Zentrum für Klinische Forschung


Hornemann Thorsten

Group Leader

Dr. Thorsten Hornemann



Name of the Institution

Institute for Clinical Chemistry
University Hospital Zurich


Rämistrasse 100


8091 Zürich


+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.


Hartmann-Müller Stiftung, Baugarten Stiftung, EMDO Stiftung and Herzog-Egli Stiftung



Link to "Forschungsdatenbank" of the University