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Identification of C...
Identification of CD66a and CD66b as the major galectin-3 receptor candidates in human neutrophils.
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- Feuk-Lagerstedt, Elisabeth, 1949 (författare)
- Gothenburg University,Göteborgs universitet,Institutionen för invärtesmedicin, Avdelningen för reumatologi och inflammationsforskning,Institute of Internal Medicine, Dept of Rheumatology and Inflammation Research
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Jordan, E T (författare)
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Leffler, H (författare)
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visa fler...
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- Dahlgren, Claes, 1949 (författare)
- Gothenburg University,Göteborgs universitet,Institutionen för invärtesmedicin, Avdelningen för reumatologi och inflammationsforskning,Institutionen för medicinsk mikrobiologi och immunologi,Institute of Internal Medicine, Dept of Rheumatology and Inflammation Research,Institute of Medical Microbiology/Immunology
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- Karlsson, Anna, 1967 (författare)
- Gothenburg University,Göteborgs universitet,Institutionen för invärtesmedicin, Avdelningen för reumatologi och inflammationsforskning,Institute of Internal Medicine, Dept of Rheumatology and Inflammation Research
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visa färre...
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(creator_code:org_t)
- 1999
- 1999
- Engelska.
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Ingår i: Journal of immunology (Baltimore, Md. : 1950). - 0022-1767. ; 163:10, s. 5592-8
- Relaterad länk:
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https://gup.ub.gu.se...
Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Immunologi inom det medicinska området (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Immunology in the medical area (hsv//eng)
Nyckelord
- 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
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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