scholarly journals Structural analysis and immunogenicity of Pseudomonas aeruginosa immunotype 2 high molecular weight polysaccharide.

1986 ◽  
Vol 77 (2) ◽  
pp. 491-495 ◽  
Author(s):  
G B Pier ◽  
S E Bennett
Keyword(s):  
Molecular Weight ◽  
Pseudomonas Aeruginosa ◽  
Structural Analysis ◽  
High Molecular Weight

Therapeutic Effects of High Molecular Weight Hyaluronic Acid in Severe Pseudomonas Aeruginosa Pneumonia in Ex Vivo Perfused Human Lungs

2021 ◽  
Author(s):  
Xiwen Zhang ◽  
Shinji Sugita ◽  
Airan Liu ◽  
Yoshifumi Naito ◽  
Wonjung Hwang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Pseudomonas Aeruginosa ◽  
Hyaluronic Acid ◽  
High Molecular Weight ◽  
Bacterial Pneumonia ◽  
Ex Vivo ◽  
Therapeutic Effects ◽  
Human Lungs ◽  
Protein Permeability

Introduction: We previously reported that extracellular vesicles (EVs) released during Escherichia coli bacterial pneumonia were inflammatory, and administration of high molecular weight hyaluronic acid (HMW HA) suppressed several indices of acute lung injury (ALI) from Escherichia coli pneumonia by binding to these inflammatory EVs. The current study was undertaken to study the therapeutic effects of HMW HA in ex vivo perfused human lungs injured with Pseudomonas aeruginosa (PA)103 bacterial pneumonia. Methods: For lungs with baseline alveolar fluid clearance (AFC)<10%/h, HMW HA 1 or 2 mg was injected intravenously after 1 h (N = 4-9), and EVs released during PA pneumonia were collected from the perfusate over 6 h. For lungs with baseline AFC>10%/h, HMW HA 2 mg was injected intravenously after 1 h (N = 6). In vitro experiments were conducted to evaluate the effects of HA on inflammation and bacterial phagocytosis. Results: For lungs with AFC<10%/h, administration of HMW HA intravenously significantly restored AFC and numerically decreased protein permeability and alveolar inflammation from PA103 pneumonia but had no effect on bacterial counts at 6 h. However, HMW HA improved bacterial phagocytosis by human monocytes and neutrophils and suppressed the inflammatory properties of EVs released during pneumonia on monocytes. For lungs with AFC>10%/h, administration of HMW HA intravenously improved AFC from PA103 pneumonia but had no significant effects on protein permeability, inflammation or bacterial counts. Discussion: In the presence of impaired alveolar epithelial transport capacity, administration of HMW HA improved the resolution of pulmonary edema from Pseudomonas PA103 bacterial pneumonia.

scholarly journals Pseudomonas aeruginosa exoenzymes U and Y induce a transmissible endothelial proteinopathy

2016 ◽  
Vol 310 (4) ◽  
pp. L337-L353 ◽  
Author(s):  
K. Adam Morrow ◽  
Cristhiaan D. Ochoa ◽  
Ron Balczon ◽  
Chun Zhou ◽  
Laura Cauthen ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Pseudomonas Aeruginosa ◽  
High Molecular Weight ◽  
Cell Injury ◽  
Microvascular Endothelial Cell ◽  
Gap Formation ◽  
Conditional Expression ◽  
Pulmonary Microvascular Endothelial Cell ◽  
Injury Characteristic ◽  
Type 3

We tested the hypothesis that Pseudomonas aeruginosa type 3 secretion system effectors exoenzymes Y and U (ExoY and ExoU) induce release of a high-molecular-weight endothelial tau, causing transmissible cell injury characteristic of an infectious proteinopathy. Both the bacterial delivery of ExoY and ExoU and the conditional expression of an activity-attenuated ExoU induced time-dependent pulmonary microvascular endothelial cell gap formation that was paralleled by the loss of intracellular tau and the concomitant appearance of high-molecular-weight extracellular tau. Transfer of the high-molecular-weight tau in filtered supernatant to naïve endothelial cells resulted in intracellular accumulation of tau clusters, which was accompanied by cell injury, interendothelial gap formation, decreased endothelial network stability in Matrigel, and increased lung permeability. Tau oligomer monoclonal antibodies captured monomeric tau from filtered supernatant but did not retrieve higher-molecular-weight endothelial tau and did not rescue the injurious effects of tau. Enrichment and transfer of high-molecular-weight tau to naïve cells was sufficient to cause injury. Thus we provide the first evidence for a pathophysiological stimulus that induces release and transmissibility of high-molecular-weight endothelial tau characteristic of an endothelial proteinopathy.

Structural analysis of high molecular weight PMSQs and their related properties for interlayer dielectric (ILD) application

2012 ◽  
Vol 20 (11) ◽  
pp. 1131-1136 ◽  
Author(s):  
He Seung Lee ◽  
Seung-Sock Choi ◽  
Kyung-Youl Baek ◽  
Eung Chan Lee ◽  
Soon Man Hong ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Structural Analysis ◽  
High Molecular Weight ◽  
Interlayer Dielectric

scholarly journals Plasmic degradation of crosslinked fibrin. I. Structural analysis of the particulate clot and identification of new macromolecular-soluble complexes

Blood ◽  
1980 ◽  
Vol 56 (3) ◽  
pp. 456-464 ◽  
Author(s):  
CW Francis ◽  
VJ Marder ◽  
SE Martin
Keyword(s):  
Molecular Weight ◽  
Structural Analysis ◽  
High Molecular Weight ◽  
Polypeptide Chain ◽  
Degradation Products ◽  
Fibrin Clot ◽  
Proteolytic Cleavages ◽  
Soluble Complexes ◽  
Covalently Bound

Abstract Plasmic degradation of crosslinked fibrin has been studied to identify the proteolytic cleavages that convert the clot into a soluble lysate and also to identify the derivatives that are likely to circulate during clot dissolution. Initial polypeptide chain cleavages do not disrupt the solid clot matrix. With continued exposure to plasmin, high molecular weight derivatives are produced that remain attached to the clot by noncovalent forces. Further degradation then results in the liberation into solution of several large, noncovalently bound complexes. Progressive degradation of the largest, initially liberated complexes to the terminal derivatives, DD/E, DD, and E, occurs in solution after their release from the clot. As the fibrin clot is exposed to plasmin for longer intervals, progressive dissolution occurs, but the structure of the covalently bound insoluble fibrin core, the noncovalently attached derivatives, and the liberated complexes remains constant. Since much of the initially liberated protein is in complexes larger than DD/E, these derivatives probably represent the more prevalent plasmic degradation products of crosslinked fibrin in vivo.

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