CHARACTERIZATION AND CELLULAR-LOCALIZATION BY MONOCLONAL-ANTIBODIES OF THE 60-KDA MANNOSE-SPECIFIC LECTIN OF HUMAN PROMYELOCYTIC CELLS, HL-60

被引:6
作者
CARPENTIER, V
VASSARD, C
PLESSIS, C
MOTTA, G
MONSIGNY, M
ROCHE, AC
机构
[1] UNIV ORLEANS, BIOCHIM GLYCOCONJUGUES & LECTINES ENDOGENES LAB, F-45071 ORLEANS 02, FRANCE
[2] CNRS, CTR BIOPHYS MOLEC, F-45071 ORLEANS 02, FRANCE
关键词
CONFOCAL MICROSCOPY; MACROPHAGE LINEAGE; NEOGLYCOPROTEINS;
D O I
10.1007/BF00731206
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Myelomonocytic lineage cells express an M(r) 60000 mannose specific lectin, MR60 (Pimpaneau et al. (1991), Carbohydr Res 213: 95-108). Under non-reducing conditions, this protein migrates as a 120000 protein. MR60 does not contain any N-glycan moiety cleavable by the action of N-glycanase. MR60 induces a sugar selective aggregation of beads coated with glycosylated albumin: beads bearing alpha-D-mannosyl residues are aggregated while beads bearing alpha-D-glucosyl residues are not. A monoclonal antibody Lec101B, specific for MR60, recognizes a single M(r) 60000 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.
引用
收藏
页码:333 / 338
页数:6
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