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Jeong, Jiyeong,Bertsch, Johannes,Hess, Verena,Choi, Sunju,Choi, In-Geol,Chang, In Seop,Mü,ller, Volker American Society for Microbiology 2015 Applied and environmental microbiology Vol.81 No.14
<P><I>Eubacterium limosum</I> KIST612 is one of the few acetogens that can produce butyrate from carbon monoxide. We have used a genome-guided analysis to delineate the path of butyrate formation, the enzymes involved, and the potential coupling to ATP synthesis. Oxidation of CO is catalyzed by the acetyl-coenzyme A (CoA) synthase/CO dehydrogenase and coupled to the reduction of ferredoxin. Oxidation of reduced ferredoxin is catalyzed by the Rnf complex and Na<SUP>+</SUP> dependent. Consistent with the finding of a Na<SUP>+</SUP>-dependent Rnf complex is the presence of a conserved Na<SUP>+</SUP>-binding motif in the <I>c</I> subunit of the ATP synthase. Butyrate formation is from acetyl-CoA via acetoacetyl-CoA, hydroxybutyryl-CoA, crotonyl-CoA, and butyryl-CoA and is consistent with the finding of a gene cluster that encodes the enzymes for this pathway. The activity of the butyryl-CoA dehydrogenase was demonstrated. Reduction of crotonyl-CoA to butyryl-CoA with NADH as the reductant was coupled to reduction of ferredoxin. We postulate that the butyryl-CoA dehydrogenase uses flavin-based electron bifurcation to reduce ferredoxin, which is consistent with the finding of <I>etfA</I> and <I>etfB</I> genes next to it. The overall ATP yield was calculated and is significantly higher than the one obtained with H<SUB>2</SUB> + CO<SUB>2</SUB>. The energetic benefit may be one reason that butyrate is formed only from CO but not from H<SUB>2</SUB> + CO<SUB>2</SUB>.</P>
Galectin-3 Reflects the Echocardiographic Grades of Left Ventricular Diastolic Dysfunction
Uzair Ansari,Michael Behnes,Julia Hoffmann,Michele Natale,Christian Fastner,Ibrahim El-Battrawy,Jonas Rusnak,김승현,Siegfried Lang,Ursula Hoffmann,Thomas Bertsch,Martin Borggrefe,Ibrahim Akin 대한진단검사의학회 2018 Annals of Laboratory Medicine Vol.38 No.4
Background: The level of Galectin-3 (Gal-3) protein purportedly reflects an ongoing cardiac fibrotic process and has been associated with ventricular remodeling, which is instrumental in the development of heart failure with preserved ejection fraction (HFpEF) syndrome. The aim of this study was to investigate the potential use of Gal-3 in improved characterization of the grades of diastolic dysfunction as defined by echocardiography. Methods: Seventy HFpEF patients undergoing routine echocardiography were prospectively enrolled in the present monocentric study. Blood samples for measurements of Gal-3 and amino-terminal pro-brain natriuretic peptide (NT-proBNP) were collected within 24 hours pre- or post-echocardiographic examination. The classification of patients into subgroups based on diastolic dysfunction grade permitted detailed statistical analyses of the derived data. Results: The Gal-3 serum levels of all patients corresponded to echocardiographic indices, suggesting HFpEF (E/A, P =0.03 and E/E’, P =0.02). Gal-3 was also associated with progressive diastolic dysfunction, and increased levels corresponded to the course of disease (P =0.012). Detailed analyses of ROC curves suggested that Gal-3 levels could discriminate patients with grade III diastolic dysfunction (area under the curve [AUC]=0.770, P =0.005). Conclusions: Gal-3 demonstrates remarkable effectiveness in the diagnosis of patients suffering from severe grade diastolic dysfunction. Increasing levels of Gal-3 possibly reflect the progressive course of HFpEF, as classified by the echocardiographic grades of diastolic dysfunction.