Abstract:
:RT6 is a glycosyl-phosphatidylinositol-linked surface molecule present on most mature rat T-cells. RT6+ T-cells can prevent the expression of autoimmune diabetes in the BB rat, but the mechanism is unknown. Because cross-linking of other glycosyl-phosphatidylinositol-linked T-cell proteins is known to activate T-cells, we investigated the signaling properties of RT6. Antibody cross-linking of RT6 enhanced expression of the alpha subunit of the interleukin-2 (IL-2) receptor and potentiated the proliferation of rat T-cells cultured in the presence of phorbol ester plus recombinant IL-2 (rIL-2) and/or rIL-4. RT6 was found to coimmunoprecipitate with five tyrosine phosphorylated proteins including p60fyn and p56lck, members of the src tyrosine kinase family. Pretreatment of T-cells with phorbol ester increased the phosphorylation of proteins that coimmunoprecipitated with RT6, altered the electrophoretic mobility of several of these coimmunoprecipitated phosphoproteins, and increased the amount of p60fyn and p56lck coimmunoprecipitated with RT6. These data indicate that RT6-mediated signaling events may prime T-cells to respond to exogenous cytokines, suggesting a possible mechanism by which surface RT6 may influence T-cell function.
journal_name
Diabetesjournal_title
Diabetesauthors
Rigby MR,Bortell R,Greiner DL,Czech MP,Klarlund JK,Mordes JP,Rossini AAdoi
10.2337/diab.45.10.1419subject
Has Abstractpub_date
1996-10-01 00:00:00pages
1419-26issue
10eissn
0012-1797issn
1939-327Xjournal_volume
45pub_type
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