Proteome analysis of apoptotic cells

  I. Introduction 00  II. Global Analyses of Apoptosis by 2DGE and MS 00A.  General Experimental Design 00B.  Identification of Protein Degradation 00C.  Identification of Other Protein Modifications 00D.  Identification of Protein Translocation 00E.  Identification of Protein Synthesis 00F.  Survey of Identified Proteins 00G.  Impact of Experimental Design 00   III. Analysis of Mitochondrial Releasing Factors by LC/MS 00   IV. Analysis of the Death‐Inducing Signaling Complex (DISC) 00    V. Analysis of IAP‐Interacting Proteins 00    VI. Chemical Proteomics of Caspases 00   VII. Conclusions and Outlook 00  VIII. Abbreviations 00 Acknowledgments 00 References 00Apoptosis, a genetically determined form of cell death, is a central and complex process involved in the development of multicellular organisms in the maintenance of cell homeostasis. During apoptosis, a large number of proteins involved in transducing signals are posttranslationally modified. Classical proteomics, the combination of protein separation by two‐dimensional gel electrophoresis (2DGE) and protein identification by mass spectrometry (MS), enabled the discovery of more than 100 proteins altered during apoptosis. Functional data about protein degradation, modification, translocation, and synthesis were obtained. In addition to classical proteomics, some specifically designed proteome studies were carried out to analyze specific apoptotic components such as the mitochondrial releasing factors, death‐inducing signaling complex (DISC), inhibitor of apoptosis (IAP) interacting proteins, and caspases. The identification of main regulators significantly influenced the elucidation of the concept underlying apoptosis signaling. Thus, the application of detailed protein analytical methods in the young field of apoptosis research was particularly fruitful. © 2004 Wiley Periodicals, Inc., Mass Spec Rev