◽  
Ketsia Hess ◽  
Francine Belleville-Nabet ◽  
...  
Keyword(s):  
Growth Factor ◽  
Human Insulin ◽  
Chinese Hamster Ovary ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Insulin Like Growth Factor ◽  
Recombinant Human Insulin ◽  
Ovary Cells ◽  
Factor Ii

Paradoxical biological effects of overexpressed insulin-like growth factor-1 receptors in chinese hamster ovary cells

1993 ◽  
Vol 156 (1) ◽  
pp. 145-152 ◽  
Author(s):  
Hisanori Kato ◽  
Teresa N. Faria ◽  
Bethel Stannard ◽  
Rachel Levy-Toledano ◽  
Simeon I. Taylor ◽  
...  
Keyword(s):  
Growth Factor ◽  
Chinese Hamster Ovary ◽  
Biological Effects ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Insulin Like Growth Factor ◽  
Ovary Cells

scholarly journals Recombinant type 1 transforming growth factor beta precursor produced in Chinese hamster ovary cells is glycosylated and phosphorylated.

1988 ◽  
Vol 8 (5) ◽  
pp. 2229-2232 ◽  
Author(s):  
A M Brunner ◽  
L E Gentry ◽  
J A Cooper ◽  
A F Purchio
Keyword(s):  
Growth Factor ◽  
Transforming Growth Factor Beta ◽  
Chinese Hamster Ovary ◽  
Transforming Growth Factor ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Tgf Beta ◽  
Ovary Cells ◽  
Growth Factor Beta

Analyses of cDNA clones coding for simian type 1 transforming growth factor beta (TGF-beta 1) suggest that there are three potential sites for N-linked glycosylation located in the amino terminus of the precursor region. Analysis of [3H]glucosamine-labeled serum-free supernatants from a line of Chinese hamster ovary cells which secrete high levels of recombinant TGF-beta 1 indicate that the TGF-beta 1 precursor, but not the mature form, is glycosylated. Digestion with neuraminidase resulted in a shift in migration of the two TGF-beta 1 precursor bands, which suggests that they contain sialic acid residues. Endoglycosidase H had no noticeable effect. Treatment with N-glycanase produced two faster-migrating sharp bands, the largest of which had a molecular weight of 39 kilodaltons. TGF-beta 1-specific transcripts produced by SP6 polymerase programmed the synthesis of a 42-kilodalton polypeptide which, we suggest, is the unmodified protein backbone of the precursor. Labeling with 32Pi showed that the TGF-beta 1 precursor was phosphorylated in the amino portion of the molecule.

Production of human mutant biologically active hepatocyte growth factor in Chinese hamster ovary cells

2017 ◽  
Vol 47 (5) ◽  
pp. 489-495 ◽  
Author(s):  
Dongsheng Xu ◽  
Aini Wan ◽  
Lin Peng ◽  
Yun Chen ◽  
Yang He ◽  
...  
Keyword(s):  
Growth Factor ◽  
Hepatocyte Growth Factor ◽  
Chinese Hamster Ovary ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Biologically Active ◽  
Ovary Cells ◽  
Hepatocyte Growth

Transforming growth factor-β1 is constitutively secreted by chinese hamster ovary cells and is functional in human cells

2011 ◽  
Vol 108 (11) ◽  
pp. 2759-2764 ◽  
Author(s):  
Richard Beatson ◽  
Daisy Sproviero ◽  
John Maher ◽  
Scott Wilkie ◽  
Joyce Taylor-Papadimitriou ◽  
...  
Keyword(s):  
Growth Factor ◽  
Chinese Hamster Ovary ◽  
Transforming Growth Factor ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Transforming Growth Factor Β1 ◽  
Human Cells ◽  
Ovary Cells

Recombinant Human Transforming Growth Factor-β1: Expression by Chinese Hamster Ovary Cells, Isolation, and Characterization

1993 ◽  
Vol 4 (2) ◽  
pp. 130-140 ◽  
Author(s):  
L. Bourdrel ◽  
C.H. Lin ◽  
S.L. Lauren ◽  
R.H. Elmore ◽  
B.J. Sugarman ◽  
...  
Keyword(s):  
Growth Factor ◽  
Chinese Hamster Ovary ◽  
Transforming Growth Factor ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Transforming Growth Factor Β1 ◽  
Ovary Cells ◽  
Isolation And Characterization
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