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RELEASE OF AN Fc‐BINDING COMPONENT FROM NORMAL OR ACTIVATED HUMAN LYMPHOCYTES
Author(s) -
Caraux Jean,
Serrou Bernard
Publication year - 1979
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1979.tb47102.x
Subject(s) - cytolysis , sepharose , antibody , chemistry , receptor , lymphocyte , cytotoxicity , antigen , microbiology and biotechnology , fc receptor , rosette formation , biochemistry , immunology , in vitro , biology , enzyme
Under cultivation at 37 degrees C in the presence or absence of Con A, human lymphocytes release a soluble component able to inhibit antibody-dependent cell-mediated cytotoxicity, EAG rosette formation and also able to hemagglutinate erythrocytes sensitized with a subagglutinating dose of IgG. These activities are selectively removed on Sepharose-aggregated-IgG or Sepharose-antigen-antibody complex, but not on Sepharose-(Fab') 2, suggesting the involvement of an Fc-binding component. These activities are not reversible by alpha-methyl-mannoside. As the appearance, in the supernatants of lymphocyte cultures, of such capacity to interact with the Fc portion of IgG is paralleled by a decrease in the capacity of such lymphocytes to form EAG rosettes or mediate antibody-dependent cell-mediated cytolysis, the isolated component might represent a soluble form of Fc receptor shed from the surface of human lymphocytes.