Composition of TCR-CD3 complex in human intestinal intraepithelial lymphocytes: lack of Fc{varepsilon}Rl{gamma} chain |
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Authors: | Balk, Steven P. Polischuk, John E. Probert, Christopher Stevens, Christopher Ebert, Ellen She, Jian Terhorst, Cox Blumberg, Richard S. |
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Affiliation: | Hematology/Oncology Division, Beth Israel Hospital, Harvard Medical School Boston, MA 02215, USA 1 Gastroenterology Division, Brigham and Women's Hospital, Harvard Medical School Boston, MA 02115, USA 2 Gastroenterology Division, Beth Israel Hospital, Harvard Medical School Boston, MA 02215, USA 3 Gastroenterology Division, Robert Wood Johnson Medical School New Brunswick, NJ 08903, USA 4 Division of Immunology, Beth Israel Hospital and Harvard Medical School Boston, MA 02215, USA |
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Abstract: | Human intestinal intraepithelial lymphocytes (DEL) are a uniquepopulation of predominantly CD8ß+ TCRß+lymphocytes and, to a lesser extent, TCR+ lymphocytes that proliferatepoorly to anti-CD3 mitogenic signals but display significantcytolytic activity. Studies in mouse model systems have shownthat the chain of the high-CD3 affinity receptor for IgE (FcRl)may substitute for the chain in the TCR-CD3 complex of iIEL.This has suggested that the functional properties of these cellsmay be associated with an altered composition of the TCR-CD3complex. We therefore analyzed the TCR-CD3 complex of normalhuman iIEL. One-and two-dimensional non-reducing/reducing SDS-PAGEanalysis of CD3, CD3, CD3, and FcRr chain immunopreclpitatesof cell surface radiolabeled proteins with subunit-specificantibodies revealed a TCR-CD3 complex without associated FcRrchains. Thus, normal human NEL contain a TCR-CD3 complex thatconsists predominantly of , homodimers in association with theß TCR and CD3, and , similar to the majority of peripherallymphocytes. This indicates that the distinct properties ofhuman DEL are not associated with substitutions of the FcRlchain in the TCR-CD3 complex. |
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Keywords: | epithelium FcR proliferation |
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