Tokui T, Yamauchi T, Yano T, Nishi Y, Kusagawa M, Yatani R, Inagaki M
Laboratory of Experimental Radiology, Aichi Cancer Center Research Institute, Japan.
Biochem Biophys Res Commun. 1990 Jun 29;169(3):896-904. doi: 10.1016/0006-291x(90)91977-z.
We have investigated the actions of Ca2(+)-calmodulin (CaM)-dependent protein kinase II on various types of non-epithelial intermediate filament proteins, vimentin, desmin, glial fibrillary acidic protein (GFAP) and neurofilament triplet proteins. Most of these filament proteins could serve as substrates. The effects of phosphorylation on the filamentous structure of vimentin were investigated in sedimentation experiments and by using electron microscopy. The amount of unassembled vimentin increased linearly with increased phosphorylation. However, the extent of the effect of phosphorylation on the potential to polymerize was also affected by the MgCl2 concentration, under conditions for reassembly. The actions of Ca2(+)-CaM-dependent protein kinase II on non-epithelial intermediate filaments under physiological conditions are given attention.
我们研究了Ca2+ - 钙调蛋白（CaM）依赖性蛋白激酶II对各种非上皮中间丝蛋白、波形蛋白、结蛋白、胶质纤维酸性蛋白（GFAP）和神经丝三联体蛋白的作用。这些丝蛋白中的大多数都可以作为底物。通过沉降实验和电子显微镜研究了磷酸化对波形蛋白丝状结构的影响。未组装的波形蛋白量随磷酸化增加而线性增加。然而，在重新组装的条件下，磷酸化对聚合潜力的影响程度也受MgCl2浓度的影响。我们关注了Ca2+ - CaM依赖性蛋白激酶II在生理条件下对非上皮中间丝的作用。
