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Article ; Online: Nuclease activity of Plasmodium falciparum Alba family protein PfAlba3.

Banerjee, Chinmoy / Nag, Shiladitya / Goyal, Manish / Saha, Debanjan / Siddiqui, Asim Azhar / Mazumder, Somnath / Debsharma, Subhashis / Pramanik, Saikat / Bandyopadhyay, Uday

Cell reports

2023 Volume 42, Issue 4, Page(s) 112292

Abstract: Plasmodium falciparum Alba domain-containing protein Alba3 (PfAlba3) is ubiquitously expressed in intra-erythrocytic stages of Plasmodium falciparum, but the function of this protein is not yet established. Here, we report an apurinic/apyrimidinic site- ... ...

Abstract	Plasmodium falciparum Alba domain-containing protein Alba3 (PfAlba3) is ubiquitously expressed in intra-erythrocytic stages of Plasmodium falciparum, but the function of this protein is not yet established. Here, we report an apurinic/apyrimidinic site-driven intrinsic nuclease activity of PfAlba3 assisted by divalent metal ions. Surface plasmon resonance and atomic force microscopy confirm sequence non-specific DNA binding by PfAlba3. Upon binding, PfAlba3 cleaves double-stranded DNA (dsDNA) hydrolytically. Mutational studies coupled with mass spectrometric analysis indicate that K23 is the essential residue in modulating the binding to DNA through acetylation-deacetylation. We further demonstrate that PfSir2a interacts and deacetylates K23-acetylated PfAlba3 in favoring DNA binding. Hence, K23 serves as a putative molecular switch regulating the nuclease activity of PfAlba3. Thus, the nuclease activity of PfAlba3, along with its apurinic/apyrimidinic (AP) endonuclease feature identified in this study, indicates a role of PfAlba3 in DNA-damage response that may have a far-reaching consequence in Plasmodium pathogenicity.
MeSH term(s)	Plasmodium falciparum/genetics ; Protein Binding ; DNA-(Apurinic or Apyrimidinic Site) Lyase/genetics ; DNA/metabolism ; DNA Repair
Chemical Substances	DNA-(Apurinic or Apyrimidinic Site) Lyase (EC 4.2.99.18) ; DNA (9007-49-2)
Language	English
Publishing date	2023-03-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2023.112292
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Article ; Online: Plasmodium falciparum

Nag, Shiladitya / Banerjee, Chinmoy / Goyal, Manish / Siddiqui, Asim Azhar / Saha, Debanjan / Mazumder, Somnath / Debsharma, Subhashis / Pramanik, Saikat / Saha, Shubhra Jyoti / De, Rudranil / Bandyopadhyay, Uday

iScience

2024 Volume 27, Issue 4, Page(s) 109467

Abstract: Alba domain proteins, owing to their functional plasticity, play a significant role in organisms. Here, we report an intrinsic DNase activity of PfAlba6 ... ...

Abstract	Alba domain proteins, owing to their functional plasticity, play a significant role in organisms. Here, we report an intrinsic DNase activity of PfAlba6 from
Language	English
Publishing date	2024-03-08
Publishing country	United States
Document type	Journal Article
ISSN	2589-0042
ISSN (online)	2589-0042
DOI	10.1016/j.isci.2024.109467
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Article ; Online: NSAID targets SIRT3 to trigger mitochondrial dysfunction and gastric cancer cell death.

Debsharma, Subhashis / Pramanik, Saikat / Bindu, Samik / Mazumder, Somnath / Das, Troyee / Pal, Uttam / Saha, Debanjan / De, Rudranil / Nag, Shiladitya / Banerjee, Chinmoy / Chandra Maiti, Nakul / Ghosh, Zhumur / Bandyopadhyay, Uday

iScience

2024 Volume 27, Issue 4, Page(s) 109384

Abstract: Gastric cancer (GC) is a deadly malignancy that demands effective therapeutic intervention capitalizing unique drug target/s. Here, we report that indomethacin, a cyclooxygenase non-selective non-steroidal anti-inflammatory drug, arrests GC cell growth ... ...

Abstract	Gastric cancer (GC) is a deadly malignancy that demands effective therapeutic intervention capitalizing unique drug target/s. Here, we report that indomethacin, a cyclooxygenase non-selective non-steroidal anti-inflammatory drug, arrests GC cell growth by targeting mitochondrial deacetylase Sirtuin 3 (SIRT3). Interaction study revealed that indomethacin competitively inhibited SIRT3 by binding to nicotinamide adenine dinucleotide (NAD)-binding site. The Cancer Genome Atlas data meta-analysis indicated poor prognosis associated with high SIRT3 expression in GC. Further, transcriptome sequencing data of human gastric adenocarcinoma cells revealed that indomethacin treatment severely downregulated SIRT3. Indomethacin-induced SIRT3 downregulation augmented SOD2 and OGG1 acetylation, leading to mitochondrial redox dyshomeostasis, mtDNA damage, respiratory chain failure, bioenergetic crisis, mitochondrial fragmentation, and apoptosis via blocking the AMPK/PGC1α/SIRT3 axis. Indomethacin also downregulated SIRT3 regulators ERRα and PGC1α. Further, SIRT3 knockdown aggravated indomethacin-induced mitochondrial dysfunction as well as blocked cell-cycle progression to increase cell death. Thus, we reveal how indomethacin induces GC cell death by disrupting SIRT3 signaling.
Language	English
Publishing date	2024-03-01
Publishing country	United States
Document type	Journal Article
ISSN	2589-0042
ISSN (online)	2589-0042
DOI	10.1016/j.isci.2024.109384
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Article ; Online: Honokiol, an inducer of sirtuin-3, protects against non-steroidal anti-inflammatory drug-induced gastric mucosal mitochondrial pathology, apoptosis and inflammatory tissue injury.

Debsharma, Subhashis / Pramanik, Saikat / Bindu, Samik / Mazumder, Somnath / Das, Troyee / Saha, Debanjan / De, Rudranil / Nag, Shiladitya / Banerjee, Chinmoy / Siddiqui, Asim Azhar / Ghosh, Zhumur / Bandyopadhyay, Uday

British journal of pharmacology

2023 Volume 180, Issue 18, Page(s) 2317–2340

Abstract: Background and purpose: Mitochondrial oxidative stress, inflammation and apoptosis primarily underlie gastric mucosal injury caused by the widely used non-steroidal anti-inflammatory drugs (NSAIDs). Alternative gastroprotective strategies are therefore ... ...

Abstract	Background and purpose: Mitochondrial oxidative stress, inflammation and apoptosis primarily underlie gastric mucosal injury caused by the widely used non-steroidal anti-inflammatory drugs (NSAIDs). Alternative gastroprotective strategies are therefore needed. Sirtuin-3 pivotally maintains mitochondrial structural integrity and metabolism while preventing oxidative stress; however, its relevance to gastric injury was never explored. Here, we have investigated whether and how sirtuin-3 stimulation by the phytochemical, honokiol, could rescue NSAID-induced gastric injury. Experimental approach: Gastric injury in rats induced by indomethacin was used to assess the effects of honokiol. Next-generation sequencing-based transcriptomics followed by functional validation identified the gastroprotective function of sirtuin-3. Flow cytometry, immunoblotting, qRT-PCR and immunohistochemistry were used measure effects on oxidative stress, mitochondrial dynamics, electron transport chain function, and markers of inflammation and apoptosis. Sirtuin-3 deacetylase activity was also estimated and gastric luminal pH was measured. Key results: Indomethacin down-regulated sirtuin-3 to induce oxidative stress, mitochondrial hyperacetylation, 8-oxoguanine DNA glycosylase 1 depletion, mitochondrial DNA damage, respiratory chain defect and mitochondrial fragmentation leading to severe mucosal injury. Indomethacin dose-dependently inhibited sirtuin-3 deacetylase activity. Honokiol prevented mitochondrial oxidative damage and inflammatory tissue injury by attenuating indomethacin-induced depletion of both sirtuin-3 and its transcriptional regulators PGC1α and ERRα. Honokiol also accelerated gastric wound healing but did not alter gastric acid secretion, unlike lansoprazole. Conclusions and implications: Sirtuin-3 stimulation by honokiol prevented and reversed NSAID-induced gastric injury through maintaining mitochondrial integrity. Honokiol did not affect gastric acid secretion. Sirtuin-3 stimulation by honokiol may be utilized as a mitochondria-based, acid-independent novel gastroprotective strategy against NSAIDs.
MeSH term(s)	Rats ; Animals ; Sirtuin 3/metabolism ; Rats, Sprague-Dawley ; Anti-Inflammatory Agents, Non-Steroidal/pharmacology ; Indomethacin/toxicity ; Gastric Mucosa/metabolism ; Apoptosis ; Inflammation/metabolism
Chemical Substances	honokiol (11513CCO0N) ; Sirtuin 3 (EC 3.5.1.-) ; Anti-Inflammatory Agents, Non-Steroidal ; Indomethacin (XXE1CET956)
Language	English
Publishing date	2023-05-16
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80081-8
ISSN	1476-5381 ; 0007-1188
ISSN (online)	1476-5381
ISSN	0007-1188
DOI	10.1111/bph.16070
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Article: The Alba protein family: Structure and function.

Goyal, Manish / Banerjee, Chinmoy / Nag, Shiladitya / Bandyopadhyay, Uday

Biochimica et biophysica acta

2016 Volume 1864, Issue 5, Page(s) 570–583

Abstract: Alba family proteins are small, basic, dimeric nucleic acid-binding proteins, which are widely distributed in archaea and a number of eukaryotes. This family of proteins bears the distinct features of regulation through acetylation/deacetylation, hence ... ...

Abstract	Alba family proteins are small, basic, dimeric nucleic acid-binding proteins, which are widely distributed in archaea and a number of eukaryotes. This family of proteins bears the distinct features of regulation through acetylation/deacetylation, hence named as acetylation lowers binding affinity (Alba). Alba family proteins bind DNA cooperatively with no apparent sequence specificity. Besides DNA, Alba proteins also interact with diverse RNA species and associate with ribonucleo-protein complexes. Initially, Alba proteins were recognized as chromosomal proteins and supposed to be involved in the maintenance of chromatin architecture and transcription repression. However, recent studies have shown increasing evidence of functional plasticity among Alba family of proteins that widely range from genome packaging and organization, transcriptional and translational regulation, RNA metabolism, and development and differentiation processes. In recent years, Alba family proteins have attracted growing interest due to their widespread occurrence in large number of organisms. Presence in multiple copies, functional crosstalk, differential binding affinity, and posttranslational modifications are some of the key factors that might regulate the biological functions of Alba family proteins. In this review article, we present an overview of the Alba family proteins, their salient features and emphasize their functional role in different organisms reported so far.
MeSH term(s)	Amino Acid Sequence ; Archaeal Proteins/chemistry ; Archaeal Proteins/genetics ; Archaeal Proteins/metabolism ; Chromatin/genetics ; Chromatin/metabolism ; Crystallography, X-Ray ; DNA/chemistry ; DNA/genetics ; DNA/metabolism ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Multigene Family/genetics ; Protein Binding/genetics ; Protein Conformation ; RNA/genetics ; RNA/metabolism ; Structure-Activity Relationship
Chemical Substances	Archaeal Proteins ; Chromatin ; DNA-Binding Proteins ; RNA (63231-63-0) ; DNA (9007-49-2)
Language	English
Publishing date	2016-05
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbapap.2016.02.015
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Article: Detection of retromer assembly in Plasmodium falciparum by immunosensing coupled to Surface Plasmon Resonance.

Iqbal, Mohd Shameel / Siddiqui, Asim Azhar / Banerjee, Chinmoy / Nag, Shiladitya / Mazumder, Somnath / De, Rudranil / Saha, Shubhra Jyoti / Karri, Suresh Kumar / Bandyopadhyay, Uday

Biochimica et biophysica acta. Proteins and proteomics

2018 Volume 1866, Issue 5-6, Page(s) 722–730

Abstract: Retromer complex plays a crucial role in intracellular protein trafficking and is conserved throughout the eukaryotes including malaria parasite, Plasmodium falciparum, where it is partially conserved. The assembly of retromer complex in RBC stages of ... ...

Abstract	Retromer complex plays a crucial role in intracellular protein trafficking and is conserved throughout the eukaryotes including malaria parasite, Plasmodium falciparum, where it is partially conserved. The assembly of retromer complex in RBC stages of malarial parasite is extremely difficult to explore because of its complicated physiology, small size, and intra-erythrocytic location. Nonetheless, understanding of retromer assembly may pave new ways for the development of novel antimalarials targeting parasite-specific protein trafficking pathways. Here, we investigated the assembly of retromer complex in P. falciparum, by an immunosensing method through highly sensitive Surface Plasmon Resonance (SPR) technique. After taking leads from the bioinformatics search and literature, different interacting proteins were identified and specific antibodies were raised against them. The sensor chip was prepared by covalently linking antibody specific to one component and the whole cell lysate was passed through it in order to trap the interacting complex. Antibodies raised against other interacting components were used to detect them in the trapped complex on the SPR chip. We were able to detect three different components in the retromer complex trapped by the immobilized antibody specific against a different component on a sensor chip. The assay was reproduced and validated in a different two-component CD74-MIF system in mammalian cells. We, thus, illustrate the assembly of retromer complex in P. falciparum through a bio-sensing approach that combines SPR with immunosensing requiring a very small amount of sample from the native source.
MeSH term(s)	Adaptor Proteins, Vesicular Transport/metabolism ; Animals ; Biosensing Techniques ; Blotting, Western ; Computational Biology ; Hep G2 Cells ; Humans ; Immunoprecipitation ; Kinetics ; Mice ; Multiprotein Complexes/genetics ; Multiprotein Complexes/immunology ; Multiprotein Complexes/metabolism ; NIH 3T3 Cells ; Plasmodium falciparum/genetics ; Plasmodium falciparum/immunology ; Plasmodium falciparum/metabolism ; Protein Binding ; Protein Transport ; Protozoan Proteins/genetics ; Protozoan Proteins/immunology ; Protozoan Proteins/metabolism ; Surface Plasmon Resonance ; Vesicular Transport Proteins/genetics ; Vesicular Transport Proteins/immunology ; Vesicular Transport Proteins/metabolism
Chemical Substances	Adaptor Proteins, Vesicular Transport ; Multiprotein Complexes ; Protozoan Proteins ; Vesicular Transport Proteins ; sortilin
Language	English
Publishing date	2018-04-11
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 1570-9639 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	1570-9639 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbapap.2018.04.005
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Article ; Online: Rab7 of Plasmodium falciparum is involved in its retromer complex assembly near the digestive vacuole.

Siddiqui, Asim Azhar / Saha, Debanjan / Iqbal, Mohd Shameel / Saha, Shubhra Jyoti / Sarkar, Souvik / Banerjee, Chinmoy / Nag, Shiladitya / Mazumder, Somnath / De, Rudranil / Pramanik, Saikat / Debsharma, Subhashis / Bandyopadhyay, Uday

Biochimica et biophysica acta. General subjects

2020 Volume 1864, Issue 10, Page(s) 129656

Abstract: Background: Intracellular protein trafficking is crucial for survival of cell and proper functioning of the organelles; however, these pathways are not well studied in the malaria parasite. Its unique cellular architecture and organellar composition ... ...

Abstract	Background: Intracellular protein trafficking is crucial for survival of cell and proper functioning of the organelles; however, these pathways are not well studied in the malaria parasite. Its unique cellular architecture and organellar composition raise an interesting question to investigate. Methods: The interaction of Plasmodium falciparum Rab7 (PfRab7) with vacuolar protein sorting-associated protein 26 (PfVPS26) of retromer complex was shown by coimmunoprecipitation (co-IP). Confocal microscopy was used to show the localization of the complex in the parasite with respect to different organelles. Further chemical tools were employed to explore the role of digestive vacuole (DV) in retromer trafficking in parasite and GTPase activity of PfRab7 was examined. Results: PfRab7 was found to be interacting with retromer complex that assembled mostly near DV and the Golgi in trophozoites. Chemical disruption of DV by chloroquine (CQ) led to its disassembly that was further validated by using compound 5f, a heme polymerization inhibitor in the DV. PfRab7 exhibited Mg Conclusion: Retromer complex was found to be interacting with PfRab7 and the functional integrity of the DV was found to be important for retromer assembly in P. falciparum. General significance: This study explores the retromer trafficking in P. falciparum and describes amechanism to validate DV targeting antiplasmodial molecules.
MeSH term(s)	Antimalarials/pharmacology ; Chloroquine/pharmacology ; Humans ; Magnesium/metabolism ; Malaria, Falciparum/drug therapy ; Malaria, Falciparum/metabolism ; Malaria, Falciparum/parasitology ; Models, Molecular ; Plasmodium falciparum/drug effects ; Plasmodium falciparum/metabolism ; Protein Interaction Maps/drug effects ; Vacuoles/drug effects ; Vacuoles/metabolism ; rab GTP-Binding Proteins/metabolism
Chemical Substances	Antimalarials ; rab7 protein (152989-05-4) ; Chloroquine (886U3H6UFF) ; rab GTP-Binding Proteins (EC 3.6.5.2) ; Magnesium (I38ZP9992A)
Language	English
Publishing date	2020-06-05
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1872-8006 ; 1879-2596 ; 1879-260X ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1872-8006 ; 1879-2596 ; 1879-260X ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbagen.2020.129656
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Article: Rab7 of Plasmodium falciparum is involved in its retromer complex assembly near the digestive vacuole

Biochimica et biophysica acta. 2020 Oct., v. 1864, no. 10

2020

Abstract: Background:Intracellular protein trafficking is crucial for survival of cell and proper functioning of the organelles; however, these pathways are not well studied in the malaria parasite. Its unique cellular architecture and organellar composition raise ...

Abstract	Background:Intracellular protein trafficking is crucial for survival of cell and proper functioning of the organelles; however, these pathways are not well studied in the malaria parasite. Its unique cellular architecture and organellar composition raise an interesting question to investigate.Methods:The interaction of Plasmodium falciparum Rab7 (PfRab7) with vacuolar protein sorting-associated protein 26 (PfVPS26) of retromer complex was shown by coimmunoprecipitation (co-IP). Confocal microscopy was used to show the localization of the complex in the parasite with respect to different organelles. Further chemical tools were employed to explore the role of digestive vacuole (DV) in retromer trafficking in parasite and GTPase activity of PfRab7 was examined.Results:PfRab7 was found to be interacting with retromer complex that assembled mostly near DV and the Golgi in trophozoites. Chemical disruption of DV by chloroquine (CQ) led to its disassembly that was further validated by using compound 5f, a heme polymerization inhibitor in the DV. PfRab7 exhibited Mg²⁺ dependent weak GTPase activity that was inhibited by a specific Rab7 GTPase inhibitor, CID 1067700, which prevented the assembly of retromer complex in P. falciparum and inhibited its growth suggesting the role of GTPase activity of PfRab7 in retromer assembly.Conclusion:Retromer complex was found to be interacting with PfRab7 and the functional integrity of the DV was found to be important for retromer assembly in P. falciparum.General significance:This study explores the retromer trafficking in P. falciparum and describes amechanism to validate DV targeting antiplasmodial molecules.
Keywords	Plasmodium falciparum ; chloroquine ; confocal microscopy ; enzyme activity ; enzyme inhibitors ; guanosinetriphosphatase ; heme ; magnesium ; malaria ; parasites ; polymerization ; precipitin tests ; protein transport ; trophozoites ; vacuoles
Language	English
Dates of publication	2020-10
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	840755-1
ISSN	0304-4165
ISSN	0304-4165
DOI	10.1016/j.bbagen.2020.129656
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Indomethacin impairs mitochondrial dynamics by activating the PKCζ-p38-DRP1 pathway and inducing apoptosis in gastric cancer and normal mucosal cells.

Mazumder, Somnath / De, Rudranil / Debsharma, Subhashis / Bindu, Samik / Maity, Pallab / Sarkar, Souvik / Saha, Shubhra Jyoti / Siddiqui, Asim Azhar / Banerjee, Chinmoy / Nag, Shiladitya / Saha, Debanjan / Pramanik, Saikat / Mitra, Kalyan / Bandyopadhyay, Uday

The Journal of biological chemistry

2019 Volume 294, Issue 20, Page(s) 8238–8258

Abstract: The subcellular mechanism by which nonsteroidal anti-inflammatory drugs (NSAIDs) induce apoptosis in gastric cancer and normal mucosal cells is elusive because of the diverse cyclooxygenase-independent effects of these drugs. Using human gastric ... ...

Abstract	The subcellular mechanism by which nonsteroidal anti-inflammatory drugs (NSAIDs) induce apoptosis in gastric cancer and normal mucosal cells is elusive because of the diverse cyclooxygenase-independent effects of these drugs. Using human gastric carcinoma cells (AGSs) and a rat gastric injury model, here we report that the NSAID indomethacin activates the protein kinase Cζ (PKCζ)-p38 MAPK (p38)-dynamin-related protein 1 (DRP1) pathway and thereby disrupts the physiological balance of mitochondrial dynamics by promoting mitochondrial hyper-fission and dysfunction leading to apoptosis. Notably, DRP1 knockdown or SB203580-induced p38 inhibition reduced indomethacin-induced damage to AGSs. Indomethacin impaired mitochondrial dynamics by promoting fissogenic activation and mitochondrial recruitment of DRP1 and down-regulating fusogenic optic atrophy 1 (OPA1) and mitofusins in rat gastric mucosa. Consistent with OPA1 maintaining cristae architecture, its down-regulation resulted in EM-detectable cristae deformity. Deregulated mitochondrial dynamics resulting in defective mitochondria were evident from enhanced Parkin expression and mitochondrial proteome ubiquitination. Indomethacin ultimately induced mitochondrial metabolic and bioenergetic crises in the rat stomach, indicated by compromised fatty acid oxidation, reduced complex I- associated electron transport chain activity, and ATP depletion. Interestingly, Mdivi-1, a fission-preventing mito-protective drug, reversed indomethacin-induced DRP1 phosphorylation on Ser-616, mitochondrial proteome ubiquitination, and mitochondrial metabolic crisis. Mdivi-1 also prevented indomethacin-induced mitochondrial macromolecular damage, caspase activation, mucosal inflammation, and gastric mucosal injury. Our results identify mitochondrial hyper-fission as a critical and common subcellular event triggered by indomethacin that promotes apoptosis in both gastric cancer and normal mucosal cells, thereby contributing to mucosal injury.
MeSH term(s)	Animals ; Apoptosis/drug effects ; Apoptosis/genetics ; Cell Line, Tumor ; Dynamins ; GTP Phosphohydrolases/genetics ; GTP Phosphohydrolases/metabolism ; Gastric Mucosa/enzymology ; Gastric Mucosa/pathology ; Humans ; Indomethacin/pharmacology ; MAP Kinase Signaling System/drug effects ; MAP Kinase Signaling System/genetics ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; Mitochondria/enzymology ; Mitochondria/genetics ; Mitochondrial Dynamics/drug effects ; Mitochondrial Dynamics/genetics ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Neoplasm Proteins/genetics ; Neoplasm Proteins/metabolism ; Protein Kinase C/genetics ; Protein Kinase C/metabolism ; Rats ; Stomach Neoplasms/enzymology ; Stomach Neoplasms/genetics ; Stomach Neoplasms/pathology ; p38 Mitogen-Activated Protein Kinases/genetics ; p38 Mitogen-Activated Protein Kinases/metabolism
Chemical Substances	Microtubule-Associated Proteins ; Mitochondrial Proteins ; Neoplasm Proteins ; protein kinase C zeta (EC 2.7.11.1) ; Protein Kinase C (EC 2.7.11.13) ; p38 Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; GTP Phosphohydrolases (EC 3.6.1.-) ; DNM1L protein, human (EC 3.6.5.5) ; Dynamins (EC 3.6.5.5) ; Indomethacin (XXE1CET956)
Language	English
Publishing date	2019-04-02
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA118.004415
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Article ; Online: Hydrazonophenol, a Food Vacuole-Targeted and Ferriprotoporphyrin IX-Interacting Chemotype Prevents Drug-Resistant Malaria.

Saha, Shubhra Jyoti / Siddiqui, Asim Azhar / Pramanik, Saikat / Saha, Debanjan / De, Rudranil / Mazumder, Somnath / Debsharma, Subhashis / Nag, Shiladitya / Banerjee, Chinmoy / Bandyopadhyay, Uday

ACS infectious diseases

2018 Volume 5, Issue 1, Page(s) 63–73

Abstract: The rapid emergence of resistance against frontline antimalarial drugs essentially warrants the identification of new-generation antimalarials. Here, we describe the synthesis of ( E)-2-isopropyl-5-methyl-4-((2-(pyridin-4-yl)hydrazono)methyl)phenol (18), ...

Abstract	The rapid emergence of resistance against frontline antimalarial drugs essentially warrants the identification of new-generation antimalarials. Here, we describe the synthesis of ( E)-2-isopropyl-5-methyl-4-((2-(pyridin-4-yl)hydrazono)methyl)phenol (18), which binds ferriprotoporphyrin-IX (Fe
MeSH term(s)	Animals ; Antimalarials/chemical synthesis ; Antimalarials/pharmacology ; Biological Assay ; Drug Resistance ; Hemeproteins/antagonists & inhibitors ; Hemeproteins/biosynthesis ; Hemin/metabolism ; Hydrazones/chemical synthesis ; Hydrazones/pharmacology ; Hydrogen-Ion Concentration ; Malaria, Falciparum/prevention & control ; Mice ; Microscopy, Confocal ; Phenols/chemistry ; Phenols/pharmacology ; Plasmodium berghei/drug effects ; Plasmodium falciparum/drug effects ; Plasmodium yoelii/drug effects ; Protein Binding ; Vacuoles/chemistry ; Vacuoles/drug effects
Chemical Substances	Antimalarials ; Hemeproteins ; Hydrazones ; Phenols ; hemozoin (39404-00-7) ; Hemin (743LRP9S7N)
Language	English
Publishing date	2018-12-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2373-8227
ISSN (online)	2373-8227
DOI	10.1021/acsinfecdis.8b00178
Database	MEDical Literature Analysis and Retrieval System OnLINE

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