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^a Centre National de la Recherche Scientifique Unité Mixte de Recherche 8603, Université René Descartes (Paris V), Institut Fédérative de Recherche Necker, 75743 Paris cedex 15, France
^b Laboratoire d'Hématologie, Université René Descartes (Paris V), Institut Fédérative de Recherche Necker, 75743 Paris cedex 15, France
^c Service d'Hématologie Clinique, Université René Descartes (Paris V), Institut Fédérative de Recherche Necker, 75743 Paris cedex 15, France
^d Institut National de la Santé et de la Recherche Médicale (INSERM) U517, Unité Fédérative de Recherche Medecine et Pharmacie, Dijon 21033, France
^e Laboratoire de Recherche d'Hémobiologie, Hôpital Cochin, 75014 Paris, France
^f INSERM U363, Hôpital Cochin, 75014 Paris, France
Service d'Hématologie Clinique and CNRS UMR 8603, Hôpital Necker, 149-161 rue de Sèvres, 75743 Paris cedex 15, France.33-1-44-49-52-8033-1-44-49-52-83

hermine{at}necker.fr

The cysteine proteases known as caspases play a central role in most apoptotic pathways. Here, we show that caspase inhibitors arrest the maturation of human erythroid progenitors at early stages of differentiation, before nucleus and chromatin condensation. Effector caspases such as caspase-3 are transiently activated through the mitochondrial pathway during erythroblast differentiation and cleave proteins involved in nucleus integrity (lamin B) and chromatin condensation (acinus) without inducing cell death and cleavage of GATA-1. These observations indicate a new function for caspases as key proteases in the process of erythroid differentiation.

Key Words: apoptosis • erythropoiesis • mitochondria • acinus • lamin B

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