Carotenoids in Sporidiobolus pararoseus ameliorate diabetic nephropathy in mice through attenuating oxidative stress
Abstract
Diabetic nephropathy (DN) is the major life-threatening complication of diabetes, and oxidative stress takes part in its initiation and development. This study was performed to evaluate the effects of carotenoids from Sporidiobolus pararoseus (CSP) on the renal function and oxidative stress status of mice with streptozotocin (STZ)-induced DN. The results indicated that CSP significantly attenuated symptoms of STZ-induced DN shown by decreased fasting blood glucose, reduced urine volume, urine albumin, serum creatinine and serum urea nitrogen, and improved kidney histological morphology. Furthermore, biochemical analysis of serum and kidney revealed a marked increase in oxidative stress of DN mice as evidenced by reduced total antioxidant capacity (T-AOC), decreased activity of antioxidant enzyme -superoxide dismutase (SOD) and increased level of malondialdehyde (MDA). However, treatment with CSP improved oxidative stress status in DN mice as compared with the mice in model group. Exploration of the potential mechanism validated that CSP ameliorated the oxidative stress status in DN mice by activating the expressions of Nrf2, NQO-1, HO-1, GST and CAT in kidney. These data revealed that CSP may retard the progression of DN by ameliorating renal function, improving the oxidative stress status and activating the Nrf2/ARE pathway.
Funding source: National Key Research and Development Program of China
Award Identifier / Grant number: 2017YFC1601806
Award Identifier / Grant number: 2018YFC1604202
Award Identifier / Grant number: 2017YFC1601704
Funding source: National first-class discipline program of Food Science and Technology
Award Identifier / Grant number: JUFSTR20180303
Funding source: Key Research and Development Program of Yantai, P. R. China
Award Identifier / Grant number: 2017ZH059
Acknowledgements
The research was conducted in the School of Food Science and Technology of Jiangnan University.
Author contributions: All the authors have accepted responsibility for the entire content of this submitted manuscript and approved submission.
Research funding: This work is supported by the National Key Research and Development Program of China (Project Nos. 2017YFC1601806, 2018YFC1604202, 2017YFC1601704), the National first-class discipline program of Food Science and Technology (JUFSTR20180303) and the Key Research and Development Program of Yantai, P. R. China (No. 2017ZH059).
Conflict of interest statement: The authors declare that they have no competing interests.
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Supplementary Material
The online version of this article offers supplementary material (https://doi.org/10.1515/hsz-2021-0127).
© 2021 Walter de Gruyter GmbH, Berlin/Boston
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- Research Articles/Short Communications
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- Structural and kinetic characterization of Porphyromonas gingivalis glutaminyl cyclase
- Molecular Medicine
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Articles in the same Issue
- Frontmatter
- Research Articles/Short Communications
- Protein Structure and Function
- Structural and kinetic characterization of Porphyromonas gingivalis glutaminyl cyclase
- Molecular Medicine
- Elucidating the anti-biofilm and anti-quorum sensing potential of selenocystine against respiratory tract infections causing bacteria: in vitro and in silico studies
- Carotenoids in Sporidiobolus pararoseus ameliorate diabetic nephropathy in mice through attenuating oxidative stress
- Cell Biology and Signaling
- Berberine improves dietary-induced cardiac remodeling by upregulating Kruppel-like factor 4-dependent mitochondrial function
- Decreased level of miR-1301 promotes colorectal cancer progression via activation of STAT3 pathway
- JMJD3-regulated expression of IL-6 is involved in the proliferation and chemosensitivity of acute myeloid leukemia cells
- Modulation of recombinant human alpha 1 glycine receptor by flavonoids and gingerols
- IL-24 inhibits the malignancy of human glioblastoma cells via destabilization of Zeb1
- Glycation of benign meningioma cells leads to increased invasion
- Proteolysis
- Marked difference in efficiency of the digestive enzymes pepsin, trypsin, chymotrypsin, and pancreatic elastase to cleave tightly folded proteins