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Activation of the n...
Activation of the neutrophil nicotinamide adenine dinucleotide phosphate oxidase by galectin-1.
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- Almkvist, Jenny, 1971 (author)
- 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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- Dahlgren, Claes, 1949 (author)
- 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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- Karlsson, Anna, 1967 (author)
- 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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- Leffler, Hakon (author)
- Lund University,Lunds universitet,Avdelningen för mikrobiologi, immunologi och glykobiologi - MIG,Institutionen för laboratoriemedicin,Medicinska fakulteten,Division of Microbiology, Immunology and Glycobiology - MIG,Department of Laboratory Medicine,Faculty of Medicine
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(creator_code:org_t)
- 2002
- 2002
- English.
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In: Journal of immunology (Baltimore, Md. : 1950). - 0022-1767. ; 168:8, s. 4034-4041
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Abstract
Subject headings
Close
- Galectins are a group of lactose-binding proteins widely distributed in nature. Twelve mammalian galectins have so far been identified, but their functions are to a large extent unknown. In this work we study galectin-1 in its interaction with human neutrophils, with regard to both cell surface binding and activation of the superoxide-producing NADPH-oxidase. We show that galectin-1 is able to activate the neutrophil NADPH-oxidase, provided that the cells have been primed by extravasation from the blood into the tissue, an activation pattern that is similar to that of galectin-3. Using in vitro priming protocols, the galectin-1 responsiveness was found to correlate to granule mobilization and galectin-1 binding to the cells, suggesting the presence of granule-localized receptors that are up-regulated to the cell surface upon priming. By galectin-1 overlay of fractionated neutrophils we identified potential galectin-1 receptor candidates localized in the membranes of the secretory vesicle and gelatinase granules. The binding of galectin-1 and galectin-3 to neutrophil proteins was compared, as were the dose dependencies for activation by the two lectins. The results suggest that, although similarities are found between the two galectins, they appear to activate the NADPH-oxidase using different receptors. In conclusion, galectin-1 appears to have proinflammatory functions, mediated through activation of the neutrophil respiratory burst.
Subject headings
- 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)
Keyword
- Adjuvants
- Immunologic
- blood
- metabolism
- physiology
- Antigens
- Differentiation
- metabolism
- Carrier Proteins
- metabolism
- Cell Degranulation
- immunology
- Cell Movement
- immunology
- Cytoplasmic Granules
- enzymology
- immunology
- metabolism
- Dose-Response Relationship
- Immunologic
- Enzyme Activation
- immunology
- Exudates and Transudates
- cytology
- enzymology
- immunology
- Galectin 1
- Galectin 3
- Hemagglutinins
- blood
- metabolism
- physiology
- Humans
- NADPH Oxidase
- blood
- metabolism
- Neutrophil Activation
- immunology
- Neutrophils
- enzymology
- metabolism
- Protein Binding
- immunology
- Receptors
- Mitogen
- metabolism
- Subcellular Fractions
- immunology
- metabolism
Publication and Content Type
- ref (subject category)
- art (subject category)
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