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1.
Cardiol Young ; : 1-3, 2024 May 28.
Article in English | MEDLINE | ID: mdl-38804021

ABSTRACT

We report the first-stage percutaneous palliation in a newborn with a rare heterotaxy syndrome variant including interrupted inferior vena cava, partial anomalous pulmonary venous drainage, and restrictive interatrial communication. Virtual reality imaging aided visualisation, decision-making, and planning. Successful atrial septoplasty performed via the internal jugular vein and anomalous pulmonary vein was followed by stenting of ductus arteriosus.

2.
Kardiol Pol ; 79(2): 161-169, 2021 02 25.
Article in English | MEDLINE | ID: mdl-33331744

ABSTRACT

BACKGROUND: Ventricular septal defect (VSD) is one of the most common congenital heart defects. Currently, surgery remains the treatment of choice. However, transcatheter techniques for closing of various types of VSDs have become an alternative. AIMS: The objective of our study was to present the outcomes of transcatheter closure of various types of VSD based on a systematic review of recent publications. METHODS: A systematic review of studies published in English between January 2014 and March 2020 was performed using the PubMed database (MEDLINE) independently by 2 reviewers. Data on success and complication rates were extracted. Studies including fewer than 5 patients and those with acquired VSD were excluded from the analysis. RESULTS: Finally, 44 studies were included for analysis, with a total number of 4050 patients. The pooled estimate of the overall success rate based on the random effects model was 97.96% (95% CI, 97.37-98.56; Q test P 0.99; I 2 = 0%) for permanent VSD. CONCLUSIONS: Transcatheter closure of selected VSDs appears to be an effective and safe method of treatment. Recent studies have shown high rates of successful interventions with a low incidence of complications.


Subject(s)
Cardiac Catheterization , Heart Septal Defects, Ventricular , Cardiac Catheterization/adverse effects , Heart Septal Defects, Ventricular/surgery , Humans , Research Design , Treatment Outcome
3.
Protoplasma ; 254(2): 713-724, 2017 Mar.
Article in English | MEDLINE | ID: mdl-27193139

ABSTRACT

The cell wall emerged as one of the important structures in plant stress responses. To investigate the effect of cold on the cell wall properties, the content and localization of pectins and pectin methylesterase (PME) activity, were studied in two maize inbred lines characterized by different sensitivity to cold. Low temperature (14/12 °C) caused a reduction of pectin content and PME activity in leaves of chilling-sensitive maize line, especially after prolonged treatment (28 h and 7 days). Furthermore, immunocytohistological studies, using JIM5 and JIM7 antibodies, revealed a decrease of labeling of both low- and high-methylesterified pectins in this maize line. The osmotic potential, quantified by means of incipient plasmolysis was lower in several types of cells of chilling-sensitive maize line which was correlated with the accumulation of sucrose. These studies present new finding on the effect of cold stress on the cell wall properties in conjunction with changes in the osmotic potential of maize leaf cells.


Subject(s)
Cell Wall/metabolism , Cold Temperature , Osmosis , Pectins/metabolism , Plant Leaves/cytology , Zea mays/cytology , Antibodies, Monoclonal/metabolism , Biomass , Carboxylic Ester Hydrolases/metabolism , Cell Wall/ultrastructure , Inbreeding , Plant Leaves/ultrastructure , Sucrose/metabolism , Zea mays/ultrastructure
4.
Elife ; 42015 Jun 02.
Article in English | MEDLINE | ID: mdl-26032562

ABSTRACT

To cause disease and persist in a host, pathogenic and commensal microbes must adhere to tissues. Colonization and infection depend on specific molecular interactions at the host-microbe interface that involve microbial surface proteins, or adhesins. To date, adhesins are only known to bind to host receptors non-covalently. Here we show that the streptococcal surface protein SfbI mediates covalent interaction with the host protein fibrinogen using an unusual internal thioester bond as a 'chemical harpoon'. This cross-linking reaction allows bacterial attachment to fibrin and SfbI binding to human cells in a model of inflammation. Thioester-containing domains are unexpectedly prevalent in Gram-positive bacteria, including many clinically relevant pathogens. Our findings support bacterial-encoded covalent binding as a new molecular principle in host-microbe interactions. This represents an as yet unexploited target to treat bacterial infection and may also offer novel opportunities for engineering beneficial interactions.


Subject(s)
Adhesins, Bacterial/metabolism , Carrier Proteins/metabolism , Inflammation/metabolism , Membrane Proteins/metabolism , Escherichia coli/enzymology , Fibrin/metabolism , Fibrinogen/metabolism , Humans , Inflammation/microbiology
5.
J Biol Chem ; 288(11): 7942-7955, 2013 Mar 15.
Article in English | MEDLINE | ID: mdl-23362277

ABSTRACT

NrdH-redoxins are small reductases with a high amino acid sequence similarity with glutaredoxins and mycoredoxins but with a thioredoxin-like activity. They function as the electron donor for class Ib ribonucleotide reductases, which convert ribonucleotides into deoxyribonucleotides. We solved the x-ray structure of oxidized NrdH-redoxin from Corynebacterium glutamicum (Cg) at 1.5 Å resolution. Based on this monomeric structure, we built a homology model of NrdH-redoxin from Mycobacterium tuberculosis (Mt). Both NrdH-redoxins have a typical thioredoxin fold with the active site CXXC motif located at the N terminus of the first α-helix. With size exclusion chromatography and small angle x-ray scattering, we show that Mt_NrdH-redoxin is a monomer in solution that has the tendency to form a non-swapped dimer at high protein concentration. Further, Cg_NrdH-redoxin and Mt_NrdH-redoxin catalytically reduce a disulfide with a specificity constant 1.9 × 10(6) and 5.6 × 10(6) M(-1) min(-1), respectively. They use a thiol-disulfide exchange mechanism with an N-terminal cysteine pKa lower than 6.5 for nucleophilic attack, whereas the pKa of the C-terminal cysteine is ~10. They exclusively receive electrons from thioredoxin reductase (TrxR) and not from mycothiol, the low molecular weight thiol of actinomycetes. This specificity is shown in the structural model of the complex between NrdH-redoxin and TrxR, where the two surface-exposed phenylalanines of TrxR perfectly fit into the conserved hydrophobic pocket of the NrdH-redoxin. Moreover, nrdh gene deletion and disruption experiments seem to indicate that NrdH-redoxin is essential in C. glutamicum.


Subject(s)
Corynebacterium glutamicum/metabolism , Escherichia coli Proteins/metabolism , Mycobacterium tuberculosis/metabolism , Thioredoxins/metabolism , Amino Acid Sequence , Antitubercular Agents/pharmacology , Catalytic Domain , Cloning, Molecular , Crystallography, X-Ray/methods , Cysteine/chemistry , Cysteine/pharmacology , Dimerization , Electrons , Glycopeptides/chemistry , Glycopeptides/pharmacology , Hydrogen-Ion Concentration , Inositol/chemistry , Inositol/pharmacology , Kinetics , Molecular Conformation , Molecular Sequence Data , Oxidation-Reduction , Protein Binding , Protein Structure, Tertiary , Ribonucleotides/chemistry , Scattering, Radiation , Sequence Homology, Amino Acid , Surface Properties , Thioredoxin-Disulfide Reductase/chemistry , X-Rays
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