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PUMA (p53 upregulated modulator of apoptosis) is a pro-apoptotic member of the BH3-only subgroup of the Bcl-2 family. It is a key mediator of p53-dependent and p53-independent apoptosis and was identified 10 years ago. The PUMA gene is mapped to the long arm of chromosome 19, a region that is frequently deleted in a large number of human cancers. PUMA mediates apoptosis thanks to its ability to directly bind known anti-apoptotic members of the Bcl-2 family. It mainly localizes to the mitochondria. The binding of PUMA to the inhibitory members of the Bcl-2 family (Bcl-2-like proteins) via its BH3 domain seems to be a critical regulatory step in the induction of apoptosis. It results in the displacement of the proteins Bax and/or Bak. This is followed by their activation and the formation of pore-like structures on the mitochondrial membrane, which permeabilizes the outer mitochondrial membrane, leading to mitochondrial dysfunction and caspase activation. PUMA is involved in a large number of physiological and pathological processes, including the immune response, cancer, neurodegenerative diseases and bacterial and viral infections.
One dimensional patterns of proteins from homogenates and four cellular fractions i. e., nuclear, mitochondrial, microsomal, and cytosolic from normal and leukemic lymphocytes were compared. Results obtained revealed that the neoplastic transformation of normal lymphocytes into CLL and ALL ones is associated with the expression of some novel proteins. Electrophoretically-specific nuclear protein of B-CLL lymphocytes with mol. wt of 38/39 kDa was used as immunogen to produce rabbit antiserum. It was observed that obtained antiserum crossreacted with 38/39 kDa antigen of nuclear fractions from CLL and ALL lymphocytes (15 of 16 studied), but not with any of normal ones. It was shown, by Western blot technique, that the expression of 38/39 kDa antigen is correlated with progression of B-CLL disease.
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