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  1. Article ; Online: Proteomics-Based Analysis and Diagnosis of Formalin-Fixed Paraffin-Embedded Amyloidosis Samples.

    Van Haver, Delphi / Dendooven, Amélie / Impens, Francis

    Methods in molecular biology (Clifton, N.J.)

    2023  Volume 2718, Page(s) 213–233

    Abstract: Amyloidosis is a group of rare pathologies characterized by abnormal folding and deposition of susceptible proteins in tissues and organs. Diagnosis of amyloidosis often relies on immunohistochemistry of formalin-fixed paraffin-embedded (FFPE) patient ... ...

    Abstract Amyloidosis is a group of rare pathologies characterized by abnormal folding and deposition of susceptible proteins in tissues and organs. Diagnosis of amyloidosis often relies on immunohistochemistry of formalin-fixed paraffin-embedded (FFPE) patient samples; however, dependency on antibodies for protein staining is one of the major pitfalls of this approach, especially for the detection of rare amyloidosis types. In recent years, mass spectrometry-based proteomics has emerged as a promising alternative for adequate detection and amyloid typing, despite the fact that preparing FFPE samples for proteomics remains a challenging task. Major hurdles are removal of formalin-induced protein cross-links and water-insoluble paraffin prior to mass spectrometry analysis. With the recent development of the suspension trapping protocol, enabling the use of high concentrations of SDS, these obstacles can be overcome. In this chapter, we describe the implementation of suspension trapping for FFPE sample processing and its application to analyze human amyloidosis samples, comparing a standard procedure with probe sonication with a more advanced workflow based on ultrasonication.
    MeSH term(s) Humans ; Paraffin Embedding ; Proteomics ; Amyloidosis/diagnosis ; Amyloidogenic Proteins ; Formaldehyde
    Chemical Substances Amyloidogenic Proteins ; Formaldehyde (1HG84L3525)
    Language English
    Publishing date 2023-08-17
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-3457-8_12
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Environmental conditions steer phenotypic switching in acute hepatopancreatic necrosis disease‐causing Vibrio parahaemolyticus, affecting PirAVP/PirBVP toxins production

    Kumar, Vikash / Roy, Suvra / Baruah, Kartik / Van Haver, Delphi / Impens, Francis / Bossier, Peter

    Environmental microbiology. 2020 Oct., v. 22, no. 10

    2020  

    Abstract: Bacteria in nature are widely exposed to differential fluid shears which are often a trigger for phenotypic switches. The latter mediates transcriptional and translation remodelling of cellular metabolism impacting among others virulence, antimicrobial ... ...

    Abstract Bacteria in nature are widely exposed to differential fluid shears which are often a trigger for phenotypic switches. The latter mediates transcriptional and translation remodelling of cellular metabolism impacting among others virulence, antimicrobial resistance and stress resistance. In this study, we evaluated the role of fluid shear on phenotypic switch in an acute hepatopancreatic necrosis disease (AHPND)‐causing Vibrio parahaemolyticus M0904 strain under both in vitro and in vivo conditions. The results showed that V. parahaemolyticus M0904 grown at lower shaking speed (110 rpm constant agitation, M0904/110), causing low fluid shear, develop cellular aggregates or floccules. These cells increased levan production (as verified by concanavalin binding) and developed differentially stained colonies on Congo red agar plates and resistance to antibiotics. In addition, the phenotypic switch causes a major shift in the protein secretome. At 120 rpm (M0904/120), PirAⱽᴾ/PirBⱽᴾ toxins are mainly produced, while at 110 rpm PirAⱽᴾ/PirBⱽᴾ toxins production is stopped and an alkaline phosphatase (ALP) PhoX becomes the dominant protein in the protein secretome. These observations are matched with a very strong reduction in virulence of M0904/110 towards two crustacean larvae, namely, Artemia and Macrobrachium. Taken together, our study provides substantial evidence for the existence of two phenotypic forms in AHPND V. parahaemolyticus strain displaying differential phenotypes. Moreover, as aerators and pumping devices are frequently used in shrimp aquaculture facilities, they can inflict fluid shear to the standing microbial agents. Hence, our study could provide a basis to understand the behaviour of AHPND‐causing V. parahaemolyticus in aquaculture settings and open the possibility to monitor and control AHPND by steering phenotypes.
    Keywords Artemia ; Macrobrachium ; Vibrio parahaemolyticus ; agar ; agitation ; alkaline phosphatase ; antibiotic resistance ; levan ; metabolism ; necrosis ; necrotizing hepatopancreatitis ; phenotype ; shrimp culture ; steers ; stress tolerance ; transcription (genetics) ; virulence
    Language English
    Dates of publication 2020-10
    Size p. 4212-4230.
    Publishing place John Wiley & Sons, Inc.
    Document type Article
    Note NAL-AP-2-clean ; JOURNAL ARTICLE
    ZDB-ID 2020213-1
    ISSN 1462-2920 ; 1462-2912
    ISSN (online) 1462-2920
    ISSN 1462-2912
    DOI 10.1111/1462-2920.14903
    Database NAL-Catalogue (AGRICOLA)

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  3. Article ; Online: Environmental conditions steer phenotypic switching in acute hepatopancreatic necrosis disease-causing Vibrio parahaemolyticus, affecting PirA

    Kumar, Vikash / Roy, Suvra / Baruah, Kartik / Van Haver, Delphi / Impens, Francis / Bossier, Peter

    Environmental microbiology

    2020  Volume 22, Issue 10, Page(s) 4212–4230

    Abstract: Bacteria in nature are widely exposed to differential fluid shears which are often a trigger for phenotypic switches. The latter mediates transcriptional and translation remodelling of cellular metabolism impacting among others virulence, antimicrobial ... ...

    Abstract Bacteria in nature are widely exposed to differential fluid shears which are often a trigger for phenotypic switches. The latter mediates transcriptional and translation remodelling of cellular metabolism impacting among others virulence, antimicrobial resistance and stress resistance. In this study, we evaluated the role of fluid shear on phenotypic switch in an acute hepatopancreatic necrosis disease (AHPND)-causing Vibrio parahaemolyticus M0904 strain under both in vitro and in vivo conditions. The results showed that V. parahaemolyticus M0904 grown at lower shaking speed (110 rpm constant agitation, M0904/110), causing low fluid shear, develop cellular aggregates or floccules. These cells increased levan production (as verified by concanavalin binding) and developed differentially stained colonies on Congo red agar plates and resistance to antibiotics. In addition, the phenotypic switch causes a major shift in the protein secretome. At 120 rpm (M0904/120), PirA
    MeSH term(s) Acute Disease ; Animals ; Artemia/microbiology ; Bacterial Toxins/metabolism ; Hepatopancreas/pathology ; Necrosis ; Palaemonidae/microbiology ; Phenotype ; Stress, Mechanical ; Vibrio parahaemolyticus/metabolism ; Vibrio parahaemolyticus/pathogenicity ; Virulence
    Chemical Substances Bacterial Toxins
    Language English
    Publishing date 2020-01-08
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2020213-1
    ISSN 1462-2920 ; 1462-2912
    ISSN (online) 1462-2920
    ISSN 1462-2912
    DOI 10.1111/1462-2920.14903
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Spatial Mechano-Signaling Regulation of GTPases through Non-Degradative Ubiquitination.

    Sewduth, Raj N / Carai, Paolo / Ivanisevic, Tonci / Zhang, Mingzhen / Jang, Hyunbum / Lechat, Benoit / Van Haver, Delphi / Impens, Francis / Nussinov, Ruth / Jones, Elizabeth / Sablina, Anna

    Advanced science (Weinheim, Baden-Wurttemberg, Germany)

    2023  Volume 10, Issue 36, Page(s) e2303367

    Abstract: Blood flow produces shear stress exerted on the endothelial layer of the vessels. Spatial characterization of the endothelial proteome is required to uncover the mechanisms of endothelial activation by shear stress, as blood flow varies in the ... ...

    Abstract Blood flow produces shear stress exerted on the endothelial layer of the vessels. Spatial characterization of the endothelial proteome is required to uncover the mechanisms of endothelial activation by shear stress, as blood flow varies in the vasculature. An integrative ubiquitinome and proteome analysis of shear-stressed endothelial cells demonstrated that the non-degradative ubiquitination of several GTPases is regulated by mechano-signaling. Spatial analysis reveals increased ubiquitination of the small GTPase RAP1 in the descending aorta, a region exposed to laminar shear stress. The ubiquitin ligase WWP2 is identified as a novel regulator of RAP1 ubiquitination during shear stress response. Non-degradative ubiquitination fine-tunes the function of GTPases by modifying their interacting network. Specifically, WWP2-mediated RAP1 ubiquitination at lysine 31 switches the balance from the RAP1/ Talin 1 (TLN1) toward RAP1/ Afadin (AFDN) or RAP1/ RAS Interacting Protein 1 (RASIP1) complex formation, which is essential to suppress shear stress-induced reactive oxygen species (ROS) production and maintain endothelial barrier integrity. Increased ROS production in endothelial cells in the descending aorta of endothelial-specific Wwp2-knockout mice leads to increased levels of oxidized lipids and inflammation. These results highlight the importance of the spatially regulated non-degradative ubiquitination of GTPases in endothelial mechano-activation.
    MeSH term(s) Animals ; Mice ; Endothelial Cells/metabolism ; GTP Phosphohydrolases/metabolism ; Reactive Oxygen Species/metabolism ; Proteome/metabolism ; rap1 GTP-Binding Proteins/genetics ; rap1 GTP-Binding Proteins/metabolism ; Mice, Knockout ; Ubiquitination
    Chemical Substances GTP Phosphohydrolases (EC 3.6.1.-) ; Reactive Oxygen Species ; Proteome ; rap1 GTP-Binding Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2023-11-09
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 2808093-2
    ISSN 2198-3844 ; 2198-3844
    ISSN (online) 2198-3844
    ISSN 2198-3844
    DOI 10.1002/advs.202303367
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: The nutritional composition and cell size of microbial biomass for food applications are defined by the growth conditions.

    Sakarika, Myrsini / Kerckhof, Frederiek-Maarten / Van Peteghem, Lotte / Pereira, Alexandra / Van Den Bossche, Tim / Bouwmeester, Robbin / Gabriels, Ralf / Van Haver, Delphi / Ulčar, Barbara / Martens, Lennart / Impens, Francis / Boon, Nico / Ganigué, Ramon / Rabaey, Korneel

    Microbial cell factories

    2023  Volume 22, Issue 1, Page(s) 254

    Abstract: Background: It is increasingly recognized that conventional food production systems are not able to meet the globally increasing protein needs, resulting in overexploitation and depletion of resources, and environmental degradation. In this context, ... ...

    Abstract Background: It is increasingly recognized that conventional food production systems are not able to meet the globally increasing protein needs, resulting in overexploitation and depletion of resources, and environmental degradation. In this context, microbial biomass has emerged as a promising sustainable protein alternative. Nevertheless, often no consideration is given on the fact that the cultivation conditions affect the composition of microbial cells, and hence their quality and nutritional value. Apart from the properties and nutritional quality of the produced microbial food (ingredient), this can also impact its sustainability. To qualitatively assess these aspects, here, we investigated the link between substrate availability, growth rate, cell composition and size of Cupriavidus necator and Komagataella phaffii.
    Results: Biomass with decreased nucleic acid and increased protein content was produced at low growth rates. Conversely, high rates resulted in larger cells, which could enable more efficient biomass harvesting. The proteome allocation varied across the different growth rates, with more ribosomal proteins at higher rates, which could potentially affect the techno-functional properties of the biomass. Considering the distinct amino acid profiles established for the different cellular components, variations in their abundance impacts the product quality leading to higher cysteine and phenylalanine content at low growth rates. Therefore, we hint that costly external amino acid supplementations that are often required to meet the nutritional needs could be avoided by carefully applying conditions that enable targeted growth rates.
    Conclusion: In summary, we demonstrate tradeoffs between nutritional quality and production rate, and we discuss the microbial biomass properties that vary according to the growth conditions.
    MeSH term(s) Biomass ; Amino Acids ; Proteome ; Cysteine ; Cell Size
    Chemical Substances Amino Acids ; Proteome ; Cysteine (K848JZ4886)
    Language English
    Publishing date 2023-12-11
    Publishing country England
    Document type Journal Article
    ZDB-ID 2091377-1
    ISSN 1475-2859 ; 1475-2859
    ISSN (online) 1475-2859
    ISSN 1475-2859
    DOI 10.1186/s12934-023-02265-1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: RHOJ controls EMT-associated resistance to chemotherapy.

    Debaugnies, Maud / Rodríguez-Acebes, Sara / Blondeau, Jeremy / Parent, Marie-Astrid / Zocco, Manuel / Song, Yura / de Maertelaer, Viviane / Moers, Virginie / Latil, Mathilde / Dubois, Christine / Coulonval, Katia / Impens, Francis / Van Haver, Delphi / Dufour, Sara / Uemura, Akiyoshi / Sotiropoulou, Panagiota A / Méndez, Juan / Blanpain, Cédric

    Nature

    2023  Volume 616, Issue 7955, Page(s) 168–175

    Abstract: The resistance of cancer cells to therapy is responsible for the death of most patients with ... ...

    Abstract The resistance of cancer cells to therapy is responsible for the death of most patients with cancer
    MeSH term(s) Actins/drug effects ; Actins/metabolism ; Carcinoma, Squamous Cell/drug therapy ; Carcinoma, Squamous Cell/metabolism ; Carcinoma, Squamous Cell/pathology ; Cell Line, Tumor ; Drug Resistance, Neoplasm/drug effects ; Drug Resistance, Neoplasm/genetics ; Epithelial-Mesenchymal Transition/drug effects ; Proteomics ; rho GTP-Binding Proteins/genetics ; rho GTP-Binding Proteins/metabolism ; Animals ; Mice ; Skin Neoplasms/drug therapy ; Skin Neoplasms/metabolism ; Skin Neoplasms/pathology ; Gene Expression Profiling ; Genome
    Chemical Substances Actins ; rho GTP-Binding Proteins (EC 3.6.5.2) ; Rhoj protein, mouse
    Language English
    Publishing date 2023-03-22
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/s41586-023-05838-7
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: An Unexpected Encounter: Respiratory Syncytial Virus Nonstructural Protein 1 Interacts with Mediator Subunit MED25.

    Van Royen, Tessa / Sedeyn, Koen / Moschonas, George D / Toussaint, Wendy / Vuylsteke, Marnik / Van Haver, Delphi / Impens, Francis / Eyckerman, Sven / Lemmens, Irma / Tavernier, Jan / Schepens, Bert / Saelens, Xavier

    Journal of virology

    2022  Volume 96, Issue 19, Page(s) e0129722

    Abstract: Human respiratory syncytial virus (RSV) is the leading cause of severe acute lower respiratory tract infections in infants worldwide. Nonstructural protein NS1 of RSV modulates the host innate immune response by acting as an antagonist of type I and type ...

    Abstract Human respiratory syncytial virus (RSV) is the leading cause of severe acute lower respiratory tract infections in infants worldwide. Nonstructural protein NS1 of RSV modulates the host innate immune response by acting as an antagonist of type I and type III interferon (IFN) production and signaling in multiple ways. Likely, NS1 performs this function by interacting with different host proteins. In order to obtain a comprehensive overview of the NS1 interaction partners, we performed three complementary protein-protein interaction screens, i.e., BioID, MAPPIT, and KISS. To closely mimic a natural infection, the BioID proximity screen was performed using a recombinant RSV in which the NS1 protein is fused to a biotin ligase. Remarkably, MED25, a subunit of the Mediator complex, was identified in all three performed screening methods as a potential NS1-interacting protein. We confirmed the interaction between MED25 and RSV NS1 by coimmunoprecipitation, not only upon overexpression of NS1 but also with endogenous NS1 during RSV infection. We also demonstrate that the replication of RSV can be enhanced in MED25 knockout A549 cells, suggesting a potential antiviral role of MED25 during RSV infection. Mediator subunits function as transcriptional coactivators and are involved in transcriptional regulation of their target genes. Therefore, the interaction between RSV NS1 and cellular MED25 might be beneficial for RSV during infection by affecting host transcription and the host immune response to infection.
    MeSH term(s) A549 Cells ; Humans ; Interferons/metabolism ; Mediator Complex/genetics ; Mediator Complex/metabolism ; Respiratory Syncytial Virus Infections/metabolism ; Respiratory Syncytial Virus, Human ; Viral Nonstructural Proteins/genetics ; Viral Nonstructural Proteins/metabolism
    Chemical Substances MED25 protein, human ; Mediator Complex ; Viral Nonstructural Proteins ; Interferons (9008-11-1)
    Language English
    Publishing date 2022-09-14
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 80174-4
    ISSN 1098-5514 ; 0022-538X
    ISSN (online) 1098-5514
    ISSN 0022-538X
    DOI 10.1128/jvi.01297-22
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Identification of the MuRF1 Skeletal Muscle Ubiquitylome Through Quantitative Proteomics.

    Baehr, Leslie M / Hughes, David C / Lynch, Sarah A / Van Haver, Delphi / Maia, Teresa Mendes / Marshall, Andrea G / Radoshevich, Lilliana / Impens, Francis / Waddell, David S / Bodine, Sue C

    Function (Oxford, England)

    2021  Volume 2, Issue 4, Page(s) zqab029

    Abstract: MuRF1 (TRIM63) is a muscle-specific E3 ubiquitin ligase and component of the ubiquitin proteasome system. MuRF1 is transcriptionally upregulated under conditions that cause muscle loss, in both rodents and humans, and is a recognized marker of muscle ... ...

    Abstract MuRF1 (TRIM63) is a muscle-specific E3 ubiquitin ligase and component of the ubiquitin proteasome system. MuRF1 is transcriptionally upregulated under conditions that cause muscle loss, in both rodents and humans, and is a recognized marker of muscle atrophy. In this study, we used in vivo electroporation to determine whether MuRF1 overexpression alone can cause muscle atrophy and, in combination with ubiquitin proteomics, identify the endogenous MuRF1 substrates in skeletal muscle. Overexpression of MuRF1 in adult mice increases ubiquitination of myofibrillar and sarcoplasmic proteins, increases expression of genes associated with neuromuscular junction instability, and causes muscle atrophy. A total of 169 ubiquitination sites on 56 proteins were found to be regulated by MuRF1. MuRF1-mediated ubiquitination targeted both thick and thin filament contractile proteins, as well as, glycolytic enzymes, deubiquitinases, p62, and VCP. These data reveal a potential role for MuRF1 in not only the breakdown of the sarcomere but also the regulation of metabolism and other proteolytic pathways in skeletal muscle.
    Language English
    Publishing date 2021-05-19
    Publishing country England
    Document type Journal Article
    ISSN 2633-8823
    ISSN (online) 2633-8823
    DOI 10.1093/function/zqab029
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Complementary peptides represent a credible alternative to agrochemicals by activating translation of targeted proteins.

    Ormancey, Mélanie / Guillotin, Bruno / Merret, Rémy / Camborde, Laurent / Duboé, Carine / Fabre, Bertrand / Pouzet, Cécile / Impens, Francis / Van Haver, Delphi / Carpentier, Marie-Christine / Clemente, Hélène San / Aguilar, Marielle / Lauressergues, Dominique / Scharff, Lars B / Pichereaux, Carole / Burlet-Schiltz, Odile / Bousquet-Antonelli, Cécile / Gevaert, Kris / Thuleau, Patrice /
    Plaza, Serge / Combier, Jean-Philippe

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 254

    Abstract: The current agriculture main challenge is to maintain food production while facing multiple threats such as increasing world population, temperature increase, lack of agrochemicals due to health issues and uprising of weeds resistant to herbicides. ... ...

    Abstract The current agriculture main challenge is to maintain food production while facing multiple threats such as increasing world population, temperature increase, lack of agrochemicals due to health issues and uprising of weeds resistant to herbicides. Developing novel, alternative, and safe methods is hence of paramount importance. Here, we show that complementary peptides (cPEPs) from any gene can be designed to target specifically plant coding genes. External application of synthetic peptides increases the abundance of the targeted protein, leading to related phenotypes. Moreover, we provide evidence that cPEPs can be powerful tools in agronomy to improve plant traits, such as growth, resistance to pathogen or heat stress, without the needs of genetic approaches. Finally, by combining their activity they can also be used to reduce weed growth.
    MeSH term(s) Weed Control ; Agrochemicals/pharmacology ; Herbicide Resistance/genetics ; Plant Weeds/genetics ; Peptides ; Crops, Agricultural/genetics
    Chemical Substances Agrochemicals ; Peptides
    Language English
    Publishing date 2023-01-17
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-35951-0
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: The mitotic checkpoint is a targetable vulnerability of carboplatin-resistant triple negative breast cancers.

    Moens, Stijn / Zhao, Peihua / Baietti, Maria Francesca / Marinelli, Oliviero / Van Haver, Delphi / Impens, Francis / Floris, Giuseppe / Marangoni, Elisabetta / Neven, Patrick / Annibali, Daniela / Sablina, Anna A / Amant, Frédéric

    Scientific reports

    2021  Volume 11, Issue 1, Page(s) 3176

    Abstract: Triple-negative breast cancer (TNBC) is the most aggressive breast cancer subtype, lacking effective therapy. Many TNBCs show remarkable response to carboplatin-based chemotherapy, but often develop resistance over time. With increasing use of ... ...

    Abstract Triple-negative breast cancer (TNBC) is the most aggressive breast cancer subtype, lacking effective therapy. Many TNBCs show remarkable response to carboplatin-based chemotherapy, but often develop resistance over time. With increasing use of carboplatin in the clinic, there is a pressing need to identify vulnerabilities of carboplatin-resistant tumors. In this study, we generated carboplatin-resistant TNBC MDA-MB-468 cell line and patient derived TNBC xenograft models. Mass spectrometry-based proteome profiling demonstrated that carboplatin resistance in TNBC is linked to drastic metabolism rewiring and upregulation of anti-oxidative response that supports cell replication by maintaining low levels of DNA damage in the presence of carboplatin. Carboplatin-resistant cells also exhibited dysregulation of the mitotic checkpoint. A kinome shRNA screen revealed that carboplatin-resistant cells are vulnerable to the depletion of the mitotic checkpoint regulators, whereas the checkpoint kinases CHEK1 and WEE1 are indispensable for the survival of carboplatin-resistant cells in the presence of carboplatin. We confirmed that pharmacological inhibition of CHEK1 by prexasertib in the presence of carboplatin is well tolerated by mice and suppresses the growth of carboplatin-resistant TNBC xenografts. Thus, abrogation of the mitotic checkpoint by CHEK1 inhibition re-sensitizes carboplatin-resistant TNBCs to carboplatin and represents a potential strategy for the treatment of carboplatin-resistant TNBCs.
    MeSH term(s) Animals ; Antineoplastic Agents/pharmacology ; Antineoplastic Combined Chemotherapy Protocols ; Carboplatin/pharmacology ; Cell Cycle Checkpoints/drug effects ; Cell Cycle Checkpoints/genetics ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Cell Line, Tumor ; Cell Proliferation/drug effects ; Checkpoint Kinase 1/genetics ; Checkpoint Kinase 1/metabolism ; DNA Damage ; Drug Resistance, Neoplasm/drug effects ; Drug Resistance, Neoplasm/genetics ; Drug Synergism ; Female ; Gene Expression Profiling ; Gene Expression Regulation, Neoplastic ; Humans ; Mice ; Neoplasm Proteins/classification ; Neoplasm Proteins/genetics ; Neoplasm Proteins/metabolism ; Protein-Tyrosine Kinases/genetics ; Protein-Tyrosine Kinases/metabolism ; Proteome/classification ; Proteome/genetics ; Proteome/metabolism ; Pyrazines/pharmacology ; Pyrazoles/pharmacology ; Signal Transduction ; Triple Negative Breast Neoplasms/drug therapy ; Triple Negative Breast Neoplasms/genetics ; Triple Negative Breast Neoplasms/metabolism ; Triple Negative Breast Neoplasms/pathology ; Xenograft Model Antitumor Assays
    Chemical Substances Antineoplastic Agents ; Cell Cycle Proteins ; Neoplasm Proteins ; Proteome ; Pyrazines ; Pyrazoles ; prexasertib ; Carboplatin (BG3F62OND5) ; Protein-Tyrosine Kinases (EC 2.7.10.1) ; WEE1 protein, human (EC 2.7.10.2) ; CHEK1 protein, human (EC 2.7.11.1) ; Checkpoint Kinase 1 (EC 2.7.11.1)
    Language English
    Publishing date 2021-02-04
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-021-82780-6
    Database MEDical Literature Analysis and Retrieval System OnLINE

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