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J. Biol. Chem., Vol. 277, Issue 36, 33338-33343, September 6, 2002
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From the Department of Environmental Biochemistry and Toxicology,
University of Shizuoka School of Pharmaceutical Sciences, 52-1 Yada,
Shizuoka 422-8526, Japan
Heat shock stress induces some heat shock
proteins, including Hsp70, and activates sodium-dependent
glucose transport in porcine renal LLC-PK1 cells, but
its mechanisms have not been described in detail. We
investigated whether sodium-dependent glucose
transporter (SGLT1) interacts with Hsp70 to increase SGLT1
activity. Heat shock stress increased SGLT1 activity without changing
SGLT1 expression. The increase of SGLT1 activity was completely
inhibited by an anti-transforming growth factor-
Up-regulation of Sodium-dependent Glucose
Transporter by Interaction with Heat Shock Protein 70*
,
1 (TGF-1)
antibody. Instead of heat shock stress, TGF-1 increased SGLT1
activity dose- and time-dependently without changing SGLT1
expression. We found that the amount of Hsp70 immunoprecipitated from
TGF-1-treated cells with an anti-SGLT1 antibody was higher than that
of the control cells. Transfection of an anti-Hsp70 antibody into the
cells inhibited the increase of SGLT1 activity. With confocal laser
microscopy, both SGLT1 and Hsp70 was localized near the apical membrane
in the TGF-1-treated cells, and an anti-Hsp70 antibody disturbed this localization. Furthermore, we clarified that an anti-Hsp70 antibody inhibited interaction of SGLT1 with Hsp70 in
vitro. These results suggest that Hsp70 forms a complex
with SGLT1 and increases the expression level of SGLT1 in the apical
membrane, resulting in up-regulation of glucose uptake.
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 81-54-264-5674;
Fax: 81-54-264-5672; E-mail: ikari@u-shizuoka-ken.ac.jp.
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