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Please use this identifier to cite or link to this item: http://repository.iitr.ac.in/handle/123456789/1293
Title: Polyphenolic flavonoid (Myricetin) upregulated proteasomal degradation mechanisms: Eliminates neurodegenerative proteins aggregation
Authors: Joshi V.
Mishra R.
Upadhyay A.
Amanullah A.
Poluri K.M.
Singh S.
Kumar A.
Mishra A.
Published in: Journal of Cellular Physiology
Abstract: Major neurodegenerative disorders are characterized by the formation of misfolded proteins aggregates inside or outside the neuronal cells. Previous studies suggest that aberrant proteins aggregates play a critical role in protein homeostasis imbalance and failure of protein quality control (PQC) mechanism, leading to disease conditions. However, we still do not understand the precise mechanisms of PQC failure and cellular dysfunctions associated with neurodegenerative diseases caused by the accumulation of protein aggregates. Here, we show that Myricetin, a flavonoid, can eliminate various abnormal proteins from the cellular environment via modulating endogenous levels of Hsp70 chaperone and quality control (QC)-E3 ubiquitin ligase E6-AP. We have observed that Myricetin treatment suppresses the aggregation of different aberrant proteins. Myricetin also enhances the elimination of various toxic neurodegenerative diseases associated proteins from the cells, which could be reversed by the addition of putative proteasome inhibitor (MG132). Remarkably, Myricetin can also stabilize E6-AP and reduce the misfolded proteins inclusions, which further alleviates cytotoxicity. Taken together these findings suggested that new mechanistic and therapeutic insights based on small molecules mediated regulation of disturbed protein quality control mechanism, which may result in the maintenance of the state of proteostasis. © 2019 Wiley Periodicals, Inc.
Citation: Journal of Cellular Physiology(2019), 234(11): 20900-20914
URI: https://doi.org/10.1002/jcp.28695
http://repository.iitr.ac.in/handle/123456789/1293
Issue Date: 2019
Publisher: Wiley-Liss Inc.
Keywords: chaperone
E6-AP
misfolded proteins
Myricetin
neurodegeneration
proteasome
ISSN: 219541
Author Scopus IDs: 56189143600
56767511300
57189335137
56188291700
55842079400
8621706700
57211078554
57203290989
Author Affiliations: Joshi, V., Cellular and Molecular Neurobiology Unit, Indian Institute of Technology, Jodhpur, Rajasthan, India
Mishra, R., Cellular and Molecular Neurobiology Unit, Indian Institute of Technology, Jodhpur, Rajasthan, India
Upadhyay, A., Cellular and M
Funding Details: Support for this work was obtained from Science & Engineering Research Board (SERB); Department of Science & Technology, Government of India grant to (AM) EMR/ 2016/000716; Ramalinganswami Fellowship, Department of Biotechnology, Governement of India, Gra
Corresponding Author: Mishra, A.; Cellular and Molecular Neurobiology Unit, Indian Institute of TechnologyIndia; email: amit@iitj.ac.in
Appears in Collections:Journal Publications [BT]

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