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J. Biol. Chem., Vol. 275, Issue 21, 16275-16280, May 26, 2000
From the Institute of Pharmacology and Toxicology, Medical Faculty,
Technical University of Aachen, D-52057 Aachen, Germany
GLUT8 is a novel glucose transporter-like protein
that exhibits significant sequence similarity with the members of the
sugar transport facilitator family (29.4% of amino acids identical
with GLUT1). Human and mouse sequence (86.2% identical amino acids) comprise 12 putative membrane-spanning helices and several conserved motifs (sugar transporter signatures), which have previously been shown
to be essential for transport activity, e.g. GRK in loop 2, PETPR in loop 6, QQLSGVN in helix 7, DRAGRR in loop 8, GWGPIPW in helix
10, and PETKG in the C-terminal tail. An expressed sequence tag (STS
A005N15) corresponding with the 3'-untranslated region of GLUT8 has
previously been mapped to human chromosome 9. COS-7 cells transfected
with GLUT8 cDNA expressed a 42-kDa protein exhibiting specific,
glucose-inhibitable cytochalasin B binding (KD = 56.6 ± 18 nM) and reconstitutable glucose transport
activity (8.1 ± 1.4 nmol/(mg protein × 10 s)
versus 1.1 ± 0.1 in control transfections). In human
tissues, a 2.4-kilobase pair transcript was predominantly found in
testis, but not in testicular carcinoma. Lower amounts of the mRNA
were detected in most other tissues including skeletal muscle, heart,
small intestine, and brain. GLUT8 mRNA was found in testis from
adult, but not from prepubertal rats; its expression in human testis
was suppressed by estrogen treatment. It is concluded that GLUT8 is a
sugar transport facilitator with glucose transport activity and a
hormonally regulated testicular function.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) Y17801 and Y17802.
GLUT8, a Novel Member of the Sugar Transport Facilitator
Family with Glucose Transport Activity*
*
This work was supported in part by Deutsche
Forschungsgemeinschaft Grant Jo 117/8-2 (to H. G. J.).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: Inst. für
Pharmakologie und Toxikologie, Medizinische Fakultät der RWTH
Aachen, Wendlingweg 2, D-52057 Aachen, Germany. Tel.: 49-241-8089120; Fax: 49-241-8888433; E-mail: joost@rwth-aachen.de.
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