Characterization and cellular localization by monoclonal antibodies of the 60 kDa mannose specific lectin of human promyelocytic cells,HL60 |
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Authors: | V. Carpentier C. Vassard C. Plessis G. Motta M. Monsigny A. C. Roche |
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Affiliation: | (1) Laboratoire de Biochimie des Glycoconjugués et lectines endogènes, Université d'Orléans et Centre de Biophysique Moléculaire, CNRS, Bât.B, 1, rue Charles Sadron, F.45071 Orléans Cedex 02, France |
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Abstract: | Myelomonocytic lineage cells express anMr 60 000 mannose specific lectin, MR60 (Pimpaneauet al. (1991),Carbohydr Res213: 95–108). Under non-reducing conditions, this protein migrates as a 120 000 protein. MR60 does not contain anyN-glycan moiety cleavable by the action ofN-glycanase. MR60 induces a sugar selective aggregation of beads coated with glycosylated albumin: beads bearing -d-mannosyl residues are aggregated while beads bearing -d-glucosyl residues are not. A monoclonal antibody Lec101B, specific for MR60, recognizes a singleMr 60 000 protein by Western blotting. This monoclonal antibody does not label the cell surface of cells expressing MR60, but decorates intracellular vesicles upon permeabilization of these cells. |
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Keywords: | confocal microscopy macrophage lineage neoglycoproteins |
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