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Hyperglycosylation of eosinophil ribonucleases in a promyelocytic leukemia cell line and in differentiated peripheral blood progenitor cells
Author(s) -
Lee Tiffany H.,
Li Fei,
Rosenberg Helene F.
Publication year - 1995
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.58.1.49
Subject(s) - eosinophil , progenitor cell , eosinophil cationic protein , microbiology and biotechnology , cell culture , biology , cd34 , immunology , stem cell , cancer research , genetics , asthma
We evaluated two independent models of eosinophil differentiation for their ability to synthesize the ribonuclease toxins eosinophil‐derived neurotoxin (EDN) and eosinophil cationic protein (ECP). Cells from the done 15 subline of HL‐60 (human promyelocytic leukemia) produced both EDN and ECP; production of EDN increased in response to butyric acid (BA). CD34 + peripheral blood progenitor cells (PBPCs) grown with cytokines promoting eosinophil differentiation also produced EDN. EDN from both the done 15 and PBPCs was more heterogeneous and heavily glycosylated ( ~ 22–45 kDa) than EDN from mature peripheral blood eosinophils (18–25 kDa). The heterogeneity of EDN from the done 15 cells was not altered by endogiycosidase H f , whereas treatment with peptide‐ N ‐giycosidase F (PNGase F) produced a single‐band immunoreactive band ( ~ 15 kDa). In contrast, only the highest molecular weight forms of EDN from differentiated PBPCs were eliminated by PNGase F (reduced to 22–35 kDa), suggesting the presence of uncharacteristic forms of posttranslational modification. Synthesis of hyperglycosylated proteins has not been previously reported in PBPCs and is a feature shared with tumor cells and cell lines. J. Leukoc. Biol. 58: 49–54; 1995.