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  1. Article: Mitochondria Endoplasmic Reticulum Contact Sites (MERCs): Proximity Ligation Assay as a Tool to Study Organelle Interaction.

    Benhammouda, Sara / Vishwakarma, Anjali / Gatti, Priya / Germain, Marc

    Frontiers in cell and developmental biology

    2021  Volume 9, Page(s) 789959

    Abstract: Organelles cooperate with each other to regulate vital cellular homoeostatic functions. This occurs through the formation of close connections through membrane contact sites. Mitochondria-Endoplasmic-Reticulum (ER) contact sites (MERCS) are one of such ... ...

    Abstract Organelles cooperate with each other to regulate vital cellular homoeostatic functions. This occurs through the formation of close connections through membrane contact sites. Mitochondria-Endoplasmic-Reticulum (ER) contact sites (MERCS) are one of such contact sites that regulate numerous biological processes by controlling calcium and metabolic homeostasis. However, the extent to which contact sites shape cellular biology and the underlying mechanisms remain to be fully elucidated. A number of biochemical and imaging approaches have been established to address these questions, resulting in the identification of a number of molecular tethers between mitochondria and the ER. Among these techniques, fluorescence-based imaging is widely used, including analysing signal overlap between two organelles and more selective techniques such as
    Language English
    Publishing date 2021-12-03
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2737824-X
    ISSN 2296-634X
    ISSN 2296-634X
    DOI 10.3389/fcell.2021.789959
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Methylglyoxal induces glycation and oxidative stress in Saccharomyces cerevisiae

    Tupe, Rashmi S / Vishwakarma, Anjali / Solaskar, Anamika / Prajapati, Anali

    Annals of microbiology. 2019 Nov., v. 69, no. 11

    2019  

    Abstract: PURPOSE: Hyperglycemia causes abnormal accumulation of methylglyoxal (MGO) and concomitant DNA, protein glycation. These pathophysiological changes further leads to diabetic complications. Yeast Saccharomyces cerevisiae is one of the best model to study ... ...

    Abstract PURPOSE: Hyperglycemia causes abnormal accumulation of methylglyoxal (MGO) and concomitant DNA, protein glycation. These pathophysiological changes further leads to diabetic complications. Yeast Saccharomyces cerevisiae is one of the best model to study MGO-induced glycation modifications. The aim of the present study was to investigate the effect of MGO on protein, DNA glycation, and oxidative stress markers using S. cerevisiae as a system. METHODS: Saccharomyces cerevisiae cells were incubated with 8 mM of MGO for 4 h and 24 h. After incubation, protein and DNA samples were isolated from the lysed cells. The samples were analyzed for various glycation (fructosamine, β-amyloid, free amino group, free thiol group, and hyperchromic shift analysis) and oxidative stress markers (total antioxidant potential, catalase, glutathione, and lipid peroxidation). RESULTS: MGO (8 mM) acted as a potent glycating agent, causing protein and DNA glycation in treated yeast cells. The glycation markers fructosamine and β-amyloid were significantly elevated when incubated for 4 h as compared to 24 h. Oxidative stress in the glycated yeast cells alleviated cellular antioxidant capacity and reduced the cell viability. CONCLUSION: MGO caused significant glycation modifications of proteins and DNA in yeast cells. It also triggered increase in intracellular oxidative stress. MGO-induced protein, DNA glycation, and oxidative stress in S. cerevisiae indicate the suitability of the yeast model to study various biochemical pathways involved in diabetic complications and even conformational pathologies.
    Keywords DNA ; Saccharomyces cerevisiae ; antioxidant activity ; biochemical pathways ; catalase ; cell viability ; diabetic complications ; glutathione ; glycation ; hyperglycemia ; lipid peroxidation ; models ; oxidative stress ; proteins ; thiols ; yeasts
    Language English
    Dates of publication 2019-11
    Size p. 1165-1175.
    Publishing place Springer International Publishing
    Document type Article
    ZDB-ID 2143009-3
    ISSN 1869-2044 ; 1590-4261
    ISSN (online) 1869-2044
    ISSN 1590-4261
    DOI 10.1007/s13213-019-01498-z
    Database NAL-Catalogue (AGRICOLA)

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