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2.
Eur Rev Med Pharmacol Sci ; 24(14): 7826-7833, 2020 07.
Article in English | MEDLINE | ID: mdl-32744710

ABSTRACT

OBJECTIVE: The outbreak of the 2019 Novel Coronavirus Disease (COVID-19) is seriously threatening the health of people all over China and the world. This study aims to investigate the clinical characteristics and outcomes of COVID-19 patients admitted at different time periods. PATIENTS AND METHODS: A total of 132 discharged cases and 10 deaths of laboratory or clinically confirmed cases were retrospectively collected from The First People's Hospital of Jingzhou, Hubei. All cases were divided into two groups according to different admission times (group 1 from 2020-1-23 to 2020-2-3 and group 2 from 2020-2-4 to 2020-2-15). Individual data, clinical data, laboratory indices and prognosis were collected for the two groups, and statistical analysis was performed using the t-test or chi-square test to assess differences between the groups. RESULTS: Among the 142 cases, there were 67 in the first group and 75 in the second group. According to the individual data and clinical manifestations of the two groups, the hospital stay in the first group was significantly longer than that of the second group (26 [9-39] compared with 20 [6-30], p=0.000). There were more clinical symptoms upon admission in group 1 than in group 2; although 66.2% of all patients had fever, the proportion of patients with fever on admission in the first group was significantly higher than that in the second group (79.1% compared with 54.7%, p=0.002). The proportion of patients with chills in the first group was higher than that in the second group (16.4% compared with 5.3%, p=0.032), and the proportion of patients with dyspnea was also higher than that in the second group (17.9% compared with 4%, p=0.007). Four of the 67 patients in the first group had symptoms of ocular discomfort, but none in the second group had this symptom (6.0% compared with 0, p=0.032). Based on laboratory examination, the inflammatory index of patients in the first group was higher than that in the second group, and the proportion of patients with a C-reactive protein (CRP) increase was also significantly higher (60% compared with 38.7%, p=0.020). The main difference in routine blood tests involved white blood cell and lymphocyte counts and the lymphocyte percentage. The proportion of patients with reduced white blood cell counts in the first group was higher than that in the second group (23.9% compared with 10.7% p=0.036). Moreover, more patients in the first group had a reduced lymphocyte count and percentage (71.6% compared with 30.7% p=0.000; 49.3% compared with 29.7% p=0.015, respectively), and the former was significantly lower than that in the second group (0.94 [0.24-2.42] compared with 1.365 [0.22-3.62], p=0.000). Regarding prognosis, the proportion of severe cases and mortality in the first group were slightly higher than in the second group (p>0.05). CONCLUSIONS: The clinical manifestations, blood changes and outcomes differed in patients admitted at different time periods. In the second group of patients, clinical symptoms were less common than in the first group, routine blood changes and inflammatory indices were milder, and the clinical prognosis was better.


Subject(s)
Coronavirus Infections/pathology , Pneumonia, Viral/pathology , Adolescent , Adult , Aged , Aged, 80 and over , Betacoronavirus/isolation & purification , C-Reactive Protein/analysis , COVID-19 , Coronavirus Infections/complications , Coronavirus Infections/mortality , Coronavirus Infections/virology , Dyspnea/diagnosis , Dyspnea/etiology , Female , Humans , Length of Stay , Lymphocyte Count , Male , Middle Aged , Pandemics , Pneumonia, Viral/complications , Pneumonia, Viral/mortality , Pneumonia, Viral/virology , Prognosis , Retrospective Studies , SARS-CoV-2 , Severity of Illness Index , Survival Rate , Time Factors , Young Adult
3.
Chem Commun (Camb) ; 54(25): 3094-3097, 2018 Mar 28.
Article in English | MEDLINE | ID: mdl-29424842

ABSTRACT

This study reports the electrochemical applications of CoV2O4 as a novel anode for lithium-ion batteries. Ex situ analyses were performed to understand the conversion that transpires during the charge-discharge cycle. Also, the effects of different binders were analyzed. With the synergistic effect of Na-carboxymethyl cellulose and styrene butadiene rubber (CMC and SBR), a reversible capacity of 727.5 mA h g-1 was obtained after 100 cycles which indicates potential applications of CoV2O4 in energy storage devices.

4.
Genet Mol Res ; 15(4)2016 Oct 17.
Article in English | MEDLINE | ID: mdl-27813589

ABSTRACT

We aimed to measure the invasion ability of Hep-2 laryngeal cancer cells after treatment with C-erbB-2-small interfering RNA (siRNA)-chitosan nanoparticles, and assess the applied value of chitosan nanoparticle-mediated C-erbB-2 interference in inhibiting laryngeal cancer invasion and metastasis. Nanoparticles of approximately 100 nm, comprising C-erbB-2 siRNA packaged with chitosan, were prepared and used to treat Hep-2 cells. Silencing of C-erbB-2 was detected by western blot and polymerase chain reaction. Cell invasion and apoptosis were estimated by transwell assay and flow cytometry, respectively. C-erbB-2-siRNA-chitosan nanoparticles significantly down-regulated C-erbB-2 expression in Hep-2 cells (P < 0.05), and cell invasion was noticeably decreased. Moreover, they significantly induced apoptosis of the Hep-2 cells (P < 0.05). Chitosan nanoparticle-mediated C-erbB-2 gene interference can inhibit the invasion of laryngeal cancer cells and induce their apoptosis.


Subject(s)
Apoptosis , Chitosan/chemistry , Gene Silencing , Genes, erbB-2 , Nanoparticles/chemistry , Blotting, Western , Cell Line, Tumor , Flow Cytometry , Humans , Laryngeal Neoplasms/pathology , Microscopy, Atomic Force , Neoplasm Invasiveness , Particle Size , RNA, Small Interfering/metabolism , Real-Time Polymerase Chain Reaction
5.
Nanoscale ; 7(6): 2708-15, 2015 Feb 14.
Article in English | MEDLINE | ID: mdl-25583066

ABSTRACT

A new one-step method for the preparation of graphene oxide (GO) nanostructures has been developed by pulsed laser ablation in GO solution. The formation of different shapes of GO nanostructures, such as ribbons, nanoflakes (including nano-squares, nano-rectangles, nano-triangles, nano-hexagons, and nano-disks) and quantum dots, has been demonstrated by scanning electron microscopy and transmission electron microscopy. Photoreduction for the GO occurred during irradiation by the pulsed laser. The GO quantum dots exhibit a blue photoluminescence, originating from recombination of the localized carriers in the zigzag-edge states.

6.
Opt Express ; 21(2): 1857-64, 2013 Jan 28.
Article in English | MEDLINE | ID: mdl-23389170

ABSTRACT

Two different types of lasing modes, vertical Fabry-Perot cavity and random lasing, were observed in ZnO epi-films of different thicknesses grown on Si (111) substrates. Under optical excitation at room temperature by a frequency tripled Nd:YVO4 laser with wavelength of 355 nm, the lasing thresholds are low due to high crystalline quality of the ZnO epitaxial films, which act as microresonators. For the thick ZnO layer (1,200 nm), its lasing action is originated from the random scattering due to the high density of crack networks developed in the thick ZnO film. However, the low crack density of the thin film (555 nm) fails to provide feedback loops essential for random scattering. Nevertheless, even the lower threshold lasing is achieved by the Fabry-Perot cavity formed by two interfaces of the thin ZnO film. The associated lasing modes of the thin ZnO film can be characterized as the transverse Gaussian modes attributed to the smooth curved surfaces.


Subject(s)
Interferometry/instrumentation , Lasers , Silicon/chemistry , Zinc Oxide/chemistry , Crystallography/methods , Equipment Design , Equipment Failure Analysis
7.
ACS Appl Mater Interfaces ; 4(10): 5333-7, 2012 Oct 24.
Article in English | MEDLINE | ID: mdl-22989018

ABSTRACT

High-quality m-plane orientated ZnO films have been successfully grown on m-plane sapphire by using radio frequency magnetron sputtering deposition. The introduction of a nanometer-thick, low-temperature-grown ZnO buffer layer effectively eliminates inclusions of other undesirable orientations. The structure characteristics of the ZnO epi-layers were thoroughly studied by synchrotron X-ray scattering and transmission electron microscopy (TEM). The in-plane epitaxial relationship between ZnO and sapphire follows (0002)(ZnO) [parallel] (112[overline]0)(sapphire) and (112[overline]0)(ZnO) [parallel] (0006)(sapphire) and the ZnO/sapphire interface structure can be described by the domain matching epitaxy along the [112[overline]0](ZnO) direction. The vibrational properties of the films were investigated by polarization dependent micro-Raman spectroscopy. Both XRD and micro-Raman results reveal that the obtained m-ZnO layers are under an anisotropic biaxial strain but still retains a hexagonal lattice.

8.
J Biol Chem ; 276(11): 8149-58, 2001 Mar 16.
Article in English | MEDLINE | ID: mdl-11060305

ABSTRACT

The heavy-chain CDR3 region of the high affinity (K(a) = 1.3 x 10(10) M(-)1) anti-digoxin monoclonal antibody 26-10 was modified previously to shift its specificity, by substitution of tryptophan 100 by arginine, toward binding analogs of digoxin containing substitutions at position 16. To further change specificity, two 5-mer libraries of the randomly mutagenized phage-displayed 26-10 HCDR3 region (positions 94-98) were panned against digoxin-bovine serum albumin (BSA) as well as against 16-acetylgitoxin-BSA. When a mutant Fab that binds 16-substituted analogs preferentially was used as a parent sequence, clones were obtained with affinities for digoxin increased 2-4-fold, by panning on digoxin-BSA yet retaining the specificity shift. Selection on 16-acetylgitoxin-BSA, however, resulted in nine clones that bound gitoxin (16-OH) up to 150-fold higher than the wild-type 26-10, due to a consensus mutation of Ser(H95) to Gly(H95). The residues at both position H95 (serine) and position H100 (tryptophan) contact hapten in the crystal structure of the Fab 26-10-digoxin complex. Thus, by mutating hapten contact residues, it is possible to reorder the combining site of a high affinity antibody, resulting in altered specificity, yet retain or substantially increase the relative affinity for the cross-reactive ligand.


Subject(s)
Antibodies/chemistry , Complementarity Determining Regions/chemistry , Digoxin/immunology , Immunoglobulin Heavy Chains/chemistry , Peptide Library , Antibody Affinity , Antibody Specificity , Binding Sites , Digoxin/analogs & derivatives , Mutagenesis, Site-Directed , Serum Albumin, Bovine/immunology , Structure-Activity Relationship
9.
Immunogenetics ; 51(8-9): 659-69, 2000 Jul.
Article in English | MEDLINE | ID: mdl-10941837

ABSTRACT

The leukocyte immunoglobulin (Ig)-like receptors (LIRs) comprise a family of cell surface receptors that couple to either activating or inhibitory signals depending on the nature of their transmembrane and cytoplasmic domains. We describe the organization and fine localization of the genes for LIR-1 and LIR-5, which are inhibitory receptors, and LIR-6, which is an activating receptor. The genomic organization of all three genes is highly conserved from the signal peptide through the membrane-proximal Ig domain but diverges thereafter depending on the inhibitory or activating nature of the gene product. The 3' untranslated region of the gene for LIR-6 contains a 37-base pair repeat not present in the LIR-1 or LIR-5 genes. 5' rapid amplification of cDNA ends defined the putative transcription initiation site of the LIR-5 gene, which is TATA-less. A nucleotide substitution in the LIR-5 gene led to loss of an intron present in the 5' untranslated region of the LIR-1 and LIR-6 genes. Differences in the genomic structure of these three LIR genes suggests possible mechanisms for their differential expression in cells of hematopoietic lineage. The three genes are in a region of Chromosome 19q13.4 that is immediately centromeric of the killer cell Ig-like receptor genes and are separated from one another by approximately 20 to 30 kb, suggesting that they arose by gene duplication from a common ancestor.


Subject(s)
Antigens, CD , Chromosomes, Human, Pair 19 , Receptors, Immunologic/genetics , Base Sequence , Chromosome Mapping , DNA, Complementary , Gene Amplification , Humans , Leukocyte Immunoglobulin-like Receptor B1 , Leukocytes/metabolism , Molecular Sequence Data , Reverse Transcriptase Polymerase Chain Reaction/methods
10.
J Virol ; 73(7): 5826-32, 1999 Jul.
Article in English | MEDLINE | ID: mdl-10364334

ABSTRACT

Variations in the polyomavirus major capsid protein VP1 underlie important biological differences between highly pathogenic large-plaque and relatively nonpathogenic small-plaque strains. These polymorphisms constitute major determinants of virus spread in mice and also dictate previously recognized strain differences in sialyloligosaccharide binding. X-ray crystallographic studies have shown that these determinants affect binding to the sialic acids. Here we report results of further experiments designed to test the importance of specific contacts between VP1 and the carbohydrate moieties of the receptor. With minor exceptions, substitutions at positions predicted from crystallography to be important in binding the terminal alpha-2,3-linked sialic acid or the penultimate sugar (galactose) destroyed the ability of the virus to replicate in cell culture. Substitutions that prevented binding to a branched disialyloligosaccharide were found to result in viruses that were both viable in culture and tumorigenic in the mouse. Conversely, substitutions that allowed recognition and binding of the branched carbohydrate chain inhibited spread in the mouse, though the viruses remained viable in culture. Mice of five different inbred strains, all highly susceptible to large-plaque virus, showed resistance to the spread of polyomavirus strains bearing the VP1 type which binds the branched-chain receptor. We suggest that glycoproteins bearing the appropriate O-linked branched sialyloligosaccharide chains are effective pseudoreceptors in the host and that they block the spread of potentially tumorigenic or virulent virus strains.


Subject(s)
Capsid Proteins , Capsid/metabolism , N-Acetylneuraminic Acid/metabolism , Polyomavirus/metabolism , Polyomavirus/pathogenicity , Receptors, Virus/metabolism , 3T3 Cells , Amino Acid Substitution , Animals , Animals, Newborn , Cricetinae , Glutamic Acid , Mice , Mice, Inbred AKR , Mice, Inbred C3H , Mice, Inbred DBA , Polyomavirus/genetics , Polyomavirus Infections/pathology , Polyomavirus Infections/virology , Sialoglycoproteins/metabolism , Tumor Virus Infections/pathology , Tumor Virus Infections/virology , Virulence
11.
J Biol Chem ; 270(3): 1416-21, 1995 Jan 20.
Article in English | MEDLINE | ID: mdl-7836409

ABSTRACT

Glycerol-3-phosphate acyltransferase (GPAT) catalyzes the acylation of sn-glycerol 3-phosphate to form 1-acyl-sn-glycerol 3-phosphate, a committed step in triacylglycerol and phospholipid biosynthesis. We have previously reported the cDNA cloning and transcriptional regulation of the murine mitochondrial GPAT (mGPAT). We now report the cloning of the 5'-flanking region of the murine mitochondrial GPAT. The transcription start site was identified by primer extension and RNase protection assays. A TATA box-like motif (TTATTAT) was located between -34 and -29 and a reverse CCAAT box (ATTGG) was located between -78 and -74, relative to the transcription start site. To begin studying mechanisms underlying transcriptional regulation of the mGPAT gene, chimeric luciferase (LUC) plasmids containing serial deletions, from -1447 to -38, of the 5'-flanking region of the murine mGPAT gene were prepared and transfected into 3T3-L1 cells. The fusion construct -1447 GPAT.LUC showed high promoter activity and deletions to -1353, -747, -322, and -86 did not markedly change the promoter activity. With all constructs, luciferase activity was 2-fold higher when plasmids were transfected into 3T3-L1 adipocytes. However, deletion of sequences between -86 and -55 resulted in a 9-fold decrease in LUC activity in both preadipocytes and adipocytes. Deletion of sequences between -55 and -38 did not alter promoter activity. DNase I footprint analysis revealed a protected region between -95 and -65 which included the putative CTF/NF1 binding site. Electrophoretic mobility shift assays demonstrated a single protein-DNA complex formation. Oligonucleotides synthesized according to the CTF/NF1 consensus sequence or the adenovirus NF-1 site showed a different and more complex pattern of protein-DNA interaction and were not able to compete away the mGPAT promoter-protein complex, indicating that a distinct protein was bound to -86/-55, a region important for the basal promoter activity in 3T3-L1 cells. Luciferase activity was increased 2.8- and 8-fold when adipocytes stably transfected with -322 GPAT.LUC were treated with 5 and 25 mM glucose, respectively, in the presence of 10 nM insulin. These results indicate that carbohydrate-responsive sequences are located within -322 base pairs of the mGPAT promoter.


Subject(s)
Glycerol-3-Phosphate O-Acyltransferase/genetics , Promoter Regions, Genetic , 3T3 Cells , Animals , Base Sequence , DNA Primers , Glycerol-3-Phosphate O-Acyltransferase/metabolism , Mice , Molecular Sequence Data , Nuclear Proteins/metabolism , Sequence Deletion
12.
Biotechnol Bioeng ; 37(2): 177-84, 1991 Jan 20.
Article in English | MEDLINE | ID: mdl-18597353

ABSTRACT

A critical problem in the storage and delivery of pharmaceutical proteins is their aggregation induced by moisture. A model system has been elaborated and investigated to elucidate the mechanism of this phenomenon. When 10 mg of bovine serum albumin lyophilized from an aqueous solution of pH 7.3 are wetted with just 3 muL of a buffered physiological saline solution and incubated in the solid state at 37 degrees C, the protein progressively loses its solubility in water; e.g., after a 24 h incubation 97% of the protein becomes insoluble. This moisture-induced aggregation of albumin has been discovered to be due to an intermolecular S-S bond formation via the thiol-disulfide interchange reaction. The dependence of the extent of the solid-state aggregation on the amount and mode of addition of moisture and the atmosphere, additives, temperature, and history of the protein powder have been investigated. The moisture-induced solid-state aggregation has also been established and studied for three other lyophilized proteins: ovalbumin, glucose oxidase, and beta-lactoglobulin. In all cases, the loss of solubility is caused by thiol-disulfide interchange either alone or in combination with a conformational (noncovalent) process. The aggregation can be minimized by lyophilizing the proteins from acidic aqueous solutions, by adding inorganic salts, by co-lyophilizing the proteins with water-soluble polymers, or by controlling the moisture content at optimal levels.

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