Sialophorin, a surface sialoglycoprotein defective in the Wiskott- Aldrich syndrome, is involved in human T lymphocyte proliferation

doi:10.1084/jem.165.5.1383

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Sialophorin, a surface sialoglycoprotein defective in the Wiskott- Aldrich syndrome, is involved in human T lymphocyte proliferation

SJ Mentzer, E Remold-O'Donnell, MA Crimmins, BE Bierer, FS Rosen and SJ Burakoff

The mAb L10 was used to determine the distribution and the function of sialophorin, the heavily glycosylated surface molecule that is deficient/defective in lymphocytes of patients with the X-linked immunodeficiency Wiskott-Aldrich syndrome. Dual-parameter FACS analysis indicated that sialophorin is expressed on CD4+ and CD8+ lymphocytes, on a subpopulation of peripheral blood B lymphocytes, on all thymocytes, and on a subpopulation of bone marrow cells. Functional studies demonstrated that L10 mAb stimulates the proliferation of peripheral blood T lymphocytes as measured by stimulation of [3H]thymidine incorporation. The time course and magnitude of increased [3H]thymidine incorporation by T lymphocytes in response to L10 mAb paralleled that induced by anti-CD3 mAb. Effective stimulation was dependent on the presence of monocytes and the Fc portion of L10 mAb. Stimulation of lymphocytes by L10, like stimulation by anti-CD3 mAb, involves increased expression of 4F2, HLA-DR, and IL-2-R. These observations suggest that sialophorin functions in T cell activation.
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Sperling, A. I., Sedy, J. R., Manjunath, N., Kupfer, A., Ardman, B., Burkhardt, J. K. (1998). Cutting Edge: TCR Signaling Induces Selective Exclusion of CD43 from the T Cell-Antigen-Presenting Cell Contact Site. J. Immunol. 161: 6459-6462 [Abstract] [Full Text]
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