Speaker
Description
Galectins, small soluble β-galactose-binding proteins, are expressed and secreted by tissue cells under normal and pathological conditions. Fifteen different galectins have been identified in mammals, with a subset (Gal-1, Gal-3, Gal-7, Gal-8, and Gal-9) known to be dysregulated during diseases such as cancer, infections, and inflammatory conditions like bowel diseases and arthritis. In these pathophysiological cases, the expression of various galectins can be elevated within the same cellular milieu. It has been observed that these galectins can form homodimers (Gal-1, Gal-2, Gal-7) or oligomers (Gal-3), and previous in vitro analyses have indicated the potential for the formation of heterodimers amongst differing galectin members or with other proteins such as chemokines. Building on these in vitro findings, we aimed to investigate the possibility of such interactions occurring within biological systems. To do so, we utilized the NanoBiT Protein-Protein Interaction (PPI) system from Promega to observe the heterodimerization of various galectins in living cells.
Our research revealed interactions beyond the homodimerization of Gal-1, specifically, the heterodimerization involving Gal-3 and Gal-7. This suggests that heterodimerization between different galectins could occur within biological systems.
The observed heterodimerization opens new avenues for understanding the signaling function of galectins in pathological conditions. Therefore, the implications of galectin heterodimers on disease processes warrant further exploration.
References
Miller MC, Ludwig AK, Wichapong K, Kaltner H, Kopitz J, Gabius HJ, Mayo KH. Adhesion/growth-regulatory galectins tested in combination: evidence for formation of hybrids as heterodimers. Biochem J. 2018 Mar 15;475(5):1003-1018. doi: 10.1042/BCJ20170658. PMID: 29321242.
| Keywords | Galectins, Galectin homodimerization, NanoBiT |
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