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. 1989 Nov;9(11):4896–4902. doi: 10.1128/mcb.9.11.4896

Detection and characterization of the fibroblast growth factor-related oncoprotein INT-2.

M Dixon 1, R Deed 1, P Acland 1, R Moore 1, A Whyte 1, G Peters 1, C Dickson 1
PMCID: PMC363640  PMID: 2557543

Abstract

Products of the fibroblast growth factor-related proto-oncogene int-2 have been detected by using a monoclonal antibody and polyclonal antisera raised against synthetic peptides predicted from the DNA sequence. COS-1 monkey cells transfected with int-2 DNA linked to the simian virus 40 early promoter contained at least four int-2-specific proteins, presumably representing modified forms of the expected 27-kilodalton primary translation product. The level of expression was increased approximately six- to eightfold by mutation of sequences around the presumed initiation codon, negating their capacity to encode a short oligopeptide in the +1 reading frame. Both tunicamycin inhibition and in vitro translation experiments indicated that some of the modifications correspond to asparagine-linked glycosylation, for which the sequence predicts a single site. In line with the similarities between INT-2 and other fibroblast growth factors, the in vitro translation products functioned as weak mitogens for mammary epithelial cells.

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Selected References

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