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- W2032724336 abstract "We describe the molecular cloning of a 1803-bp cDNA coding for a product termed interferon-induced immunoglobulin-binding protein (IIBP) from a library of IFN-α-induced primary bone marrow macrophages. The open reading frame encodes a protein of 26-kDa containing two immunoglobulin-like and one Fc receptor-like domain. Due to the constitutive release of low amounts of IFN-β, the IIBP mRNA is already present in macrophage-colony-stimulating factor-cultured macrophages. Its expression could be blocked in the presence of either anti-IFN-β or interleukin-4, which down-regulates the endogenous IFN-β production. Upon addition of rIFN-α4 a 3-5-fold superinduction of IIBP mRNA was observed. Rat monoclonal antibodies detected a protein of the predicted size exclusively in cell culture supernatants of primary bone marrow macrophages and a B-cell line. In immunoprecipitation experiments an unknown 30-kDa protein co-precipitated. The secreted IIBP showed considerable binding to nonspecific rat IgG2a and could be precipitated using mouse IgG2a, IgG2b and IgG3 antibodies of irrelevant specificities, indicating that this gene product is a novel secreted immunoglobulin-binding protein with a new IgG isotype binding pattern that differs to that of known Fc receptors." @default.
- W2032724336 created "2016-06-24" @default.
- W2032724336 creator A5033857585 @default.
- W2032724336 creator A5090153362 @default.
- W2032724336 creator A5090317439 @default.
- W2032724336 date "1999-05-01" @default.
- W2032724336 modified "2023-09-26" @default.
- W2032724336 title "Molecular cloning of a macrophage-derived, interferon-inducible secreted immunoglobulin-binding protein" @default.
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- W2032724336 doi "https://doi.org/10.1002/(sici)1521-4141(199905)29:05<1504::aid-immu1504>3.0.co;2-t" @default.
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