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      An unusual subcellular localization of GLUT1 and link with metabolism in oocytes and preimplantation mouse embryos.

      Biology of reproduction
      Animals, Blastocyst, metabolism, ultrastructure, Blotting, Western, Cell Membrane, chemistry, Cell Nucleus, Cells, Cultured, Embryo, Mammalian, Embryonic Development, Female, Glucose, Glucose Transporter Type 1, Glutamine, Immunohistochemistry, Mice, Microscopy, Confocal, Monosaccharide Transport Proteins, analysis, genetics, physiology, Oligonucleotides, Antisense, pharmacology, Oocytes, Pregnancy, Pyruvic Acid, Zygote

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          Abstract

          Although mouse oocytes and cleavage-stage embryos prefer pyruvate and lactate for metabolic fuels, they do take up and metabolize glucose. Indeed, presentation of glucose during the cleavage stages is required for subsequent blastocyst formation, which normally relies on uptake and metabolism of large amounts of glucose. Expression of the facilitative glucose transporter GLUT1 was examined using immunohistochemistry and Western blotting, and in polyspermic oocytes, metabolism of glucose was measured and compared with that of pyruvate and glutamine. GLUT1 was observed in all oocytes and embryos, and membrane and vesicular staining was present. Additionally, however, in polyspermic oocytes, the most intense staining was in the pronuclei, and this nuclear staining persisted in cleaving normal embryos. Furthermore, GLUT1 expression appeared to be up-regulated both in nuclei and plasma membranes following culture of oocytes in the absence of glucose. In polyspermic oocytes, the metabolism of glucose, but not of pyruvate or glutamine, was directly proportional to the number of pronuclei formed. After compaction, nuclear staining diminished, and GLUT1 localized to basolateral membranes of the outer cells and trophectoderm. In blastocysts, a weak but uniform staining of inner-cell-mass plasma membranes was apparent. The results are discussed in terms of potential roles for GLUT1 in pronuclei of oocytes and zygotes, nuclei of cleavage-stage embryos, and a transepithelial transport function for GLUT1, probably coupled with GLUT3, in compacted embryos and blastocysts.

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