Biochemistry of γ-Secretase

Prof. Dr. Harald Steiner

Areas of investigation/research focus

Accumulation of the amyloid-β peptide (Aβ) in senile plaques is an invariable pathological hallmark of Alzheimer´s disease (AD). Aβ is derived by proteolytic processing of the β-amyloid precursor protein (APP) through the combined action of the membrane bound aspartyl proteases β-secretase and γ-secretase. γ-Secretase is a large protein complex composed of the AD-associated presenilin (PS) proteins as catalytic subunit, nicastrin (NCT), APH-1 and PEN-2 and cleaves APP within its transmembrane domain. To allow a better understanding of the mode of action of γ-secretase and of intramembrane proteolysis in general research our group currently focuses on following aspects of γ-secretase biochemistry:

  1. Molecular recognition of γ-secretase substrates
  2. Modulation of γ-secretase activity


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