Chaperoning Against Amyloid Aggregation: Monitoring In Vitro and In Vivo

  • Ravichandran Vignesh
  • Gopala Krishna AradhyamEmail author
Part of the Methods in Molecular Biology book series (MIMB, volume 1929)


Protein aggregation and inclusion body formation have been a key causal phenomenon behind a majority of neurodegenerative disorders. Various approaches aimed at preventing the formation/elimination of protein aggregates are being developed to control these diseases. Molecular chaperones are a class of protein that not only direct the functionally relevant fold of the protein but also perform quality control against stress, misfolding/aggregation. Genes that encode molecular chaperones are induced and expressed in response to extreme stress conditions to “salvage” the cell by the “unfolded protein response” (UPR) signaling pathway. Here we describe in detail the various in vitro and in vivo assays involved in identifying the chaperone activity of proteins using human calnuc as a model protein. Calnuc is a Golgi resident, calcium-binding protein, identified as chaperone protein and is reported to protect the cells against the cytotoxicity caused by amyloidosis and ER stress. Calnuc is also reported to regulate Gαi activity and inflammation apart from the role of chaperoning against amyloid proteins.

Key words

Protein aggregation Molecular chaperones Misfolding Calnuc Calcium Stress 


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Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2019

Authors and Affiliations

  • Ravichandran Vignesh
    • 1
  • Gopala Krishna Aradhyam
    • 1
    Email author
  1. 1.Signal Transduction Laboratory, Department of Biotechnology, Bhupat and Jyoti Mehta School of BiosciencesIndian Institute of Technology MadrasChennaiIndia

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