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 Pinnacle Studio 16 Ultimate v16.0.0.75 Multilingual with Content. Pinnacle Studio Ultimate is the easy-to-use power tool for creating.
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Identification of a macrophage receptor(s) for the HIV type 1 envelope protein gp120.
Cynomolgus monkey peritoneal macrophages were incubated with a highly purified gp120 preparation derived from the ABL3 strain of HIV-1. gp120 bound specifically to monkey peritoneal macrophages, whereas gp120 preparations derived from other strains of HIV-1 (HXB2, RF, ACH, IIIB, BAL) failed to bind to monkey macrophages. Immunofluorescence staining of the macrophages revealed that only the macrophages that bound gp120 expressed surface glycoproteins and that the gp120 binding cells were also stellate shaped. Biochemical studies indicated that these stellate cells were characterized by the presence of high affinity receptors for gp120. Scatchard analysis indicated that peritoneal macrophages bound approximately 1 ng of gp120/cell. The binding of gp120 to these macrophages was time and temperature dependent. The binding was Ca2+ independent and was inhibited by monoclonal antibodies to the CD4 receptor. Immunofluorescence microscopy of biotin-labeled macrophages demonstrated that the gp120 binding cells expressed not only the CD4 receptor, but also the transferrin receptor. Binding of gp120 to macrophages induced a rapid, dose-dependent increase in the levels of steady state messenger RNA (mRNA) for the major lymphokines, IL-1 beta, IL-6 and TNF alpha. Treatment of gp120-treated cells with the protein synthesis inhibitor cycloheximide prevented the increase in steady state mRNA levels for IL-1 beta, IL-6 and TNF alpha, indicating that the increase in cytokine mRNA levels was dependent on de novo protein synthesis. These studies demonstrate that a cell surface molecule(s) capable of interacting with the HIV type 1 envelope protein gp120 specifically binds to macrophages and that this binding induces an increase in mRNA for macrophage-produced IL-1 beta, IL-6 82fe58eafd

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