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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
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Cubilin, a Binding Partner for Galectin-3 in the Murine Utero-Placental Complex*

Sunday Crider-PirkleDagger , Peggy BillingsleyDagger , Charles FaustDagger , Daniel M. HardyDagger , Vaughan LeeDagger , and Harry WeitlaufDagger §

From the Departments of Dagger  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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