Uber den Einfluss der Phrenicusexairese auf die Magenfunktion. II. Mitteilung : Experimentelle Studien an Hunden mit Hilfe des Rontgenverfahren

Was den Einfluss der Phrenicusexairese auf die Magenfunktion, besonders Magenfunktionsveranderung direkt nach Phrenicusexairese mit Hilfe des Magenkurvenverfahrens anbelangt, hat Verfasser schon in der vorigen Mitteilung berichtet. Er hat weiternoch uber ihre Dauerresultate geforscht. Zur Untersuchung hat er das Rontgenverfahren angewandt, womit er die Bewegungs- und Passagezustande des Inhaltes beobachten konnte. Als Versuchstier hat er erwachsene kleine Hunde gebraucht. Die Resultate sind folgendermassen:- 1. Der Magen verandert seine Form durch den Hochstand infolge gelahmten Zwerchfells, d. h. bei der rechtseitigen Phrenicusexairese wird Pylorus nach oben gezogen und bei der linksseitigen nach links unten. 2. Der Magentonus sinkt deutlich bald nach der Operation ab und zeigt den Zustand von Dilatation und Atonie. Und er stellt sich allmahlich wieder her bis zur Norm und zwar bei einseitiger Exairese nach einigen Wochen, bei beiderseitiger nach einigen Monaten. 3. Die Entleerung des Mageninhalts wird gestort und es verzogert sich der Initialzeitpunkt, in dem der Inhalt den Pylorus passiert, und auch die vollige Entleerungszeit. Diese Storungen zeigen eine allmahliche Wiederherstellung und sie kommen mit der Peristaltik zum normalen erst nach einigen Wochen zuruck. 4. Auch zeigt das Duodenum die Herabsetzung des Tonus und Dilatatation und der Dunndarm zeigt schnelle Passage und schmale Rontgenbilder. (Autoreferat.

Bulletin mensuel de statistique / Institut national de la statistique et des études économiques...

septembre 19941994/09 (N9)

Universal Stress Protein Regulates Electron Transfer and Superoxide Generation Activities of the Cytochrome <i>bc</i>₁ Complex from <i>Rhodobacter sphaeroides</i>

Interactions between <i>Rhodobacter sphaeroides</i> cytochrome <i>bc</i>₁ complex (<i>Rsbc</i>₁) and soluble cytosolic proteins were studied by a precipitation pull-down technique. After being purified, detergent-dispersed <i>Rsbc</i>₁ complex was incubated with soluble cytosolic fraction and then dialyzed in the absence of detergent; the interacting proteins were coprecipitated with <i>Rsbc</i>₁ complex upon centrifugation. One of the cytosolic proteins pulled down by <i>Rsbc</i>₁ complex was identified by liquid chromatography-coupled tandem mass spectrometry (LC/MS/MS) to be the reported <i>R. sphaeroides</i> universal stress protein (UspA). Incubating purified UspA with the detergent dispersed <i>bc</i>₁ complex resulted in an increase in the <i>Rsbc</i>₁ complex activity by 60% and a decrease in superoxide generation activity by the complex by more than 70%. These UspA effects were only observed with <i>Rsbc</i>₁ complexes containing subunit IV and assayed under aerobic conditions. These results suggest that the interaction between UspA and <i>Rsbc</i>₁ complex may play an important role in <i>R. sphaeroides</i> cells during oxidative stress. Using a biotin label transfer technique, cytochrome <i>c</i>₁ of the <i>Rsbc</i>₁ complex was identified as the interacting site for UspA

ERα36, a variant of estrogen receptor α, is predominantly localized in mitochondria of human uterine smooth muscle and leiomyoma cells

<div><p>ERα36 is a naturally occurring, membrane-associated, isoform of estrogen receptor α. The expression of ERα36 is due to alternative splicing and different promoter usage. ERα36 is a dominant-negative effector of ERα66-mediated transactivational activities and has the potential to trigger membrane-initiated mitogenic, nongenomic, estrogen signaling; however, the subcellular localization of ERα36 remains controversial. To determine the cellular localization of ERα36 in estrogen-responsive human uterine smooth muscle (ht-UtSMC) and leiomyoma (fibroid; ht-UtLM) cells, we conducted systematic confocal microscopy and subcellular fractionation analysis using ERα36 antibodies. With Image J colocalizaton analysis plugin, confocal images were analyzed to obtain a Pearson’s Correlation Coefficient (PCC) to quantify signal colocalization of ERα36 with mitochondrial, endoplasmic reticulum, and cytoskeletal components in both cell lines. When cells were double-stained with an ERα36 antibody and a mitochondrial-specific dye, MitoTracker, the PCC for the two channel signals were both greater than 0.75, indicating strong correlation between ERα36 and mitochondrial signals in the two cell lines. A blocking peptide competition assay confirmed that the mitochondria-associated ERα36 signal detected by confocal analysis was specific for ERα36. In contrast, confocal images double-stained with an ERα36 antibody and endoplasmic reticulum or cytoskeletal markers, had PCCs that were all less than 0.4, indicating no or very weak signal correlation. Fractionation studies showed that ERα36 existed predominantly in membrane fractions, with minimal or undetected amounts in the cytosol, nuclear, chromatin, and cytoskeletal fractions. With isolated mitochondrial preparations, we confirmed that a known mitochondrial protein, prohibitin, was present in mitochondria, and by co-immunoprecipitation analysis that ERα36 was associated with prohibitin in ht-UtLM cells. The distinctive colocalization pattern of ERα36 with mitochondria in ht-UtSMC and ht-UtLM cells, and the association of ERα36 with a mitochondrial-specific protein suggest that ERα36 is localized primarily in mitochondria and may play a pivotal role in non-genomic signaling and mitochondrial functions.</p></div

Comparison of ERα36 and ERα66 domain structures and subcellular ERα36 staining patterns in human uterine smooth muscle (ht-UtSMC) and leiomyoma cells (ht-UtLM).

<p>(A) The top structure shows six conserved domains of ERα66 (labeled A-F), the amino acid sequence numbers, and the transactivation function domains (AF-1 and AF-2). The function of each domain is indicated. In the domain structure of ERα36, the last unique 27 amino acids of ERα36 are indicated as a filled box. The diagram is drawn proportionally to domain size. The drawing is based on the publication by Wang et. al., 2005 and GenBank entry CAE45969.1. (B) In ht-UtSMC cells (1), distinctive ERα36 signals were detected along the plasma membrane as shown by the arrow, but mostly localized within a robust intracytoplasmic network. In ht-UtLM cells (2), the ERα36 signals were detected mostly in a robust network structure within the cytoplasm. The cell samples were stained with ERα36 antibody and DAPI.</p

ERα36 Expression in subcellular fractions.

<p>Cellular Fraction Abbreviations: CE (cytoplasmic extract); ME (membrane extract); CB (chromatin-bound extract); NE (nuclear extract, nuclear soluble); PE (pellet extract, cytoskeleton); T (total cellular protein extract).</p

Interactions of ERα36 and prohibitin in human uterine leiomyoma cells.

<p>The interactions between ERα36 and prohibitin were determined with a co-immunoprecipitation (Co-IP). Ht-UtLM cells were treated with vehicle control, 10⁻⁸ M E₂, and 10⁻⁶ M E₂ for 24 hours. The blots presented are representative results that were repeated at least three times. PHB: prohibitin; IB: Immunobotting; IP: Immunoprecipitation.</p