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1.
Acta Cardiol ; 69(3): 281-8, 2014 Jun.
Article in English | MEDLINE | ID: mdl-25029873

ABSTRACT

PURPOSE: Echocardiographic evaluation of systolic function in patients with single right ventricles (SRV) is important but remains challenging. Minimal data exist correlating echocardiographic indices with catheterization data in this population. The goal of this study was to evaluate which echocardiographic measurement correlated best with dP/dt (max) obtained by cardiac catheterization in SRV patients. METHODS: Patients with SRV physiology who underwent simultaneous echocardiography and cardiac catheterization were evaluated. Echocardiographic data included fractional area change % (FAC), displacement, TDI s'wave, myocardial performance index (MPI), global systolic strain, and global SR s wave. Maximum positive rate of ventricular pressure change measured as dP/dt (max) was obtained from the cardiac catheterization report. Correlations of echocardiographic and catheterization variables were examined using the Pearson correlation. RESULTS: Twenty-seven SRV patients were studied. Median age at the time of the catheterization was 11.4 months (range 0 - 132 months). dP/dt (max) values ranged from 337-1860 mmHg/s with a median of 994 mmHg/s. Mean FAC was 27.15 +/- 7.13%, displacement was 7.35 +/- 2.88 mm, TDI s' was 4.98 +/- 1.93 cm/sec, MPI was 0.41 +/- 0.17, global strain was-14.85 +/- 4.32%, and global SR s wave was -1.03 +/- 0.34 sec(-1). There were no significant correlations between dP/dt (max) and any of the echocardiographic measurements of systolic function in SRV patients. CONCLUSION: In patients with SRV physiology, catheterization-derived dP/dt (max) did not correlate with echocardiographic measurements of systolic function. Larger studies are needed to determine which non-invasive parameter best describes systolic function in patients with SRV.


Subject(s)
Cardiac Catheterization , Echocardiography, Doppler , Heart Defects, Congenital/diagnosis , Heart Ventricles , Cardiac Catheterization/methods , Cardiac Catheterization/standards , Comparative Effectiveness Research , Cross-Sectional Studies , Echocardiography, Doppler/methods , Echocardiography, Doppler/standards , Female , Heart Ventricles/abnormalities , Heart Ventricles/diagnostic imaging , Heart Ventricles/physiopathology , Hemodynamics/physiology , Humans , Infant , Infant, Newborn , Male , Prospective Studies , Statistics as Topic , United States , Ventricular Function/physiology
2.
J Biomol Screen ; 10(4): 355-64, 2005 Jun.
Article in English | MEDLINE | ID: mdl-15964937

ABSTRACT

The m7GpppN cap at the 5' end of eukaryotic mRNAs is important for transcript stability and translation. Three enzymatic activities that generate the mRNA cap include an RNA 5'-triphosphatase, an RNA guanylyltransferase, and an RNA (guanine-7-) -methyltransferase. The physical organization of the genes encoding these enzymes differs between mammalian cells and yeast, fungi, or viruses. The catalytic mechanism used by the RNA triphosphatases of mammalian cells also differs from that used by the yeast, fungal, or viral enzymes. These structural and functional differences suggest that inhibitors of mRNA capping might be useful antifungal or antiviral agents. The authors describe several whole-cell yeast-based assays developed to identify and characterize inhibitors of fungal mRNA capping. They also report the identification and characterization of the natural product sinefungin in the assays. Their characterization of this S-adenosylmethionine analog suggests that it inhibits mRNA cap methyltransferases and exhibits approximately 5- to 10-fold specificity for the yeast ABD1 and fungal CCM1 enzymes over the human Hcm1 enzyme expressed in yeast cells.


Subject(s)
Adenosine/analogs & derivatives , Enzyme Inhibitors/analysis , Nucleotidyltransferases/antagonists & inhibitors , Saccharomyces cerevisiae/genetics , Adenosine/chemistry , Amino Acid Sequence , Genes, Reporter , Molecular Sequence Data , Nucleotidyltransferases/chemistry , Nucleotidyltransferases/genetics , Plasmids , Sequence Homology, Amino Acid
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