Clonospecific structural heterogeneity in the Thy-1 molecule from mouse T lymphocytes |
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Authors: | Suzanne Pont André Van Agthoven Philippe Naquet Anne Pierres Anne-Marie Schmitt-Verhulst Dr. Michel Pierres |
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Affiliation: | (1) Centre d'Immunologie INSERM-CNRS de Marseille-Luminy, Case 906, 13288 Marseille cédex 9, France |
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Abstract: | The Thy-1 molecule immunoprecipitated from detergent-solubilized, 125I-labeled cell-surface proteins was shown to be processed in two distinct ways by mouse T lymphocytes: one leading to the expression by thymocytes, concanavalin A-activated spleen blasts, and six of nine T-cell clones of a molecule of 25–28 kd, and another, observed in three other T-cell clones, leading to the expression at their surface of a so far undescribed low Mr (23 kd) form of Thy-1. The results of two-dimensional gel electrophoresis and neuraminidase, endoglycosidase H, and endoglycosidase F treatment revealed that the observed heterogeneity of Thy-1 molecules from peripheral cloned T cells was due to major differences in the maturation and sialylation of their N-linked complex-type oligosaccharide residues. It was also found that a given T-cell clone could express T200, LFA.1, and transferrin receptor molecules with a low or high Mr. Furthermore, and in contrast to previously reported results, this study revealed that the differences in cell-surface glycoprotein profiles could not be correlated with the Lyt-2,3/T4 phenotypes, the specificity for allo-H-2, allo-I-A, allo-I-E, or GAT + I-Ak determinants, nor with the cytolytic or helper/amplifier potential of the various T-cell clones examined. The possible implications of these findings are discussed. |
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