Abstract
We previously reported that the expression and the activity of SHP-1, a non-transmembrane protein tyrosine phosphatase (PTPase) increased during myeloid differentiation of an acute promyelocytic leukemia cell line (HT93) induced by all-trans retinoic acid (ATRA). To examine whether inhibition of SHP-1 activity attenuates myeloid differentiation, we used a new PTPase inhibitor, 3,4-dephostatin, and studied its effect on myeloid differentiation. Suppressive effects on immunoprecipitated SHP-1 phosphatase activity and myeloid cell differentiation were detected. These results suggest that SHP-1 is a substrate for 3,4-dephostatin, and that SHP-1 PTPase activity is closely related to myeloid differentiation.
MeSH terms
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Cell Differentiation / drug effects*
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Enzyme Inhibitors / pharmacology*
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Gene Expression Regulation, Enzymologic
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Granulocytes / enzymology
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Humans
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Hydroquinones / pharmacology*
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Intracellular Signaling Peptides and Proteins
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Leukemia, Promyelocytic, Acute / enzymology
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Leukemia, Promyelocytic, Acute / pathology*
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Macrophage-1 Antigen / metabolism
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Protein Tyrosine Phosphatase, Non-Receptor Type 11
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Protein Tyrosine Phosphatase, Non-Receptor Type 6
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Protein Tyrosine Phosphatases / antagonists & inhibitors*
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Protein Tyrosine Phosphatases / metabolism
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Tretinoin / antagonists & inhibitors*
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Tretinoin / pharmacology
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Tumor Cells, Cultured
Substances
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Enzyme Inhibitors
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Hydroquinones
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Intracellular Signaling Peptides and Proteins
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Macrophage-1 Antigen
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dephostatin
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Tretinoin
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PTPN11 protein, human
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PTPN6 protein, human
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Protein Tyrosine Phosphatase, Non-Receptor Type 11
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Protein Tyrosine Phosphatase, Non-Receptor Type 6
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Protein Tyrosine Phosphatases