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J. Biol. Chem., Vol. 275, Issue 27, 20896-20902, July 7, 2000
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From the Department of Internal Medicine and Molecular Science,
Graduate School of Medicine, Osaka University, 2-2 Yamadaoka, Suita,
565-0871, Japan
Adipose tissue is a major site of glycerol
production in response to energy balance. However, molecular basis of
glycerol release from adipocytes has not yet been elucidated. We
recently cloned a novel member of the aquaporin family, aquaporin
adipose (AQPap), which has glycerol permeability. The current study was designed to examine the hypothesis that AQPap serves as a glycerol channel in adipocytes. Adipose tissue expressed AQPap mRNA in high
abundance, but not the mRNAs for the other aquaglyceroporins, AQP3
and AQP9, indicating that AQPap is the only known aquaglyceroporin expressed in adipose tissue. Glycerol release from 3T3-L1 cells was
increased during differentiation in parallel with AQPap mRNA levels
and suppressed by mercury ion, which inhibits the function of AQPs,
supporting AQPap functions as a glycerol channel in adipocytes. Fasting
increased and refeeding suppressed adipose AQPap mRNA levels in
accordance with plasma glycerol levels and oppositely to plasma insulin
levels in mice. Insulin dose-dependently suppressed AQPap
mRNA expression in 3T3-L1 cells. AQPap mRNA levels and adipose glycerol concentrations measured by the microdialysis technique were
increased in obese mice with insulin resistance. Accordingly, negative
regulation of AQPap expression by insulin was impaired in the
insulin-resistant state. Exposure of epinephrine translocated AQPap
protein from perinuclear cytoplasm to the plasma membrane in 3T3-L1
adipocytes. These results strongly suggest that AQPap plays an
important role in glycerol release from adipocytes.
The nucleotide sequence of mouse AQP3 and AQP9 has been submitted
to the DDBJ/GenBandTM/EBI Data Bank with accession numbers
AB019039 and AB037180, respectively.
Aquaporin Adipose, a Putative Glycerol Channel in Adipocytes*
,,
*
This work was supported in part by the fund from the
"Research for the Future" Program from the Japan Society for the
Promotion of Science: JSPS-RFTF97L00801 and Ministry of Education,
Science, Sports and Culture of Japan Grants-in-aid 09307019, 10557100, 10557101, and 10671035.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.
Contributed equally to the results of this work.
§
To whom correspondence should be addressed: Dept. of Internal
Medicine and Molecular Science, Graduate School of Medicine, Osaka
University, 2-2 Yamadaoka, Suita, 565-0871, Japan. Tel.: 81-6-6879-3732; Fax: 81-6-6879-3739; E-mail:
tohru@imed2.med.osaka-u.ac.jp.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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