The DNA-repair enzyme uracil-DNA glycosylase in the human hematopoietic system.
The expression of the DNA base-excision-repair enzyme uracil-DNA glycosylase in the human hematopoietic system followed a tightly regulated pattern: high enzyme activities were recorded in proliferating bone marrow progenitor cells and in peripheral blood T- and B-cells, both groups of cells requiring the integrity of their genetic information for their proper function. The blood quiescent immunocompetent cells retained their DNA-uracil exclusion capacity, even in the oldest age groups. Peripheral blood mature end cells, granulocytes, platelets and red cells had little activity, consistent with the fact that these cells are anuclear or short-lived, so that no template-primer functions of their DNA are required. Uracil-DNA glycosylase expression is high in all types of human leukemia, providing a selective advantage for survival of leukemic cells. Overall results show that a deficiency of this DNA base-excision-repair pathway is not likely to be an etiopathogenetic factor in the formation of non-random or other chromosomal abnormalities or in the leukemogenesis itself.
Vilpo
J A
JA
Laboratory of Molecular Hematology, Biocenter, Oulu, Finland.
D000749:Anemia, Megaloblastic / Q000201:enzymology; D001973:Bromodeoxyuridine / Q000494:pharmacology; D002455:Cell Division; D002869:Chromosome Aberrations; D045647:DNA Glycosylases; D004260:DNA Repair; D005472:Fluorouracil / Q000494:pharmacology; D005493:Folic Acid Antagonists / Q000494:pharmacology; D006410:Hematopoiesis; D006412:Hematopoietic Stem Cells / Q000201:enzymology*; D006801:Humans; D007938:Leukemia / Q000201:enzymology; D009699:N-Glycosyl Hydrolases / Q000378:metabolism*; D009363:Neoplasm Proteins / Q000378:metabolism; D051981:Uracil-DNA Glycosidase
D005493:Folic Acid Antagonists; D009363:Neoplasm Proteins; D045647:DNA Glycosylases; D009699:N-Glycosyl Hydrolases; D051981:Uracil-DNA Glycosidase; D001973:Bromodeoxyuridine; D005472:Fluorouracil