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Heidi Olzscha
Hartl Lab
Max Planck Institute of Biochemistry, Department of Cellular Biochemistry, Am Klopferspitz 18, D-82152 Martinsried
(+49-89) 8578 2209, (+49-89) 8578 2224
(+49-89) 8578 2211

The Department of Cellular Biochemistry, Max Planck Institute of Biochemistry (Prof. Dr. F.-Ulrich Hartl), is investigating the mechanisms of protein folding in the cell. Protein folding is required for the realization of genetic information at the level of functional proteins and as such is one of the most fundamental reactions in all of biology. The long-term goal is to reach a comprehensive understanding, at the structural and functional level, of how the machinery of molecular chaperones assists in co- and posttranslational protein folding.

Furthermore, Ulrich Hartl and the department of Cellular Biochemistry are interested in causes and consequences of the intracellular protein misfolding and subsequent aggregation processes.

Specifically, I am analyzing structural features of aggregating proteins in human cells, encompassing artificial de novo amyloid polypeptides, huntingtin, and aggregation caused by non-canonical amino acid incorporation in proteins, and focused on following questions:

Do artificial de novo amyloid proteins and non-canonical amino acids cause cytotoxicity and if so, to what extent? Cell viability assays, assay for apoptosis.

Which structures determine the cytotoxicity of natural amyloid proteins like huntingtin and de novo amyloid proteins? Investigation of sequence elements determining aggregation and cellular toxicity of the amyloid proteins: analysis of mutant and modified versions of huntingtin and de novo amyloid proteins.

Which species are responsible for observed cytotoxicity? Using size-exclusion chromatography and ultracentrifugation in combination with structure specific antibodies (e. g. A11) for determination of the different species (monomers, oligomers, aggregates).

What are the differences between naturally aggregating proteins and the artificially generated amyloid proteins? Comparison of the cellular and biochemical differences between natural (Ab, huntingtin) and artificial (de novo polypeptides) aggregating proteins (solubility, localization, turn-over, processing).

Which proteins do interact with the naturally aggregating and artificially generated aggregating proteins? Determination of the interactomes of ab and de novo amyloid proteins via SILAC, Co-IP and LC-MS/MS.

How can the cytotoxicity be abolished? Do molecular chaperones help in protecting proteins against aggregation and causing cytotoxicity? Upregulation of molecular chaperones by usage of chemical compounds or overexpression of molecular chaperones in presence of the aggregation-prone proteins.


May 2011 - present
Postdoctoral
EMBO fellow at the Department of Oncology, University of Oxford (Prof. Dr. Nicholas B. La Thangue), Oxford, UK.

November 2010 - March 2011
Research at the
Max Planck Institute of Biochemistry, Department of Cellular Biochemistry (Prof. Dr. F.-Ulrich Hartl), Martinsried, Germany.

January 2005 - October 2010
PhD student at the
Max Planck Institute of Biochemistry, Department of Cellular Biochemistry (Prof. Dr. F.-Ulrich Hartl), Martinsried, Germany. PhD thesis title: "Analyse struktureller Determinanten der toxischen Wirkung amyloider Proteine" (Analysis of structural determinants underlying the toxic effects of amyloid proteins"), affiliation: Ludwig-Maximilians University, Munich; PhD supervisor: Prof. Dr. F.-Ulrich Hartl.

July 2004
Diploma (equivalent to an MSc) in
biochemistry.

January 2004 – July 2004
Diploma thesis at the
Institute of Clinical Chemistry/Central Laboratories (Prof. Dr. Christoph Wagener), Center for Diagnostics, University Hospital Hamburg-Eppendorf, Germany. Diploma thesis title: „Charakterisierung der Phosphotyrosinbindungsstellen des humanen FLT3-Rezeptors mittels modularer Domänen“ (Characterization of phosphotyrosine binding sites of the human FLT3 receptor with modular domains“). Diploma thesis supervisors: Prof. Dr. Christoph Wagener, Dr. Peter Nollau.

January 2003 – July 2003
Research project at the
Department of Biochemistry, Molecular Biology and Cell Biology, Judd A. and Marjorie Weinberg College of Arts and Sciences, Northwestern University, Evanston/Chicago, USA. Title: „Investigation of direct interactions between the clathrin adaptor complex AP-1B and the co-adaptor PACS-1“. Supervisor: Prof. Dr. Heike Fölsch.

June 2002 – August 2002
Research project at the
Institute of Clinical Chemistry/Central Laboratories (Prof. Dr. Christoph Wagener), Center for Diagnostics, University Hospital Hamburg-Eppendorf, Germany. Title: „mRNA assay of CEACAM1 in different cell lines after stimulation with the tumorpromotor TPA“. Supervisors: Prof. Dr. Christoph Wagener, Dr. Peter Nollau.

October 1999 – August 2004
Undergraduate studies
biochemistry/molecular biology, University of Hamburg, Germany. Major: Biochemistry/molecular biology; minors: Pharmacology/toxicology, virology, tumor biology.

June 1999 – August 1999
Research project at the
Center for Molecular Neurobiology Hamburg (ZMNH), Molecular Pathomechanisms of Alzheimer’s Disease Laboratory (Prof. Dr. Roger Nitsch), University Hospital Hamburg-Eppendorf, Germany. Title: „Expression of the gene rgig2 as a GFP fusion protein and its localization in the cell“. Supervisors: Prof. Dr. Roger Nitsch, Dr. Manuel Mayhaus.

June 1997
A-levels at the humanistic grammar school
Christianeum, Hamburg-Othmarschen, Germany.


Heidi Olzscha1, Sonya M. Schermann1, Andreas C. Woerner, Stefan Pinkert, Michael H. Hecht, Gian G. Tartaglia, Michele Vendruscolo, Manajit Hayer-Hartl, F. Ulrich Hartl, and R. Martin Vabulas. (2011). Amyloid-like Aggregates Sequester Numerous Metastable Proteins with Essential Cellular Functions. Cell. 144, 67-78.

Heidi Olzscha, Andreas C. Woerner, Michael H. Hecht, R. Martin Vabulas, F.-Ulrich Hartl. Cytotoxicity of de novo amyloid-like proteins in eukaryotic and prokaryotic cells. EMBO Conference SeriesCellular protein homeostasis in disease and ageing“. Dubrovnik (Croatia), May 2009.

Heidi Olzscha, Andreas C. Woerner, Michael H. Hecht, R. Martin Vabulas, F.-Ulrich Hartl. Cytotoxicity of de novo amyloid-like proteins. FASEB Summer Research Conference Protein folding in the Cell“. Saxtons River (USA), July 2008.

Heidi Olzscha, R. Martin Vabulas, Michael H. Hecht, F.-Ulrich Hartl. Cytotoxicity of de novo amyloid proteins in mammalian cells. Gordon ConferenceStress Proteins in Growth, Development and Disease“. Oxford (United Kingdom), August 2007.

 


 

July 2011 – present: EMBO long-term fellowship, Department of Oncology, University of Oxford, Oxford, UK.

May 2011: MPIB Junior Research Award 2011 for outstanding research in biochemistry, Martinsried, Germany.

September 2010: Doctoral degree Dr. rer. nat. (equivalent to PhD) in biochemistry.

May 2009: Poster award (1st place) "Cytotoxicity of de novo amyloid protein in eukaryotic and prokaryotic cells", EMBO-conference series "Cellular protein homeostasis in disease and ageing", Dubrovnik, Croatia.

October 2006 - present: Member of the Elite Network Bavaria, international graduate program "Protein Dynamics in Health and Disease".

June 2006: Participation in the 56th meeting of Nobel Laureates in Lindau.

July 2005 to June 2007: PhD Kekulé Scholarship from the Fonds of the Chemical Industry (FCI, Germany).


Organizer of our first ENB seminar "Hopes and Concerns in Science", inviting of four speakers.


Member of the International Graduate Program "Protein Dynamics in Health and Disease" in the Elite Network of Bavaria.

Member of the German Society for Biochemistry and Molecular Biology (GBM).

Member of the Society for Alumni and Supporters of the program for studies Biochemistry/Molecular Biology at the University of Hamburg (EFBM).

Postdoctoral fellow at the Department of Oncology, University of Oxford, UK

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Heidi Olzscha
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Alumni
Biochemistry
Max Planck Institute of Biochemistry, Department of Cellular Biochemistry