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Molecular basis for a polymorphism involving Fc receptor II on human monocytes.

M R Clark, S B Clarkson, P A Ory, N Stollman and I M Goldstein
J Immunol September 1, 1989, 143 (5) 1731-1734;
M R Clark
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S B Clarkson
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P A Ory
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N Stollman
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I M Goldstein
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Abstract

IgG Fc receptor II (Fc gamma RII) on human monocytes is polymorphic with respect to its appearance on gels after isoelectric focusing and with respect to its ability to mediate T lymphocyte proliferation induced by murine anti-CD3 mAb of the IgG1 isotype (i.e., its ability to bind murine IgG1). To determine the molecular basis for this polymorphism, we isolated total cellular RNA from PBMC of responders and nonresponders (defined by Leu-4-induced [3H] thymidine incorporation) and synthesized corresponding cDNA. Sequences encoding the extracellular domain of Fc gamma RII were then amplified using the Taq polymerase chain reaction. Amplified DNA fragments were cloned into pUC vectors, and sequenced. Analysis of clones from two nonresponders revealed a single base change (G for A) at position 519, which would result in the substitution of a histidine for an arginine at residue 133 in the mature Fc gamma RII protein. These findings suggest that the polymorphism involving human monocyte Fc gamma RII results from allelic variation of a single gene.

  • Copyright © 1989 by American Association of Immunologists

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The Journal of Immunology
Vol. 143, Issue 5
1 Sep 1989
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Molecular basis for a polymorphism involving Fc receptor II on human monocytes.
M R Clark, S B Clarkson, P A Ory, N Stollman, I M Goldstein
The Journal of Immunology September 1, 1989, 143 (5) 1731-1734;

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Molecular basis for a polymorphism involving Fc receptor II on human monocytes.
M R Clark, S B Clarkson, P A Ory, N Stollman, I M Goldstein
The Journal of Immunology September 1, 1989, 143 (5) 1731-1734;
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Print ISSN 0022-1767        Online ISSN 1550-6606