caa a22 4500 46908264X CHVBK 20180323132955.0 cr unu---uuuuu 170328e19920301xx s 000 0 eng 10.1007/BF00319362 doi (NATIONALLICENCE)springer-10.1007/BF00319362 Localization of erythrocyte/HepG2-type glucose transporter (GLUT1) in human placental villi [Elektronische Daten] [Kuniaki Takata, Toshiko Kasahara, Michihiro Kasahara, Osamu Ezaki, Hiroshi Hirano] Summary: The syncytiotrophoblast covering the surface of the placental villi contains the machinery for the transfer of specific substances between maternal and fetal blood, and also serves as a barrier. Existence of a facilitated-diffusion transporter for glucose in the syncytiotrophoblast has been suggested. Using antibodies to erythrocyte/HepG2-type glucose transporter (GLUT1), one isoform of the facilitated-diffusion glucose transporters, we detected a 50 kD protein in human placenta at term. By use of immunohistochemistry, GLUT1 was found to be abundant in both the syncytiotrophoblast and cytotrophoblast. Endothelial cells of the fetal capillaries also showed positive staining for GLUT1. Electron-microscopic examination revealed that GLUT1 was concentrated at both the microvillous apical plasma membrane and the infolded basal plasma membrane of the syncytiotrophoblast. Plasma membrane of the cytotrophoblast was also positive for GLUT1. GLUT1 at the apical plasma membrane of the syncytiotrophoblast may function for the entry of glucose into its cytoplasm, while GLUT1 at the basal plasma membrane may be essential for the exit of glucose from the cytoplasm into the stroma of the placental villi. Thus, GLUT1 at the plasma membranes of syncytiotrophoblast and endothelial cells may play an important role in the transport of glucose across the placental barrier. Springer-Verlag, 1992 Placenta nationallicence Glucose transporter, GLUT1 nationallicence Syncytiotrophoblast nationallicence Placental barrier nationallicence Human nationallicence Takata Kuniaki Department of Anatomy, Kyorin University School of Medicine, Shinkawa, 181, Mitaka, Tokyo, Japan aut Kasahara Toshiko Laboratory of Biophysics, School of Medicine, Teikyo University, 192-03, Hachioji, Tokyo, Japan aut Kasahara Michihiro Laboratory of Biophysics, School of Medicine, Teikyo University, 192-03, Hachioji, Tokyo, Japan aut Ezaki Osamu Division of Clinical Nutrition, National Institute of Health and Nutrition, 162, Toyama, Tokyo, Japan aut Hirano Hiroshi Department of Anatomy, Kyorin University School of Medicine, Shinkawa, 181, Mitaka, Tokyo, Japan aut Cell and Tissue Research Springer-Verlag 267/3(1992-03-01), 407-412 0302-766X 267:3<407 1992 267 441 https://doi.org/10.1007/BF00319362 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00319362 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Takata Kuniaki Department of Anatomy, Kyorin University School of Medicine, Shinkawa, 181, Mitaka, Tokyo, Japan aut NATIONALLICENCE 700 1- Kasahara Toshiko Laboratory of Biophysics, School of Medicine, Teikyo University, 192-03, Hachioji, Tokyo, Japan aut NATIONALLICENCE 700 1- Kasahara Michihiro Laboratory of Biophysics, School of Medicine, Teikyo University, 192-03, Hachioji, Tokyo, Japan aut NATIONALLICENCE 700 1- Ezaki Osamu Division of Clinical Nutrition, National Institute of Health and Nutrition, 162, Toyama, Tokyo, Japan aut NATIONALLICENCE 700 1- Hirano Hiroshi Department of Anatomy, Kyorin University School of Medicine, Shinkawa, 181, Mitaka, Tokyo, Japan aut NATIONALLICENCE 773 0- Cell and Tissue Research Springer-Verlag 267/3(1992-03-01), 407-412 0302-766X 267:3<407 1992 267 441 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer