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Article ; Online: Omaveloxolone (Skyclarys

Dayalan Naidu, Sharadha / Dinkova-Kostova, Albena T

2023 Volume 44, Issue 6, Page(s) 394–395

MeSH term(s)	Humans ; Friedreich Ataxia/drug therapy ; Triterpenes
Chemical Substances	omaveloxolone (G69Z98951Q) ; Triterpenes
Language	English
Publishing date	2023-05-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	282846-7
ISSN	1873-3735 ; 0165-6147
ISSN (online)	1873-3735
ISSN	0165-6147
DOI	10.1016/j.tips.2023.03.005
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Zs.A 1513: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 6: Show issues

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Article ; Online: KEAP1, a cysteine-based sensor and a drug target for the prevention and treatment of chronic disease.

Dayalan Naidu, Sharadha / Dinkova-Kostova, Albena T

Open biology

2020 Volume 10, Issue 6, Page(s) 200105

Abstract: Redox imbalance and persistent inflammation are the underlying causes of most chronic diseases. Mammalian cells have evolved elaborate mechanisms for restoring redox homeostasis and resolving acute inflammatory responses. One prominent mechanism is that ... ...

Abstract	Redox imbalance and persistent inflammation are the underlying causes of most chronic diseases. Mammalian cells have evolved elaborate mechanisms for restoring redox homeostasis and resolving acute inflammatory responses. One prominent mechanism is that of inducing the expression of antioxidant, anti-inflammatory and other cytoprotective proteins, while also suppressing the production of pro-inflammatory mediators, through the activation of transcription factor nuclear factor-erythroid 2 p45-related factor 2 (NRF2). At homeostatic conditions, NRF2 is a short-lived protein, which avidly binds to Kelch-like ECH-associated protein 1 (KEAP1). KEAP1 functions as (i) a substrate adaptor for a Cullin 3 (CUL3)-based E3 ubiquitin ligase that targets NRF2 for ubiquitination and proteasomal degradation, and (ii) a cysteine-based sensor for a myriad of physiological and pharmacological NRF2 activators. Here, we review the intricate molecular mechanisms by which KEAP1 senses electrophiles and oxidants. Chemical modification of specific cysteine sensors of KEAP1 results in loss of NRF2-repressor function and alterations in the expression of NRF2-target genes that encode large networks of diverse proteins, which collectively restore redox balance and resolve inflammation, thus ensuring a comprehensive cytoprotection. We focus on the cyclic cyanoenones, the most potent NRF2 activators, some of which are currently in clinical trials for various pathologies characterized by redox imbalance and inflammation.
MeSH term(s)	Chronic Disease/drug therapy ; Chronic Disease/prevention & control ; Clinical Trials as Topic ; Humans ; Kelch-Like ECH-Associated Protein 1/chemistry ; Kelch-Like ECH-Associated Protein 1/metabolism ; Models, Molecular ; Molecular Targeted Therapy ; NF-E2-Related Factor 2/chemistry ; NF-E2-Related Factor 2/metabolism ; Proteasome Endopeptidase Complex/metabolism ; Small Molecule Libraries/pharmacology ; Small Molecule Libraries/therapeutic use ; Ubiquitination
Chemical Substances	KEAP1 protein, human ; Kelch-Like ECH-Associated Protein 1 ; NF-E2-Related Factor 2 ; NFE2L2 protein, human ; Small Molecule Libraries ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2020-06-24
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2630944-0
ISSN	2046-2441 ; 2046-2441
ISSN (online)	2046-2441
ISSN	2046-2441
DOI	10.1098/rsob.200105
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Article ; Online: Detection of thermal shift in cellular Keap1 by protein-protein interaction inhibitors using immunoblot- and fluorescence microplate-based assays.

Dayalan Naidu, Sharadha / Dikovskaya, Dina / Moore, Terry W / Dinkova-Kostova, Albena T

STAR protocols

2022 Volume 3, Issue 2, Page(s) 101265

Abstract: Pharmacologic inhibition of the protein-protein interaction (PPI) interface of the Keap1:Nrf2 complex, which leads to Nrf2 activation and cytoprotective gene expression, offers a promising strategy for disease prevention and treatment. To facilitate ... ...

Abstract	Pharmacologic inhibition of the protein-protein interaction (PPI) interface of the Keap1:Nrf2 complex, which leads to Nrf2 activation and cytoprotective gene expression, offers a promising strategy for disease prevention and treatment. To facilitate identification and validation of small-molecule Keap1:Nrf2 PPI inhibitors in the cellular environment in a low- and medium-throughput manner, we detail two adapted cellular thermal shift assay (CETSA) protocols, Keap1-CETSA, an immunoblotting-based methodology for detecting endogenous Keap1, and Keap1-Glow CETSA, a microtiter plate assay of overexpressed fluorescently-tagged Keap1. For an example of the use and execution of this protocol, please refer to Dayalan Naidu et al. (2021).
MeSH term(s)	Biological Assay ; Immunoblotting ; Kelch-Like ECH-Associated Protein 1/genetics ; NF-E2-Related Factor 2/genetics ; Protein Binding
Chemical Substances	Kelch-Like ECH-Associated Protein 1 ; NF-E2-Related Factor 2
Language	English
Publishing date	2022-04-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2666-1667
ISSN (online)	2666-1667
DOI	10.1016/j.xpro.2022.101265
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Article ; Online: Author Correction: C151 in KEAP1 is the main cysteine sensor for the cyanoenone class of NRF2 activators, irrespective of molecular size or shape.

Dayalan Naidu, Sharadha / Muramatsu, Aki / Saito, Ryota / Asami, Soichiro / Honda, Tadashi / Hosoya, Tomonori / Itoh, Ken / Yamamoto, Masayuki / Suzuki, Takafumi / Dinkova-Kostova, Albena T

Scientific reports

2024 Volume 14, Issue 1, Page(s) 4774

Language	English
Publishing date	2024-02-27
Publishing country	England
Document type	Published Erratum
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-024-55265-5
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Article: Pirin, an Nrf2-Regulated Protein, Is Overexpressed in Human Colorectal Tumors

Zhang, Ying / Knatko, Elena V. / Higgins, Maureen / Dayalan Naidu, Sharadha / Smith, Gillian / Honda, Tadashi / de la Vega, Laureano / Dinkova-Kostova, Albena T.

Antioxidants. 2022 Jan. 28, v. 11, no. 2

2022

Abstract: The evolutionary conserved non-heme Fe-containing protein pirin has been implicated as an important factor in cell proliferation, migration, invasion, and tumour progression of melanoma, breast, lung, cervical, prostate, and oral cancers. Here we found ... ...

Abstract	The evolutionary conserved non-heme Fe-containing protein pirin has been implicated as an important factor in cell proliferation, migration, invasion, and tumour progression of melanoma, breast, lung, cervical, prostate, and oral cancers. Here we found that pirin is overexpressed in human colorectal cancer in comparison with matched normal tissue. The overexpression of pirin correlates with activation of transcription factor nuclear factor erythroid 2 p45-related factor 2 (Nrf2) and increased expression of the classical Nrf2 target NAD(P)H:quinone oxidoreductase 1 (NQO1), but interestingly and unexpectedly, not with expression of the aldo-keto reductase (AKR) family members AKR1B10 and AKR1C1, which are considered to be the most overexpressed genes in response to Nrf2 activation in humans. Using pharmacologic and genetic approaches to either downregulate or upregulate Nrf2, we show that pirin is regulated by Nrf2 in human and mouse cells and in the mouse colon in vivo. The small molecule pirin inhibitor TPhA decreased the viability of human colorectal cancer (DLD1) cells, but this decrease was independent of the levels of pirin. Our study demonstrates the Nrf2-dependent regulation of pirin and encourages the pursuit for specific pirin inhibitors.
Keywords	aldo-keto reductases ; breasts ; cell proliferation ; colon ; colorectal neoplasms ; humans ; lungs ; melanoma ; mice ; neoplasm progression ; transcription factors ; viability
Language	English
Dates of publication	2022-0128
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
ZDB-ID	2704216-9
ISSN	2076-3921
ISSN	2076-3921
DOI	10.3390/antiox11020262
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Regulation of the mammalian heat shock factor 1.

Dayalan Naidu, Sharadha / Dinkova-Kostova, Albena T

The FEBS journal

2017 Volume 284, Issue 11, Page(s) 1606–1627

Abstract: Living organisms are endowed with the capability to tackle various forms of cellular stress due to the presence of molecular chaperone machinery complexes that are ubiquitous throughout the cell. During conditions of proteotoxic stress, the transcription ...

Abstract	Living organisms are endowed with the capability to tackle various forms of cellular stress due to the presence of molecular chaperone machinery complexes that are ubiquitous throughout the cell. During conditions of proteotoxic stress, the transcription factor heat shock factor 1 (HSF1) mediates the elevation of heat shock proteins, which are crucial components of the chaperone complex machinery and function to ameliorate protein misfolding and aggregation and restore protein homeostasis. In addition, HSF1 orchestrates a versatile transcriptional programme that includes genes involved in repair and clearance of damaged macromolecules and maintenance of cell structure and metabolism, and provides protection against a broad range of cellular stress mediators, beyond heat shock. Here, we discuss the structure and function of the mammalian HSF1 and its regulation by post-translational modifications (phosphorylation, sumoylation and acetylation), proteasomal degradation, and small-molecule activators and inhibitors.
MeSH term(s)	Acetylation ; Adaptation, Physiological/genetics ; Adaptation, Physiological/physiology ; Animals ; DNA-Binding Proteins/agonists ; DNA-Binding Proteins/antagonists & inhibitors ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/physiology ; Gene Expression Regulation ; Heat Shock Transcription Factors ; Hot Temperature ; Mammals/genetics ; Mammals/physiology ; Models, Molecular ; Phosphorylation ; Phylogeny ; Proteasome Endopeptidase Complex/metabolism ; Protein Conformation ; Protein Folding ; Protein Processing, Post-Translational ; Stress, Physiological/genetics ; Stress, Physiological/physiology ; Sumoylation ; Transcription Factors/agonists ; Transcription Factors/antagonists & inhibitors ; Transcription Factors/chemistry ; Transcription Factors/physiology ; Transcription, Genetic
Chemical Substances	DNA-Binding Proteins ; Heat Shock Transcription Factors ; Transcription Factors ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2017-02-01
Publishing country	England
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.13999
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Zs.A 260: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

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Article ; Online: Nrf2 depletion in the context of loss-of-function Keap1 leads to mitolysosome accumulation.

Dayalan Naidu, Sharadha / Angelova, Plamena R / Knatko, Elena V / Leonardi, Chiara / Novak, Miroslav / de la Vega, Laureano / Ganley, Ian G / Abramov, Andrey Y / Dinkova-Kostova, Albena T

Free radical biology & medicine

2023 Volume 208, Page(s) 478–493

Abstract: Transcription factor nuclear factor erythroid 2 p45-related factor 2 (Nrf2) is the principal determinant of the cellular redox homeostasis, contributing to mitochondrial function, integrity and bioenergetics. The main negative regulator of Nrf2 is Kelch- ... ...

Abstract	Transcription factor nuclear factor erythroid 2 p45-related factor 2 (Nrf2) is the principal determinant of the cellular redox homeostasis, contributing to mitochondrial function, integrity and bioenergetics. The main negative regulator of Nrf2 is Kelch-like ECH associated protein 1 (Keap1), a substrate adaptor for Cul3/Rbx1 ubiquitin ligase, which continuously targets Nrf2 for ubiquitination and proteasomal degradation. Loss-of-function mutations in Keap1 occur frequently in lung cancer, leading to constitutive Nrf2 activation. We used the human lung cancer cell line A549 and its CRISPR/Cas9-generated homozygous Nrf2-knockout (Nrf2-KO) counterpart to assess the role of Nrf2 on mitochondrial health. To confirm that the observed effects of Nrf2 deficiency are not due to clonal selection or long-term adaptation to the absence of Nrf2, we also depleted Nrf2 by siRNA (siNFE2L2), thus creating populations of Nrf2-knockdown (Nrf2-KD) A549 cells. Nrf2 deficiency decreased mitochondrial respiration, but increased the mitochondrial membrane potential, mass, DNA content, and the number of mitolysosomes. The proportion of ATG7 and ATG3 within their respective LC3B conjugates was increased in Nrf2-deficient cells with mutant Keap1, whereas the formation of new autophagosomes was not affected. Thus, in lung cancer cells with loss-of-function Keap1, Nrf2 facilitates mitolysosome degradation thereby ensuring timely clearance of damaged mitochondria.
MeSH term(s)	Humans ; Cullin Proteins/genetics ; Cullin Proteins/metabolism ; Intracellular Signaling Peptides and Proteins/genetics ; Intracellular Signaling Peptides and Proteins/metabolism ; Kelch-Like ECH-Associated Protein 1/genetics ; Kelch-Like ECH-Associated Protein 1/metabolism ; Lung Neoplasms/genetics ; NF-E2-Related Factor 2/genetics ; NF-E2-Related Factor 2/metabolism ; Mitochondria/metabolism ; A549 Cells
Chemical Substances	Cullin Proteins ; Intracellular Signaling Peptides and Proteins ; Kelch-Like ECH-Associated Protein 1 ; NF-E2-Related Factor 2
Language	English
Publishing date	2023-09-14
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	807032-5
ISSN	1873-4596 ; 0891-5849
ISSN (online)	1873-4596
ISSN	0891-5849
DOI	10.1016/j.freeradbiomed.2023.09.009
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Zs.A 2109: Show issues

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Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

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Article: Regulation of the mammalian heat shock factor 1

Dayalan Naidu, Sharadha / Albena T. DinkovaâKostova

FEBS journal. 2017 June, v. 284, no. 11

2017

Abstract	Living organisms are endowed with the capability to tackle various forms of cellular stress due to the presence of molecular chaperone machinery complexes that are ubiquitous throughout the cell. During conditions of proteotoxic stress, the transcription factor heat shock factor 1 (HSF1) mediates the elevation of heat shock proteins, which are crucial components of the chaperone complex machinery and function to ameliorate protein misfolding and aggregation and restore protein homeostasis. In addition, HSF1 orchestrates a versatile transcriptional programme that includes genes involved in repair and clearance of damaged macromolecules and maintenance of cell structure and metabolism, and provides protection against a broad range of cellular stress mediators, beyond heat shock. Here, we discuss the structure and function of the mammalian HSF1 and its regulation by postâtranslational modifications (phosphorylation, sumoylation and acetylation), proteasomal degradation, and smallâmolecule activators and inhibitors.
Keywords	acetylation ; cell structures ; genes ; heat shock proteins ; heat stress ; homeostasis ; mammals ; phosphorylation ; post-translational modification ; protein folding ; transcription (genetics) ; transcription factors
Language	English
Dates of publication	2017-06
Size	p. 1606-1627.
Publishing place	John Wiley & Sons, Ltd
Document type	Article
Note	REVIEW
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.13999
Database	NAL-Catalogue (AGRICOLA)

In stock of ZB MED Bonn / Germany

Z 2006/704: Show issues

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Article ; Online: The Cell-Permeable Derivative of the Immunoregulatory Metabolite Itaconate, 4-Octyl Itaconate, Is Anti-Fibrotic in Systemic Sclerosis.

Henderson, John / Dayalan Naidu, Sharadha / Dinkova-Kostova, Albena T / Przyborski, Stefan / Stratton, Richard / O Reilly, Steven

Cells

2021 Volume 10, Issue 8

Abstract: Systemic sclerosis (SSc) is an autoimmune connective tissue disease that leads to skin fibrosis. Altered metabolism has recently been described in autoimmune diseases and SSc. Itaconate is a product of the Krebs cycle ... ...

Abstract	Systemic sclerosis (SSc) is an autoimmune connective tissue disease that leads to skin fibrosis. Altered metabolism has recently been described in autoimmune diseases and SSc. Itaconate is a product of the Krebs cycle intermediate
MeSH term(s)	Animals ; Antioxidant Response Elements/drug effects ; Antioxidant Response Elements/genetics ; Collagen/metabolism ; Connective Tissue Growth Factor/metabolism ; Down-Regulation/drug effects ; Fibroblasts/cytology ; Fibroblasts/drug effects ; Fibroblasts/metabolism ; Heme Oxygenase-1/genetics ; Heme Oxygenase-1/metabolism ; Humans ; Interleukin-6/metabolism ; Mice ; Mice, Knockout ; MicroRNAs/genetics ; MicroRNAs/metabolism ; NAD(P)H Dehydrogenase (Quinone)/genetics ; NAD(P)H Dehydrogenase (Quinone)/metabolism ; NF-E2-Related Factor 2/deficiency ; NF-E2-Related Factor 2/genetics ; Reactive Oxygen Species/metabolism ; Scleroderma, Systemic/metabolism ; Scleroderma, Systemic/pathology ; Succinates/pharmacology ; Transforming Growth Factor beta1/pharmacology ; Up-Regulation/drug effects
Chemical Substances	4-octyl itaconate ; Interleukin-6 ; MIRN29 microRNA, mouse ; MicroRNAs ; NF-E2-Related Factor 2 ; Nfe2l2 protein, mouse ; Reactive Oxygen Species ; Succinates ; Transforming Growth Factor beta1 ; Connective Tissue Growth Factor (139568-91-5) ; Collagen (9007-34-5) ; Heme Oxygenase-1 (EC 1.14.14.18) ; NAD(P)H Dehydrogenase (Quinone) (EC 1.6.5.2) ; Nqo1 protein, mouse (EC 1.6.5.2) ; itaconic acid (Q4516562YH)
Language	English
Publishing date	2021-08-10
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells10082053
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Article: Pirin, an Nrf2-Regulated Protein, Is Overexpressed in Human Colorectal Tumors.

Zhang, Ying / Knatko, Elena V / Higgins, Maureen / Dayalan Naidu, Sharadha / Smith, Gillian / Honda, Tadashi / de la Vega, Laureano / Dinkova-Kostova, Albena T

Antioxidants (Basel, Switzerland)

2022 Volume 11, Issue 2

Abstract	The evolutionary conserved non-heme Fe-containing protein pirin has been implicated as an important factor in cell proliferation, migration, invasion, and tumour progression of melanoma, breast, lung, cervical, prostate, and oral cancers. Here we found that pirin is overexpressed in human colorectal cancer in comparison with matched normal tissue. The overexpression of pirin correlates with activation of transcription factor nuclear factor erythroid 2 p45-related factor 2 (Nrf2) and increased expression of the classical Nrf2 target NAD(P)H:quinone oxidoreductase 1 (NQO1), but interestingly and unexpectedly, not with expression of the aldo-keto reductase (AKR) family members AKR1B10 and AKR1C1, which are considered to be the most overexpressed genes in response to Nrf2 activation in humans. Using pharmacologic and genetic approaches to either downregulate or upregulate Nrf2, we show that pirin is regulated by Nrf2 in human and mouse cells and in the mouse colon in vivo. The small molecule pirin inhibitor TPhA decreased the viability of human colorectal cancer (DLD1) cells, but this decrease was independent of the levels of pirin. Our study demonstrates the Nrf2-dependent regulation of pirin and encourages the pursuit for specific pirin inhibitors.
Language	English
Publishing date	2022-01-28
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2704216-9
ISSN	2076-3921
ISSN	2076-3921
DOI	10.3390/antiox11020262
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