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Título

A phosphatidylinositol-linkage-deficient T-cell mutant contains insulin-sensitive glycosyl-phosphatidylinositol

AutorAvila, Matías A.; Clemente, Rosa; Varela-Nieto, Isabel
Fecha de publicación15-mar-1992
EditorPortland Press
CitaciónBiochemical Journal 282(Pt. 3): 681-686 (1992)
ResumenGlycosyl-phosphatidylinositol molecules, acting as both signal transduction elements and membrane protein anchors, have been proposed to play a role during T-cell activation. The MVB2 cell line is a mutant, derived from the wild-type T-T hybrid YH.16.33, which has a defect in the biosynthesis of PtdIns-protein linkages. As a consequence, MVB2 mutants are defective in activation through the T-cell receptor. Despite the lack of glycosyl-PtdIns anchors in the mutant MVB2 cells, a comparison of the levels and structural features of the insulin-sensitive glycosyl-PtdIns between the MVB2 and YH.16.33 lineages indicates that both cell lines are identical in this respect. The time course for insulin-responsiveness coincides in both cell lines, with maximal hydrolysis 30 s after insulin addition. The ultimate localization of insulin-regulated glycosyl-PtdIns at the outer surface of the cell membrane is also similar. These data indicate that the glycosyl-PtdIns whose hydrolysis is regulated by insulin is not anchoring proteins at the cell surface of T-lymphocytes.
Descripción6 pages, 3 figures, 1 table.
Versión del editorhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC1130841/pdf/biochemj00139-0067.pdf
URIhttp://hdl.handle.net/10261/23796
ISSN0264-6021
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