Motojima K, Goto S
Department of Biochemistry, School of Pharmaceutical Sciences, Toho University, Chiba, Japan.
FEBS Lett. 1993 Mar 15;319(1-2):75-9. doi: 10.1016/0014-5793(93)80040-2.
A novel protein kinase is induced in rat liver plasma membrane by the administration of peroxisome proliferators. A 36 kDa protein (P36) on the membrane was rapidly phosphorylated in vitro by the kinase and the phosphorylated amino acid was identified as phosphohistidine. Histidine phosphorylation of P36 was activated in vitro by recombinant Ras protein and GTP; both decreased Michaelis constant (Km) for ATP from 1.25 to 0.25 microM. The novel histidine kinase, products of which have been overlooked due to their acid lability, may participate in cellular signaling and peroxisome proliferators may perturb the pathway.
过氧化物酶体增殖剂给药可诱导大鼠肝细胞膜产生一种新型蛋白激酶。膜上的一种36 kDa蛋白(P36)在体外被该激酶迅速磷酸化,磷酸化氨基酸被鉴定为磷酸组氨酸。P36的组氨酸磷酸化在体外被重组Ras蛋白和GTP激活;两者均使ATP的米氏常数(Km)从1.25 μM降至0.25 μM。这种新型组氨酸激酶的产物因其酸不稳定性而被忽视,可能参与细胞信号传导,而过氧化物酶体增殖剂可能会干扰该途径。