Expression of the 14 kDa galactose-binding protein, galectin-1, on human tubular epithelial cells
Expression of the 14kDa galactose-binding protein, galectin-1, on human tubular epithelial cells. By reverse phase PCR and Northern blotting, RNA of the 14kDa galactose-binding protein (galectin-1) could be identified in primary cultures of human tubular epithelial cells. To assess protein synthesis...
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| Hauptverfasser: | , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
September 1996
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| In: |
Kidney international
Year: 1996, Jahrgang: 50, Heft: 3, Pages: 754-759 |
| ISSN: | 1523-1755 |
| DOI: | 10.1038/ki.1996.373 |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1038/ki.1996.373 Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S0085253815596671 
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| Verfasserangaben: | Antje Bürger, Sabine Filsinger, Douglas N. W. Cooper, Gertrud Maria Hänsch |
MARC
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| 520 | |a Expression of the 14kDa galactose-binding protein, galectin-1, on human tubular epithelial cells. By reverse phase PCR and Northern blotting, RNA of the 14kDa galactose-binding protein (galectin-1) could be identified in primary cultures of human tubular epithelial cells. To assess protein synthesis and the possible function of galectin-1 on TEC, the cellular proteins were biosyntheticically labeled with [35S]-methionine and adsorbed to immobilized laminin. Multiple radiolabeled proteins were eluted, a strong band in the area of 14kDa was seen, coinciding with the galectin-1 band as identified by Western blotting. Surface expression of galectin-1 was seen by cytofluorometry with two different polyclonal antibodies to galectin-1. These data are in line with the finding that tubular epithelial cells adhere to laminin, partly in a Ca2+-independent manner. | ||
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