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- W326568789 abstract "The binding of tumor necrosis factor-α (TNF-α) to a human osteogenic sarcoma cell line (Saos-2) was investigated. These cells express two types of receptors as determined by biochemical and immunological methods. Activation of protein kinase C (PKC) by phorbol esters prevented almost completely TNF-α binding to its receptors (down-regulation). This effect was reversed by staurosporine, calphostin C or by protein kinase C depletion. On the other hand, activators of protein kinase A such as dibutyryl cyclic adenosine monophosphate (db-cAMP) increases TNF-α binding to the type II (a) receptor (up-regulation). Okadaic acid, a phosphatases inhibitor, mimicked the effects of phorbol esters. Vinblastine, under conditions causing full microtubule disassembly, produced only a 50% decrease of TNF-α binding probably by interfering with the normal translocation to the membrane of the type I (β) receptor. Vinblastine plus phorbol myristate acetate (PMA) were additive in fully preventing TNF-α binding. It is suggested that the degree of binding of TNF-α to its receptors in Saos-2 cells is under the control of a microtubule-dependent and of a microtubule-independent regulatory pathway." @default.
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- W326568789 date "1993-01-01" @default.
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- W326568789 title "The Regulation of TNF-α Receptors in Human Osteosarcoma Cells" @default.
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- W326568789 doi "https://doi.org/10.1007/978-3-0348-5663-8_21" @default.
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