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PGF 2α increases FGF‐2 and FGFR2 trafficking in Py1a rat osteoblasts via clathrin independent and importin β dependent pathway
Author(s) -
Marchetti Luigi,
Sabbieti Maria G.,
Agas Dimitrios,
Menghi Maura,
Materazzi Giovanni,
Menghi Giovanna,
Hurley Marja M.
Publication year - 2005
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.20746
Subject(s) - fibroblast growth factor , microbiology and biotechnology , fibroblast growth factor receptor 2 , importin , clathrin , chemistry , endocytic cycle , nuclear transport , biology , cytoplasm , endocytosis , cell nucleus , receptor , biochemistry
Previous studies showed that prostaglandin F 2α (PGF 2α ) stimulated fibroblast growth factor‐2 (FGF‐2) and fibroblast growth factor receptor 2 (FGFR2) cytosolic and nuclear accumulation, however, the endocytic pathway has not been elucidated. This study demonstrates that although PGF 2α increased the formation of clathrin‐coated structures in Py1a rat osteoblasts, they were not involved in FGF‐2 and FGFR2 trafficking. PGF 2α increased binding of FGF‐2 and FGFR2 and co‐localization of reactive sites in addition to nuclear translocation at the nuclear pore complex level. FGF‐2 and FGFR2 were in close spatial correlation with importin β, further supporting nuclear import of the FGF‐2/FGFR2 complex. Immunogold and immunofluorescence techniques as well as Western blotting demonstrated increased importin β protein labeling in response to PGF 2α . Similar to PGF 2α , phorbol 12‐myristate 13‐acetate (PMA) also increased importin β protein. These data strongly suggest that prostaglandins may regulate osteoblast metabolism via FGF‐2/FGFR2/importin β nuclear trafficking. J. Cell. Biochem. 97: 1379–1392, 2006. © 2005 Wiley‐Liss, Inc.