Proteome analysis of apoptotic cells

Publisher Website
Google Scholar
Abstract
I. Introduction 00 II. Global Analyses of Apoptosis by 2DGE and MS 00 A. General Experimental Design 00 B. Identification of Protein Degradation 00 C. Identification of Other Protein Modifications 00 D. Identification of Protein Translocation 00 E. Identification of Protein Synthesis 00 F. Survey of Identified Proteins 00 G. 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 00 Apoptosis, 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