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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1990-3-29
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pubmed:abstractText |
The Fc epsilon receptor II (Fc epsilon RII/CD23) has been proposed to have multiple functions as a membrane-bound or soluble molecule: a function in B cell growth and differentiation and a role in the effector phase of IgE-mediated immunity. We recently demonstrated the presence of two forms of Fc epsilon RII (Fc epsilon RIIa and Fc epsilon RIIb) whose structures differ only at their N-terminal cytoplasmic regions. The regulatory mechanisms of their expression strongly suggest that Fc epsilon RIIa and Fc epsilon RIIb function in B cells and in the effector cells of IgE-mediated immunity, respectively. To elucidate the function of soluble Fc epsilon RII/CD23 (sFc epsilon RII) the recombinant soluble molecule was produced. This recombinant receptor could competitively block the IgE binding of eosinophils, monocytes and even basophils and could inhibit the IgE-mediated function of effector cells such as monocytes. These findings suggested that sFc epsilon RII could competitively regulate the function of effector cells in IgE-mediated immunity and that the recombinant sFc epsilon RII could be applied clinically for the control of allergic reactions. The expression of Fc epsilon RII on Fc epsilon RII-negative B and T cell lines by cDNA transfection resulted in homocytic aggregation. The function of Fc epsilon RII on B cells as an adhesion molecule was also demonstrated.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
0300-5208
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
147
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
23-31; discussion 31-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading | |
pubmed:year |
1989
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pubmed:articleTitle |
Structure and function of Fc epsilon receptor II (Fc epsilon RII/CD23): a point of contact between the effector phase of allergy and B cell differentiation.
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pubmed:affiliation |
Institute for Molecular and Cellular Biology, Osaka University, Japan.
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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