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High expression of udp‐n‐acetylglucosamine: β‐d mannoside β‐1, 4‐n‐acetylglucosaminyltransferase III (GnT‐III) in chronic myelogenous leukemia in blast crisis
Author(s) -
Yoshimura Masafumi,
Nishikawa Atsushi,
Ihara Yoshito,
Nishiura Tetsuo,
Nakao Hirohisa,
Kanayama Yoshio,
Matuzawa Yuji,
Taniguchi Naoyuki
Publication year - 1995
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/ijc.2910600404
Subject(s) - chronic myelogenous leukemia , western blot , leukemia , microbiology and biotechnology , cell culture , glycoprotein , gene isoform , biology , gene expression , gene , chemistry , immunology , cancer research , biochemistry , genetics
The activity and mRNA expression of UDP‐N‐acetylglucosamine: β‐D mannoside β‐1,4‐N‐acetylglucosaminyl transferase III (GnT‐III: EC 2.4.1.144) were investigated in hematological malignancies. GnT‐III activity was elevated in patients with chronic myelogenous leukemia (CML) in blast crisis and patients with multiple myeloma (MM), as compared to normal healthy subjects and patients with other hematological malignancies including CML in chronic phase. The GnT‐III transcript was the same size in leukemic cells from various hematological diseases and cell lines, while expression of the transcript was not found to correlate significantly with enzyme activity, implying that posttranslational modification might regulate the activity of GnT‐III. Southernblot analysis showed no significant variation in the structure and position of the GnT‐III genome, indicating that the gene is present as a single copy without isoforms. Furthermore, analyses by immunoprecipitation and Western blot revealed that high GnT‐III activity in KU812 cell, a CML cell line, resulted in an increase in E 4 ‐PHA binding to CD45, a major surface glycoprotein of the leukocyte, indicating that more bisecting GlcNAc was added to CD45 catalyzed by elevated GnT‐III.