Poly(A) polymerase distribution in normal and malignant lymphoid cells.
The incorporation of ATP on poly(A) primers catalyzed by poly(A) polymerase was investigated in normal and neoplastic lymphoid cells from animal and human sources. High levels of the enzyme were found in mouse thymus, in chicken bursa and thymus, as well as in neoplastic cells from patients affected by lymphoblastic and Burkitt's lymphomas. Low or very low quantities were found in peripheral blood lymphocytes, chronic lymphocytic leukemia cells, normal lymph nodes and solid lymphoid tissues of Hodgkin's disease. In general, the enzymatic content of neoplastic lymphoid cells reflected those of their normal counterpart. No effect of fasting or cortisone treatment on poly(A) polymerase in mouse spleen, thymus or liver was found. No particular relationships with B, T or non-T, non-B lineages were observed, but some relationship with DNA polymerase alpha was found. Therefore, it may be that poly(A) polymerase levels are related to the proliferative activity of the cellular populations.
D000818:Animals; D001853:Bone Marrow / Q000201:enzymology; D002051:Burkitt Lymphoma / Q000201:enzymology; D002060:Bursa of Fabricius / Q000201:enzymology; D002645:Chickens; D006689:Hodgkin Disease / Q000201:enzymology; D006801:Humans; D007938:Leukemia / Q000201:enzymology*; D008198:Lymph Nodes / Q000201:enzymology; D008214:Lymphocytes / Q000201:enzymology*; D008223:Lymphoma / Q000201:enzymology*; D008228:Lymphoma, Non-Hodgkin / Q000201:enzymology; D051379:Mice; D008807:Mice, Inbred BALB C; D009713:Nucleotidyltransferases / Q000378:metabolism*; D011062:Polynucleotide Adenylyltransferase / Q000378:metabolism*; D013154:Spleen / Q000201:enzymology; D013950:Thymus Gland / Q000201:enzymology
D009713:Nucleotidyltransferases; D011062:Polynucleotide Adenylyltransferase