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J Biol Chem, Vol. 274, Issue 24, 16917-16922, June 11, 1999

Calreticulin Is Expressed on the Cell Surface of Activated Human Peripheral Blood T Lymphocytes in Association with Major Histocompatibility Complex Class I Molecules

Fernando A. ArosaDagger , Orlando de JesusDagger , Graça PortoDagger parallel , Alexandre M. CarmoDagger , and Maria de SousaDagger

Dagger  Laboratory of Molecular Immunology, Institute for Molecular and Cell Biology, University of Porto, 4150 Porto and parallel  Department of Hematology, Santo António General Hospital, 4050 Porto, Portugal

Calreticulin is an endoplasmic reticulum resident molecule known to be involved in the folding and assembly of major histocompatibility complex (MHC) class I molecules. In the present study, expression of calreticulin was analyzed in human peripheral blood T lymphocytes. Pulse-chase experiments in [35S]methionine-labeled T cell blasts showed that calreticulin was associated with several proteins in the endoplasmic reticulum and suggested that it was expressed at the cell surface. Indeed, the 60-kDa calreticulin was labeled by cell surface biotinylation and precipitated from the surface of activated T cells together with a protein with an apparent molecular mass of 46 kDa. Cell surface expression of calreticulin by activated T lymphocytes was further confirmed by immunofluorescence and flow cytometry, studies that showed that both CD8+ and CD4+ T cells expressed calreticulin in the plasma membrane. Low amounts of cell surface calreticulin were detected in resting T lymphocytes. By sequential immunoprecipitation using the conformation independent monoclonal antibody HC-10, we provided evidence that the cell surface 46-kDa protein co-precipitated with calreticulin is unfolded MHC I. These results show for the first time that after T cell activation, significant amounts of calreticulin are expressed on the T cell surface, where they are found in physical association with a pool of beta 2-free MHC class I molecules.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.


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