The Thy-1 antigen exhibits rapid lateral diffusion in the plasma membrane of rodent lymphoid cells and fibroblasts.

Thy-1 is a plasma membrane protein, but its primary structure lacks the typical membrane-spanning sequence. Recent studies revealed that a glycophospholipid is covalently bound to the carboxyl terminus, suggesting that the protein is integrated into the plasma membrane by this lipid moiety. Lateral diffusion of Thy-1 was measured in mouse thymocytes, lymphoma cells, and fibroblasts by the fluorescence recovery after photobleaching technique. Thy-1 was labeled with rhodamine-conjugated anti-Thy-1 monoclonal antibodies. Diffusion coefficients of 2-4 X 10(-9) cm2/sec were obtained for the antigen-antibody complex in all the cell types. About 50% of the Thy-1 was mobile. The diffusion coefficient for the mobile fraction of Thy-1 is considerably larger than the diffusion coefficients of many other plasma membrane proteins. Rather, the diffusion coefficient of Thy-1 is similar to those of lipid analogs embedded in the same membrane, providing strong support for the suggested lipid anchoring of this antigen.