Two types of adenosine deaminase (EC 126.96.36.199) were found in cultured cells of central-nervous-system origin. The predominant and more active enzyme was obtained in soluble form from the cytosol of mouse neuroblastoma (N-18), neonatal hamster astrocytes (NN), human oligodendroglioma (HOL) and human astrocytoma (Cox Clone). Particulate adenosine deaminase was probably associated with the plasma membrane. When radioactive adenosine was added to superfusates of monolayer cultures it was rapidly converted into inosine and hypoxanthine. The metabolic conversion required adenosine uptake by the cells, a probable transition through the intracellular ATP pool(s) and a rapid excretion into the superfusate of the catabolic products. We discuss the evidence that points to adenosine and its derivatives as neurohumoral modulators of central-nervous-system function.
Research Article|December 01 1975
Adenosine deaminase of cultured brain cells
Eberhard G. Trams;
Biochem J (1975) 152 (3): 681-687.
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Eberhard G. Trams, Carl J. Lauter; Adenosine deaminase of cultured brain cells. Biochem J 1 December 1975; 152 (3): 681–687. doi: https://doi.org/10.1042/bj1520681
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