Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1934406 | Biochemical and Biophysical Research Communications | 2009 | 5 Pages |
Abstract
The functional spectrum of human galectins is currently explored, with a wide range of activities being described. The role of galectin-3 as adhesin for bacteria is based on its strong binding to lipopolysaccharides (LPSs), which brings the possibility of such a contamination in galectin preparations to awareness. This assumption was verified in three independent functional assay systems using polymyxin B as inhibitor of LPS-dependent effects. Moreover, a commercial LPS quantification kit also revealed LPS in galectin preparations. Chromatography was effective in removing LPS, suggesting that such a technique needs to be applied to prevent assigning cellular responses to galectins rather than LPS.
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Authors
Kerstin Sarter, Sabine André, Herbert Kaltner, Martin Lensch, Connie Schulze, Vilma Urbonaviciute, Georg Schett, Martin Herrmann, Hans-Joachim Gabius,