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Purine Metabolic Enzymes in Lymphocytes
Author(s) -
KURASHIGE S.,
AKUZAWA Y.,
MITSUHASHI S.
Publication year - 1985
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1985.tb01853.x
Subject(s) - adenosine deaminase , purine nucleoside phosphorylase , xanthine oxidase , phytohaemagglutinin , adenosine , hypoxanthine , deoxycoformycin , biochemistry , inosine , purine , adenosine kinase , biology , chemistry , microbiology and biotechnology , enzyme , in vitro
Coformycin, which is an inhibitor of adenosine deaminase, significantly inhibited in vitro blastogenic responses of human lymphocytes to both phytohaemagglutinin (PHA) and pokeweed mitogen (PWM), whereas blastogenic responses to bacterial lipopolysaccharide (LPS) were rather enhanced by the addition of coformycin. Blastogenic responses of lymphocytes to PHA and PWM were markedly suppressed by the addition of adenosine, which is a substrate of adenosine deaminase. Allopurinol, which is an inhibitor of xanthine oxidase, inhibited blastogenic responses of human lymphocytes to PHA, PWM, and bacterial LPS. Inosine (a substrate of purine nucleoside phosphorylase) and hypoxanthine (a substrate of xanthine oxidase) showed no or only a small effect on blastogenic responses of human lymphocytes. These results suggest that adenosine deaminase activity is associated with the T‐cell response but not with the B‐cell response and that the impaired T‐cell response in adenosine deaminase deficiency is the result of intracellular retention of adenosine in T cells. The results also suggest that purine nucleoside phosphorylase or xanthine oxidase activity is associated with both T‐ and B‐cell responses.