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Aluminum inhibits proteolytic degradation of amyloid β peptide by cathepsin D: A potential link between aluminum accumulation and neuritic plaque deposition
Author(s) -
Sakamoto Takashi,
Saito Hisaka,
Ishii Kazuyuki,
Takahashi Hidenobu,
Tanabe Shinzo,
Ogasawara Yuki
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.10.075
Subject(s) - senile plaques , cathepsin , peptide , chemistry , cathepsin d , cathepsin b , proteolysis , biochemistry , cathepsin s , amyloid (mycology) , alzheimer's disease , enzyme , pathology , medicine , disease , inorganic chemistry
Neuritic plaques are the key pathological feature of Alzheimer's disease, and amyloid β (Aβ) peptides are major component of these plaques. In this study, we demonstrated the influence of aluminum (Al) on the Aβ peptide degradation by cathepsin D. Al did not directly affect the cathepsin D activity using small synthetic substrate. However, when Aβ peptides were used as substrate, the apparent inhibitory effect of Al on cathepsin D activity was observed. This inhibitory effect disappeared by treatment of desferrioxamine. These results indicate that Al has the potential to interact and disrupt Aβ peptide catabolism via the inhibition of proteolytic degradation.