Faculty Collaboration Database

Further studies of the human platelet receptor for quinine- and quinine-dependent antibodies. J Immunol 1981 Feb;126(2):398-402

Date

02/01/1981

Pubmed ID

7451983

Scopus ID

2-s2.0-0019432411 (requires institutional sign-in at Scopus site)   65 Citations

Abstract

Previous studies have shown that the receptor for quinine- and quinidine-dependent antibodies is not expressed on the surface of platelets from patients with the Bernard-Soulier (B-S) syndrome. We now report data to suggest that these platelets lack the receptor for these antibodies. Since B-S platelets are also missing 2 related components of the GP I complex, GP lb and glycocalicin, our findings suggest that the receptor for quinine- and quinidine-dependent antibodies may be associated with this complex on normal platelets. An antibody previously shown to be directed against a surface antigen that migrated in the GP I position on SDS-polyacrylamide gel electrophoresis specifically blocked the reaction of the receptor with quinine- or quinidine-dependent antibodies. Purified glycocalicin, however, lacked detectable receptor activity. In contrast, a mixture of GP lb and a putative structural analog of this glycoprotein (Mr 210,000) eluted from wheat germ affinity columns after chromatography of Triton X soluble preparations of platelets or membranes was shown to contain at least 80% of the total receptor activity. Our results strongly suggest that the receptor is associated with GP lb and/or its high m.w. structural analog(s).

Author List

Kunicki TJ, Russell N, Nurden AT, Aster RH, Caen JP

Author

Richard H. Aster MD Professor in the Medicine department at Medical College of Wisconsin

MESH terms used to index this publication - Major topics in bold

Antibodies
Antibody Specificity
Blood Platelet Disorders
Blood Platelets
Cell Membrane
Chromatography, Affinity
Glycoproteins
Humans
Quinidine
Quinine
Receptors, Drug
Solubility