Issam Arrouss, Didier Decaudin, Sylvain Choquet, Nabih Azar, Christophe Parizot, Jean M. Zini, Fariba Nemati and Angelita Rebollo Pages 539 - 546 ( 8 )
PP2A is a serine/threonine phosphatase critical to a number of physiological and developmental processes. In this manuscript, we show that a peptide, specifically blocking the caspase- 9/PP2A interaction, DPT-C9h, induces apoptosis in primary tumour B cells isolated from peripheral blood mononuclear cells or bone marrow of chronic lymphocytic leukemia (CLL) patients, but not on B cells obtained from healthy donors (HD). Moreover, in both CLL patients and HD, DPT-C9h does not induce apoptosis on T- and NKcells and monocytes. Our results strongly suggest that DPT-C9h peptide has tumour specificity and that caspase-9/PP2Ac interaction constitutes a novel therapeutic approach for the treatment in CLL patients.
apoptosis, Caspase-9, CLL, penetrating peptides, PP2A.
CIMI Paris, Universite Pierre et Marie Curie, 91 bd de l’hopital 75013 Paris, France.