Divecha N, Rhee S G, Letcher A J, Irvine R F
Department of Biochemistry, AFRC Institute of Animal Physiology and Genetics Research, Cambridge, U.K.
Biochem J. 1993 Feb 1;289 ( Pt 3)(Pt 3):617-20. doi: 10.1042/bj2890617.
The presence of phosphoinositide-mobilizing enzymes has been investigated in purified rat liver nuclei by radiolabelling and by probing with antibodies. A Ca(2+)-activated phosphoinositidase C (PIC) is present and was shown immunologically to be the beta 1 isoform. No gamma- or delta-PIC was found. However, only 5% of the total beta 1-PIC isoform is nuclear, with the majority being cytosolic. G alpha q and G alpha 11, the suggested physiological activators of beta 1-PIC, were not present. A PtdIns4P 5-kinase is also present, which immunologically is shown to be the C isoform. All of these nuclear inositide enzymes still remained after the removal of the nuclear envelope with Triton X-100, consistent with the concept of an intranuclear inositide cycle [Divecha, Banfic and Irvine (1991) EMBO. J. 10, 3207-3214].
通过放射性标记和抗体检测,对纯化的大鼠肝细胞核中磷酸肌醇动员酶的存在情况进行了研究。发现存在一种钙激活的磷脂酶C(PIC),免疫分析表明其为β1亚型。未发现γ-或δ-PIC。然而,β1-PIC亚型总量中只有5%位于细胞核内,大部分位于细胞质中。β1-PIC的假定生理激活剂Gαq和Gα11并不存在。还存在一种磷脂酰肌醇-4-磷酸5-激酶,免疫分析表明其为C亚型。在用Triton X-100去除核膜后,所有这些核内肌醇酶仍然存在,这与核内肌醇循环的概念一致[迪韦查、班菲克和欧文(1991年)《欧洲分子生物学组织杂志》10,3207 - 3214]。