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Molecular & Cellular Proteomics 1:387-393, 2002.
© 2002 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

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^,||

Institute of Cancer Research, University of Vienna, 1090 Vienna, Austria
University Children’s Hospital, 89077 Ulm, Germany
^¶ Institute of Molecular Biology, University of Graz, 8010 Graz, Austria

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 -chain dimer, degradation products of antiplasmin and laminin -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 was strongly inhibited in the presence of plasma from cancer patients.

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