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      Protective role of l‐threonine against cadmium toxicity in Saccharomyces cerevisiae

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      https://www.riss.kr/link?id=O106360016

      • 저자
      • 발행기관
      • 학술지명
      • 권호사항
      • 발행연도

        2021년

      • 작성언어

        -

      • Print ISSN

        0233-111X

      • Online ISSN

        1521-4028

      • 등재정보

        SCOPUS;SCIE

      • 자료형태

        학술저널

      • 수록면

        339-350   [※수록면이 p5 이하이면, Review, Columns, Editor's Note, Abstract 등일 경우가 있습니다.]

      • 구독기관
        • 전북대학교 중앙도서관  
        • 성균관대학교 중앙학술정보관  
        • 부산대학교 중앙도서관  
        • 전남대학교 중앙도서관  
        • 제주대학교 중앙도서관  
        • 중앙대학교 서울캠퍼스 중앙도서관  
        • 인천대학교 학산도서관  
        • 숙명여자대학교 중앙도서관  
        • 서강대학교 로욜라중앙도서관  
        • 계명대학교 동산도서관  
        • 충남대학교 중앙도서관  
        • 한양대학교 백남학술정보관  
        • 이화여자대학교 중앙도서관  
        • 고려대학교 도서관  
      • ⓒ COPYRIGHT THE BRITISH LIBRARY BOARD: ALL RIGHT RESERVED
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      다국어 초록 (Multilingual Abstract)

      Environment and food contamination with cadmium (Cd) can cause serious toxicity, posing a severe threat to agricultural production and human health. However, how amino acids contribute to defenses against oxidative stress caused by Cd in cells is not ...

      Environment and food contamination with cadmium (Cd) can cause serious toxicity, posing a severe threat to agricultural production and human health. However, how amino acids contribute to defenses against oxidative stress caused by Cd in cells is not fully understood. As a model eukaryote with a relatively clear genetic background, Saccharomyces cerevisiae has been commonly used in Cd toxicity research. To gain insight into Cd toxicity and cell defenses against it, 20 amino acids were screened for protective roles against Cd stress in S. cerevisiae. The results showed that threonine (Thr, T) had the strongest protective effect against Cd‐induced mortality and membrane damage in the cells. Compared to the antioxidant vitamin C (VC), Thr exhibited a higher efficacy in restoring the superoxide dismutase (SOD) activity that was inhibited by Cd but not by H2O2 in vivo. Thr exhibited evident DPPH (2,2‐diphenyl‐1‐picrylhydrazyl) activity but weak ABTS (2,2′‐azino‐bis(3‐ethylbenzothiazoline‐6‐9 sulfonic acid)) scavenging activity, giving it a weaker effect against Cd‐induced lipid peroxidation and superoxide radical O2−, compared to VC. More importantly, compared to the chelating agent EDTA, Thr showed stronger chelation of Cd, giving it a stronger protective effect on SOD against Cd than VC in vitro. The results of the in vivo and in vitro experiments revealed that the role Thr plays in cell defenses against Cd may be attributed to its protection of the SOD enzyme, predominantly through the preferential chelation of Cd. Our results provide insights into the protective mechanisms of amino acid Thr that ameliorate Cd toxicity and suggest that a supplement of Thr might help to reduce Cd‐induced oxidative damage.

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