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...

Full description

Saved in:
Bibliographic Details
Main Authors: Bürger, Antje (Author) , Filsinger, Sabine (Author) , Cooper, Douglas N. W. (Author) , Hänsch, Gertrud Maria (Author)
Format: Article (Journal)
Language:English
Published: September 1996
In: Kidney international
Year: 1996, Volume: 50, Issue: 3, Pages: 754-759
ISSN:1523-1755
DOI:10.1038/ki.1996.373
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1038/ki.1996.373
Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S0085253815596671
Get full text
Author Notes:Antje Bürger, Sabine Filsinger, Douglas N. W. Cooper, Gertrud Maria Hänsch
Description
Summary: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.
Item Description:Artikel-Version: 16. Dezember 2015
Gesehen am 24.07.2025
Physical Description:Online Resource
ISSN:1523-1755
DOI:10.1038/ki.1996.373