A5021498518- Ion Transport and Channel Regulation
- Pediatric Hepatobiliary Diseases and Treatments
- Drug Transport and Resistance Mechanisms
- Hormonal Regulation and Hypertension
- RNA Interference and Gene Delivery
- Mitochondrial Function and Pathology
- Cholesterol and Lipid Metabolism
- Polymer composites and self-healing
- ATP Synthase and ATPases Research
- Adipose Tissue and Metabolism
- CRISPR and Genetic Engineering
- Carbohydrate Chemistry and Synthesis
- Hepatitis B Virus Studies
- Synthesis of Organic Compounds
- Innovative Microfluidic and Catalytic Techniques Innovation
- Lipid metabolism and biosynthesis
- Cancer therapeutics and mechanisms
- Metabolomics and Mass Spectrometry Studies
- Renal function and acid-base balance
- Liver Disease and Transplantation
- 3D Printing in Biomedical Research
- Bacterial biofilms and quorum sensing
- RNA and protein synthesis mechanisms
Jožef Stefan Institute
2023
Consejo Nacional de Investigaciones Científicas y Técnicas
2015-2021
National University of Rosario
2015-2021
Tufts University
2017
Jean Mayer Human Nutrition Research Center on Aging
2017
University of Miami
2017
The adenoviral gene transfer of human aquaporin-1 (hAQP1) water channels to the liver 17α-ethinylestradiol-induced cholestatic rats improves bile flow, in part by enhancing canalicular hAQP1-mediated osmotic secretion. To gain insight into mechanisms 17α-ethinylestradiol cholestasis improvement, we studied biliary output salts (BS) and functional expression BS export pump (BSEP; ABCB11). Adenovector encoding hAQP1 (AdhAQP1) or control vector was administered retrograde intrabiliary infusion....
Lipopolysaccharides (LPS) are known to cause cholestasis in sepsis. There is evidence that a defective expression of canalicular aquaporin water channels contributes bile secretory failure LPS-induced cholestasis. Thus, we studied whether the hepatic adenovirus-mediated transfer human aquaporin-1 gene (haqp1) can improve induced by LPS. Adenoviral vector encoding hAQP1 (AdhAQP1) or control was administered rats retrograde intrabiliary infusion. Hepatocyte assessed liver immunostaining and...
Hepatocyte mitochondrial aquaporin-8 (mtAQP8) works as a multifunctional membrane channel protein that facilitates the uptake of ammonia for its detoxification to urea well release hydrogen peroxide. Since early oligonucleotide microarray studies in liver cholesterol-fed mice showed an AQP8 downregulation, we tested whether alterations cholesterol content per se modulate mtAQP8 expression human hepatocyte-derived Huh-7 cells. Cholesterol loading with methyl-β-cyclodextrin (mβCD):cholesterol...
This article reports experimental data related to the research entitled "Mitochondrial aquaporin-8 is involved in SREBP-controlled hepatocyte cholesterol biosynthesis" [Danielli et al., 2019]. We present about hydrogen peroxide (H2O2) release from mitochondria isolated rat hepatocytes with or without silencing of (AQP8) protein expression. The rate mitochondrial H2O2 (pmoles/min/mg protein) was found be decreased by 50% AQP8-knockdown mitochondria.
It has been proposed that, during metabolic acidosis, the liver downregulates mitochondrial ammonia detoxification via ureagenesis, a bicarbonate-consuming process. Since we previously demonstrated that hepatocyte aquaporin-8 channels (mtAQP8) facilitate uptake of and its metabolism into urea, studied whether mtAQP8 is involved in adaptive response to acidosis. Primary cultured rat hepatocytes were adapted acidosis by exposing them culture medium at pH 7.0 for 40 h. Control cells exposed...