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Dr. Harald Steiner

Professor
Center for Neurodegenerative Diseases
German Centre for Neurodegenerative Diseases (Deutsches Zentrum für Neurodegenerative Erkrankungen)
Germany

Biography

Prof. Steiner studied Chemistry at the University of Stuttgart. In 1996 he received his doctoral degree at the Ludwig-Maximilians-Universität (LMU) Munich in Biochemistry. Since his postdoctoral studies at the University of Heidelberg (Central Institute of Mental Health Mannheim) and back at the LMU as a senior scientist and group leader in 1999, Prof. Steiner has been interested in the molecular mechanisms of the development of β-amyloid peptide (Aβ), which plays a central role in Alzheimer´s disease (AD) pathogenesis. Following his Habilitation (2002) at the LMU and activity as private lecturer (2003-2007) he has been appointed as Professor of Biochemistry at the LMU in 2007. Since 2009 he is associated member of the DZNE Munich. His research group investigates the function of γ-secretase, a complex protease, which is involved in Aβ generation and thus an important drug target for therapeutic intervention of AD. For his research studies, Prof. Steiner has been awarded with the Alzheimer Research Prize of the Hans and Ilse Breuer Foundation.

Research Interest

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 (Fig. 1). 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: Molecular composition and subunit architecture of γ-secretase Structure/function analysis of γ-secretase subunits PS, NCT, APH-1 and PEN-2 Molecular recognition of γ-secretase substrates Modulation of γ-secretase activity

Publications

  • Three-amino acid spacing of presenilin endoproteolysis suggests a general stepwise cleavage of γ-secretase-mediated intramembrane proteolysis. Fukumori. A., Fluhrer. R., Steiner. H. & Haass. C. (2010), J. Neurosci., 30, 7853-7862.

  • APP mutants respond to {gamma}-secretase modulators. Page RM, Gutsmiedl A, Fukumori A, Winkler E, Haass C, Steiner H.; J Biol Chem. 2010

  • Regulated intramembrane proteolysis--lessons from amyloid precursor protein processing. SF Lichtenthaler, C Haass, H Steiner; J Neurochem. 2011 Jun;117(5):779-96.

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