McLeish K R, Lederer E D, Klein J B
Veterans Administration Medical Center, Louisville, KY.
Biochem Biophys Res Commun. 1993 Dec 15;197(2):763-70. doi: 10.1006/bbrc.1993.2544.
The role of isoprenylation in formyl peptide receptor-mediated G protein activation was studied using plasma membranes isolated from normal HL-60 granulocytes and from cells in which isoprenylation was inhibited with mevastatin. Plasma membrane expression of formyl peptide receptors and G protein beta subunits, but not alpha i2 and alpha i3, was significantly reduced by inhibition of isoprenylation. This reduced expression resulted in impaired basal and fMet-Leu-Phe-stimulated G protein activation.
利用从正常HL-60粒细胞以及用美伐他汀抑制异戊二烯化的细胞中分离得到的质膜,研究了异戊二烯化在甲酰肽受体介导的G蛋白激活中的作用。抑制异戊二烯化可显著降低甲酰肽受体和G蛋白β亚基的质膜表达,但对αi2和αi3无影响。这种表达降低导致基础和fMet-Leu-Phe刺激的G蛋白激活受损。