Galectin-3 type-C self-association on neutrophil surfaces; The carbohydrate recognition domain regulates cell function

Author:

Sundqvist Martina1,Welin Amanda1,Elmwall Jonas1,Osla Veronica1,Nilsson Ulf J.2,Leffler Hakon3,Bylund Johan4,Karlsson Anna1

Affiliation:

1. Department of Rheumatology and Inflammation Research; Sahlgrenska Academy at the University of Gothenburg; Gothenburg Sweden

2. Centre for Analysis and Synthesis; Department of Chemistry; Lund University; Lund Sweden

3. Department of Laboratory Medicine; Section of Microbiology; Immunology and Glycobiology; Lund University; Lund Sweden

4. Department of Oral Microbiology and Immunology; Sahlgrenska Academy at the University of Gothenburg; Gothenburg Sweden

Publisher

Wiley

Subject

Cell Biology,Immunology,Immunology and Allergy

Reference66 articles.

1. Mechanisms in neutrophil priming: characterization of the oxidative response induced by formylmethionyl-leucyl-phenylalanine in human exudated cells;Follin;Scand J Immunol,1991

2. Mobilization of granules and secretory vesicles during in vivo exudation of human neutrophils;Sengeløv;J Immunol,1995

3. A human lectin, galectin-3 (epsilon bp/Mac-2), stimulates superoxide production by neutrophils;Yamaoka;J Immunol,1995

4. Galectin-3 activates the NADPH-oxidase in exudated but not peripheral blood neutrophils;Karlsson;Blood,1998

5. Newcastle disease virus neuraminidase primes neutrophils for stimulation by galectin-3 and formyl-Met-Leu-Phe;Almkvist;Exp Cell Res,2004

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