Adenosine deaminase of cultured brain cells

E G Trams; C J Lauter

doi:10.1042/bj1520681

Adenosine deaminase of cultured brain cells

Biochem J. 1975 Dec;152(3):681-7. doi: 10.1042/bj1520681.

Authors

E G Trams¹, C J Lauter

Affiliation

¹ Laboratory of Neurochemistry, National Institute of Neurological and Communicative Disorders and Stroke, National Institutes of Health, Bethesda, MD 20014, U.S.A.

Abstract

Two types of adenosine deaminase (EC 3.5.4.4) 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.