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Originally published In Press as doi:10.1074/jbc.M200331200 on February 20, 2002
J. Biol. Chem., Vol. 277, Issue 18, 15904-15912, May 3, 2002
Cubilin, a Binding Partner for Galectin-3 in the Murine
Utero-Placental Complex*
Sunday
Crider-Pirkle ,
Peggy
Billingsley ,
Charles
Faust ,
Daniel M.
Hardy ,
Vaughan
Lee , and
Harry
Weitlauf §¶
From the Departments of Cell Biology and Biochemistry
and § Ob/Gyn, Texas Tech University Health Sciences Center,
Lubbock, Texas 79430
Galectin-3 is a lectin important in animal
development and regulatory processes and is found selectively localized
at the implantation site of the mouse embryo. To better understand the role of galectin-3 at the maternal-fetal interface, a binding partner
was isolated and characterized. Homogenates of uteroplacental tissue
were incubated with immobilized recombinant galectin-3, and
specifically bound proteins were eluted using lactose. The principal
protein, p400, had an Mr of 400,000 in
SDS-PAGE. Physical properties of p400 and amino acid sequences of seven
tryptic peptides were similar to cubilin from rats, humans, and dogs,
identifying p400 as the murine ortholog of cubilin. This was further
supported by the tissue distribution observed only in yolk sac, kidney, and ileum with monospecific antiserum for p400. Cubilin occurred in
yolk sac epithelium throughout pregnancy, but galectin-3 was there only
during the last week. Unexpectedly, cubilin was found only in
perforin-containing granules of uterine natural killer (uNK) cells,
although galectin-3 occurred throughout the cell cytoplasm. In
situ hybridization revealed cubilin mRNA in yolk sac
epithelium but not uNK cells, implying that yolk sac-derived cubilin is
endocytosed by uNK cells via galectin-3. This is consistent with
cubilin being an endogenous partner of galectin-3 at the maternal-fetal
interface and suggests an important role for cubilin in uNK cell function.
*
This work was supported by National Institutes of Health
Grants HD-29801 (to H. M. W.), HD-35166 (to D. M. H.), and HD-07271 (to S. C.-P.), the South Plains Foundation, the Houston Endowment, and
the Texas Tech University Health Sciences Center Laboratory for the
Study of Reproduction.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: Dept. of Cell
Biology and Biochemistry, Texas Tech University Health Sciences Center,
3601 4th St., Lubbock, TX 79430. Fax: 806-743-2990; E-mail: harry.weitlauf@ttuhsc.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.
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