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Activation of the neutrophil nicotinamide adenine dinucleotide phosphate oxidase by galectin-1.

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
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
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.
In: Journal of immunology (Baltimore, Md. : 1950). - 0022-1767. ; 168:8, s. 4034-4041
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • 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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