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Bacterially expressed murine CSF-1 possesses agonistic activity in its monomeric form

: Krautwald, S.; Baccarini, M.


Biochemical and biophysical research communications 192 (1993), No.2, pp.720-727
ISSN: 0006-291X
Journal Article
Fraunhofer ITA ( ITEM) ()
biological chemistry; cell division; cell line; genetics; glutathione; macrophage; molecular cloning; mouse; platelet-derived growth factor; protein

CSF-1 is a dimeric peptide growth factor, stabilized by disulfide bonds. We expressed mouse CSF-1 in bacteria as a fusion protein either with glutathione S-transferase (GST) or with a six histidine tag (His-tag). Large amounts of recombinant material were obtained and purified by a single affinity chromatography step. Purified CSF-1-His-tag monomers efficiently dimerized in vitro, but the presence of variable amounts of GST-moiety in CSF-1 preparations obtained by thrombin cleavage of GST-fusion proteins interfered with dimerization. However, the thrombin-released CSF-1 monomers possessed agonistic activity, being capable of stimulating tyrosine phosphorylation of the CSF-1 receptor and of an array of cellular proteins in living macrophages and of supporting their growth. These results show that CSF-1 dimerization is not essential for receptor activation in vivo.