Increased N‐Acetylglucosamine‐l‐phosphotransferase Activity in Sera from Patients with Leukemia

In human cancer, lysosomal hydrolases contain increased amounts of phosphorylated sugar chains. Sugar chains of the hydrolases undergo post‐translational processing which is catalyzed by N‐acetyl‐glucosamine‐1‐phosphotransferase (GIcNAc‐phosphotransferase) at the first step. In the present study we...

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Bibliographic Details
Published in:Cancer science 1991-01, Vol.82 (1), p.82-85
Main Authors: Uehara, Yoshio, Gasa, Shinsei, Makita, Akira, Sakurada, Keisuke, Tamotsu, Tamotsu
Format: Article
Language:English
Subjects:
Acute lymphoblastic leukemia
Chemotherapy
Chronic myeloid leukemia
GlcNAc‐phosphotransferase ‐Leukemia
Glucosamine
Leukemia
Lymphatic leukemia
Myelodysplastic syndrome
Myeloid leukemia
N-Acetylglucosamine
Phosphorylation
Phosphotransferase
Serum
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Summary:In human cancer, lysosomal hydrolases contain increased amounts of phosphorylated sugar chains. Sugar chains of the hydrolases undergo post‐translational processing which is catalyzed by N‐acetyl‐glucosamine‐1‐phosphotransferase (GIcNAc‐phosphotransferase) at the first step. In the present study we estimated serum GlcNAc‐phosphotransferase in 50 adults suffering from leukemia and myelo‐dysplastic syndrome. The serum GlcNAc‐phosphotransferase was increased to moderate or high levels in patients with acute nonlymphocytic leukemia (ANLL), acute lymphoblastic leukemia and chronic myelogenous leukemia, suggesting that the serum transferase is released from leukemic cells. In many cases of ANLL examined,activity of the transferase was decreased concomitantly with reduction of peripheral blastic cells by effective chemotherapy.
ISSN:0910-5050
1347-9032
1349-7006
1876-4673
DOI:10.1111/j.1349-7006.1991.tb01749.x