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J Biol Chem, Vol. 273, Issue 29, 18347-18352, July 17, 1998
From the Kolling Institute of Medical Research, University of
Sydney, Royal North Shore Hospital, Sydney,
New South Wales 2065, Australia
Insulin-like growth factor-binding proteins
(IGFBPs) play an integral role in modifying insulin-like growth factor
actions in a wide variety of cell types. Recent evidence suggests that IGFBP-3 and IGFBP-5 also have effects on cell growth that are insulin-like growth factor-independent. In investigating possible mechanisms for this effect, the intracellular trafficking of IGFBP-3 and IGFBP-5, both of which contain sequences with the potential for
nuclear localization, was studied in T47D cells. Nuclear uptake of
fluorescently labeled IGFBP-3 and IGFBP-5 was observed in a proportion
of T47D cells that appeared to be rapidly dividing. IGFBP-1 and
IGFBP-2, which do not possess the putative domain for nuclear
translocation, were not transported to the nuclei of T47D cells. When
T47D cells were preincubated with excess unlabeled IGFBP-3, nuclear
localization of labeled IGFBP-3 or IGFBP-5 was not detected, indicating
that their nuclear translocation involves a common pathway. Inhibition
of receptor-mediated endocytosis did not affect nuclear uptake of
IGFBP-3, suggesting that it uses an alternative non-classical import
pathway for transport across the plasma membrane. In addition, a
variant form of IGFBP-3 with a mutation in the putative nuclear
localization sequence was unable to translocate to the nuclei of T47D
cells, suggesting that nuclear translocation of IGFBP-3 was dependent
on these carboxyl-terminal basic residues.
Insulin-like Growth Factor-binding Protein (IGFBP)-3 and IGFBP-5
Share a Common Nuclear Transport Pathway in T47D Human Breast Carcinoma
Cells
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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