Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin inhibits the proliferation of ARPE-19 cells

<p>Abstract</p> <p>Background</p> <p>The antiproliferative effect of the Hsp90 inhibitor 17-AAG (17-allylamino-17-demethoxygeldanamycin) on human retinal pigment epithelial cells is investigated.</p> <p>Methods</p> <p>MTT and flow cytometry were used to study the antiproliferative effects of the 17-AAG treatment of ARPE-19 cells. 2D gel electrophoresis (2-DE) and mass spectrometry were applied to detect the altered expression of proteins, which was verified by real-time PCR. Gene Ontology analysis and Ingenuity Pathway Analysis (IPA) were utilized to analyze the signaling pathways, cellular location, function, and network connections of the identified proteins. And SOD assay was employed to confirm the analysis.</p> <p>Results</p> <p>17-AAG suppressed the proliferation of ARPE-19 cells by inducing cell cycle arrest and apoptosis. Proteomic analysis revealed that the expression of 94 proteins was altered by a factor of more than 1.5 following exposure to 17-AAG. Of these 94, 87 proteins were identified. Real-time PCR results indicated that Hsp90 and Hsp70, which were not identified by proteomic analysis, were both upregulated upon 17-AAG treatment. IPA revealed that most of the proteins have functions that are related to oxidative stress, as verified by SOD assay, while canonical pathway analysis revealed glycolysis/gluconeogenesis.</p> <p>Conclusions</p> <p>17-AAG suppressed the proliferation of ARPE-19 cells by inducing cell cycle arrest and apoptosis, and possibly by oxidative stress.</p

Poly[[tetra­kis­(μ-2-anilinobenzoato-κ2 O:O′)tetra-μ1,1,1-azido-tetra-μ1,1-azido-octa­methano­lhexa­nickel(II)] methanol hexa­solvate]

The crystal structure of the title compound, [Ni6(C13H10NO2)4(N3)8(CH3OH)8]·6CH3OH, consists of a centrosymmetric hexa­nuclear [NiII 6(C13H10NO2)4(N3)8(CH3OH)8] mol­ecule and six methanol solvent mol­ecules. In the hexa­nuclear unit, the six octa­hedrally coordinated NiII atoms are linked by four μ1,1,1-azide and four μ1,1-azide bridges, forming a face-sharing Ni6N8 tetra­cubane-like unit with four missing corners. The NiII atoms are further bridged by four μ1,2-carboxalate groups. Neighbouring hexa­nuclear units are connected via N—H⋯O hydrogen-bonding inter­actions into a three-dimensional structure. Although the H atoms of the methanol OH groups could not be located, O⋯N/O contacts between 2.65 and 2.86 Å suggest that these mol­ecules participate in hydrogen bonding

Rapid and Unconditional Parametric Reset Protocol for Tunable Superconducting Qubits

Qubit initialization is a critical task in quantum computation and communication. Extensive efforts have been made to achieve this with high speed, efficiency and scalability. However, previous approaches have either been measurement-based and required fast feedback, suffered from crosstalk or required sophisticated calibration. Here, we report a fast and high-fidelity reset scheme, avoiding the issues above without any additional chip architecture. By modulating the flux through a transmon qubit, we realize a swap between the qubit and its readout resonator that suppresses the excited state population to 0.08% $\pm$ 0.08% within 34 ns (284 ns if photon depletion of the resonator is required). Furthermore, our approach (i) can achieve effective second excited state depletion, (ii) has negligible effects on neighbouring qubits, and (iii) offers a way to entangle the qubit with an itinerant single photon, useful in quantum communication applications.Comment: 38 pages, 15 figure

Angiotensin-Converting Enzyme-2 Overexpression Improves Left Ventricular Remodeling and Function in a Rat Model of Diabetic Cardiomyopathy

ObjectivesThe aim of this study was to test the hypothesis that angiotensin (Ang)-converting enzyme-2 (ACE2) overexpression may inhibit myocardial collagen accumulation and improve left ventricular (LV) remodeling and function in diabetic cardiomyopathy.BackgroundHyperglycemia activates the renin-Ang system, which promotes the accumulation of extracellular matrix and progression of cardiac remodeling and dysfunction.MethodsNinety male Wistar rats were divided randomly into treatment (n = 80) and control (n = 10) groups. Diabetes was induced in the treatment group by a single intraperitoneal injection of streptozotocin. Twelve weeks after streptozotocin injection, rats in the treatment group were further divided into adenovirus-ACE2, adenovirus–enhanced green fluorescent protein, losartan, and mock groups (n = 20 each). LV volume; LV systolic and diastolic function; extent of myocardial fibrosis; protein expression levels of ACE2, Ang-converting enzyme, and Ang-(1-7); and matrix metalloproteinase–2 activity were evaluated. Cardiac myocyte and fibroblast culture was performed to assess Ang-II and collagen protein expression before and after ACE2 gene transfection.ResultsFour weeks after ACE2 gene transfer, the adenovirus-ACE2 group showed increased ACE2 expression, matrix metalloproteinase–2 activity, and LV ejection fractions and decreased LV volumes, myocardial fibrosis, and ACE, Ang-II, and collagen expression in comparison with the adenovirus–enhanced green fluorescent protein and control groups. ACE2 was superior to losartan in improving LV remodeling and function and reducing collagen expression. The putative mechanisms may involve a shift in balance toward an inhibited fibroblast-myocyte cross-talk for collagen and transforming growth factor–beta production and enhanced collagen degradation by matrix metalloproteinase–2.ConclusionsACE2 inhibits myocardial collagen accumulation and improves LV remodeling and function in a rat model of diabetic cardiomyopathy. Thus, ACE2 provides a promising approach to the treatment of patients with diabetic cardiomyopathy

Feather mites of the genus Passeroptes Fain (Acariformes: Dermationidae) from passerines (Aves: Passeriformes) of China

Mu, Ning, Kuang, Xi-Jun, Liu, Huai, Wang, Zi-Ying (2015): Feather mites of the genus Passeroptes Fain (Acariformes: Dermationidae) from passerines (Aves: Passeriformes) of China. Zootaxa 3985 (1): 53-68, DOI: 10.11646/zootaxa.3985.1.