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Volume 272, Number 35, Issue of August 29, 1997 pp. 21735-21744
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

TLiSA1 (PTA1) Activation Antigen Implicated in T Cell Differentiation and Platelet Activation Is a Member of the Immunoglobulin Superfamily Exhibiting Distinctive Regulation of Expression

(Received for publication, September 30, 1996, and in revised form, June 9, 1997)

Paul D. Sherrington , Judith L. Scott ^¶ , Boquan Jin ^¶ , David Simmons ^** , Douglas J. Dorahy ^¶ , Jennifer Lloyd , Joan H. Brien ^¶ , Ruedi H. Aebersold , Janet Adamson , Mirko Zuzel and Gordon F. Burns ^¶

From the  Department of Haematology, University of Liverpool, Liverpool L69 3BX, United Kingdom, the ^¶ Cancer Research Unit, The University of Newcastle, New South Wales 2300, Australia, the ^** Institute of Molecular Medicine, University of Oxford, Oxford OX3 9DU, United Kingdom, and the  Biomedical Research Centre, Vancouver, British Columbia V6T1W5, Canada

T lineage-specific activation antigen 1 (TLiSA1) antigen was initially described as a T lineage-specific activation antigen involved in the differentiation of human cytotoxic T cells. Subsequently, the antigen was identified on platelets and was shown to be involved in platelet activation, hence it was renamed platelet and T cell antigen 1 (PTA1), although identity between the two antigens was not established. In the present study we have cloned the cDNA encoding TLiSA1 from Jurkat cells and show it to be a novel member of the immunoglobulin superfamily with the unusual structure of two V domains only. Identity between TLiSA1 and platelet PTA1 is established by immunological criteria, by internal peptide sequences obtained from the purified platelet glycoprotein and by sequencing the platelet transcript after reverse transcriptase-polymerase chain reaction. In Jurkat cells, TLiSA1/PTA1 mRNA and surface protein expression is greatly stimulated by treatment of the cells with phorbol ester, but the T cell proliferative signal of phorbol ester and ionophore combined greatly reduces or abrogates this response, and this suppressive effect of the ionophore is not reversed by incorporating FK506 to inhibit calcineurin. Together with the known signaling role of PTA1, these data substantiate the notion that this molecule is implicated in T cell differentiation, perhaps by engagement of an adhesive ligand.

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