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Protein kinase CK2 phosphorylates and interacts with deoxyhypusine synthase in HeLa cells
KeeRyeonKang,SooIlChung 생화학분자생물학회 2003 Experimental and molecular medicine Vol.35 No.6
Deoxyhypusine is a modified lysine and formed postranslationaly to be the eukaryotic initiation factor eIF5A by deoxyhypusine synthase, employ-ing spermidine as butylamine donor. Subsequent hydroxylation of this deoxyhypusine-containing in-termediate completes the maturation of eIF5A. The previous report showed that deoxyhypusine synth-ase was phosphorylated by PKC in vivo and the association of deoxyhypusine synthase with PKC in CHO cels was PMA-, and Ca2+/phospholipid-de-pendent. We have extended study on the phos-phorylation of deoxyhypusine synthase by protein kinase CK2 in order to define its role on the re-gulation of eIF5A in the cell. The results showed that deoxyhypusine synthase was phosphorylated by CK2 in vivo as wel as in vitro. Endogenous CK2 in HeLa cells and the cell lysate was able to phosphorylate deoxyhypusine synthase and this modification is enhanced or decreased by the adi-tion of CK2 efectors such as polylysine, heparin, and poly(Glu, Tyr) 4:1. Phosphoamino acid analy-sis of this enzyme revealed that deoxyhypusine synthase is mainly phosphorylated on threonine residue and less intensely on serine. These results suggest that phosphorylation of deoxyhypusine synthase is CK2-dependent celular event as wel as PKC-mediated effect. However, there were no observable changes in enzyme activity betwen the phosphorylated and unphosphorylated forms of deoxyhypusine synthase. Taken together, be-sides its established function in hypusine modifi-synthase and its phosphorylation modification may have other independent celular functions because of versatile roles of deoxyhypusine synthase.
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김광세,Yong-KilHong,YoonLee,Joo-YoungShin,Soo-IkChang,SooIlChung,YoungAeJoe 생화학분자생물학회 2003 Experimental and molecular medicine Vol.35 No.6
The serine protease urokinase-type plasminogen activator (uPA) is im plicated in pericellular proteolysis in a variety of physiological and pathological processes including angiogenesis and tumor metastasis. The kringle domain of uPA (UK1) has proven to be an anti-angiogenic molecule with unknown mechanism and amino terminal fragment of uPA (u-ATF) with additional growth factor-like domain can be used for blocking interaction of uPA and uPA receptor. Here, we compared anti-angiogenic activities of these two molecules in vitro and in vivo. The recombinant u-ATF from E. coli and refolded in vitro was found to bind to uPAR with high affinity, whereas E. coli-derived UK1 showed no binding by Biacore analysis. In contrast to UK1 having potent inhibitory effect, u-ATF exhibited low inhibitory effect on bovine capillary endothelial cell growth (ED50>320 nM). Furthermore, u-ATF inhibition of VEGF-induced migration of human umbilical vein endothelial cell was far less sensitive (IC50 = 600 nM) than those observed with UK1, and angiogenesis inhibition was marginal in chorioallantoic membrane. These results suggest that kringle domain alone is sufficient for potent antiangiogenic activity and additional growth factor-like domain diverts this molecule in undergoing different mechanism such as inhibition of uPA/uPAR interaction rather than undergoing distinct antiangiogenic mechanism driven by kringle domain.
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