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Many proteins in living organisms are glycosylated. As their glycan patterns exhibit protein-, cell-, and tissue-specific heterogeneity, changes in the glycosylation levels could serve as useful indicators of various pathological and physiological states. Thus, the identification of glycoprotein biomarkers from specific changes in the glycan profiles of glycoproteins is a trending field. Lectin microarrays provide a new glycan analysis platform, which enables rapid and sensitive analysis of complex glycans without requiring the release of glycans from the protein. Recent developments in lectin microarray technology enable high-throughput analysis of glycans in complex biological samples. In this review, we will discuss the basic concepts and recent progress in lectin microarray technology, the application of lectin microarrays in biomarker discovery, and the challenges and future development of this technology. Given the tremendous technical advancements that have been made, lectin microarrays will become an indispensable tool for the discovery of glycoprotein biomarkers. © 2020 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.Thin coatings of Bi2O3 were deposited on glass substrates by ultrasonic spray coating of THF solutions of the molecular precursor [Bi38O45(OMc)24(DMSO)9] ⋅ 2DMSO ⋅ 7H2O (OMc=O2CC3H5) followed by hydrolysis and subsequent annealing. Depending on the synthetic protocol, the bismuth oxido cluster was transformed into either α- or β-Bi2O3. The as-synthesized Bi2O3 coatings were characterized by powder X-ray diffraction (PXRD), thickness measurements, diffuse reflectance UV-Vis spectroscopy (DRS), photoluminescence (PL) spectroscopy, Raman spectroscopy and scanning electron microscopy (SEM). The thin coatings (thickness 5-16 μm) were compared with regard to their performance in photocatalytic rhodamine B (RhB) decomposition under visible light irradiation. The β-Bi2O3 coatings, that showed the highest photocatalytic activity, were used for the photocatalytic decomposition of other pollutants such as triclosan and ethinyl estradiol. In addition, the interplay between the photooxidation that is induced by the excitation of the catalyst using visible light and the photosensitized decomposition pathway was studied by degradation experiments of aqueous rhodamine B solutions using β-Bi2O3 coatings. © 2020 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.The aim of the current study was to test the hypothesis that a functional polymorphism in the synaptosome associated protein 25 (SNAP25) gene could be associated with impulsivity scores in a sample of young Colombian subjects. Impulsivity has been postulated as an endophenotype for several psychiatric disorders of high epidemiological relevance. There is a need for the study of additional candidate genes for impulsivity. One hundred seventy-five young Colombian subjects completed the Spanish version of the short form of the Barratt Impulsiveness Scale (BIS-15S). A TaqMan assay was used to genotype a functional polymorphism (rs3746544) in the SNAP25 gene. A significant association was found between the functional polymorphism in the SNAP25 gene and impulsivity in the Colombian sample, with subjects carrying T/T and G/G genotypes showing lower mean scores in the non-planning subfactor (p = 0.02). This is the first report of an association of a functional polymorphism in the SNAP25 gene and a subfactor of the BIS-15S scale of impulsivity. In addition, this the first genetic study of impulsivity scores in a Latin American sample. Future studies should explore additional variants in brain-expressed miRNAs and in their binding sites as candidates for impulsivity in different populations. © King Abdulaziz City for Science and Technology 2020.In the present study, febuxostat (FBX)-loaded PEG-coated PLGA nanoparticles (FBX-PLGA-PEG) were developed and its anticancer activity on lung cancer cells was evaluated. FBX-PLGA-PEG were prepared by nanoprecipitation technique and characterized for particle size, size distribution, entrapment efficiency, and in vitro drug release study. The optimized formulations were used to evaluate cell viability, apoptosis, cell cycle, and caspase activity in A549 lung cancer cells. The optimized formulation showed spherical particle with average particle size of 180 ± 4.72 nm, particle-size distribution 0.223 ± 0.003, entrapment efficiency (70 ± 2.56%), and drug release (99.1 ± 2.33%) at 12 h. MTT cytotoxicity assay showed better cytotoxic potential of FBX-NPs than FBX solution against NSCLC A549 cells. The lower IC50 of FBX-NP (52.62 ± 2.52 µg/mL) compared to FBX (68.0 ± 4.12 µg/mL) are suggestive of a potential cytotoxic effect of nano-formulation compared to the drug itself. Furthermore, flow cytometry analysis showed significantly higher percentage of total apoptotic cells in FBX-NPs (10.38 ± 1.57%) as compared to FBX solution (2.76 ± 0.17%) showed strong proapoptotic potential of FBX nano-formulation. The increased caspase activity and percent of cells at G2/M phase of cell cycle increased for FBX nanoparticles were more effective than FBX solution in increasing caspase activity and percent of cells at G2/M phase of cell cycle. Our studies with FBX nanoparticles exhibited promising outcome which could be used as a strategies to combat lung cancer. SNX-5422 concentration © King Abdulaziz City for Science and Technology 2020.Even though cell-cell adhesion molecule carcinoembryonic antigen-related cell adhesion molecule 1 (CEACAM1) is extensively studied since the discovery, the role of CEACAM1 in different cancers is not completely clarified. In the present study, we examined CEACAM1 expression and its association with patient survival in various cancers by analysis of multiple databases. Oncomine database analysis revealed that CEACAM1 expression was upregulated in lung and pancreatic cancers, but downregulated in colorectal and head and neck cancers. PrognoScan and Kaplan‑Meier analyses showed that colorectal cancer patients as well as head and neck cancer patients with high CEACAM1 expression exhibited a higher overall survival rate. STRING analysis identified CEACAM3, CEACAM8, FN1, etc. as CEACAM1 interactors. Gene alteration analysis showed that CEACAM1 mutation predominantly occurred in the N-terminal. Coexpression analysis demonstrated that CEACAM1 had distinct coexpressed genes in different cancers, but KRT protein was consistently coexpressed with CEACAM1 in diverse cancer types.

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