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Endocrinology Vol. 143, No. 7 2693-2699
Copyright © 2002 by The Endocrine Society

GROWTH FACTORS-CYTOKINES-ONCOGENES

IGF-Binding Protein-3-Induced Growth Inhibition and Apoptosis Do Not Require Cell Surface Binding and Nuclear Translocation in Human Breast Cancer Cells

Alison J. Butt, Kristie A. Fraley, Sue M. Firth and Robert C. Baxter

Kolling Institute of Medical Research, University of Sydney, Royal North Shore Hospital, St. Leonards, New South Wales 2065, Australia

Address all correspondence and requests for reprints to: Alison J. Butt Ph.D., Kolling Institute of Medical Research, Royal North Shore Hospital, St. Leonards, New South Wales 2065, Australia. E-mail: . abutt{at}med.usyd.edu.au

IGF-binding protein-3 (IGFBP-3) has both antiproliferative and proapoptotic effects on the growth of human breast cancer cells in vitro. However, the mechanisms governing these effects are not well understood. IGFBP-3 has been shown to associate with the cell surface through carboxyl-terminal residues. This suggests that it may interact with a specific cell surface receptor, although a signaling receptor for IGFBP-3 has not yet been fully characterized. IGFBP-3 also translocates to the nucleus and has been shown to interact with the nuclear RXR{alpha}, with evidence that this interaction may mediate its growth inhibitory and proapoptotic effects. Here we demonstrate that a mutant form of IGFBP-3 that has reduced cell surface binding and does not translocate to the nucleus is still growth inhibitory, elicits a potent G1 cell cycle arrest, and induces apoptosis via modulation of Bcl-2 family members in human breast cancer cells. This suggests the existence of multiple pathways by which IGFBP-3 elicits its growth effects.




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