Expression of nuclear factor-κB in hepatocellular carcinoma and its relation with the X protein of hepatitis B virus. World J Gastroenterol, 2001;7(3):340-344 Abstract AIM In this study we investigated the relationship of the X protein of HBV and nuclear factor-κ κ κ κ κB (NF-κ κ κ κ κB) and the expression of NF-κ κ κ κ κB in human hepatocellular carcinoma tissues. METHODS Immunohistochemistry SP method was used to detect the expression of NF-κ κ κ κ κB and the X protein of HBV in human hepatocellular carcinoma tissues of 52 cases. Gene transfection mediated by lipofectamine was used to transfect the eukaryotic expression vector pCDNA3-1-HBX of HBV x gene into human hepatocellular carcinoma cell line HCC-9204 and NF-κ κ κ κ κB was detected. RESULTS NF-κ κ κ κ κB was widely expressed in human hepatocellular carcinoma tissues in a total of 52 cases and its expression was related to the X protein of HBV. NF-κ κ κ κ κB was localized both in the cytoplasm and the nuclei of hepatocellular carcinoma cells in 11 cases which were positive for the X protein of HBV while in 41 cases negative for the X protein of HBV, NF-κ κ κ κ κB was only localized in the cytoplasm of hepatocellular carcinoma cells but translocated to the nuclei of hepatocellular carcinoma cells after the eukaryotic expression vector pCDNA3-1-HBX was transfected into HCC-9204 cells. CONCLUSION This study strongly suggests that the nuclear factor NF-κ κ κ κ κB is widely expressed in hepatocellular carcinoma tissues in different styles according to the expression of the X protein of HBV. NF-κ κ κ κ κB is abnormally activated in hepatocellular carcinoma, which is probably related to the X protein of HBV. The X protein of HBV can activate NF-κ κ κ κ κB to translocate into nuclei of hepatocellular carcinoma cells.
Three new iso‐structural ammonium metal formates of [dmpnH2][M2(HCOO)6], in which dmpnH22+=N,N′‐dimethyl‐1,3‐propylenediammoium and M=divalent Co, Zn and Mg ions, are reported. They possess niccolite metal formate frameworks with long‐shaped cavities for the accommodation of dmpnH22+ cations. The three materials display reversible phase transitions of similar mechanism from ordered, antipolar or antiferroelectric, low‐temperature phases in space group C2/c, to disordered, paraelectric, high‐temperature phases in space group Ptrue3‾ 1c, with quite high critical temperatures of 366, 370, and 334 K for Co, Zn, and Mg members, respectively. On warming, the dmpnH22+ cation experiences an ordered state with gradual increase of the local vibration motions of the central CH2 and terminal CH3 groups, a partially disordered state with gradually enhanced flipping motion between the major and minor orientations, and finally a twisting or rotating motion after the phase transition, accompanied by prominent anisotropic thermal expansions and dielectric anomalies/relaxations. The phase transition characters and relevant properties also exhibit a subtle metal‐dependence. The Co member shows spin‐canted antiferromagnetism below the Néel temperature of 16.1 K, with unusual large spontaneous magnetization and coercive field.
A wide range of pathologies have been targeted with bimodular aptamers that contain both G-quadruplex (G4) and duplex motifs, while the structures and functions are poorly understood. G4-selective fluorescent dyes have served as facile tools to probe G4s, but not for bimodular aptamers, yet. Here, taking the 29-mer thrombin binding aptamer (TBA29) as an example, we demonstrated that 3,6-dimethyl-2-(4-dimethylaminophenyl)-benzothiazolium (ThT) was the most effective dye compared to NMM and PPIX in recognizing TBA29. Binding studies indicate that ThT recognized TBA29 via distinct buffer-dependent mechanisms. Specifically, ThT induced the formation of a bimolecular parallel G4 in cation-deficient buffer, showing 341-fold fluorescent enhancement. The competitive binding of thrombin disrupted the complex, leading to the monotonic fluorescence decrease. A similar mechanism was previously reported for the interaction between ThT and the 15-mer thrombin binding aptamer (TBA15). However, TBA29 bound with ThT in a more favorable state than TBA15, showing hyperchromic effects and two times stronger fluorescence enhancement. Differently, ThT bound with antiparallel TBA29/TBA15 in an intercalating/groove binding mode in 100 mM KCl, generating 181/28-fold fluorescence enhancement, respectively. These results revealed that ThT recognized both parallel and antiparallel G4s of TBA29 more efficiently than it recognized TBA15. The duplex structure of TBA29 may play an important role in its interaction with ThT. Our study broadens the application of ThT in screening G4 to bimodular aptamers and provides some insights into the structures of TBA29, along with the interaction between ThT and TBA29. Our study also is useful for the development of structure-switching-based biosensors using bimodular aptamers. Graphical abstract The buffer-dependent binding mechanisms of ThT with TBA29, and the competitive (top)/noncompetitive (bottom) binding of thrombin with TBA29-ThT complex.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
hi@scite.ai
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.