
Mass spectrometric characterization of the surfactant protein A (SP-A) receptor 210 (SP-R210) led to the identification of myosin (Myo) XVIIIA and nonmuscle myosin IIA. Antibodies generated against the unique C-terminal tail of MyoXVIIIA revealed that MyoXVIIIA, MyoIIA, and SP-R210 have overlapping tissue distribution, all being highly expressed in myeloid cells, bone marrow, spleen, lymph nodes, and lung. Western blot analysis of COS-1 cells stably transfected with either MyoXVIIIA or MyoIIA indicated that SP-R210 antibodies recognize MyoXVIIIA. Furthermore, MyoXVIIIA but not MyoIIA localized to the surface of COS-1 cells, and most importantly, expression of MyoXVIIIA in COS-1 cells conferred SP-A binding. Western analysis of recombinant MyoXVIIIA domains expressed in bacteria mapped the epitopes of previously derived SP-R210 antibodies to the neck region of MyoXVIIIA. Antibodies raised against the neck domain of MyoXVIIIA blocked the binding of SP-A to macrophages. Together, these findings indicate that MyoXVIIIA constitutes a novel receptor for SP-A.
DNA, Complementary, Bacteria, Base Sequence, Dose-Response Relationship, Drug, Macrophages, Blotting, Western, Cell Membrane, Blotting, Northern, Flow Cytometry, Mass Spectrometry, Epitopes, Mice, Immunoglobulin G, COS Cells, Chlorocebus aethiops, Animals, Humans, Immunoprecipitation, Amino Acid Sequence, Cells, Cultured
DNA, Complementary, Bacteria, Base Sequence, Dose-Response Relationship, Drug, Macrophages, Blotting, Western, Cell Membrane, Blotting, Northern, Flow Cytometry, Mass Spectrometry, Epitopes, Mice, Immunoglobulin G, COS Cells, Chlorocebus aethiops, Animals, Humans, Immunoprecipitation, Amino Acid Sequence, Cells, Cultured
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