Enzyme activities of NADPH-forming metabolic pathways in normal and leukemic leukocytes.
Clin Chem, 1975/6;21(7):880-3.
Belfiore F, Borzi V, Vecchio LL, Napoli E, Rabuazzo AM
PMID: 236846
Impact factor: 12.167
Abstract
With respect to the enzymes of NADPH-forming metabolic pathways in human leukocytes: (a) Glucose-6-phosphate dehydrogenase and phosphogluconate dehydrogenase (decarboxylating) were less active in leukocytes (mostly myeloblasts) from eight patients with acute myeloblastic leukemia (I) than in leukocytes (mostly granulocytes) from 16 normal subjects (II). (b) Of the enzymes of the citrate cleavage pathway, ATP citrate lyase and malate dehydrogenase (decarboxylating) (NADP+) were virtually absent in the cells studied. (c) Isocitrate dehydrogenase (NADP+), aspartate aminotransferase, and alanine aminotransferase, which, together with the much more active malate dehydrogenase, constitute a newly proposed NADPH-forming metabolic cycle, showed a higher activity in I than in II or III, and therefore could compensate, as concerns NADPH-generation, for the low activity of pentose cycle dehydrogenases. We are not sure whether the enzymatic characteristic of I cells is attributable to their immaturity or to their leukemic nature.
MeSH terms
ATP Citrate (pro-S)-Lyase; Alanine Transaminase; Aspartate Aminotransferases; Glucosephosphate Dehydrogenase; Humans; Isocitrate Dehydrogenase; Leukemia, Myeloid; Leukemia, Myeloid, Acute; Leukocytes; Malate Dehydrogenase; NADP; Phosphogluconate Dehydrogenase
More resources
EndNote: Download