Hornemann Thorsten
Group Leader
Dr. Thorsten Hornemann
Name of the Institution
Institute for Clinical Chemistry
University Hospital Zurich
Street
Rämistrasse 100
City
8091 Zürich
Phone
+41-44-255 47 19
Group Members
Richard Stephane, Dipl. Biol., Ph.D. Student (stephane.richard@usz.ch)
Main Field(s) of Research, Abstract
The main field of our research is the influence of sphigolipid metabolism on cellular signalling and apoptosis. Ceramides and metabolites thereof are ubiquitous constituents of membrane lipids in mammalian cells and involved in various cellular events like apoptosis, signal transduction and membrane trafficking. A dysfunctuion of the ceramide pathway is the cause for various deseases like HSN1 or Fabry. In our research we investigate the role of de novo sphingolipid synthesis on peripheral neuronal development and axonal regeneration as well as its possible influence in other neurodegenerative diseases like diabetic sensory neuropathy (DSN) or Alzheimer desease. Currently the main focus of our work is the function and regulation of the serine-palmitoyltransferase, a keyenzyme in the de-novo synthesis pathway of sphingolipids.
Main Fields of Research, Keywords
Serine Palmitoyltransferase, Sphigolipids, Lipid metabolism, peripheral neuropatie,HSN1, Sphigosin, Sphinganines
Special Techniques and Equipment
Molecular biology, 2D Gelelektrophoresis, Protein expression/puirification, HPLC, LC-MS/MSs
Education and Training
We have training opportunities for PhD students, PostDocs and medical dissertations.
Selected Publications
Hornemann T, Kempa S, Himmel M, Fürst DO, Wallimann T. Muscle type creatine kinase interacts with central domains of the M-band proteins myomesin and M-protein J Mol Biol. 2003 Sep 26;332(4):877-87
Stolz M, Hornemann T, Schlattner U, Wallimann T. Mutation of conserved active-site threonine residues in creatine kinase affects autophosphorylation and enzyme kinetics. Biochem J. 2002 May 1;363(Pt 3):785-92.
Kraft T, Hornemann T, Stolz M, Nier V, Wallimann T. Coupling of creatine kinase to glycolytic enzymes at the sarcomeric I-band of skeletal muscle: a biochemical study in situ. J Muscle Res Cell Motil. 2000;21(7):691-703.
Hornemann T, Rutishauser D, Wallimann T. Why is creatine kinase a dimer? Evidence for cooperativity between the two subunits. Biochim Biophys Acta. 2000 Jul 14;1480(1-2):365-73.
Hornemann T, Stolz M, Wallimann T. Isoenzyme-specific interaction of muscle-type creatine kinase with the sarcomeric M-line is mediated by NH(2)-terminal lysine charge-clamps. J Cell Biol. 2000 Jun 12;149(6):1225-34.
Funding
Hartmann-Müller Stiftung, Baugarten Stiftung, EMDO Stiftung and Herzog-Egli Stiftung
URL
Link to "Forschungsdatenbank" of the University
http://www.research-projects.uzh.ch/med/unit42100/area678/p3271.htm