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A more recent version of this article appeared on May 1, 2002.
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Submitted on January 10, 2002
Revised on May 17, 2002
Accepted on May 21, 2002

Plasma from cancer patients featuring a characteristic protein composition mediates protection against apoptosis

Susanne Vejda, Carsten Posovszky, Sieglinde Zelzer, Barbara Peter, Editha Bayer, Dieter Gelbmann, Rolf Schulte-Hermann, and Christopher Gerner

Dept. of Cell Biology, Institute of Cancer Research, University of Vienna, Vienna A-1090

Corresponding Author: Christopher.Gerner{at}univie.ac.at

By comparative proteome analysis we searched for characteristic alterations of human plasma accompanying neoplastic disease. We identified protein alterations in plasma of prostate-, lung- and breast-cancer patients in comparison to controls, comprising elevated levels of fibrinogen gamma-chain dimer, degradation products of antiplasmin and laminin gamma-chain, and elevated levels of acute phase proteins. The latter proteins and laminin fragments have been described as anti-apoptotic factors. We raised the question whether these alterations may have any relevance for the regulation of apoptosis. In contrast to plasma derived from healthy donors, samples from prostate-, lung- and breast-cancer patients selectively inhibited Fas- and staurosporine induced apoptosis in Jurkat cells, but remained ineffective upon UV light-induced apoptosis. These data suggested that inhibition occurred by extracellular interference with apoptosis induction. Supporting this hypothesis, we found that formation of the CD95-death inducing signal complex (DISC) was strongly inhibited in the presence of plasma from cancer patients.


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