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Originally published In Press as doi:10.1074/jbc.M210640200 on January 3, 2003
J. Biol. Chem., Vol. 278, Issue 10, 8586-8596, March 7, 2003
Characterization of Prominin-2, a New Member of the
Prominin Family of Pentaspan Membrane Glycoproteins*,
Christine A.
Fargeas ,
Mareike
Florek§,
Wieland B.
Huttner ¶, and
Denis
Corbeil §
From the Max-Planck-Institute of Molecular Cell
Biology and Genetics, Pfotenhauerstrasse 108 and
§ Medical Clinic and Polyclinic I TU-Dresden,
Fetscherstrasse 74, D-01307 Dresden, Germany
Prominin/CD133 is a 115/120-kDa integral membrane
glycoprotein specifically associated with plasma membrane protrusions
in epithelial and non-epithelial cells including neuroepithelial and
hematopoietic stem cells. Here we report the identification as well as
molecular and cell biological characterization of mouse, rat, and human
prominin-2, a 112-kDa glycoprotein structurally related to prominin
(referred to as prominin-1). Although the amino acid identity between
prominin-2 and prominin-1 is low (<30%), their genomic organization
is strikingly similar, suggesting an early gene duplication event. Like
prominin-1, prominin-2 exhibits a characteristic membrane topology with
five transmembrane segments and two large glycosylated extracellular
loops. Upon its ectopic expression in Chinese hamster ovary cells as a
green fluorescent protein fusion chimera, prominin-2 was also found to
be associated with plasma membrane protrusions, as revealed by its
co-localization with prominin-1, suggesting a related role. Consistent
with this, prominin-2 shows a similar tissue distribution to
prominin-1, being highly expressed in the adult kidney and detected all
along the digestive tract as well as in various other epithelial
tissues. However, in contrast to prominin-1, prominin-2 was not
detected in the eye, which perhaps explains why a loss-of function
mutation in the human prominin-1 gene causes retinal
degeneration but no other obvious pathological signs. Finally, we
present evidence for the existence of a family of pentaspan membrane
proteins, the prominins, which are conserved in evolution.
*
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.
The on-line version of this article (available at
http://www.jbc.org) contains additional text, Fig. 1, and Tables
I-III.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF508942, AF269062, AF128113, AF245303, AF245304, AF160970,
AF373869, AF127935, AF197345, and AF406812.
¶
Supported by Deutsche Forschungsgemeinschaft Grants Hu 275/7-1
and Hu 275/8-1, the German-Israeli Foundation for Scientific Research
and Development, and the Fonds der Chemischen Industrie. To whom
correspondence may be addressed. Tel.: 49-351-210-1500; Fax:
49-351-210-1600; E-mail: HUTTNER@mpi-cbg.de.
To whom correspondence may be addressed. Tel.:
49-351-210-1488; Fax: 49-351-210-1489; E-mail:
CORBEIL@mpi-cbg.de.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.

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