CYCLIC-AMP PHOSPHODIESTERASE IN HUMAN LYMPHOCYTES AND LYMPHOBLASTS

  • 1 January 1978
    • journal article
    • research article
    • Vol. 4  (2) , 123-132
Abstract
Cyclic nucleotide phosphodiesterase activities were examined in lymphocytes from 12 transformed human B [bone marrow-derived] cell lines, 2 T [thymus-derived] cell lines, 6 patients with lymphocytic leukemia and 10 normal donors. A consistent difference between cells from the normal and leukemic state was observed. The cyclic AMP phosphodiesterase activity from normal lymphocytes is inhibited greater than 80% by .mu.M cyclic GMP while this concentration of nucleotide has little or no effect on the enzyme from transformed lymphocytic cell lines or from lymphocytic cells of leukemia patients. The reported lack of cyclic GMP phosphodiesterase in human lymphocytes from several sources is confirmed. The apparent absence of a cyclic GMP degradation mechanism and of cyclic GMP control of cyclic AMP hydrolysis may be related to defective lymphocyte growth control.

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