Apoptosis: Techniques and Protocols (Neuromethods) by Andréa C. LeBlanc

By Andréa C. LeBlanc

During this revised and extended moment version, professional specialists describe in step by step element their most sensible cutting-edge ideas for learning neuronal cellphone demise. those easily reproducible equipment clear up a wide selection of study difficulties, together with the detection of the most important proteins considering neuronal apoptosis (Bax protein, cytochrome c, and caspases), the direct evaluate of the position of pro-apoptotic proteins in neurons via viral infections and microinjections, and the detection of pro-apoptotic proteins in situ. There also are hands-on tools for the research of apoptosis mechanisms in neuronal cubicles, for learning synaptosis, and for constructing gene expression profiles in neurodegenerative mind tissues through the use of DNA microarrays.

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4. Inhibitors of Caspases Anomalous activation of caspases can be detrimental; therefore protection mechanisms were evolved to avoid this problem. Inhibitors of caspases were first described in viruses. CrmA and p35 are two viral proteins that directly inhibit some caspases. CrmA, a cowpox virus serpin, inhibits most caspases but not group II caspases and caspase-6 (reviewed in ref. 21). The baculoviral p35 is less specific and inhibits most caspases. The discovery of the baculoviral inhibitor of apoptosis (IAP) has prompted many researchers to investigate the existence of mammalian homologues.

Once inside the OMM, apocytochrome-c is covalently attached to a heme group to form mature holocytochrome-c. Holocytochromec is more globular and is trapped between the mitochondrial membranes. However, proapoptotic stimuli can cause the release of cytochrome-c and other proteins of the intermembrane space into the cytoplasm by an as yet unknown mechanism. Once released from mitochondria, cytochrome-c can interact with Apaf-1, which makes Apaf-1 capable of recruiting procaspase-9, forming an apoptosome.

2000) Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins. Cell 102(1), 43–53. 8. , Susin, S. , et al. (2001) Essential role of the mitochondrial apoptosis-inducing factor in programmed cell death. Nature 410(6828), 549–554. 9. Stennicke, H. R. and Salvesen, G. S. (1999) Catalytic properties of the caspases. Cell Death Differ. 6(11), 1054–1059. 10. Bossy-Wetzel, E. and Green, D. R. (2000) Assays for cytochrome c release from mitochondria during apoptosis.

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