Butyrylcholinesterase interactions with amylin may protect pancreatic cells in metabolic syndrome.
Bottom Line: However, the activity differences remained unexplained.We demonstrate that BChE interacts with amylin through its core domain and efficiently attenuates both amylin fibril and oligomer formation.Taken together, our results suggest that MetS-associated BChE increases could protect pancreatic β-cells in vivo by decreasing the formation of toxic amylin oligomers.
Affiliation: Department of Neurology and Internal Medicine, Tel Aviv Sourasky Medical Center, Sackler Faculty of Medicine, Tel Aviv University, Tel Aviv, Israel.Show MeSH
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Mentions: To examine the involvement of BChE protein–peptide interactions in the shift from MetS to T2DM, we performed PICUP of highly purified rhBChE of the U variant (Fig. 3A) with the amylin peptide. This method enables the covalent cross-linking of proteins or peptides found in close proximity, without the use of modifications or chemical cross-linkers. Following incubation and cross-linking, the resultant complexes of rBChE and amylin were separated by gel electrophoresis and immune-stained for amylin. A pronounced double band of over 250 kD is seen (Fig. 3C), representing rhBChE tetramers (∼280 kD) complexed with amylin (the doublet may represent two distinct forms of these complexes), as well as an amylin hexamer band (∼27 kD). Samples containing rhBChE alone showed no staining for amylin.
Affiliation: Department of Neurology and Internal Medicine, Tel Aviv Sourasky Medical Center, Sackler Faculty of Medicine, Tel Aviv University, Tel Aviv, Israel.