Expression of Gal beta 1,4GlcNAc alpha 2,6-sialyltransferase and alpha 2,6-linked sialoglycoconjugates in normal human and rat tissuesY Kaneko, H Yamamoto, KJ Colley and JR Moskal Chicago Institute for Neurosurgery and Neuroresearch, Illinois 60614, USA. We performed histochemical studies on normal human and rat tissues using anti-Gal beta 1,4GlcNAc alpha 2,6-sialyltransferase (alpha 2,6- ST) antibody and Sambucus nigra agglutinin (SNA). alpha 2,6-ST and its products were detected in almost all tissues examined. However, the staining intensities varied significantly with different cell types. Some secretory epithelial cells, such as hepatocytes and choroid plexus cells, were vividly stained with either anti-alpha 2,6-ST or SNA. In several cell types the intensity of alpha 2,6-ST staining did not always correlate with SNA stainability. Neurons and gastrointestinal epithelia were rarely stained with SNA, even though they were positive for alpha 2,6-ST. In contrast, the endothelial cells of blood vessels strongly reacted with SNA despite their weak alpha 2,6-ST expression. The precise physiological roles played by alpha 2,6-linked sialylated glycoconjugates have been unclear. However, the findings described here lend further support to their important role in cell growth and differentiation, since immature blood cells, including megakaryocytes in bone marrow, were intensely stained with anti-alpha 2,6-ST and SNA, and SNA reaction products were primarily observed in the basal and suprabasal layers of the stratified epithelia rather than in the more differentiated upper layers. In view of the vivid reactivity of anti- alpha 2,6-ST in the decidual cells of the placenta, it seems likely that alpha 2,6-ST expression is under hormonal control.
Volume 43,
Issue 9,
pp. 945-954,
09/01/1995
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F. Dall'Olio, M. Chiricolo, A. D'Errico, E. Gruppioni, A. Altimari, M. Fiorentino, and W. F. Grigioni Expression of {beta}-galactoside {alpha}2,6 sialyltransferase and of {alpha}2,6-sialylated glycoconjugates in normal human liver, hepatocarcinoma, and cirrhosis Glycobiology, January 1, 2004; 14(1): 39 - 49. [Abstract] [Full Text] [PDF] |
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F. Ulloa and F. X. Real Differential Distribution of Sialic Acid in {{alpha}}2,3 and {{alpha}}2,6 Linkages in the Apical Membrane of Cultured Epithelial Cells and Tissues J. Histochem. Cytochem., April 1, 2001; 49(4): 501 - 510. [Abstract] [Full Text] |
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O. T. Keppler, S. Hinderlich, J. Langner, R. Schwartz-Albiez, W. Reutter, and M. Pawlita UDP-GlcNAc 2-Epimerase: A Regulator of Cell Surface Sialylation Science, May 21, 1999; 284(5418): 1372 - 1376. [Abstract] [Full Text] |
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L. G. Baum, K. Derbin, N. L. Perillo, T. Wu, M. Pang, and C. Uittenbogaart Characterization of Terminal Sialic Acid Linkages on Human Thymocytes J. Biol. Chem., May 3, 1996; 271(18): 10793 - 10799. [Abstract] [Full Text] [PDF] |
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