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Submitted on March 6, 2002
Revised on May 14, 2002
Accepted on May 14, 2002

Alterations in the mouse and human proteome caused by Huntington disease

Claus Zabel, Daniel C. Chamrad, Josef Priller, Ben Woodman, Helmut E. Meyer, Gillian P. Bates, and Joachim Klose

Institut für Humangenetik, Universitätsklinikum Charite, Berlin, Berlin 13353

Corresponding Author: claus.zabel{at}charite.de

Huntington disease is an autosomal dominantly inherited disease that usually starts in midlife and inevitably leads to death. In our effort to identify proteins involved in processes upstream or downstream of the disease causing huntingtin, we studied the proteome of a well-established mouse model by large-gel 2D electrophoresis. We could demonstrate for the first time at the protein level that alpha 1-antitrypsin and alpha B-crystalline both decrease in expression over the course of disease. Importantly, the alpha 1-antitrypsin-decrease in the brain precedes that in liver and testes in mice. Reduced expression of the serine protease inhibitors alpha 1-antitrypsin and contraspin was found in liver, heart and testes close to terminal disease. Decreased expression of the chaperone alpha B-crystalline was found exclusively in the brain. In three brain regions obtained post-mortem from Huntington’s disease patients, alpha 1-antitrypsin expression was also altered. Reduced expression of the major urinary proteins not found in the brain, was seen in the liver of affected mice, demonstrating that the disease exerts its influence outside the brain of transgenic mice at the protein level. Maintaining alpha 1-antitrypsin and alpha B-crystalline availability during the course of Huntington’s disease might prevent neuronal cell death and therefore could be useful in delaying the disease progression.


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