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 ◽  
...  
1994 ◽  
Vol 36 (1) ◽  
pp. 75-83
Author(s):  
Hicham Bekkari ◽  
Driss Sekkat ◽  
Jean Straczek ◽  
Ketsia Hess ◽  
Francine Belleville-Nabet ◽  
...  

2000 ◽  
Vol 16 (5) ◽  
pp. 698-702 ◽  
Author(s):  
N.-A.S. Sunstrom ◽  
R.D. Gay ◽  
D.C. Wong ◽  
N.A. Kitchen ◽  
L. DeBoer ◽  
...  

1986 ◽  
Vol 261 (30) ◽  
pp. 14076-14081
Author(s):  
J M Podskalny ◽  
D G Rouiller ◽  
G Grunberger ◽  
R C Baxter ◽  
A McElduff ◽  
...  

1988 ◽  
Vol 8 (5) ◽  
pp. 2229-2232 ◽  
Author(s):  
A M Brunner ◽  
L E Gentry ◽  
J A Cooper ◽  
A F Purchio

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.


2011 ◽  
Vol 108 (11) ◽  
pp. 2759-2764 ◽  
Author(s):  
Richard Beatson ◽  
Daisy Sproviero ◽  
John Maher ◽  
Scott Wilkie ◽  
Joyce Taylor-Papadimitriou ◽  
...  

1991 ◽  
Vol 6 (3) ◽  
pp. 231-239 ◽  
Author(s):  
P. McKinnon ◽  
M. Ross ◽  
J. R. E. Wells ◽  
F. J. Ballard ◽  
G. L. Francis

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.


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