Amyloid Synthesis Essay
Most of the lesions in the brain of an AD patient are from plaques, which consist of beta amyloid peptides that are derived from APP (amyloid precursor protein) 7. APP (amyloid precursor protein) is located on the cell membrane and consists of N extracellular terminal, short C intracellular terminal, a single hydrophobic transmembrane domain and a metal binding site 16, and there are two ways for APP cleaving (figure 2): The first one is non–amyloidogenic pathway which is done by α–secretase to form the soluble sAPPα and the membrane bound C83, and then γ–secretase cut the residue of the membrane part to get p3 and AICD protein 7,17. The second one is amyloidogenic pathway in which it starts when β–secretase cut the APP to shorter sAPPβ than sAPPα and C99 terminal then γ–secretase cut the c99 to Aβ: Amyloid β (40–42 amino acids), and ACID protein (plays an important role in gene transcription of the protein that responsible for degradation of the beta amyloid monomer) then beta amyloid is normally degraded by zinc metalloproteases (NEP, IDE ) 7,17 (see figure 2) and then LRP1 protein escorts amyloid beta proteins out of the brain through BBB24. Whereas when the concentration of the mis–regulated metals
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