Background: Oxidative stress and inflammation play important roles in high-fat diet (HFD) induced kidney damage. Previous studies show that the collagen extracted from the skin of monkfish () with pepsin (pepsin-solubilized collagen, PSC) exhibits good biological activities. This study investigates the protective effect of PSCP against chronic kidney injury in HFD-fed mice.
Methods: Pepsin-solubilized collagen was further hydrolyzed into collagen peptides, and the compound with the best 2,2-diphenyl-1-picrylhydrazyl (DPPH) clearance rate was named pepsin-solubilized collagen peptide (PSCP). A group of mice were fed an HFD for 4 weeks, and then for another 6 weeks PSCP was added to their diet at the amount of either 100 or 200 mg/kg.
Results: Pepsin-solubilized collagen peptide treatment (200 mg/kg) reduced the mice's serum levels of uric acid (UA), creatinine (CRE), and blood urea nitrogen (BUN) by 27, 20, and 37%, respectively. This treatment also remarkably improved renal histopathology. Moreover, the activities of superoxide dismutase (SOD), glutathione peroxidase (GSH-Px), and catalase (CAT) were increased by 96, 52, and 74%, respectively, and decreased the malondialdehyde (MDA) level by 36%. Additionally, PSCP activated the Nrf2 pathway and inhibited NLRP3 signaling to significantly reduce the levels of inflammatory cytokines IL-1β, IL-6, and TNF-α.
Conclusions: Our results indicate that compound PSCP has the potential to prevent or control chronic kidney damage.
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http://dx.doi.org/10.3389/fnut.2022.798708 | DOI Listing |
PeerJ
October 2024
Institute of Integrated Science and Technology, Nagasaki University, Nagasaki, Japan.
Acta Biomater
September 2024
Faculty of Engineering, School of Mechanical, Medical and Process Engineering, Queensland University of Technology, Brisbane, Australia; Centre for Biomedical Technologies, Queensland University of Technology, Brisbane, Australia; ARC Training Centre for Cell and Tissue Engineering Technologies, Queensland University of Technology, Brisbane, Australia; Max Planck Queensland Centre (MPQC) for the Materials Science of Extracellular Matrices, Queensland University of Technology, Brisbane, Australia; Centre for Microbiome Research, Queensland University of Technology, Brisbane, Australia. Electronic address:
Decellularized extracellular matrix (dECM) hydrogels provide tissue-specific microenvironments which accommodate physiological cellular phenotypes in 3D in vitro cell cultures. However, their formation hinges on collagen fibrillogenesis, a complex process which limits regulation of physicochemical properties. Hence, achieving reproducible results with dECM hydrogels poses as a challenge.
View Article and Find Full Text PDFFood Chem
September 2023
College of Ocean Food and Biological Engineering, Jimei University, Xiamen 361021, China. Electronic address:
Many factors are responsible for the diminished quality of shrimp during cold storage, while the role of collagen has rarely been studied. This study therefore investigated the relationship between collagen degradation and changes of textural properties of Pacific white shrimp, and its hydrolysis by endogenous proteinases. The textural properties of shrimp decreased gradually along with disruption of shrimp muscle tissues, and the chewiness property of shrimp muscle showed a linear relationship with collagen contents in muscle during 6-day-storage at 4 °C.
View Article and Find Full Text PDFGels
December 2022
Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao 266071, China.
Acid-solubilized (ASC) and pepsin-solubilized collagen (PSC) extracted at 4 °C (ASC-4 and PSC-4), 12 °C (ASC-12 and PSC-12), and 20 °C (ASC-20 and PSC-20) from the skin of farmed pufferfish () was characterized by SDS-polyacrylamide gel electrophoresis (SDS-PAGE), Fourier-transform infrared spectroscopy (FTIR), and fibril-forming tests. The results indicate that extraction at 12 °C can effectively improve the extraction efficiency of natural collagen compared with extraction at 4 °C. However, extraction at 20 °C results in a decrease in molecular integrity, thus, inducing the resultant collagen to degrade or even lose fibril-forming ability.
View Article and Find Full Text PDFPolymers (Basel)
December 2022
Department of Fishery Products, Faculty of Fisheries, Kasetsart University, Bangkok 10900, Thailand.
The tail tendons of skipjack tuna (), a by-product from the meat-separation process in canned-tuna production, was used as an alternative source of collagen extraction. The acid-solubilized collagens using vinegar (VTC) and acetic-acid (ATC) extraction and pepsin-solubilized collagen (APTC) were extracted from tuna-tail tendon. The physiochemical properties and characteristics of those collagens were investigated.
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