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Mannose in animal cells is phosphorylated by hexokinase (HK) and later isomerised by mannose phosphate isomerase (MPI) to fructose-6-P, which is incorporated in the glycolysis pathway. In this paper we report a significant decrease of MPI activity in splenic lymphoid cells from AKR/J old mice with lymphocytic leukaemia in comparison to that found in splenic lymphocytes from AKR/J non-leukaemic young mice and BALB/c young and old control mice. However, HK with mannose as substrate presents a normal activity in AKR/J leukaemic mice. This marked shortage of MPI explains the in vitro mannose toxicity found by us here in splenic lymphoid cells from AKR/J leukaemic mice. MPI activity was also decreased in peripheral blood lymphocytes from 4 out of the 6 patients studied with chronic lymphocytic leukaemia in relation to the activity found in the lymphocytes from healthy donors. The utility of analysing MPI activity in leukaemia patients and the use of mannose as an innocuous chemotherapic supporting agent in patients with decreased MPI activity is proposed.

Enzymes of mannose metabolism in murine and human lymphocytic leukaemia