2024-03-29T08:10:46Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/237962018-10-03T09:40:39Zcom_10261_22com_10261_1col_10261_275
00925njm 22002777a 4500
dc
Ávila, Matías A.
author
Clemente, Rosa
author
Varela-Nieto, Isabel
author
1992-03-15
Glycosyl-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.
Biochemical Journal 282(Pt. 3): 681-686 (1992)
0264-6021
http://hdl.handle.net/10261/23796
A phosphatidylinositol-linkage-deficient T-cell mutant contains insulin-sensitive glycosyl-phosphatidylinositol