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Insulin-degrading enzyme is activated by the C-terminus of α-synuclein.

Sandeep K Sharma ; Erik Chorell ; Pernilla Wittung-Stafshede (Institutionen för biologi och bioteknik, Kemisk biologi)
Biochemical and biophysical research communications (1090-2104). Vol. 466 (2015), 2, p. 192-5.
[Artikel, refereegranskad vetenskaplig]

The insulin-degrading enzyme (IDE) plays a key role in type-2 diabetes and typically degrades small peptides such as insulin, amyloid β and islet amyloid polypeptide. We recently reported a novel non-proteolytical interaction in vitro between IDE and the Parkinson's disease 140-residue protein α-synuclein that resulted in dual effects: arrested α-synuclein oligomers and, simultaneously, increased IDE proteolysis activity. Here we demonstrate that these outcomes arise due to IDE interactions with the C-terminus of α-synuclein. Whereas a peptide containing the first 97 residues of α-synuclein did not improve IDE activity and its aggregation was not blocked by IDE, a peptide with the C-terminal 44 residues of α-synuclein increased IDE proteolysis to the same degree as full-length α-synuclein. Because the α-synuclein C-terminus is acidic, the interaction appears to involve electrostatic attraction with IDE's basic exosite, known to be involved in activation.

Nyckelord: Enzyme Activation, Insulysin, metabolism, Microscopy, Atomic Force, alpha-Synuclein, chemistry, metabolism

Denna post skapades 2016-12-22. Senast ändrad 2017-10-03.
CPL Pubid: 246468


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