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NAD + ‐metabolizing ecto‐enzymes shape tumor–host interactions: The chronic lymphocytic leukemia model
Author(s) -
Vaisitti Tiziana,
Audrito Valentina,
Serra Sara,
Bologna Cinzia,
Brusa Davide,
Malavasi Fabio,
Deaglio Silvia
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.04.036
Subject(s) - cd38 , nad+ kinase , nicotinamide adenine dinucleotide , chronic lymphocytic leukemia , extracellular , enzyme , biochemistry , nucleotide , purinergic receptor , biology , intracellular , nucleoside , nicotinamide mononucleotide , adenosine , chemistry , microbiology and biotechnology , leukemia , immunology , gene , stem cell , cd34
Nicotinamide adenine dinucleotide (NAD + ) is an essential co‐enzyme that can be released in the extracellular milieu. Here, it may elicit signals through binding purinergic receptors. Alternatively, NAD + may be dismantled to adenosine, up‐taken by cells and transformed to reconstitute the intracellular nucleotide pool. An articulated ecto‐enzyme network is responsible for the nucleotide–nucleoside conversion. CD38 is the main mammalian enzyme that hydrolyzes NAD + , generating Ca 2+ ‐active metabolites. Evidence suggests that this extracellular network may be altered or used by tumor cells to (i) nestle in protected areas, and (ii) evade the immune response. We have exploited chronic lymphocytic leukemia as a model to test the role of the ecto‐enzyme network, starting by analyzing the individual elements that make up the whole picture.