Caspases: Their Role in Cell Death and Cell Survival by Marek Los, Henning Walczak

By Marek Los, Henning Walczak

The amount deals perception into the major study subject matters that contain caspases. best specialists from a number of parts of biology and medication have compiled this quantity in order that either the amateur and the pro will use this because the major reference for caspases for future years. The reader will know about the position of caspases in apoptosis signaling, irritation and melanoma remedy whereas being up-to-date at the method used to check caspases and the efforts of pharmaceutical study in focusing on caspases.

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Extra info for Caspases: Their Role in Cell Death and Cell Survival (Molecular Biology Intelligence Unit)

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9). When comparing 26 Caspases—Their Role in Cell Death and Cell Survival Figure 10. This analysis reveals two separate clusters: CARD and PYRIN containing prodomains (groups A1 and A2) and the DED-containing prodomains (group B). The group A1 CARD prodomains are part of the inflammatory caspases, while group A2 CARD prodomains belong to apoptotic caspases. 314,315 Hydra vulgaris (hy), Danio rerio (z), Xenopus laevis (x), Gallus gallus (g), Mus musculus (m), Homo sapiens (h). human procaspases, procaspase-4 and -5 have an amino acid sequence identity of 77%, the next highest identity score being 55% (between procaspase-1 and -4).

Ruiz-Vela A, Gonzalez de Buitrago G et al. Implication of calpain in caspase activation during B cell cloal deletion. EMBO J 1999; 18:4988-98. 47. Nakagawa T, Yuan J. Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis. Cell Biol 2000; 150:887-94. 48. Walker NP, Talanian RV, Brady KD et al. Crystal structure of the cysteine protease interleukin-1 beta- converting enzyme: a (p20/p10)2 homodimer. Cell 1994; 78:343-52. 49. Wilson KP, Black JA, Thomson JA et al.

In Figure 9 a phylogenetic analysis of the enzymatic relevant domains of the known Hydra vulgaris, Caenorhabditis elegans, Drosophila melanogaster, Xenopus laevis, Danio rerio, Gallus gallus, Mus musculus and Homo sapiens caspases shows divergence in three main clusters. It is immediately apparent that all three clusters contain functionally related members. 82-84 All C. elegans caspases gather in cluster I. All vertebrate and insect apoptosis-related executioner caspases belong to cluster II. These executioner caspases have a short prodomain, with the exception of Drosophila STRICA.

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