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Contact information:
Peter Nollau
University Medical Center Hamburg-Eppendorf (UKE)
Diagnostic Center, Institute for Clinical Chemistry
CAMPUS Research Building, N27
Martinistraße 52
20246 Hamburg
Germany
Phone: int. acc. code +49 (0) 40-7410-51906
Fax:: int. acc. code +49 (0) 40-7410-54971
E-mail: nollau@uke.uni-hamburg.de
Curriculum vitae
1991
MD degree, University Medical Center Hamburg-Eppendorf, Hamburg, Germany
since 1992
clinical research assistant, Institute of Clinical Chemistry, University Medical Hamburg Eppendorf
1999-2001
postdoctoral fellowship, Mayer Lab, Children's Hospital, Harvard Medical School, Boston, USA
since 2002
primary investigator, Institute of Clinical Chemistry, University Medical Center Hamburg-Eppendor
Awards
2007 research award of the "Hamburger Krebsgesellschaft"
Group members
Technical Research Assistants
Helwe Gerull
Birgit Klampe
Graduate students
Alexandra Samsen, M.Sc. Biochemistry/Molecular Biology
Hardy Schweigel, M.Sc. Biochemistry/Molecular Biology
Malik Khenkar (undergraduate)
Christoph Maßlo (undergraduate)
Malte Klüssendorf (undergraduate)
Open positions
Currently, no funded positions are available. We are always seeking for highly motivated students with a background in biochemistry or molecular biology interested in studying cell signalling pathways.
Research interests
Deciphering complex cell signalling processes and the role of posttranslational protein modifications in humane diseases, particularly in cancer, is the main research interest of our group. Among posttranslational modifications, the phosphorylation of tyrosine residues and glycosylation of membrane proteins play a pivotal role in the control of many important biological processes such as proliferation, apoptosis, cell differentiation and migration. To study the role of posttranslational modifications in human diseases, we have established a broad spectrum of analytical tools and techniques. Key components of our assay systems are a battery of natural occurring, in vitro generated src homology region 2 (SH2) and carbohydrate recognition domains (CRD) used as probes for the analysis of the cellular state of phosphorylation and glycosylation. Based on Far Western Blot analysis, oligonucleotide tagged multiplex assay (OTM) and immunhistochemistry, these modular binding domains are currently applied for the detailed and comprehensive analyses of various normal and malignant tissues with the aim to identify critical signalling pathways in cancer and other diseases. By global profiling of posttranslational protein modifications, we hope to develop novel diagnostics for improved classification of diseases and stratification of patients guiding the rational development and application of disease-specific therapeutics. An example of differential signal activity in human breast cancer samples determined by SH2-domain based profiling is given below.
Funding
Cooperations
Selected Publications
Dierck K, Machida K, Mayer BJ, Nollau P. (2009). Profiling the Tyrosine Phosphorylation State Using SH2 Domains. Methods Mol Biol 527:131-55.
Machida K, Thompson CM, Dierck K, Jablonowski K, Kärkkäinen S, Liu B, Zhang H, Nash PD, Newman DK, Nollau P, Pawson T, Renkema GH, Saksela K, Schiller MR, Shin DG, Mayer BJ. (2007). High-throughput phosphotyrosine profiling using SH2 domains. Mol Cell 26:899-915.
Bogoevska V, Nollau P, Lucka L, Grunow D, Klampe B, Uotila LM, Samsen A, Gahmberg CG, Wagener C. (2007). DC-SIGN binds ICAM-3 isolated from peripheral human leukocytes through Lewis x residues. Glycobiology 17:324-33.
Dierck K, Machida K, Voigt A, Thimm J, Horstmann M, Fiedler W, Mayer BJ, Nollau P. (2006). Quantitative multiplexed profiling of cellular signaling networks using phosphotyrosine-specific DNA-tagged SH2 domains. Nat Methods 3:737-44.
Bogoevska V, Horst A, Klampe B, Lucka L, Wagener C, Nollau P. (2006). CEACAM1, an adhesion molecule of human granulocytes, is fucosylated by fucosyltransferase IX and interacts with DC-SIGN of dendritic cells via Lewis x residues. Glycobiology 16:197-209.
Machida K, Mayer BJ, Nollau P. (2003). Profiling the global tyrosine phosphorylation state. Mol Cell Proteomics 2:215-33.
