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Preservation of renal endothelial integrity and reduction of renal edema by aprotinin does not preserve renal perfusion and function following experimental cardiopulmonary bypass

Dekker, Nicole A. M. ; van Leeuwen, Anoek L. I. ; van Meurs, Matijs ; [et al.]

Springer Science and Business Media LLC ; 2021

In: Intensive Care Medicine Experimental Vol. 9, No. 1 ( 2021-12)

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In: Intensive Care Medicine Experimental, Springer Science and Business Media LLC, Vol. 9, No. 1 ( 2021-12)

Abstract: Acute kidney injury is a severe complication following cardiopulmonary bypass (CPB) and is associated with capillary leakage and microcirculatory perfusion disturbances. CPB-induced thrombin release results in capillary hyperpermeability via activation of protease-activated receptor 1 (PAR1). We investigated whether aprotinin, which is thought to prevent thrombin from activating PAR1, preserves renal endothelial structure, reduces renal edema and preserves renal perfusion and reduces renal injury following CPB. Methods Rats were subjected to CPB after treatment with 33.000 KIU/kg aprotinin ( n = 15) or PBS ( n = 15) as control. A secondary dose of 33.000 KIU/kg aprotinin was given 60 min after initiation of CPB. Cremaster and renal microcirculatory perfusion were assessed using intravital microscopy and contrast echography before CPB and 10 and 60 min after weaning from CPB. Renal edema was determined by wet/dry weight ratio and renal endothelial structure by electron microscopy. Renal PAR1 gene and protein expression and markers of renal injury were determined. Results CPB reduced cremaster microcirculatory perfusion by 2.5-fold (15 (10–16) to 6 (2–10) perfused microvessels, p 〈 0.0001) and renal perfusion by 1.6-fold (202 (67–599) to 129 (31–292) au/sec, p = 0.03) in control animals. Both did not restore 60 min post-CPB. This was paralleled by increased plasma creatinine ( p 〈 0.01), neutrophil gelatinase-associated lipocalin (NGAL; p = 0.003) and kidney injury molecule-1 (KIM-1; p 〈 0.01). Aprotinin treatment preserved cremaster microcirculatory perfusion following CPB (12 (7–15) vs. 6 (2–10) perfused microvessels, p = 0.002), but not renal perfusion (96 (35–313) vs. 129 (31–292) au/s, p 〉 0.9) compared to untreated rats. Aprotinin treatment reduced endothelial gap formation (0.5 ± 0.5 vs. 3.1 ± 1.4 gaps, p 〈 0.0001), kidney wet/dry weight ratio (4.6 ± 0.2 vs. 4.4 ± 0.2, p = 0.046), and fluid requirements (3.9 ± 3.3 vs. 7.5 ± 3.0 ml, p = 0.006) compared to untreated rats. In addition, aprotinin treatment reduced tubulointerstitial neutrophil influx by 1.7-fold compared to untreated rats (30.7 ± 22.1 vs. 53.2 ± 17.2 neutrophil influx/section, p = 0.009). No differences were observed in renal PAR1 expression and plasma creatinine, NGAL or KIM-1 between groups. Conclusions Aprotinin did not improve renal perfusion nor reduce renal injury during the first hour following experimental CPB despite preservation of renal endothelial integrity and reduction of renal edema.

Type of Medium: Online Resource

ISSN: 2197-425X

URL: Article

DOI: 10.1186/s40635-021-00393-9

Language: English

Publisher: Springer Science and Business Media LLC

Publication Date: 2021

detail.hit.zdb_id: 2740385-3

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Effect of cisplatin exposure on platinum accumulation and growth inhibition in human neoplastic and normal squamous epithelial cells of the mucosa of the upper-aerodigestive tract

Braakhuis, Boudewijn J.M ; Welters, Marij J.P ; Cloos, Jacqueline ; [et al.]

Elsevier BV ; 1999

In: Cancer Letters Vol. 138, No. 1-2 ( 1999-4), p. 217-220

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In: Cancer Letters, Elsevier BV, Vol. 138, No. 1-2 ( 1999-4), p. 217-220

Type of Medium: Online Resource

ISSN: 0304-3835

URL: Article

DOI: 10.1016/S0304-3835(99)00016-6

Language: English

Publisher: Elsevier BV

Publication Date: 1999

detail.hit.zdb_id: 195674-7

detail.hit.zdb_id: 2004212-7

SSG: 12

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Dopamine induces lipid accumulation, NADPH oxidase-related oxidative stress, and a proinflammatory status of the plasma membrane in H9c2 cells

Begieneman, Mark P. V. ; ter Horst, Ellis N. ; Rijvers, Liza ; [et al.]

American Physiological Society ; 2016

In: American Journal of Physiology-Heart and Circulatory Physiology Vol. 311, No. 5 ( 2016-11-01), p. H1097-H1107

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In: American Journal of Physiology-Heart and Circulatory Physiology, American Physiological Society, Vol. 311, No. 5 ( 2016-11-01), p. H1097-H1107

Abstract: Excess catecholamine levels are suggested to be cardiotoxic and to underlie stress-induced heart failure. The cardiotoxic effects of norepinephrine and epinephrine are well recognized. However, although cardiac and circulating dopamine levels are also increased in stress cardiomyopathy patients, knowledge regarding putative toxic effects of excess dopamine levels on cardiomyocytes is scarce. We now studied the effects of elevated dopamine levels in H9c2 cardiomyoblasts. H9c2 cells were cultured and treated with dopamine (200 μM) for 6, 24, and 48 h. Subsequently, the effects on lipid accumulation, cell viability, flippase activity, reactive oxygen species (ROS) production, subcellular NADPH oxidase (NOX) protein expression, and ATP/ADP and GTP/GDP levels were analyzed. Dopamine did not result in cytotoxic effects after 6 h. However, after 24 and 48 h dopamine treatment induced a significant increase in lipid accumulation, nitrotyrosine levels, indicative of ROS production, and cell death. In addition, dopamine significantly reduced flippase activity and ATP/GTP levels, coinciding with phosphatidylserine exposure on the outer plasma membrane. Furthermore, dopamine induced a transient increase in cytoplasmic and (peri)nucleus NOX1 and NOX4 expression after 24 h that subsided after 48 h. Moreover, while dopamine induced a similar transient increase in cytoplasmic NOX2 and p47 phox expression, in the (peri)nucleus this increased expression persisted for 48 h where it colocalized with ROS. Exposure of H9c2 cells to elevated dopamine levels induced lipid accumulation, oxidative stress, and a proinflammatory status of the plasma membrane. This can, in part, explain the inflammatory response in patients with stress-induced heart failure.

Type of Medium: Online Resource

ISSN: 0363-6135 , 1522-1539

URL: Article

DOI: 10.1152/ajpheart.00633.2015

RVK:

WA 15000

Language: English

Publisher: American Physiological Society

Publication Date: 2016

detail.hit.zdb_id: 1477308-9

SSG: 12

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Lipid and Nucleocapsid N-Protein Accumulation in COVID-19 Patient Lung and Infected Cells

Grootemaat, Anita E. ; van der Niet, Sanne ; Scholl, Edwin R. ; [et al.]

American Society for Microbiology ; 2022

In: Microbiology Spectrum Vol. 10, No. 1 ( 2022-02-23)

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In: Microbiology Spectrum, American Society for Microbiology, Vol. 10, No. 1 ( 2022-02-23)

Abstract: The pandemic of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has caused a global outbreak and prompted an enormous research effort. Still, the subcellular localization of the coronavirus in lungs of COVID-19 patients is not well understood. Here, the localization of the SARS-CoV-2 proteins is studied in postmortem lung material of COVID-19 patients and in SARS-CoV-2-infected Vero cells, processed identically. Correlative light and electron microscopy on semithick cryo-sections demonstrated induction of electron-lucent, lipid-filled compartments after SARS-CoV-2 infection in both lung and cell cultures. In lung tissue, the nonstructural protein 4 and the stable nucleocapsid N-protein were detected on these novel lipid-filled compartments. The induction of such lipid-filled compartments and the localization of the viral proteins in lung of patients with fatal COVID-19 may explain the extensive inflammatory response and provide a new hallmark for SARS-CoV-2 infection at the final, fatal stage of infection. IMPORTANCE Visualization of the subcellular localization of SARS-CoV-2 proteins in lung patient material of COVID-19 patients is important for the understanding of this new virus. We detected viral proteins in the context of the ultrastructure of infected cells and tissues and discovered that some viral proteins accumulate in novel, lipid-filled compartments. These structures are induced in Vero cells but, more importantly, also in lung of patients with COVID-19. We have characterized these lipid-filled compartments and determined that this is a novel, virus-induced structure. Immunogold labeling demonstrated that cellular markers, such as CD63 and lipid droplet marker PLIN-2, are absent. Colocalization of lipid-filled compartments with the stable N-protein and nonstructural protein 4 in lung of the last stages of COVID-19 indicates that these compartments play a key role in the devastating immune response that SARS-CoV-2 infections provoke.

Type of Medium: Online Resource

ISSN: 2165-0497

URL: Article

DOI: 10.1128/spectrum.01271-21

Language: English

Publisher: American Society for Microbiology

Publication Date: 2022

detail.hit.zdb_id: 2807133-5

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