Cellular proteolytic modification of tumor-suppressor CYLD is critical for the initiation of human T-cell acute lymphoblastic leukemia
Copyright policy )Cellular proteolytic modification of tumor-suppressor CYLD is critical for the initiation of human T-cell acute lymphoblastic leukemia
There exists a general recognition of the fact that post translational modification of CYLD protein through proteolytic cleavage by MALT-1 results in sustained cellular NF-kB activity which is conspicuously found to be associated with cancer in general and hematological malignancies in particular. The present study was directed to understand the contribution of MALT-1 and deubiquitinase CYLD to the initiation of T-cell acute lymphoblastic leukemia (T-ALL). Such a study revealed for the first time that the 35kDa CYLD cleaved factor generated by MALT-1 mediated proteolytic cleavage was conspicuously present in human T- ALL subjects of pediatric age group. Further, over-expression of this 35kDa CYLD factor within normal human peripheral blood mononuclear cells had the inherent capacity to program the genome of these cells resulting in T-cell lineage ALL. Based upon these results, we propose that MALT1 inhibitors may be of crucial importance in the treatment of T-ALL subjects of pediatric age group.
Male, Adolescent, Tumor Suppressor Proteins, Precursor T-Cell Lymphoblastic Leukemia-Lymphoma, Deubiquitinating Enzyme CYLD, Neoplasm Proteins, Mucosa-Associated Lymphoid Tissue Lymphoma Translocation 1 Protein, Caspases, Child, Preschool, Proteolysis, Tumor Cells, Cultured, Humans, Female, Child, Protein Modification, Translational
Male, Adolescent, Tumor Suppressor Proteins, Precursor T-Cell Lymphoblastic Leukemia-Lymphoma, Deubiquitinating Enzyme CYLD, Neoplasm Proteins, Mucosa-Associated Lymphoid Tissue Lymphoma Translocation 1 Protein, Caspases, Child, Preschool, Proteolysis, Tumor Cells, Cultured, Humans, Female, Child, Protein Modification, Translational
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