scholarly journals Hyaluronic acid-binding insulin-like growth factor-1: Creation of a gene encoding a bifunctional fusion protein

2020 ◽  
Vol 47 (12) ◽  
pp. 9749-9756
Author(s):  
Shuiliang Shi ◽  
Congrong Wang ◽  
Stephen B. Trippel
Keyword(s):  
Hyaluronic Acid ◽  
Growth Factor ◽  
Fusion Protein ◽  
Insulin Like Growth Factor ◽  
Gene Encoding ◽  
Bifunctional Fusion Protein ◽  
Hyaluronic Acid Binding

scholarly journals Enhanced Production of Insulin-Like Growth Factor I Fusion Protein in Escherichia coli by Coexpression of the Down-Regulated Genes Identified by Transcriptome Profiling

2003 ◽  
Vol 69 (8) ◽  
pp. 4737-4742 ◽  
Author(s):  
Jong Hyun Choi ◽  
Sang Jun Lee ◽  
Seok Jae Lee ◽  
Sang Yup Lee
Keyword(s):  
Escherichia Coli ◽  
Growth Factor ◽  
Fusion Protein ◽  
Transcriptome Profiling ◽  
Insulin Like Growth Factor ◽  
Gene Encoding ◽  
Factor I ◽  
Enhanced Production ◽  
Igf I ◽  
Growth Factor I

ABSTRACT The transcriptome profiles of recombinant Escherichia coli producing human insulin-like growth factor I fusion protein (IGF-If) during the high-cell-density fed-batch culture were analyzed using DNA microarrays. The expression levels of 529 genes were significantly altered after induction. About 200 genes were significantly down-regulated during the production of IGF-If after induction. Among these down-regulated genes, we rationally selected and coexpressed in E. coli producing IGF-If the prsA gene (encoding a phosphoribosyl pyrophosphate synthetase) and the glpF gene (encoding a glycerol transporter), which are involved in an early key step in the biosynthetic pathway of nucleotides and amino acids (Trp and His) and the first step in glycerol utilization, respectively. As a result, the production of IGF-If could be increased from 1.8 ± 0.13 (± standard deviation) to 4.3 ± 0.24 g/liter. The volumetric productivity was also increased from 0.36 ± 0.027 to 0.82 ± 0.048 g/liter/h. These results demonstrate that transcriptome profiling can provide invaluable information in designing engineered strains showing enhanced performance.

Chromosomal localization and preliminary characterization of the human gene encoding insulin-like growth factor II

1985 ◽  
Vol 69 (2) ◽  
pp. 170-173 ◽  
Author(s):  
P. de Pagter-Holthuizen ◽  
J. W. M. Höppener ◽  
M. Jansen ◽  
A. H. M. Geurts van Kessel ◽  
G. J. B. van Ommen ◽  
...  
Keyword(s):  
Growth Factor ◽  
Chromosomal Localization ◽  
Human Gene ◽  
Insulin Like Growth Factor ◽  
Gene Encoding ◽  
Preliminary Characterization ◽  
Factor Ii

The human gene encoding insulin-like growth factor I is located on chromosome 12

1985 ◽  
Vol 69 (2) ◽  
pp. 157-160 ◽  
Author(s):  
J. W. M. Höppener ◽  
P. de Pagter-Holthuizen ◽  
A. H. M. Geurts van Kessel ◽  
M. Jansen ◽  
S. D. Kittur ◽  
...  
Keyword(s):  
Growth Factor ◽  
Human Gene ◽  
Chromosome 12 ◽  
Insulin Like Growth Factor ◽  
Gene Encoding ◽  
Factor I ◽  
Growth Factor I

Cloning and characterization of the gene encoding murine insulin-like growth factor-binding protein-2, migfbp-2

Gene ◽  
1993 ◽  
Vol 124 (2) ◽  
pp. 281-286 ◽  
Author(s):  
J. Landwehr ◽  
K. Kaupmann ◽  
G. Heinrich ◽  
J. Schwander
Keyword(s):  
Growth Factor ◽  
Binding Protein ◽  
Insulin Like Growth Factor ◽  
Gene Encoding ◽  
Factor Binding

Production and characterization of recombinant insulin-like growth factor-I (IGF-I) and potent analogues of IGF-I, with Gly or Arg substituted for Glu 3, following their expression in Escherichia coli as fusion proteins

1992 ◽  
Vol 8 (1) ◽  
pp. 29-41 ◽  
Author(s):  
R. King ◽  
J. R. E. Wells ◽  
P. Krieg ◽  
M. Snoswell ◽  
J. Brazier ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Growth Factor ◽  
Fusion Protein ◽  
Fusion Proteins ◽  
Expression System ◽  
Insulin Like Growth Factor ◽  
Factor I ◽  
Igf I ◽  
Igf Binding ◽  
Growth Factor I

ABSTRACT The development of an efficient expression system for insulin-like growth factor-I (IGF-I) in Escherichia coli as a fusion protein is described. The fusion protein consists of an N-terminal extension made up of the first 46 amino acids of methionyl porcine GH ([Met1]-pGH) followed by the dipeptide Val-Asn. The latter two residues provide a unique hydroxylamine-sensitive link between [Met1]-pGH(1-46) and the N-terminal Gly of IGF-I. Downstream processing of the fusion proteins involved isolation of inclusion bodies, cleavage at the Asn-Gly bond, refolding of the reduced IGF-I peptide and purification to homogeneity. This expression system was also used to produce two variants of IGF-I in which Glu3 was substituted by either Gly or Arg to give [Gly3]-IGF-I and [Arg3]-IGF-I respectively. Production of milligram quantities of IGF-I peptide was readily achieved. The purity of the IGF-I, [Gly3]-IGF-I and [Arg3]-IGF-I was established by high-performance liquid chromatography and N-terminal sequence analysis. [Gly3]-IGF-I and [Arg3]-IGF-I were more potent than IGF-I in biological assays measuring stimulation of protein synthesis and DNA synthesis or inhibition of protein breakdown in rat L6 myoblasts. Both analogues bound very poorly to bovine IGF-binding protein-2 and slightly less well than IGF-I to the type-1 receptor on rat L6 myoblasts. We conclude that reduced binding to IGF-binding proteins rather than increased receptor binding is the likely explanation for the greater biological potency of the analogues compared with IGF-I.

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