Characterization of Microcirculatory Disturbance in a Novel Model of Pancreatic Ischemia–Reperfusion Using Intravital Fluorescence–Microscopy

Pancreas ◽  
2002 ◽  
Vol 25 (2) ◽  
pp. 142-148 ◽  
Author(s):  
R. Obermaier ◽  
S. Benz ◽  
E. von Dobschuetz ◽  
O. Drognitz ◽  
W. Schareck ◽  
...  
Keyword(s):  
Fluorescence Microscopy ◽  
Ischemia Reperfusion ◽  
Intravital Fluorescence Microscopy ◽  
Microcirculatory Disturbance ◽  
Pancreatic Ischemia ◽  
Novel Model

scholarly journals Characterization of urinary exosomal release of aquaporin-1 and -2 after renal ischemia-reperfusion in rats

2018 ◽  
Vol 314 (4) ◽  
pp. F584-F601 ◽  
Author(s):  
Siree Asvapromtada ◽  
Hiroko Sonoda ◽  
Minami Kinouchi ◽  
Sayaka Oshikawa ◽  
Saki Takahashi ◽  
...  
Keyword(s):  
Renal Fibrosis ◽  
Ischemia Reperfusion ◽  
Kidney Injury ◽  
Interacting Protein ◽  
Aquaporin 1 ◽  
Water Handling ◽  
Marker Proteins ◽  
Apical Trafficking ◽  
Renal Expression

Acute kidney injury (AKI) is an important risk factor for the development of chronic kidney disease (CKD), and an alteration in renal water handling has been observed during the transition of AKI to CKD. Urinary exosomal release of aquaporin-1 (AQP1) and AQP2, important proteins for renal water handling, has recently been reported to predict their levels of renal expression. Therefore, we examined the patterns of urinary exosomal release of AQP1 and AQP2, and the exosomal marker proteins tumor susceptibility 101 protein (TSG101) and ALG-2 interacting protein X (Alix), in the acute and chronic phases following induction of AKI by renal bilateral ischemia/reperfusion (I/R) in rats. Blood tests and histological examinations indicated that AKI occurred before at 7 days after renal I/R ( day 7) and that renal fibrosis developed progressively thereafter. Immunoblotting demonstrated significant decreases in the urinary exosomal release of AQP1 and AQP2 during severe AKI. Urinary exosomal release of Alix and TSG101 was significantly increased on day 7. These data were also confirmed in rats with unilateral renal I/R causing more serious AKI. Urinary exosomal release of either the Ser-256- or Ser-269-phosphorylated form of AQP2, both of which are involved in apical trafficking of AQP2, was positively correlated with that of total AQP2. These results suggest that urinary exosomal release of AQP1 and AQP2 is reduced in I/R-induced AKI, whereas that of Alix and TSG101 is increased in the initial phase of renal fibrosis. Furthermore, apical trafficking of AQP2 appears to be related to urinary exosomal release of AQP2.

Assessing Bypassed Hydrocarbons

2021 ◽  
Author(s):  
Stanley Oifoghe ◽  
Nora Alarcon ◽  
Lucrecia Grigoletto
Keyword(s):  
Continental Shelf ◽  
Reservoir Characterization ◽  
Gamma Ray ◽  
West African ◽  
The Novel ◽  
The West ◽  
Present Case Study ◽  
Novel Model

Abstract Hydrocarbons are bypassed in known fields. This is due to reservoir heterogeneities, complex lithology, and limitations of existing technology. This paper seeks to identify the scenarios of bypassed hydrocarbons, and to highlight how advances in reservoir characterization techniques have improved assessment of bypassed hydrocarbons. The present case study is an evaluation well drilled on the continental shelf, off the West African Coastline. The targeted thin-bedded reservoir sands are of Cenomanian age. Some technologies for assessing bypassed hydrocarbon include Gamma Ray Spectralog and Thin Bed Analysis. NMR is important for accurate reservoir characterization of thinly bedded reservoirs. The measured NMR porosity was 15pu, which is 42% of the actual porosity. Using the measured values gave a permeability of 5.3mD as against the actual permeability of 234mD. The novel model presented in this paper increased the porosity by 58% and the permeability by 4315%.

Abstract MP30: Circulating Sars-cov-2 Spike Protein 1 Causes Microarteriolar Oxidative Stress, Endothelial Dysfunction And Enhanced Thromboxane And Endothelin Contractility That Are Prevented By Spironolactone.

Hypertension ◽  
2021 ◽  
Vol 78 (Suppl_1) ◽  
Author(s):  
Dan Wang ◽  
Christopher S Wilcox
Keyword(s):  
Oxidative Stress ◽  
Endothelial Cells ◽  
Endothelial Dysfunction ◽  
Fluorescence Microscopy ◽  
Vascular Dysfunction ◽  
Microvascular Complications ◽  
Spike Protein ◽  
Ros Generation ◽  
Intravenous Injections ◽  
Novel Model

Introduction and hypothesis: Following bodily entry, the SARS-CoV-2 virus undergoes pulmonary replication with release of circulating viral spike protein 1 (SP1) into the bloodstream. Uptake of SP1 by endothelial cells might provoke vascular dysfunction and thrombosis. We hypothesized that spironolactone could prevent microvascular complications from circulating SP1 in COVID-19. Methods: male C57Bl/6 mice received spironolactone (100 mg · kg -1 · d -1 PO x 3d) or vehicle and intravenous injections of recombinant full-length human SP1 (10 μg per mouse) or vehicle. They were euthanized after 3 days. Mesenteric resistant arterioles (n=4 per group) were dissected and mounted on isometric myographs. Acetylcholine-induced EDRF responses and L-NAME-inhibitable NO generation (DAF-FM fluorescence) were studied in pre-constricted vessels and contraction to endothelin 1 (ET1) or thromboxane (U-46, 619) and ET1-induced ROS (PEG-SOD inhibitable ethidium: dihydroethidium fluorescence) were studied by fluorescence microscopy in other vessels. Results: SP1 reduced acetylcholine-induced EDRF (17 ± 3 vs 27 ± 5 % mean ± sem; P < 0.05) and NO generation (0.21 ± 0.03 vs 0.36 ± 0.04, F 1 /F 0 ; P < 0.05) while increasing contraction to ET1 (10 -7 mol·l -1 : 124 ± 13 vs 89 ± 4 %; P < 0.05) and U-46, 619 (10 -6 mol·l -1 :114± 5 vs 87± 6 %; P < 0.05) and ET1-induced ROS generation(0.30± 0.08 vs 0.09± 0.03; P < 0.05). Spironolactone did not modify any of these responses in vessels from normal mice but prevented all the effects of SP1. Conclusion: these preliminary studies provide a novel model to study COVID-19 vasculopathy. They indicate that spironolactone can provide protection from microvascular oxidative stress, endothelial dysfunction and enhanced contractility and might thereby moderate COVID-19 complications.

scholarly journals Characterization of The Interaction Between RIN13 (RPM1-Interacting13) and Sumo Proteins in Arabidopsis Thaliana

2017 ◽  
Vol 9 (2) ◽  
Author(s):  
Venny Santosa ◽  
Mio Nagabuchi ◽  
Sachiko Okada ◽  
Katsunori Tanaka
Keyword(s):  
Arabidopsis Thaliana ◽  
Fluorescence Microscopy ◽  
Hypersensitive Response ◽  
Stress Responses ◽  
Molecular Interaction ◽  
Nuclear Body ◽  
Chromosome Organization ◽  
Post Translational Modification ◽  
Molecular Studies

<p>Small Ubiquitin-related MOdifier (SUMO) proteins can be found in many organisms, including <em>A. thaliana</em>, which possesses 9 SUMO genes. SUMO binds to various target proteins in a reversible reaction called SUMOylation. SUMOylation participates in transcription, chromosome organization, proteins localizations and stress responses. Our study showed that RIN13 (<span style="text-decoration: underline;">R</span>PM1-<span style="text-decoration: underline;">In</span>teracting<span style="text-decoration: underline;">13</span>/At2g20310) is a target of SUMOylation, which was initially found by interaction between this protein and AtSCE1a (E2). Recent report showed that overexpression of RIN13 enhanced the resistance to pathogen without inducing hypersensitive response. However, the molecular interaction between RIN13 and SUMO proteins and its significance have not been studied yet. Thus, our study aimed to characterize the interaction between RIN13 and SUMO proteins in <em>A. thaliana</em>. The result showed an isoform-specific SUMOylation between RIN13 and SUMO proteins. RIN13 is SUMOylated by SUMO1, 2, 3, and 5. Though expressed ubiquitously in <em>A.thaliana</em>, fluorescence microscopy showed that RIN13 localizes subcellularly in the nuclear body. Moreover, complete abolishment of SUMOylation with inactive E2 suggests the exclusion of RIN13 from nuclear body. These results showed that SUMOylation affected RIN13 localization, and indirectly influenced its interaction to other proteins and putative function. This paper presents evidence of RIN13 SUMOylation. Furthermore, RIN13 function in pathogenic resistance is shown to be supported by SUMOylation. Thus, this study enhanced the understanding of SUMO in plants and served as reference to molecular studies concerning post-translational modification of SUMO.</p>

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