Cysteine 73 in Bleomycin Hydrolase Is Critical for Amyloid Precursor Protein Processing
作者： Iliya M. Lefterov , Radosveta P. Koldamova , Martina I. Lefterova , Donald R. Schwartz , John S. Lazo
关键词: Cysteine 、 Biology 、 P3 peptide 、 Bleomycin hydrolase 、 Amyloid beta 、 Biochemistry 、 Amino acid 、 Cysteine protease 、 Molecular biology 、 Serine 、 Amyloid precursor protein 、 Biophysics 、 Cell biology
摘要: Abstract Human bleomycin hydrolase (hBH) is a neutral cysteine protease that may regulate the secretion of soluble amyloid precursor protein (APP) and beta (Aβ), which major constituent Alzheimer's disease-associated plaques. We have now determined APP interacts with hBH by using yeast two hybrid methods in vitro binding studies revealed interacted 68 amino acid region includes catalytic domain hBH. Ectopic expression increased Aβ but not second secreted protein, apolipoprotein A-I. Expression 73 was mutated to serine failed increase secretion. These results indicate critical role for mediating processing.
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