Characterization of fibroblast growth factor-6 expressed by Chinese hamster ovary cells as a glycosylated mitogen for human vascular endothelial cells.
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The gene for fibroblast growth factor (FGF)-6/hst-2 was originally identified by its close homology with the FGF-4/hst-1 gene. Aside from its ability to transform cultured fibroblasts, the characteristics of FGF-6 protein have only been studied using a simple preparation from E. coli. In the present study, we expressed FGF-6 cDNA in CHO cells and characterized the resultant protein. We found that CHO cells secreted several forms of the FGF-6 polypeptide, and that there were multiple N-terminal modifications. The longest form (18-kDa) contained the sequence, SerProAlaGlyAlaArg, as its N-terminus, which was consistent with the signal peptide cleavage site predicted from its primary structure. The core polypeptide was primarily modified by heterogeneous N-glycans that were sialylated to a small degree; among them, biantennary structures were found to predominate. Moreover, possible O-glycosylation was also detected. N-glycosylated FGF-6 potently induced DNA synthesis and proliferation of human vascular endothelial cells, whereas in the absence of N-glycosylation, FGF-6 mitogenicity was substantially diminished. The results clearly indicate that FGF-6 expressed by mammalian cells is a glycosylated mitogen for vascular endothelial cells and further suggests that N-glycosylation plays a key role in determining the mitogenicity of FGF-6.
Original language | English |
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Journal | Growth Factors |
Volume | 16 |
Issue number | 4 |
Pages (from-to) | 293-303 |
Number of pages | 10 |
ISSN | 0897-7194 |
Publication status | Published - 1999 |
Externally published | Yes |
Bibliographical note
Keywords: Animals; CHO Cells; Cricetinae; Endothelium, Vascular; Fibroblast Growth Factor 6; Fibroblast Growth Factors; Gene Expression; Glycosylation; Humans; Mitogens; Proto-Oncogene Proteins; Umbilical Veins
ID: 5277365