Prostate carcinoma (PC-3) cell proliferation is stimulated by the 22–25-kDa proteolytic fragment (1–160) and inhibited by the 16-kDa fragment (1–95) of recombinant human insulin-like growth factor binding protein-3
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Cited by (24)
Insulin-like growth factor (IGF)-binding protein-3 mutants that do not bind IGF-I or IGF-II stimulate apoptosis in human prostate cancer cells
2002, Journal of Biological ChemistryCitation Excerpt :Candidate IGFBP-3 receptors include the type V TGF-β receptor or a related serine-threonine kinase receptor (34, 64), and other proteins in cell lysates and membranes that bind IGFBP-3 (4, 30, 36, 65). IGFBP-3 signaling has been proposed to involve phosphorylation of Smad2 and Smad3 (11), nuclear localization (6, 66-70), and proteolysis (31, 71,72). Smad2 and Smad3, signaling molecules downstream from the TGF-βI receptor that function as transcription comodulators (73), were increased in anti-phosphoserine immunoprecipitates of lysates from IGFBP-3-treated T47D breast cancer cells (11).
Signaling through the Smad pathway by insulin-like growth factor-binding protein-3 in breast cancer cells. Relationship to transforming growth factor-β1 signaling
2002, Journal of Biological ChemistryCitation Excerpt :For example, plasminogen binds to IGFBP-3 in vivo, an interaction proposed to lead to IGFBP-3 proteolysis (15). Plasmin-derived IGFBP-3 fragments can exert both inhibitory and stimulatory effects on cell proliferation and show greatly decreased IGF binding, Thus, plasmin proteolysis of IGFBP-3 can regulate IGF bioavailability (42). IGF-I in turn decreases plasminogen activity in cell-conditioned medium (16), suggesting a complex regulatory loop.
A non-IGF binding mutant of IGFBP-3 modulates cell function in breast epithelial cells
2002, Biochemical and Biophysical Research CommunicationsCitation Excerpt :These effects of IGFBP-3 can vary between different cells and within a cell type depending on the concentration of IGFBP-3 as determined in the MCF-10A cells. A major mechanism affecting IGFBP-3 is its limited proteolysis which it undergoes in biological fluids and in cell culture media [30] and which generates different fragments that might be biologically active [31]. Originally, it was considered that proteolysis lowered the affinity of IGF binding and was therefore a mechanism for modulating IGF availability.
Characterization of an amino-terminal fragment of insulin-like growth factor binding protein-3 and its effects in MCF-7 breast cancer cells
2000, Growth Hormone and IGF Research