Research Topics
Genomes and Genes | Stefan F LichtenthalerSummaryAffiliation: University of Munich Country: Germany Publications
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Publications
Alpha-secretase cleavage of the amyloid precursor protein: proteolysis regulated by signaling pathways and protein traffickingStefan F Lichtenthaler
DZNE German Center for Neurodegenerative Diseases, 80336 Munich, Germany
Curr Alzheimer Res 9:165-77. 2012..This review highlights the role of signaling pathways and protein trafficking in the control of APP α-secretase cleavage...- Ectodomain shedding of the amyloid precursor protein: cellular control mechanisms and novel modifiersStefan F Lichtenthaler
Adolf Butenandt Institute, Ludwig Maximilians University, Munich, Germany
Neurodegener Dis 3:262-9. 2006..Moreover, it highlights the particular importance of endocytic APP trafficking as a prime modulator of APP shedding... 
Alpha-secretase in Alzheimer's disease: molecular identity, regulation and therapeutic potentialStefan F Lichtenthaler
DZNE German Center for Neurodegenerative Diseases, Munich, Germany
J Neurochem 116:10-21. 2011..This review focuses on the recent progress made in unraveling the molecular identity, regulation and therapeutic potential of α-secretase in Alzheimer's disease...
Sheddases and intramembrane-cleaving proteases: RIPpers of the membrane. Symposium on regulated intramembrane proteolysisStefan F Lichtenthaler
Adolf-Butenandt-Institute, Department of Biochemistry, Laboratory of Alzheimer's and Parkinson's Disease Research, Ludwig-Maximilians-University, Schillerstrasse 44, 80336 Munich, Germany
EMBO Rep 8:537-41. 2007- Amyloid at the cutting edge: activation of alpha-secretase prevents amyloidogenesis in an Alzheimer disease mouse modelStefan F Lichtenthaler
Adolf Butenandt Institut, Laboratory for Alzheimer s and Parkinson s Disease Research, Ludwig Maximilians Universitat, Munich, Germany
J Clin Invest 113:1384-7. 2004..alpha-Secretase cleaves within the A beta peptide domain and thus precludes A beta peptide generation. Now, new results demonstrate that activation of alpha-secretase indeed reduces A beta peptide generation and toxicity in vivo... - A novel sorting nexin modulates endocytic trafficking and alpha-secretase cleavage of the amyloid precursor proteinSusanne Schöbel
Center for Integrated Protein Science and the Adolf Butenandt Institut, Ludwig Maximilians University, Munich, Germany
J Biol Chem 283:14257-68. 2008.... - Expression cloning screen for modifiers of amyloid precursor protein sheddingSusanne Schöbel
Adolf Butenandt Institut, Ludwig Maximilians University, Schillerstr 44, 80336 Munich, Germany
Int J Dev Neurosci 24:141-8. 2006..In summary, this study shows that expression cloning is a suitable way to identify proteins controlling ectodomain shedding of membrane proteins... - Determination of the proteolytic cleavage sites of the amyloid precursor-like protein 2 by the proteases ADAM10, BACE1 and γ-secretaseSebastian Hogl
German Center for Neurodegenerative Diseases, Munich, Germany
PLoS ONE 6:e21337. 2011..Determination of the APLP2 cleavage sites enables functional studies of the different APLP2 ectodomain fragments and the production of cleavage-site specific antibodies for APLP2, which may be used for biomarker development... - Amyloid precursor-like protein 1 influences endocytosis and proteolytic processing of the amyloid precursor proteinStephanie Neumann
Adolf Butenandt Institut, Ludwig Maximilians University, Schillerstrasse 44, 80336 Munich, Germany
J Biol Chem 281:7583-94. 2006..In summary, our study provides a novel mechanism for APP shedding, in which APLP1 affects the endocytosis of APP and makes more APP available for alpha-secretase cleavage... - Secretome protein enrichment identifies physiological BACE1 protease substrates in neuronsPeer Hendrik Kuhn
DZNE German Center for Neurodegenerative Diseases, Munich, Germany
EMBO J 31:3157-68. 2012..SPECS is also suitable for quantitative secretome analyses of primary cells and may be used for the discovery of biomarkers secreted from tumour or stem cells... - Expression of the anti-amyloidogenic secretase ADAM10 is suppressed by its 5'-untranslated regionSven Lammich
German Center for Neurodegenerative Diseases DZNE and Adolf Butenandt Institute, Biochemistry, Ludwig Maximilians University, 80336 Munich, Germany
J Biol Chem 285:15753-60. 2010..Thus, we provide evidence that the 5'-UTR of ADAM10 may have an important role for post-transcriptional regulation of ADAM10 expression and consequently Abeta production... - The novel membrane protein TMEM59 modulates complex glycosylation, cell surface expression, and secretion of the amyloid precursor proteinSylvia Ullrich
German Center for Neurodegenerative Diseases Munich DZNE and Adolf Butenandt Institute, Biochemistry, Ludwig Maximilians University Munich, 80336 Munich, Germany
J Biol Chem 285:20664-74. 2010.... - Regulated intramembrane proteolysis of the interleukin-1 receptor II by alpha-, beta-, and gamma-secretasePeer Hendrik Kuhn
Adolf Butenandt Institut, Ludwig Maximilians University, Schillerstrasse 44, 80336 Munich, Germany
J Biol Chem 282:11982-95. 2007..This study reveals a similar proteolytic processing of IL-1R2 and APP and may provide an explanation for the increased IL-1R2 secretion observed in AD... - Transmembrane protein 147 (TMEM147) is a novel component of the Nicalin-NOMO protein complexUlf Dettmer
German Center for Neurodegenerative Diseases DZNE and the Adolf Butenandt Institute, Biochemistry, Ludwig Maximilians University, D 80336 Munich, Germany
J Biol Chem 285:26174-81. 2010..We conclude that TMEM147 is a novel core component of the Nicalin-NOMO complex, further emphasizing its similarity with gamma-secretase... - ADAM10 is the physiologically relevant, constitutive alpha-secretase of the amyloid precursor protein in primary neuronsPeer Hendrik Kuhn
Adolf Butenandt Institute, Biochemistry, Ludwig Maximilians University, Munich, Germany
EMBO J 29:3020-32. 2010..We conclude that ADAM10 is the physiologically relevant, constitutive alpha-secretase of APP... - Dimerization of beta-site beta-amyloid precursor protein-cleaving enzymeGil G Westmeyer
Adolf Butenandt Institute, Department of Biochemistry, Laboratory for Alzheimer s and Parkinson s Disease Research, Schillerstrasse 44, Ludwig Maximilians University, 80336 Munich, Germany
J Biol Chem 279:53205-12. 2004..Dimerization of BACE might, thus, facilitate binding and cleavage of physiological substrates... - Specific amino acids in the BAR domain allow homodimerization and prevent heterodimerization of sorting nexin 33Bastian Dislich
German Center for Neurodegenerative Diseases, Munich, 80336 Munich, Germany
Biochem J 433:75-83. 2011.... - Regulated intramembrane proteolysis--lessons from amyloid precursor protein processingStefan F Lichtenthaler
DZNE German Center for Neurodegenerative Diseases, Adolf Butenandt Institute, Biochemistry, Ludwig Maximilians University, Munich, Germany
J Neurochem 117:779-96. 2011..Focusing on APP as the best-studied RIP substrate, this review describes the function and mechanism of the APP RIP proteases with the goal to elucidate cellular mechanisms and common principles of the RIP process in general... - The cell adhesion protein P-selectin glycoprotein ligand-1 is a substrate for the aspartyl protease BACE1Stefan F Lichtenthaler
Massachusetts General Hospital Harvard Medical School, Department of Molecular Biology, Boston, Massachusetts 02114, USA
J Biol Chem 278:48713-9. 2003..The cleavage occurred at a Leu-Ser peptide bond as identified by mass spectrometry using a synthetic peptide. We conclude that PSGL-1 is an additional substrate for BACE1... - Expression of the Alzheimer protease BACE1 is suppressed via its 5'-untranslated regionSven Lammich
Department of Biochemistry, Laboratory for Alzheimer's and Parkinson's Disease Research, Adolf Butenandt Institute, Ludwig Maximilians University, Schillerstrasse 44, 80336 Munich, Germany
EMBO Rep 5:620-5. 2004..Our data therefore demonstrate translational repression as a new mechanism controlling BACE1 expression... - Bepridil and amiodarone simultaneously target the Alzheimer's disease beta- and gamma-secretase via distinct mechanismsStefan Mitterreiter
German Center for Neurodegenerative Diseases Munich and Adolf Butenandt Institute, Biochemistry, University of Munich, 80336 Munich, Germany
J Neurosci 30:8974-83. 2010..In addition to Alzheimer's disease, compounds with dual properties may also be useful for drug development targeting other membrane proteins... - gamma-Secretase cleavage site specificity differs for intracellular and secretory amyloid betaHeike S Grimm
Center for Molecular Biology Heidelberg ZMBH, University of Heidelberg, Im Neuenheimer Feld 282, D 69120 Heidelberg, Germany
J Biol Chem 278:13077-85. 2003.... - The transmembrane domain of the amyloid precursor protein in microsomal membranes is on both sides shorter than predictedBeate Grziwa
Center for Molecular Biology Heidelberg, University of Heidelberg, INF 282, D 69120 Heidelberg, Germany
J Biol Chem 278:6803-8. 2003..Moreover, the center of the TMD is positioned at the gamma-cleavage site at residue 42. Our data are consistent with a model in which gamma-secretase is a membrane protein that cleaves at the center of the membrane... - No alterations of hippocampal neuronal number and synaptic bouton number in a transgenic mouse model expressing the beta-cleaved C-terminal APP fragmentBart P F Rutten
Department of Psychiatry and Neuropsychology, University of Maastricht, Maastricht, The Netherlands
Neurobiol Dis 12:110-20. 2003..These data implicate that expression of beta-CTF per se is not neurotoxic, and that other mechanisms are responsible for the neurotoxic events in Alzheimer's disease brain... - GGA1 acts as a spatial switch altering amyloid precursor protein trafficking and processingChristine A F von Arnim
Alzheimer Disease Research Laboratory, Massachusetts General Hospital, Harvard Medical School, Charlestown, Massachusetts 02129, USA
J Neurosci 26:9913-22. 2006..GGA1 may act as a specific spatial switch influencing APP trafficking and processing, so that APP-GGA1 interactions may have pathophysiological relevance in AD... - The novel sorting nexin SNX33 interferes with cellular PrP formation by modulation of PrP sheddingAndreas Heiseke
Institute of Virology, Technical University of Munich, Trogerstr 30, 81675 Munich, Germany
Traffic 9:1116-29. 2008..Using deletion mutants, we demonstrate that production of PrP fragment N1 is not influenced by SNX33. Our data provide new insights into the cellular mechanisms of PrP(c) shedding and show how this can affect cellular PrP(Sc) conversion... - Transcriptional and translational regulation of BACE1 expression--implications for Alzheimer's diseaseSteffen Rossner
Paul Flechsig Institute for Brain Research, Department of Neurochemistry, University of Leipzig, Jahnallee 59, 04109 Leipzig, Germany
Prog Neurobiol 79:95-111. 2006.... - The intramembrane cleavage site of the amyloid precursor protein depends on the length of its transmembrane domainStefan F Lichtenthaler
Massachusetts General Hospital Harvard Medical School, Wellman Building, 50 Blossom Street, Boston, MA 02114, USA
Proc Natl Acad Sci U S A 99:1365-70. 2002..One cleavage site was located around the middle of the TMD, regardless of its actual length. An additional cleavage occurred within the N-terminal half of their TMD and thus at the opposite side of the Notch cleavage site... - Identification of candidate substrates for ectodomain shedding by the metalloprotease-disintegrin ADAM8Silvia Naus
Entwicklungsbiologie und Molekulare Pathologie, W7, , D-33615 Bielefeld, Germany
Biol Chem 387:337-46. 2006..Taken together, the results allowed us to identify novel candidate substrates that could be cleaved by ADAM8 in vivo under pathologic conditions... - SPPL2a and SPPL2b promote intramembrane proteolysis of TNFalpha in activated dendritic cells to trigger IL-12 productionElena Friedmann
Institute of Biochemistry, Swiss Federal Institute of Technology ETH, ETH Hoenggerberg, 8092 Zurich, Switzerland
Nat Cell Biol 8:843-8. 2006..Our study reveals a critical function for SPPL2a and SPPL2b in the regulation of innate and adaptive immunity...