3 years ago

Adhesion/growth-regulatory galectins tested in combination: evidence for formation of hybrids as heterodimers.

Kevin H Mayo, Hans-Joachim Gabius, Kanin Wichapong, Anna-Kristen Ludwig, Herbert Kaltner, Michelle C Miller, Jürgen Kopitz
The delineation of the physiological significance of protein (lectin)-glycan recognition and the structural analysis of individual lectins have directed our attention to studying them in combination. In this report, we tested the hypothesis of hybrid formation by using binary mixtures of homodimeric galectins-1 and -7 as well as a proteolytically truncated version of chimera-type galectin-3. Initial supportive evidence is provided by affinity chromatography using resin-presented galectin-7. Intriguingly, extent of cell binding by cross-linking of surface counter-receptor increased significantly for monomeric galectin-3 form by presence of galectin-1 or -7. Pulsed field gradient (PFG) NMR diffusion measurements on these galectin mixtures indicated formation of heterodimers as opposed to larger oligomers. 15N-1H HSQC NMR spectroscopy and molecular dynamics simulations allowed us to delineate how different galectins interact in the heterodimer. The possibility of domain exchange between galectins introduces a new concept for understanding the spectrum of their functionality, particularly when these effector molecules are spatially and temporally co-expressed as found in vivo.

Publisher URL: http://doi.org/10.1042/BCJ20170658

DOI: 10.1042/BCJ20170658

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