Journal ArticleDOI
Negative regulation of erythropoiesis by caspase-mediated cleavage of GATA-1
Ruggero De Maria,Ruggero De Maria,Ann Zeuner,Ann Zeuner,Adriana Eramo,Cristina Domenichelli,Désirée Bonci,Francesco Grignani,Francesco Grignani,Srinivasa M. Srinivasula,Emad S. Alnemri,Ugo Testa,Cesare Peschle,Cesare Peschle +13 more
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TLDR
It is shown that immature erythroid cells express several death receptors whose ligands are produced by mature erythroblasts, and caspase-mediated cleavage of GATA-1 may represent an important negative control mechanism in erythropoiesis.Abstract:
The production of red blood cells follows the sequential formation of proerythroblasts and basophilic, polychromatophilic and orthochromatic erythroblasts, and is promoted by the hormone erythropoietin (Epo) in response to tissue hypoxia. However, little is known about the negative regulation of this process. Death receptors are a family of surface molecules that trigger caspase activation and apoptosis in a variety of cell types. Here we show that immature erythroid cells express several death receptors whose ligands are produced by mature erythroblasts. Exposure of erythroid progenitors to mature erythroblasts or death-receptor ligands resulted in caspase-mediated degradation of the transcription factor GATA-1, which is associated with impaired erythroblast development. Expression of a caspase-resistant GATA-1 mutant, but not of the wild-type gene, completely restored erythroid expansion and differentiation following the triggering of death receptors, indicating that there is regulatory feedback between mature and immature erythroblasts through caspase-mediated cleavage of GATA-1. Similarly, erythropoiesis blockade following Epo deprivation was largely prevented by the expression of caspase-inhibitory proteins or caspase-resistant GATA-1 in erythroid progenitors. Caspase-mediated cleavage of GATA-1 may therefore represent an important negative control mechanism in erythropoiesis.read more
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Guidelines for the use and interpretation of assays for monitoring cell death in higher eukaryotes
Lorenzo Galluzzi,Lorenzo Galluzzi,Lorenzo Galluzzi,Stuart A. Aaronson,John M. Abrams,Emad S. Alnemri,David W. Andrews,Eric H. Baehrecke,Nicolas G. Bazan,Mikhail V. Blagosklonny,Klas Blomgren,Klas Blomgren,Christoph Borner,Dale E. Bredesen,Dale E. Bredesen,Catherine Brenner,Maria Castedo,Maria Castedo,Maria Castedo,John A. Cidlowski,Aaron Ciechanover,Gerald M. Cohen,V De Laurenzi,R De Maria,Mohanish Deshmukh,Brian David Dynlacht,Wafik S. El-Deiry,Richard A. Flavell,Richard A. Flavell,Simone Fulda,Carmen Garrido,Carmen Garrido,Pierre Golstein,Pierre Golstein,Pierre Golstein,Marie-Lise Gougeon,Douglas R. Green,Hinrich Gronemeyer,Hinrich Gronemeyer,Hinrich Gronemeyer,György Hajnóczky,J. M. Hardwick,Michael O. Hengartner,Hidenori Ichijo,Marja Jäättelä,Oliver Kepp,Oliver Kepp,Oliver Kepp,Adi Kimchi,Daniel J. Klionsky,Richard A. Knight,Sally Kornbluth,Sharad Kumar,Beth Levine,Beth Levine,Stuart A. Lipton,Enrico Lugli,Frank Madeo,Walter Malorni,Jean-Christophe Marine,Seamus J. Martin,Jan Paul Medema,Patrick Mehlen,Patrick Mehlen,Gerry Melino,Gerry Melino,Ute M. Moll,Ute M. Moll,Eugenia Morselli,Eugenia Morselli,Eugenia Morselli,Shigekazu Nagata,Donald W. Nicholson,Pierluigi Nicotera,Gabriel Núñez,Moshe Oren,Josef M. Penninger,Shazib Pervaiz,Marcus E. Peter,Mauro Piacentini,Jochen H. M. Prehn,Hamsa Puthalakath,Gabriel A. Rabinovich,Rosario Rizzuto,Cecília M. P. Rodrigues,David C. Rubinsztein,Thomas Rudel,Luca Scorrano,Hans-Uwe Simon,Hermann Steller,Hermann Steller,J. Tschopp,Yoshihide Tsujimoto,Peter Vandenabeele,Ilio Vitale,Ilio Vitale,Ilio Vitale,Karen H. Vousden,Richard J. Youle,Junying Yuan,Boris Zhivotovsky,Guido Kroemer,Guido Kroemer,Guido Kroemer +103 more
TL;DR: A nonexhaustive comparison of methods to detect cell death with apoptotic or nonapoptotic morphologies, their advantages and pitfalls is provided and the importance of performing multiple, methodologically unrelated assays to quantify dying and dead cells is emphasized.
Journal ArticleDOI
Four deaths and a funeral: from caspases to alternative mechanisms.
Marcel Leist,Marja Jäättelä +1 more
TL;DR: A single family of proteases, the caspases, has long been considered the pivotal executioner of all programmed cell death, but recent findings of evolutionarily conserved, caspase-independent controlled death mechanisms have opened new perspectives on the biology of cell demise.
Journal ArticleDOI
Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis.
Toshiyuki Nakagawa,Junying Yuan +1 more
TL;DR: It is proposed that disturbance to intracellular calcium storage as a result of ischemic injury or amyloid β peptide cytotoxicity may induce apoptosis through calpain- mediated caspase-12 activation and Bcl-xL inactivation, suggesting a novel apoptotic pathway involving calcium-mediated calpain activation and cross-talks between calpain and caspases families.
Journal ArticleDOI
Many cuts to ruin: a comprehensive update of caspase substrates
TL;DR: This review summarizes the known caspase substrates comprising a bewildering list of more than 280 different proteins and highlights some recent aspects inferred by the cleavage of certain proteins in apoptosis.
Journal ArticleDOI
Hsp27 negatively regulates cell death by interacting with cytochrome c
Jean-Marie Bruey,Cécile Ducasse,Philippe Bonniaud,Luigi Ravagnan,Santos A. Susin,Chantal Diaz-Latoud,Sandeep Gurbuxani,André-Patrick Arrigo,Guido Kroemer,Eric Solary,Carmen Garrido +10 more
TL;DR: Hsp27 binds to cytochrome c released from the mitochondria to the cytosol and prevents cy tochrome-c-mediated interaction of Apaf-1 with procaspase-9, which interferes specifically with the mitochondrial pathway of caspases-dependent cell death.
References
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Journal ArticleDOI
Caspases: Enemies Within
TL;DR: This work has shown that understanding caspase regulation is intimately linked to the ability to rationally manipulate apoptosis for therapeutic gain.
Journal ArticleDOI
Death receptors: signaling and modulation
Avi Ashkenazi,Vishva M. Dixit +1 more
TL;DR: Apoptosis is a cell suicide mechanism that enables metazoans to control cell number in tissues and to eliminate individual cells that threaten the animal's survival.
Journal ArticleDOI
Apoptosis by death factor.
TL;DR: This work was supported in part by Grants-in-Aid from the Ministry of Education, Science, and Culture of Japan and by a Research Grant from the Princess Takamatsu Cancer Research Fund, and performed in part through Special Coordination Funds of the Science and Technology Agency of the Japanese Government.
Journal ArticleDOI
Caspases: the executioners of apoptosis
TL;DR: The importance of caspase prodomains in the regulation of apoptosis is further highlighted by the recognition of adapter molecules, such as RAIDD [receptor-interacting protein (RIP)-associated ICH-1/CED-3-homologous protein with a death domain]/CRADD (caspase and RIP adapter with death domain), which binds to the prodomain of cspase-2 and recruits it to the signalling complex.
Journal ArticleDOI
Inhibition of death receptor signals by cellular FLIP
Martin Irmler,Margot Thome,Michael Hahne,Pascal Schneider,Kay Hofmann,Véronique Steiner,Jean-Luc Bodmer,Michael Schröter,Kim Burns,Chantal Mattmann,Donata Rimoldi,Lars E. French,Jürg Tschopp +12 more
TL;DR: The characterization of an inhibitor of apoptosis is reported, designated FLIP (for FLICE-inhibitory protein), which is predominantly expressed in muscle and lymphoid tissues and may be implicated in tissue homeostasis as an important regulator of apoptotic regulation.
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