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Characterization of Human Phagocytic Cell Receptors for C5A and PlateletActivating Factor Expressed in Xenopus Oocytes

机译:非洲爪蟾卵母细胞中人类吞噬细胞受体C5a和血小板活化因子的表征

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Platelet activating factor (PAF) and the active cleavage product of the fifthcomponent of complement, C5a, are potent anaphylotoxins and mediators of inflammation. Both substances engage distinct guanine nucleotide binding regulatory protein-coupled receptors on a variety of cell types, thereby activating a signaling cascade that results in the mobilization of intracellular calcium stores, and in functional responses such as neutrophil chemotaxis and smooth muscle contraction. Little is known about the structure of PAF and C5a receptors or about the intracellular signaling pathways used by them. We have used the Xenopus oocyte expression system to demonstrate acquired C5a and PAF receptor activity in oocytes injected with mRNA from the promyelocytic leukemia cell line HL60 differentiated with dibutyryl cAMP. Activity was determined by measuring acquired ligand-dependent efflux of intracellular Ca and by measuring ligand-activated transmembrane currents in voltage clamped oocytes.

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