Hyperglycosylation of eosinophil ribonucleases in a promyelocytic leukemia cell line and in differentiated peripheral blood progenitor cells

Autor: Helene F. Rosenberg, Fei Li, H. L. Tiffany
Rok vydání: 1995
Předmět:
Zdroj: Journal of Leukocyte Biology. 58:49-54
ISSN: 1938-3673
0741-5400
DOI: 10.1002/jlb.58.1.49
Popis: 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 Hf, 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.
Databáze: OpenAIRE
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