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• W1975698355 startingPage "95" @default.
• W1975698355 abstract "Most mammalian macrophages express D-mannose-specific receptor (membrane lectin, Mr 175,000) allowing endocytosis of their ligands, but cells of the monocytic lineage (HL60, U937, monocyte) lack this receptor. However, after permeabilization, promyelocytic, promonocytic cells and monocytes bound fluoresceinylated D-mannose-terminated neoglycoproteins as evidenced by flow cytometry. Under these conditions, confocal analysis confirmed the intracellular membrane localization of the labeling and the absence of nuclear binding. An intracellular D-mannose-specific receptor was isolated from the human promyelocytic cell line HL60, by affinity chromatography on 4-isothiocyanatophenyl alpha-D-mannopyranoside-substituted Affi-gel as a 60,000-Mr membrane protein requiring divalent cations for the ligand binding. Under the same conditions, mouse macrophages were shown to express a 175,000-Mr D-mannose-specific receptor but not the 60,000-Mr receptor." @default.
• W1975698355 created "2016-06-24" @default.
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• W1975698355 date "1991-06-01" @default.
• W1975698355 modified "2023-10-11" @default.
• W1975698355 title "Characterization and isolation of an intracellular d-mannose-specific receptor from human promyelocytic HL60 cells" @default.
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• W1975698355 doi "https://doi.org/10.1016/s0008-6215(00)90601-3" @default.
• W1975698355 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/1933956" @default.
• W1975698355 hasPublicationYear "1991" @default.
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