*Division of Pharmacology, Department of Medicine and Care, and â Division of Cell Biology, Department of Biomedicine and Surgery, Linkoping University, Linkoping, Sweden ¨ ¨ We studied whether the acute-phase protein 1-acid glycoprotein (AGP) induces rises in [Ca2 ]i in neutrophils and sought to identify the corresponding AGP receptor (or receptors). We found that AGP elicited a minimal rise in [Ca2 ]i in Fura-2-loaded neutrophils, and this response was markedly enhanced by pretreatment with anti-L-selectin antibodies. (The EC50 value of the AGP-induced Ca2 response was 9 g/ml.) Activation of phospholipase-C, Src tyrosine kinases, and PI3 kinases proved to be essential for the AGP-mediated increase in [Ca2 ]i, whereas the p38 MAPK and SYK signaling pathways were not involved. Furthermore, antibodies against sialic acid binding, immunoglobulin-like lectin 5 (Siglec-5) and oligosaccharide 3 -sialyl-lactose both antagonized the AGP-induced response and caused an immediate increase in [Ca2 ]i in anti-L-selectin-treated neutrophils, which indicates a signaling capacity of Siglec-5. We used modiï¬ed forms of AGP (treated with mild periodate or neuraminidase) to establish the importance of sialic acid residues. The modiï¬ed forms of AGP caused a much smaller rise in [Ca2 ]i than did unaltered AGP. Afï¬nity chromatography conï¬rmed that unchanged AGP,
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The acute-phase protein α 1 -acid glycoprotein (AGP) induces rises in cytosolic Ca 2+ in neutrophil granulocytes via sialic acid binding immunoglobulin-like lectins (Siglecs)
Peter Gunnarsson , Louise Levander , Peter Påhlsson , and Magnus Grenegård
Follow The FASEB Journal
, Volume 21 (14): 4059
Fed of American Socs for Experimental Biology – Dec 1, 2007
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