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Expression of cDNA encoding human basic fibroblast growth factor in E. coli.

M Iwane, T Kurokawa, R Sasada

Biochemical and Biophysical Research Communications

|July 31, 1987

Summary

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Researchers purified human basic fibroblast growth factor (hbFGF) from E. coli. Four distinct hbFGF forms were isolated, showing varied but confirmed fibroblast, endothelial cell growth, and angiogenesis activities.

Area of Science:

Biochemistry
Molecular Biology
Cell Biology

Background:

Human basic fibroblast growth factor (hbFGF) plays crucial roles in cell growth and tissue repair.
Understanding the properties and activities of recombinant hbFGF is essential for therapeutic applications.

Purpose of the Study:

To express and purify human basic fibroblast growth factor (hbFGF) in E. coli.
To characterize the distinct forms of bacterially synthesized hbFGF and assess their biological activities.

Main Methods:

Expression of human basic fibroblast growth factor cDNA in E. coli using a trp promoter.
High-performance liquid chromatography (HPLC) with heparin affinity column for hbFGF purification.
Analysis using SDS-PAGE, amino acid composition, and partial terminal sequence analysis.

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Main Results:

Highly purified hbFGF was obtained, eluting as four distinct molecular forms.
These forms were biochemically similar, showing no differences in SDS-PAGE, amino acid composition, or partial sequence analysis.
All four hbFGF forms stimulated fibroblast and endothelial cell growth, with variations in specific activity.
The angiogenesis activity of the purified hbFGF molecules was confirmed.

Conclusions:

Bacterial expression and heparin affinity chromatography are effective for hbFGF purification.
The distinct eluted forms of hbFGF possess conserved biological activities, including cell growth stimulation and angiogenesis.
Variations in specific activity among hbFGF forms warrant further investigation for potential differential applications.