Literature DB >> 3276308

Calcium-mediated hemagglutination by serum amyloid P component and the inhibition by specific glycosaminoglycans.

H Hamazaki1.   

Abstract

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.

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Year:  1988        PMID： 3276308     DOI： 10.1016/0006-291x(88)90507-4

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


  4 in total

1.  Detection and characterization of natural and inducible lectins in human serum.

Authors:  Beulaja Manikandan; Manikandan Ramar
Journal:  Results Immunol       Date:  2012-06-07

2.  On the association between amyloid fibrils and glycosaminoglycans; possible interactive role of Ca2+ and amyloid P-component.

Authors:  T Stenstad; J H Magnus; K Syse; G Husby
Journal:  Clin Exp Immunol       Date:  1993-10       Impact factor: 4.330

3.  Human serum amyloid P is a multispecific adhesive protein whose ligands include 6-phosphorylated mannose and the 3-sulphated saccharides galactose, N-acetylgalactosamine and glucuronic acid.

Authors:  R W Loveless; G Floyd-O'Sullivan; J G Raynes; C T Yuen; T Feizi
Journal:  EMBO J       Date:  1992-03       Impact factor: 11.598

Review 4.  An overview on human serum lectins.

Authors:  S Beulaja Manikandan; R Manikandan; M Arumugam; P Mullainadhan
Journal:  Heliyon       Date:  2020-08-27
  4 in total

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