Open AccessThe defect seen in the phosphatidylinositol hydrolysis pathway in HIV‐infected lymphocytes and lymphoblastoid cells is due to inhibition of the inositol 1,4,5‐trisphosphate 1,3,4,5‐tetrakisphosphate 5‐phosphomonoesterase
Author(s) -
NYE K. E.,
RILEY G. A.,
PINCHING A. J.
Publication year - 1992
Publication title -
clinical & experimental immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.329
H-Index - 135
eISSN - 1365-2249
pISSN - 0009-9104
DOI - 10.1111/j.1365-2249.1992.tb06883.x
Subject(s) - phosphatidylinositol , inositol , immunology , lymphoblast , human immunodeficiency virus (hiv) , inositol phosphate , biology , virology , biochemistry , cell culture , signal transduction , receptor , genetics
SUMMARY Lymphocytes infected in vivo with HIV or lymphoblastoid cells exposed in vitro to either HIV or its envelope glycoprotein (gp120) show a defect in inositol polyphosphate‐mediated signal transduction together with an associated abnormality in intracellular calcium regulation. The defect in patients reverses after treatment with the anti‐retroviral agent zidovudine (AZT). We present evidence that the defect is at the level of the lns (1,3,4,5)P 4 5‐phosphomonoesterase (PME) in these cells and that, though elevation of the intracellular ATP level partially down‐regulates the activity of this enzyme. such changes alone are unable to account for the complete inhibition seen in HIV‐infected cells.