作者: J M Roch , I P Shapiro , M P Sundsmo , D A Otero , L M Refolo
DOI: 10.1016/S0021-9258(18)45864-4
关键词: Binding site 、 Peptide 、 Protease inhibitor (biology) 、 Biology 、 Amino acid 、 Peptide sequence 、 Active site 、 Protein precursor 、 Biochemistry 、 Amyloid beta
摘要: The secreted form of Alzheimer amyloid beta/A4 protein precursor (APP) has been shown to be involved in cell growth regulation (Saitoh, T., Sundsmo, M., Roch, J.-M., Kimura, N., Cole, G., Schubert, D., Oltersdorf, and Schenk, D.B. (1989) Cell 58, 615-622). Using a strong prokaryotic expression system, we expressed, Escherichia coli, peptide fragments covering different regions the APP-695. longest these (KB75, 572 amino acids from Val-20 Ile-591), which contained neither Kunitz-type protease inhibitor (KPI) domain nor beta/A4-protein domain, was purified biologically active terms regulation. Two other APP (KB48, 316 Met-335; RB17, 150 Thr-296 Pro-445), overlapping by only 40 at close site C-terminal KPI insertion site, were also active. Furthermore, chemically synthesized 40-residue corresponding this region overlap stimulated A-1 fibroblasts. These results establish presence growth-promoting activity APP-695 suggest that lies within 40-amino acid next site.