Proceedings of the National Academy of Sciences · 1980 · 26 citations · 19 references
Life SciencesCell BiologyImmunologyCellular ImmunologyMolecular ImmunologyMonoclonal AntibodiesAntibody CharacterizationAntibody-antigen RecognitionAntigen RecognitionCell-surface GlycansGlycan-protein InteractionsHuman Leukocyte Antigen SystemAntibody SubclassesCarbohydrate Sequence AnalysisGlycan Recognition By AntibodiesImmune Recognition Of GlycansImmunoglobulin-like Carbohydrate RecognitionPeripheral Blood Lymphocyte Analysis
Surface immunofluorescence experiments using a human anti-i and two anti-I antisera have been performed on human peripheral blood lymphocytes. These are known to contain cold-reactive monoclonal IgM antibodies against the carbohydrate sequence: (formula: see text). A high proportion of B- and T-type lymphocytes express these I and i determinants. In the presence of anti-human immunoglobulin, the cold-reactive membrane-associated complexes of I-anti-I and i-anti-i become stabilized, and redistribution (with patching and capping) can be elicited at 37 degrees C. Dual fluorescence experiments have shown striking concordant staining of I or i (fluorescein) caps and patches with concanavalin A (rhodamine) reactive sites on normal and leukemic cells, suggesting that a proportion of I and i active structures of lymphocyte membranes are structurally associated or physiologically coupled with glycoproteins carrying oligosaccharides with branched mannosyl cores.
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Ten Feizi, Kabat Ea, Giuseppe Vicari et al. · PubMed · 1971 · 208 citations
Heiner Niemann, Kiyohiro Watanabe, Sen‐itiroh Hakomori et al. · Biochemical and Biophysical Research Communications · 1978 · 199 citations