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- W1965818158 abstract "Heme oxygenase‐1 (HO‐1), an inducible enzyme with broad tissue expression, is up‐regulated in response to hematopoietic stress and preserves vascular homeostasis. We investigated the involvement of HO‐1 in the differentiation of HL‐60 cells. Dimethylsulfoxide (DMSO), a representative differentiation inducer of HL‐60 cells, induced completely decrease HO‐1 expression in a time‐dependent manner, but increase CD11b, indicating that HO‐1 might have negative function in DMSO‐induced differentiation of HL‐60 cells. Zinc protoporphyrin (ZnPP), a strong inhibitor of HO‐1, induced differentiation of HL‐60 cells, as evidenced by a marked increase in the expression of CD11b following ZnPP treatment. In contrast, treatment with cobalt protoporphyrin (CoPP), an activator of HO‐1, decreased CD11b expression. ZnPP induced down‐regulation of HO‐1 protein expression in HL‐60 cells, while CoPP induced up‐regulation. In addition, ZnPP treatment caused a decrease in pRb and cyclin D 1 expression and an increase in p21 and p27 expression. These results suggest that down‐regulation of HO‐1 might be necessary for DMSO‐induced HL‐60 differentiation. This study provides the first evidence that HO‐1 plays an important role in DMSO‐induced differentiation of HL‐60 cells. Citation Information: Mol Cancer Ther 2009;8(12 Suppl):A113." @default.
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- W1965818158 date "2009-12-10" @default.
- W1965818158 modified "2023-09-25" @default.
- W1965818158 title "Abstract A113: Involvement of heme oxygenase‐1 (HO‐1) in the differentiation of human promyelocytic leukemic cells by DMSO" @default.
- W1965818158 doi "https://doi.org/10.1158/1535-7163.targ-09-a113" @default.
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