Poltronieri L, Melloni E, Rubini M, Selvatici R, Mazzilli C, Baricordi R, Gandini E
Istituto di Genetica Medica, Universita' degli Studi di Ferrara, Italy.
Biochem Biophys Res Commun. 1988 Oct 14;156(1):46-53. doi: 10.1016/s0006-291x(88)80803-9.
Cytoplasmic protein kinase C (PKC) has been studied in phytohemagglutinin (PHA) activated peripheral blood mononuclear cells (PBMC) and macrophage depleted E+ cell culture. Within 10' after contemporanous addition of PHA and anti HLA class I monoclonal antibody 01.65 (MoAb) PKC is depleted in both cell types. Enzyme activity recovers in the following hours however at 72 hours is at control values in E+ cultures while in PBMC cultures it is still depleted at 68% of the control. Anti HLA class I MoAb induced tritiated lymidine (3H-TdR) incorporation inhibition appears to be related to low levels of PKC activity.
已在植物血凝素(PHA)激活的外周血单个核细胞(PBMC)和巨噬细胞耗竭的E +细胞培养物中研究了细胞质蛋白激酶C(PKC)。在同时添加PHA和抗HLA I类单克隆抗体01.65(MoAb)后10分钟内,两种细胞类型中的PKC均被耗尽。然而,酶活性在接下来的几个小时内恢复,在E +培养物中72小时时达到对照值,而在PBMC培养物中,在72小时时仍以对照值的68%被耗尽。抗HLA I类MoAb诱导的氚化胸腺嘧啶核苷(3H-TdR)掺入抑制似乎与低水平的PKC活性有关。