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Concanavalin A-mediated binding and sphering of human red blood cells by homologous monocytes

Human red blood cells sensitized with concanavalin A became bound to homologous peripheral blood monocytes. Binding occured at a concentration of 10(5) molecules of tetrameric Con A per red blood cell (RBC) and increased with additional Con A. RBC binding began within 5 min and was maximal at 90 min...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1976
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2190474/
https://www.ncbi.nlm.nih.gov/pubmed/1003110
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description Human red blood cells sensitized with concanavalin A became bound to homologous peripheral blood monocytes. Binding occured at a concentration of 10(5) molecules of tetrameric Con A per red blood cell (RBC) and increased with additional Con A. RBC binding began within 5 min and was maximal at 90 min. Phagocytosis of sensitized RBCs was minimal. RBC attachment was prevented by 0.01 M alpha-methyl-D- mannopyranoside, and, once the RBC-monocyte rosette was established, bound RBCs were largely removed with this specific saccharide inhibitor of Con A. RBCs attached to monocytes became spherocytic and osmotically fragile. The recognition of concanavalin A (Con A)-coated RBCs was not mediated through the monocyte IgG-Fc receptor. These studies demonstrate that, like IgG and C3b, Con A is capable of mediating the binding of human RBCs to human monocytes. Red cells so bound are damaged at the monocyte surface.
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spelling pubmed-21904742008-04-17 Concanavalin A-mediated binding and sphering of human red blood cells by homologous monocytes J Exp Med Articles Human red blood cells sensitized with concanavalin A became bound to homologous peripheral blood monocytes. Binding occured at a concentration of 10(5) molecules of tetrameric Con A per red blood cell (RBC) and increased with additional Con A. RBC binding began within 5 min and was maximal at 90 min. Phagocytosis of sensitized RBCs was minimal. RBC attachment was prevented by 0.01 M alpha-methyl-D- mannopyranoside, and, once the RBC-monocyte rosette was established, bound RBCs were largely removed with this specific saccharide inhibitor of Con A. RBCs attached to monocytes became spherocytic and osmotically fragile. The recognition of concanavalin A (Con A)-coated RBCs was not mediated through the monocyte IgG-Fc receptor. These studies demonstrate that, like IgG and C3b, Con A is capable of mediating the binding of human RBCs to human monocytes. Red cells so bound are damaged at the monocyte surface. The Rockefeller University Press 1976-12-01 /pmc/articles/PMC2190474/ /pubmed/1003110 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Concanavalin A-mediated binding and sphering of human red blood cells by homologous monocytes
title Concanavalin A-mediated binding and sphering of human red blood cells by homologous monocytes
title_full Concanavalin A-mediated binding and sphering of human red blood cells by homologous monocytes
title_fullStr Concanavalin A-mediated binding and sphering of human red blood cells by homologous monocytes
title_full_unstemmed Concanavalin A-mediated binding and sphering of human red blood cells by homologous monocytes
title_short Concanavalin A-mediated binding and sphering of human red blood cells by homologous monocytes
title_sort concanavalin a-mediated binding and sphering of human red blood cells by homologous monocytes
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2190474/
https://www.ncbi.nlm.nih.gov/pubmed/1003110