Cubilin, a binding partner for galectin-3 in the murine utero-placental complex
Autor: | Daniel M. Hardy, Harry M. Weitlauf, Peggy Billingsley, Sunday Crider-Pirkle, Charles Faust, Vaughan H. Lee |
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Rok vydání: | 2002 |
Předmět: |
food.ingredient
Transcription Genetic Galectin 3 Placenta Molecular Sequence Data Extraembryonic Membranes Receptors Cell Surface In situ hybridization Biology Biochemistry Chromatography Affinity Mice food Dogs Pregnancy Yolk medicine Animals Humans Amino Acid Sequence Embryo Implantation Yolk sac Molecular Biology Yolk Sac Membrane Glycoproteins Sequence Homology Amino Acid Uterus Gene Expression Regulation Developmental Embryo Cell Biology Cubilin Embryo Mammalian Antigens Differentiation Epithelium Cell biology Rats medicine.anatomical_structure Cytoplasm embryonic structures Female Carrier Proteins Sequence Alignment |
Zdroj: | The Journal of biological chemistry. 277(18) |
ISSN: | 0021-9258 |
Popis: | 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 M(r) 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. |
Databáze: | OpenAIRE |
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