Calcium-mediated hemagglutination by serum amyloid P component and the inhibition by specific glycosaminoglycans.
Human serum amyloid P component (SAP) was found to agglutinate erythrocytes in the presence of calcium ion. The hemagglutination was strongly inhibited by hyaluronic acid as well as by heparan sulfate and dermatan sulfate, but not by chondroitin 4-sulfate and keratan sulfate. A specific binding of SAP to hyaluronic acid, heparan sulfate, and dermatan sulfate was also confirmed by the fact that these glycosaminoglycans blocked the binding of SAP to agarose, a specific ligand of SAP.
Hamazaki
H
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Department of Biology, Kitasato University School of Medicine, Kanagawa, Japan.
D000818:Animals; D002118:Calcium / Q000494:pharmacology*; D003871:Dermatan Sulfate / Q000378:metabolism / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D006025:Glycosaminoglycans / Q000378:metabolism / Q000494:pharmacology*; D006384:Hemagglutination / Q000187:drug effects*; D006497:Heparan Sulfate / Q000378:metabolism / Q000494:pharmacology; D006801:Humans; D006820:Hyaluronic Acid / Q000378:metabolism / Q000494:pharmacology; D007163:Immunosorbent Techniques; D011817:Rabbits; D000683:Serum Amyloid P-Component / Q000378:metabolism / Q000494:pharmacology*
D002118:Calcium; D003871:Dermatan Sulfate; D006025:Glycosaminoglycans; D006497:Heparan Sulfate; D006820:Hyaluronic Acid; D000683:Serum Amyloid P-Component