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Identification of CD66a and CD66b as the major galectin-3 receptor candidates in human neutrophils.

Artikel i vetenskaplig tidskrift
Författare Elisabeth Feuk-Lagerstedt
E T Jordan
H Leffler
Claes Dahlgren
Anna Karlsson
Publicerad i Journal of immunology (Baltimore, Md. : 1950)
Volym 163
Nummer/häfte 10
Sidor 5592-8
ISSN 0022-1767
Publiceringsår 1999
Publicerad vid Institutionen för invärtesmedicin, Avdelningen för reumatologi och inflammationsforskning
Institutionen för medicinsk mikrobiologi och immunologi
Sidor 5592-8
Språk en
Länkar www.ncbi.nlm.nih.gov/entrez/query.f...
Ämnesord Antigens, CD, biosynthesis, blood, metabolism, Antigens, Differentiation, biosynthesis, blood, metabolism, pharmacology, Carrier Proteins, blood, Cell Adhesion Molecules, Cell Differentiation, drug effects, Cytoplasmic Granules, metabolism, Dimethyl Sulfoxide, pharmacology, Galectin 3, Gelatinases, blood, HL-60 Cells, Humans, Lysosome-Associated Membrane Glycoproteins, Macrophage-1 Antigen, biosynthesis, Membrane Glycoproteins, biosynthesis, Neutrophil Activation, immunology, Neutrophils, immunology, metabolism, Receptors, Mitogen, biosynthesis, blood, metabolism, Subcellular Fractions, immunology, metabolism
Ämneskategorier Immunologi inom det medicinska området

Sammanfattning

The mammalian lectin galectin-3 is a potent stimulus of human neutrophils, provided that the receptor(s) for the lectin has been mobilized to the cell surface before activation. We have recently shown that the receptors for galectin-3 are stored in intracellular mobilizable granules. Here we show supportive evidence for this in that DMSO-differentiated (neutrophil-like) HL-60 cells, which lack gelatinase and specific granules, are nonresponsive when exposed to galectin-3. Neutrophil granules were subsequently used for isolation of galectin-3 receptors by affinity chromatography. Proteins eluted from a galectin-3-Sepharose column by lactose were analyzed on SDS-polyacrylamide gels and showed two major bands of 100 and 160 kDa and a minor band of 120 kDa. By immunoblotting, these proteins were shown to correspond to CD66a (160 kDa), CD66b (100 kDa), and lysosome-associated membrane glycoprotein-1 and -2 (Lamp-1 and -2; 120 kDa). The unresponsive HL-60 cells lacked the CD66 Ags but contained the Lamps, implying that neutrophil CD66a and/or CD66b may be the functional galectin-3 receptors. This conclusion was supported by the subcellular localization of the CD66 proteins to the gelatinase and specific granules in resting neutrophils.

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