Background: Ischemia/reperfusion injury in organ transplantation is a multifactor process that may lead to delayed graft function (DGF), and has a significant impact on short- and long-term graft survival. The activation of the renin-angiotensin system may be important in the pathophysiology of DGF. Preservation solutions are thought to diminish the ischemic injury, and appropriate choice of the solution should contribute to improved graft function and better prognosis for graft survival. The aim of this study was to examine the effect of preservation solutions UW and EC on the expression of renin I, angiotensinogen and angiotensin I-converting enzyme genes in rat kidney.
Material/methods: The study was carried out on Wistar rat kidneys divided into 3 groups: kidneys perfused with 0.9% NaCl (control group), with UW preservation solution, and with EC preservation solution. We investigated the expressions of renin I, angiotensinogen- and angiotensin I-converting enzyme genes in kidneys perfused with EC and UW solutions after 12 min (minutes) and 24 h (hours) of cold ischemia and 30 min of warm ischemia.
Results: The perfusion with UW and EC solution caused an increase of renin I, angiotensinogen and angiotensin I-converting enzyme genes expression in kidneys. This increase was enhanced in kidneys perfused with UW solution in comparison with kidneys perfused with EC solution. The 24 h preservation with UW solution resulted in a decrease of renin-angiotensin activity increased in cold ischemia.
Conclusions: UW preservation of 24 h decreased renin-angiotensin system activity activated in cold ischemia but not in warm ischemia.
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http://dx.doi.org/10.12659/aot.882002 | DOI Listing |
Chem Pharm Bull (Tokyo)
December 2024
Department of Pharmacognosy, Faculty of Pharmaceutical Sciences, Nagasaki International University.
Sesame (Sesamum indicum L.) is an important oilseed crop, and its seeds are a source of edible oil and widely used as a nutritious food that is beneficial to health in oriental countries. Phytochemical and biological investigations of the seeds have been well reported; however, those of the leaves have been limited.
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December 2024
Center for Research Innovation and Biomedical Informatics, Faculty of Medical Technology, Mahidol University, Bangkok 10700, Thailand. Electronic address:
Identifying angiotensin-I-converting enzyme (ACE) inhibitory peptides accurately is crucial for understanding the primary factor that regulates the renin-angiotensin system and for providing guidance in developing new potential drugs. Given the inherent experimental complexities, using computational methods for in silico peptide identification could be indispensable for facilitating the high-throughput characterization of ACE inhibitory peptides. In this paper, we propose a novel deep stacking-based ensemble learning framework, termed Deepstack-ACE, to precisely identify ACE inhibitory peptides.
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December 2024
School of Food Science and Engineering, South China University of Technology, Guangzhou 510640, China; Guangdong Food Green Processing and Nutrition Regulation Technologies Research Center, Guangzhou 510650, China. Electronic address:
Soybean peptide (SP) exhibits significant angiotensin-I-converting enzyme inhibitory (ACEI) activity, however, its strong bitterness restricts its use in food industry. This study aimed to reduce the bitterness of SP by natural deep eutectic solvent (NADES)-driven Maillard reaction (MR). Results showed that both the mixtures of Glucose-NADES and the Glucose-Xylose-NADES formed the hydrogen bonds and shown good thermal stability analyzed by using Fourier transform infrared (FTIR), Differential scanning calorimetry (DSC) and Thermogravimetric analysis (TGA).
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December 2024
Key Laboratory of Aquatic Product Processing, Ministry of Agriculture and Rural Affairs, National R&D Center for Aquatic Product Processing, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou, China.
Introduction: Hypertension is a chronic cardiovascular disease, which can trigger some disease such as heart failure, loss of vision or kidney. There were various peptides derived from food that are recognized for their ability to inhibit ACE activity, potentially leading to a reduction in blood pressure levels . The primary objective of this research is to discover ACE inhibitory peptides from protein hydrolysates of eel bone collagen (EBCHs).
View Article and Find Full Text PDFInt J Mol Sci
November 2024
Clinical and Research Laboratory (LACIUS, C.N., CONAHCYT National Laboratory, LANIBIOC), Deparment of Chemical, Biological, and Agricultural Sciences (DC-QB), Faculty of Biological and Health Sciences, University of Sonora, Navojoa 85880, Sonora, Mexico.
Lupin ( L.) proteins are potential sources of bioactive peptides (LBPs) that can inhibit dipeptidyl peptidase IV (DPP-IV) and angiotensin I-converting enzyme (ACE-I) activity. However, the capacity of different enzymes to release LBPs, the pharmacokinetic and bioactivities of the peptides released, and their binding affinities with the active sites of DPP-IV and ECA-I are topics scarcely addressed.
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