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J Thorac Imaging ; 2020 Feb 06.
Artigo em Inglês | MEDLINE | ID: mdl-32032250


OBJECTIVE: We sought to introduce a localization procedure (methylene blue-stained N-butyl cyanoacrylate and N-octyl cyanoacrylate glue) in localizing pulmonary small nodules and ground-glass opacities before thoracoscopic resection, and to evaluate its efficacy. METHODS: A total of 20 patients with pulmonary small nodules and/or ground-glass opacities, who underwent video-assisted thoracoscopic surgery from August 1, 2017 to March 1 2018, were included in the study. RESULTS: A total of 24 lesions in 20 patients underwent blue-stained glue localization. The success rate of localization was 100%, with a mean dose of 0.04±0.01 mL blue dye and 1 mL glue used for each lesion. The average time for the whole localization procedure was 15.4±6.3 minutes. All lesions were intraoperatively localized by visual inspection in combination with palpation. The complications related to the localization procedure included mild pneumothorax occurring in 9 patients and minor pulmonary hematoma in 4 patients. No pain or distress was reported. CONCLUSIONS: Blue-stained glue injection is technically feasible and safe to localize pulmonary small nodules and ground-glass opacities before thoracoscopic resection.

EBioMedicine ; 51: 102583, 2020 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-31901866


BACKGROUND: Heterogeneous nuclear ribonucleoprotein (hnRNP) A2/B1 is an important RNA-binding protein that affects the RNA processing, splicing, transport and stability of many genes. hnRNPA2/B1 is expressed during proliferation and metastasis of various cancer types and promotes such processes. However, the precise role and mechanism of hnRNPA2/B1 in breast cancer remain unclear. METHODS: The association of hnRNPA2/B1 with breast cancer metastasis was assessed using tissue chips, mouse models and publicly available data. The role and mechanism of hnRNPA2/B1 in breast cancer metastasis were studied in cell lines and mouse models. FINDINGS: In contrast to other cancer research findings, hnRNPA2/B1 expression was negatively correlated with breast cancer metastasis. hnRNPA2/B1 inhibited MDA-MB-231 triple-negative breast cancer (TNBC) cell metastasis in vitro and in vivo. hnRNPA2/B1 knockout activated ERK-MAPK/Twist and GR-beta/TCF4 pathways but inhibited STAT3 and WNT/TCF4 signalling pathways. Profilin 2 (PFN2) promoted breast cancer cell migration and invasion, whereas hnRNPA2/B1 bound directly to the UAGGG locus in the 3'-untranslated region of PFN2 mRNA and reduced the stability of PFN2 mRNA. INTERPRETATION: Our data supported the role of hnRNPA2/B1 in tumour metastasis risk and survival prediction in patients with breast cancer. The inhibitory role of hnRNPA2/B1 in metastasis was a balance of downstream multiple genes and signalling pathways. PFN2 downregulation by hnRNPA2/B1 might partly explain the inhibitory mechanism of hnRNPA2/B1 in breast cancer metastasis. Therefore, hnRNPA2/B1 might be used as a new prognostic biomarker and valuable molecular target for breast cancer treatments.

J Cell Biochem ; 118(12): 4697-4707, 2017 12.
Artigo em Inglês | MEDLINE | ID: mdl-28513872


Reactive oxygen species (ROS) play both deleterious and beneficial roles in cancer cells. Nucleophosmin (NPM) is heavily implicated in cancers of diverse origins, being its gene over-expression in solid tumors or frequent mutations in hematological malignancies. However, the role and regulatory mechanism of NPM in oxidative stress are unclear. Here, we found that NPM regulated the expression of peroxiredoxin 6 (PRDX6), a member of thiol-specific antioxidant protein family, consequently affected the level and distribution of ROS. Our data indicated that NPM knockdown caused the increase of ROS and its relocation from cytoplasm to nucleoplasm. In contrast, overexpression or cytoplasmic localization of NPM upregulated PRDX6, and decreased ROS. In addition, NPM knockdown decreased peroxiredoxin family proteins, including PRDX1, PRDX4, and PRDX6. Co-immunoprecipitation further confirmed the interaction between PRDX6 and NPM. Moreover, NSC348884, an inhibitor specifically targeting NPM oligomerization, decreased PRDX6 and significantly upregulated ROS. These observations demonstrated that the expression and localization of NPM affected the homeostatic balance of oxidative stress in tumor cells via PRDX6 protein. The regulation axis of NPM/PRDX/ROS may provide a novel therapeutic target for cancer treatment. J. Cell. Biochem. 118: 4697-4707, 2017. © 2017 Wiley Periodicals, Inc.

Antioxidantes/metabolismo , Proteínas de Neoplasias/metabolismo , Neoplasias/metabolismo , Proteínas Nucleares/metabolismo , Estresse Oxidativo , Peroxirredoxina VI/metabolismo , Espécies Reativas de Oxigênio/metabolismo , Linhagem Celular Tumoral , Humanos , Indóis/farmacologia , Proteínas de Neoplasias/antagonistas & inibidores , Proteínas de Neoplasias/genética , Neoplasias/tratamento farmacológico , Neoplasias/genética , Neoplasias/patologia , Proteínas Nucleares/genética , Peroxirredoxina VI/antagonistas & inibidores , Peroxirredoxina VI/genética
Dalton Trans ; 39(39): 9321-8, 2010 Oct 21.
Artigo em Inglês | MEDLINE | ID: mdl-20697610


A series of Pt(ii) complexes containing silole-based ligands with diphenylphosphino groups terminally bound to a conjugated organic linker unit coordinated to the silole ring in the 2- or 2,5-positions, 1,1-dimethyl-2-(5'-diphenylphosphino-2'-thienyl)-3,4-diphenylsilole (4), 1,1-dimethyl-2,5-bis(5'-diphenylphosphino-2'-thienyl)-3,4-diphenylsilole (5), and 1,1-dimethyl-2,5-bis(4'-diphenylphosphinophenyl)-3,4-diphenylsilole (8), have been prepared from (cod)PtX(2) (X = Cl, Me, C(2)Ph) precursors. Mononuclear, cis-P(2)PtX(2) (P = 4) complexes 6-7 were produced from silole 4 whereas dinuclear macrocyclic, cis-cis-X(2)Pt(P-P)(2)PtX(2) (P-P = 5 or 8) complexes 9-13 were produced from siloles 5 and 8. The solid state structure of the dinuclear complex 13 obtained from reaction of (cod)Pt(C(2)Ph)(2) with silole 8, was confirmed by X-ray crystallography. The optical properties of the siloles and the platinum complexes were studied by UV-vis and fluorescence spectroscopy in solution and were found to exhibit long wavelength absorption and emission bands attributed to the π-π* transitions of the silole core.

Inorg Chem ; 46(14): 5651-64, 2007 Jul 09.
Artigo em Inglês | MEDLINE | ID: mdl-17511449


Preparation and characterization of a series of rodlike binuclear ruthenium polyynediyl complexes capped with redox-active organometallic fragments [(bph)(PPh3)2Ru]+ (bph=N-(benzoyl)-N'-(picolinylidene)-hydrazine) or [(Phtpy)(PPh3)2Ru]2+ (Phtpy=4'-phenyl-2,2':6',2' '-terpyridine) have been carried out. The length of the molecular rods is extended by successive insertion of 2,5-thiophene or 1,4-phenylene spacers in the bridging ligands. Oxidation of thiophene-containing Ru2II,II complexes induces isolation of stable Ru2II,III or Ru2III,III species. Electrochemical and UV-vis-NIR spectral studies demonstrate that the polyynediyl bridges with 2,5-thiophene units are more favorable for metal-metal charge transfer compared with those containing the same number of 1,4-phenylene units. Successive increase of thiophene spacers in mixed-valence complexes {RuII}-CC(C4H2S)mCC-{RuIII} (m=1, 2, 3) induced a smooth transition from almost electronic delocalization (m=1) to localization (m=3). For binuclear ruthenium complexes with intramolecular electron transfer transmitted across nine Ru-C and C-C bonds, electronic conveying capability follows {Ru}-CC(CC)2CC-{Ru}>{Ru}-CC(C4H2S)CC-{Ru}>{Ru}-CC(C6H4)CC-{Ru}>{Ru}-CC(CH=CH)2CC-{Ru}. It is revealed that molecular wires capped with electron-rich (bph)(PPh3)2Ru endgroups are much more favorable for electronic communication than the corresponding electron-deficient (Phtpy)(PPh3)2Ru-containing counterparts. The intermetallic electronic communication is fine-tuned by modification of both the bridging spacers and the ancillary ligands.

Inorg Chem ; 43(4): 1481-90, 2004 Feb 23.
Artigo em Inglês | MEDLINE | ID: mdl-14966986


Reactions of oxo-centered triruthenium acetate complexes [Ru3O(OAc)6(py)2(CH3OH)](PF6) (py = pyridine, OAc = CH3COO-) (1) with nearly equimolar amounts of dppa [bis(diphenylphosphino)acetylene] or dppen [trans-1,2-bis(diphenylphosphino)ethylene] gave [Ru3O(OAc)6(py)2(L)](PF6) (L = dppa, 2; dppen, 3). With 2.4 equiv of 1, the reactions provided diphosphine-linked triruthenium dimers, [[Ru3O(OAc)6(py)2]2(L)](PF6)2 (L = dppa, 4; L = dppen, 5), respectively. Similarly, the reactions of [Ru3O(OAc)6(L')2(MeOH)]+ [L' = dmap (4-(dimethylamino)pyridine), 1a; L' = abco (1-azabicyclo[2.2.2]octane), 1b] with dppen gave dppen-linked dimers, [[Ru3O(OAc)6(dmap)2]2(dppen)](SbF6)2 (6) and [[Ru3O(OAc)6(abco)2]2(dppen)](BF4)2 (7), respectively. The chemical reduction of 2, 4, and 5 by hydrazine afforded one- or two-electron-reduced, neutral products, Ru3O(OAc)6(py)2(dppa) (2a), [Ru3O(OAc)6(py)2]2(dppa) (4a), and [Ru3O(OAc)6(py)2]2(dppen) (5a), respectively. The complexes were characterized by elemental analyses, ES-MS, UV-vis, IR, and 31P NMR spectroscopies, and cyclic and differential-pulse voltammetries. The molecular structures of compounds 2, 4, 5, 5a, 6, and 7 were determined by single-crystal X-ray diffraction. In 0.1 M (Bu4N)PF6-acetone, the monomers and dimers of triruthenium clusters show reversible and multistep redox responses. The two triruthenium cluster centers in dimers undergo stepwise reductions and oxidations due to the identical redox processes of the individual Ru3O cluster cores, suggesting the presence of electronic communications between them through the conjugated diphosphine spacer. The redox wave splitting mediated by dppa containing an ethynyl group (C triple bond C) is found to be more extensive than that by dppen containing an ethenyl (C=C) one. It appears that the redox wave splitting is enhanced by the introduction of electron-donating substituents on the auxiliary pyridine rings.