Solid-Phase N-Terminus PEGylation of Recombinant Human Fibroblast Growth Factor 2 on Heparin-Sepharose Column

2012 ◽  
Vol 23 (4) ◽  
pp. 740-750 ◽  
Author(s):  
Zhifeng Huang ◽  
Chaohui Ye ◽  
Zhijun Liu ◽  
Xiaojie Wang ◽  
Huaibin Chen ◽  
...  
Keyword(s):  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Human Fibroblast ◽  
Solid Phase ◽  
Fibroblast Growth Factor 2 ◽  
Fibroblast Growth ◽  
Sepharose Column ◽  
N Terminus

scholarly journals A New 34-Kilodalton Isoform of Human Fibroblast Growth Factor 2 Is Cap Dependently Synthesized by Using a Non-AUG Start Codon and Behaves as a Survival Factor

1999 ◽  
Vol 19 (1) ◽  
pp. 505-514 ◽  
Author(s):  
Emmanuelle Arnaud ◽  
Christian Touriol ◽  
Christel Boutonnet ◽  
Marie-Claire Gensac ◽  
Stéphan Vagner ◽  
...  
Keyword(s):  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Human Fibroblast ◽  
The Other ◽  
In Vitro Translation ◽  
Start Codon ◽  
Fibroblast Growth Factor 2 ◽  
Initiation Codon ◽  
Fibroblast Growth

ABSTRACT Four isoforms of human fibroblast growth factor 2 (FGF-2) result from alternative initiations of translation at three CUG start codons and one AUG start codon. Here we characterize a new 34-kDa FGF-2 isoform whose expression is initiated at a fifth initiation codon. This 34-kDa FGF-2 was identified in HeLa cells by using an N-terminal directed antibody. Its initiation codon was identified by site-directed mutagenesis as being a CUG codon located at 86 nucleotides (nt) from the FGF-2 mRNA 5′ end. Both in vitro translation and COS-7 cell transfection using bicistronic RNAs demonstrated that the 34-kDa FGF-2 was exclusively expressed in a cap-dependent manner. This contrasted with the expression of the other FGF-2 isoforms of 18, 22, 22.5, and 24 kDa, which is controlled by an internal ribosome entry site (IRES). Strikingly, expression of the other FGF-2 isoforms became partly cap dependent in vitro in the presence of the 5,823-nt-long 3′ untranslated region of FGF-2 mRNA. Thus, the FGF-2 mRNA can be translated both by cap-dependent and IRES-driven mechanisms, the balance between these two mechanisms modulating the ratio of the different FGF-2 isoforms. The function of the new FGF-2 was also investigated. We found that the 34-kDa FGF-2, in contrast to the other isoforms, permitted NIH 3T3 cell survival in low-serum conditions. A new arginine-rich nuclear localization sequence (NLS) in the N-terminal region of the 34-kDa FGF-2 was characterized and found to be similar to the NLS of human immunodeficiency virus type 1 Rev protein. These data suggest that the function of the 34-kDa FGF-2 is mediated by nuclear targets.

scholarly journals Purification of the human fibroblast growth factor 2 using novel animal-component free materials

2020 ◽  
Vol 1626 ◽  
pp. 461367
Author(s):  
Svenja Nicolin Bolten ◽  
Anne-Sophie Knoll ◽  
Zhaopeng Li ◽  
Pia Gellermann ◽  
Iliyana Pepelanova ◽  
...  
Keyword(s):  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Human Fibroblast ◽  
Fibroblast Growth Factor 2 ◽  
Fibroblast Growth ◽  
Animal Component

scholarly journals Tumour suppressor p53 inhibits human fibroblast growth factor 2 expression by a post-transcriptional mechanism

Oncogene ◽  
2001 ◽  
Vol 20 (14) ◽  
pp. 1669-1677 ◽  
Author(s):  
Bruno Galy ◽  
Laurent Créancier ◽  
Catherine Zanibellato ◽  
Anne-Catherine Prats ◽  
Hervé Prats
Keyword(s):  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Human Fibroblast ◽  
Tumour Suppressor ◽  
Fibroblast Growth Factor 2 ◽  
Fibroblast Growth ◽  
Tumour Suppressor P53
Sign in / Sign up

Export Citation Format

Share Document