Casabo Guelfi, Lucia; (1992) Regulation of surface expression of the T lymphocyte differentiation antigen, CD8. Doctoral thesis (Ph.D), UCL (University College London).

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Abstract

The murine T lymphocyte glycoprotein CDS is a disulphide bonded heterodimer, composed of αβ or α'β chains, which plays a critical role in regulating the antigen responses of class I MHC-restricted T cells. CDS must interact not only with its ligand, class I MHC, on antigen-expressing target cells, but also with other proteins on the surface of the T ceil itself, such as the antigen-specific T cell receptor. In the present study two additional molecules, of 26 kD and 29 kD molecular weight, associated with the CDS complex have been identified and characterised. The 26 kD molecule is a novel polypeptide preferentially associated with the "immature" forms of CDS (α'β and β alone) and is only found within the cell. The data presented suggest that the 26 kD molecular weight protein may be involved in the developmentally regulated transport of CD8. The second molecule, of 29 kD molecular weight, is found on the cell surface of mature and immature T cells. This molecule appears to be another form of the CD8β polypeptide, with the major difference being the presence of variable amounts of sialic acid. The extent of this sialylation correlates not only with the differentiation status of the T cell but also with its state of activation. The changes in levels of sialic acid may have a significant influence on how CD8 interacts with other molecules. This is the first clear indication of a possible role for the CD8β chain, as previous evidence of CD8 function has been correlated exclusively with the CD8α chain.

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