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https://www.readbyqxmd.com/read/29218092/hsp90-inhibitor-sensitizes-trail-mediated-apoptosis-via-chop-dependent-dr5-upregulation-in-colon-cancer-cells
#1
Zhicheng Yao, Ang Chen, Xin Li, Zhiyong Zhu, Xin Jiang
Heat shock protein 90 (Hsp90), a molecular chaperone, is involved in a variety of physiological and pathological processes. Targeting Hsp90 by small molecules has been developed as an attractive strategy of anticancer therapy. In this study, we investigated the mechanism of Hsp90 inhibitor suppresses CRC growth and potentiates effects of other chemotherapeutic drugs. We found that Hsp90 inhibitor induces chop-dependent DR5 upregulation regardless of p53 status. Furthermore, DR5 is required for Hsp90 inhibitor-induced apoptosis...
2017: American Journal of Translational Research
https://www.readbyqxmd.com/read/29216330/genome-wide-analysis-of-the-brachypodium-distachyon-l-p-beauv-hsp90-gene-family-reveals-molecular-evolution-and-expression-profiling-under-drought-and-salt-stresses
#2
Ming Zhang, Zhiwei Shen, Guoqing Meng, Yu Lu, Yilei Wang
The structure, evolution, and function of heat shock proteins 90 (Hsp90s) have been investigated in great detail in fungi and animals. However, studies on the Hsp90 genes in plants are generally limited. Brachypodium distachyon (L.) P. Beauv., as a model plant for cereal crops, has become a potential biofuel grass. During its long evolution, the Hsp90 gene family in Brachypodium has developed some strategies to cope with adverse environments. How the Hsp90 gene family in Brachypodium evolved in different plant lineages and what its role is in plant responses to drought and salt stresses remains to be elucidated...
2017: PloS One
https://www.readbyqxmd.com/read/29212943/the-cellular-chaperone-heat-shock-protein-90-is-required-for-foot-and-mouth-disease-virus-capsid-precursor-processing-and-assembly-of-capsid-pentamers
#3
Joseph Newman, Amin S Asfor, Stephen Berryman, Terry Jackson, Stephen Curry, Tobias J Tuthill
Productive picornavirus infection requires the hijack of host cell pathways to aid with the different stages of virus entry, synthesis of the viral polyprotein and viral genome replication. Many picornaviruses, including foot-and-mouth disease virus (FMDV), assemble capsids via the multimerisation of several copies of a single capsid precursor protein into a pentameric subunit which further encapsidates the RNA. Pentamer formation is preceded by co- and post-translational modification of the capsid precursor (P1-2A) by viral and cellular enzymes, and the subsequent rearrangement of P1-2A into a structure amenable to pentamer formation...
December 6, 2017: Journal of Virology
https://www.readbyqxmd.com/read/29209046/cdc7-dbf4-mediated-phosphorylation-of-hsp90-s164-stabilizes-hsp90-hclk2-mrn-complex-to-enhance-atr-atm-signaling-that-overcomes-replication-stress-in-cancer
#4
An Ning Cheng, Chi-Chen Fan, Yu-Kang Lo, Cheng-Liang Kuo, Hui-Chun Wang, I-Hsin Lien, Shu-Yu Lin, Chung-Hsing Chen, Shih Sheng Jiang, I-Shou Chang, Hsueh-Fen Juan, Ping-Chiang Lyu, Alan Yueh-Luen Lee
Cdc7-Dbf4 kinase plays a key role in the initiation of DNA replication and contributes to the replication stress in cancer. The activity of human Cdc7-Dbf4 kinase remains active and acts as an effector of checkpoint under replication stress. However, the downstream targets of Cdc7-Dbf4 contributed to checkpoint regulation and replication stress-support function in cancer are not fully identified. In this work, we showed that aberrant Cdc7-Dbf4 induces DNA lesions that activate ATM/ATR-mediated checkpoint and homologous recombination (HR) DNA repair...
December 5, 2017: Scientific Reports
https://www.readbyqxmd.com/read/29207638/jolkinolide-b-induces-apoptosis-of-colorectal-carcinoma-through-ros-er-stress-ca2-mitochondria-dependent-pathway
#5
Jing Zhang, Yang Wang, Ye Zhou, Qing-Yu He
Colorectal carcinoma (CRC) remains one of the leading causes of death in cancer-related diseases. In this study, we aimed to investigate the anticancer effect of Jolkinolide B (JB), a bioactive diterpenoid component isolated from the dried roots of Euphorbia fischeriana Steud, on CRC cells and its underlying mechanisms. We found that JB suppressed the cell viability and colony formation of CRC cells, HT29 and SW620. Annexin V/PI assay revealed that JB induced apoptosis in CRC cells, which was further confirmed by the increased expression of cleaved-caspase3 and cleaved-PARP...
October 31, 2017: Oncotarget
https://www.readbyqxmd.com/read/29207057/molecular-mechanism-and-targeted-therapy-of-hsp90-involved-in-lung-cancer-new-discoveries-and-developments-review
#6
Biaoxue Rong, Shuanying Yang
The exploration of the molecular mechanisms and signaling pathways on lung cancer is very important for developing new strategies of diagnosis and treatment to this disease, such as finding valuable lung cancer markers and molecularly targeted therapies. Previously, a number of studies disclose that heat shock protein 90 (Hsp90) is upregulated in cancer cells, tissues and serum of lung cancer patients, and its upregulation intimately correlates with the occurrence, development and outcome of lung cancer. On the contrary, inhibition of Hsp90 can suppress cell proliferation, motility and metastasis of lung cancer and promote apoptosis of lung cancer cells via complex signaling pathways...
November 29, 2017: International Journal of Oncology
https://www.readbyqxmd.com/read/29206196/the-fkbp51-glucocorticoid-receptor-co-chaperone-regulation-function-and-implications-in-health-and-disease
#7
REVIEW
Gabriel R Fries, Nils C Gassen, Theo Rein
Among the chaperones and co-chaperones regulating the glucocorticoid receptor (GR), FK506 binding protein (FKBP) 51 is the most intensely investigated across different disciplines. This review provides an update on the role of the different co-chaperones of Hsp70 and Hsp90 in the regulation of GR function. The development leading to the focus on FKBP51 is outlined. Further, a survey of the vast literature on the mechanism and function of FKBP51 is provided. This includes its structure and biochemical function, its regulation on different levels-transcription, post-transcription, and post-translation-and its function in signaling pathways...
December 5, 2017: International Journal of Molecular Sciences
https://www.readbyqxmd.com/read/29206141/-epigallocatechin-3-gallate-inhibits-the-chaperone-activity-of-plasmodium-falciparum-hsp70-chaperones-and-abrogates-their-association-with-functional-partners
#8
Tawanda Zininga, Lebogang Ramatsui, Pertunia Bveledzani Makhado, Stanley Makumire, Ikechukwu Achilinou, Heinrich Hoppe, Heini Dirr, Addmore Shonhai
Heat shock proteins (Hsps), amongst them, Hsp70 and Hsp90 families, serve mainly as facilitators of protein folding (molecular chaperones) of the cell. The Hsp70 family of proteins represents one of the most important molecular chaperones in the cell. Plasmodium falciparum, the main agent of malaria, expresses six Hsp70 isoforms. Two (PfHsp70-1 and PfHsp70-z) of these localize to the parasite cytosol. PHsp70-1 is known to occur in a functional complex with another chaperone, PfHsp90 via a co-chaperone, P. falciparum Hsp70-Hsp90 organising protein (PfHop)...
December 5, 2017: Molecules: a Journal of Synthetic Chemistry and Natural Product Chemistry
https://www.readbyqxmd.com/read/29203717/hsp90-and-fkbp51-complex-regulators-of-psychiatric-diseases
#9
REVIEW
Marangelie Criado-Marrero, Theo Rein, Elisabeth B Binder, James T Porter, John Koren, Laura J Blair
Mood disorders affect nearly a quarter of the world's population. Therefore, understanding the molecular mechanisms underlying these conditions is of great importance. FK-506 binding protein 5 (FKBP5) encodes the FKBP51 protein, a heat shock protein 90 kDa (Hsp90) co-chaperone, and is a risk factor for several affective disorders. FKBP51, in coordination with Hsp90, regulates glucocorticoid receptor (GR) activity via a short negative feedback loop. This signalling pathway rapidly restores homeostasis in the hypothalamic-pituitary-adrenal (HPA) axis following stress...
January 19, 2018: Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
https://www.readbyqxmd.com/read/29203715/the-role-of-heat-shock-proteins-and-co-chaperones-in-heart-failure
#10
REVIEW
Mark J Ranek, Marisa J Stachowski, Jonathan A Kirk, Monte S Willis
The ongoing contractile and metabolic demands of the heart require a tight control over protein quality control, including the maintenance of protein folding, turnover and synthesis. In heart disease, increases in mechanical and oxidative stresses, post-translational modifications (e.g., phosphorylation), for example, decrease protein stability to favour misfolding in myocardial infarction, heart failure or ageing. These misfolded proteins are toxic to cardiomyocytes, directly contributing to the common accumulation found in human heart failure...
January 19, 2018: Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
https://www.readbyqxmd.com/read/29203712/heat-shock-protein-90-its-inhibition-and-function
#11
REVIEW
Abbey D Zuehlke, Michael A Moses, Len Neckers
The molecular chaperone heat shock protein 90 (Hsp90) facilitates metastable protein maturation, stabilization of aggregation-prone proteins, quality control of misfolded proteins and assists in keeping proteins in activation-competent conformations. Proteins that rely on Hsp90 for function are delivered to Hsp90 utilizing a co-chaperone-assisted cycle. Co-chaperones play a role in client transfer to Hsp90, Hsp90 ATPase regulation and stabilization of various Hsp90 conformational states. Many of the proteins chaperoned by Hsp90 (Hsp90 clients) are essential for the progression of various diseases, including cancer, Alzheimer's disease and other neurodegenerative diseases, as well as viral and bacterial infections...
January 19, 2018: Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
https://www.readbyqxmd.com/read/29203709/heat-shock-proteins-and-cancer-intracellular-chaperones-or-extracellular-signalling-ligands
#12
REVIEW
Stuart K Calderwood
Heat shock proteins (HSPs) are found at elevated concentrations in tumour cells, and this increase reflects the proteotoxic stress experienced by the cells due to expanding levels of the mutated oncoproteins that drive tumorigenesis. The protection of oncogenic proteins by HSPs offers a window of vulnerability in tumour metabolism that has been exploited using Hsp90-targeting drugs. Such compounds have been shown to cause inhibition and degradation of a wide range of proteins essential for oncogenesis. Recently, Hsp90 has also been shown to be secreted by tumour cells and to interact in autocrine or paracrine manners with the surfaces of adjacent cells, leading to increased growth and metastasis...
January 19, 2018: Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
https://www.readbyqxmd.com/read/29203708/protein-moonlighting-what-is-it-and-why-is-it-important
#13
REVIEW
Constance J Jeffery
Members of the GroEL/HSP60 protein family have been studied for many years because of their critical roles as ATP-dependent molecular chaperones, so it might come as a surprise that some have important functions in ATP-poor conditions, for example, when secreted outside the cell. At least some members of each of the HSP10, HSP70, HSP90, HSP100 and HSP110 heat shock protein families are also 'moonlighting proteins'. Moonlighting proteins exhibit more than one physiologically relevant biochemical or biophysical function within one polypeptide chain...
January 19, 2018: Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
https://www.readbyqxmd.com/read/29202402/design-synthesis-and-biological-evaluation-of-a-series-of-resorcinol-based-n-benzyl-benzamide-derivatives-as-potent-hsp90-inhibitors
#14
Sun You Park, Yong Jin Oh, Yunmee Lho, Ju Hui Jeong, Kwang-Hyeon Liu, Jaeyoung Song, Soong-Hyun Kim, Eunyoung Ha, Young Ho Seo
Heat shock protein 90 (Hsp90) is a ubiquitous molecular chaperone that is responsible for the stabilization and maturation of many oncogenic proteins. Therefore, Hsp90 has emerged as an attractive target in the field of cancer chemotherapy. In this study, we report the design, synthesis, and biological evaluation of a series of Hsp90 inhibitors. In particular, compound 30f shows a significant Hsp90α inhibitory activity with IC50 value of 5.3 nM and an excellent growth inhibition with GI50 value of 0.42 μM against non-small cell lung cancer cells, H1975...
November 21, 2017: European Journal of Medicinal Chemistry
https://www.readbyqxmd.com/read/29194075/cutaneous-angiosarcoma-update-on-biology-and-latest-treatment
#15
Yoshihiro Ishida, Atsushi Otsuka, Kenji Kabashima
PURPOSE OF REVIEW: The present review aims to provide readers with the latest updates on the biology and clinical management of cutaneous angiosarcoma (cAS). RECENT FINDINGS: The genomic alteration of cAS is heterogeneous. Mutations are enriched in the mitosis-activated kinase (MAPK) pathway. Functional analysis has identified molecules that may serve as potential markers and therapeutic targets of angiosarcoma. These molecules include survivin, HSP90, FOXM1, miR-497-5p, KCa3...
November 30, 2017: Current Opinion in Oncology
https://www.readbyqxmd.com/read/29191421/comparative-studies-of-the-low-resolution-structure-of-two-p23-co-chaperones-for-hsp90-identified-in-plasmodium-falciparum-genome
#16
Noeli S M Silva, Thiago V Seraphim, Karine Minari, Leandro R S Barbosa, Júlio C Borges
The p23 proteins are small acidic proteins that aid the functional cycle of the Hsp90 molecular chaperone. Such co-chaperone acts by temporarily inhibiting the ATPase activity of Hsp90 and exhibits intrinsic chaperone activity, suggesting independent roles. A search for p23 in the Plasmodium falciparum genome led to the identification of two putative proteins showing 13% identity to each other and approximately 20% identity to human p23. To understand the presence of two p23 proteins in this organism, we generated recombinant p23 proteins (Pfp23A and Pfp23B) and investigated their structure and function...
November 27, 2017: International Journal of Biological Macromolecules
https://www.readbyqxmd.com/read/29190920/a-cassaine-diterpene-alkaloid-3%C3%AE-acetyl-nor-erythrophlamide-suppresses-vegf-induced-angiogenesis-and-tumor-growth-via-inhibiting-enos-activation
#17
Nara Tae, Tran Manh Hung, Okwha Kim, Namho Kim, Suhyun Lee, Sunghun Na, Byung-Sun Min, Jeong-Hyung Lee
Angiogenesis is one of the hallmarks of cancer, playing an essential role in tumor growth, invasion, and metastasis. 3β-Acetyl-nor-erythrophlamide (3-ANE), a cassaine diterpene alkaloid compound from Erythrophleum fordii, exerts various pharmacological effects, including antitumor activity. However, the effects of 3-ANE on tumor angiogenesis and its potential molecular mechanism are still unknown. Here, we demonstrated that 3-ANE inhibited the vascular endothelial growth factor (VEGF)-mediated proliferation, migration, invasion, and capillary-like tube formation of human umbilical vascular endothelial cells (HUVECs), without inducing apoptosis...
November 3, 2017: Oncotarget
https://www.readbyqxmd.com/read/29187525/humanin-is-an-endogenous-activator-of-chaperone-mediated-autophagy
#18
Zhenwei Gong, Inmaculada Tasset, Antonio Diaz, Jaime Anguiano, Emir Tas, Lingguang Cui, Regina Kuliawat, Honghai Liu, Bernhard Kühn, Ana Maria Cuervo, Radhika Muzumdar
Chaperone-mediated autophagy (CMA) serves as quality control during stress conditions through selective degradation of cytosolic proteins in lysosomes. Humanin (HN) is a mitochondria-associated peptide that offers cytoprotective, cardioprotective, and neuroprotective effects in vivo and in vitro. In this study, we demonstrate that HN directly activates CMA by increasing substrate binding and translocation into lysosomes. The potent HN analogue HNG protects from stressor-induced cell death in fibroblasts, cardiomyoblasts, neuronal cells, and primary cardiomyocytes...
November 29, 2017: Journal of Cell Biology
https://www.readbyqxmd.com/read/29186352/atm-is-required-for-the-prolactin-induced-hsp90-mediated-increase-in-cellular-viability-and-clonogenic-growth-after-dna-damage
#19
Ödül Karayazi Atici, Anna Urbanska, Sesha Gopal Gopinathan, Florence Boutillon, Vincent Goffin, Carrie S Shemanko
Prolactin acts as a survival factor for breast cancer cells, but the prolactin signaling pathway and the mechanism is unknown. Previously, we identified the master chaperone, heat shock protein 90α (HSP90α), as a prolactin-Janus-Kinase-(JAK2)-signal-transducer-and-activator-of-transcription-5-(STAT5) target gene involved in survival, and here we investigated the role of HSP90 in the mechanism of prolactin-induced viability in response to DNA damage. The ataxia-telangiectasia mutated kinase protein (ATM) plays a critical role in the cellular response to double strand DNA damage...
November 24, 2017: Endocrinology
https://www.readbyqxmd.com/read/29180187/glutamine-reduces-myocardial-cell-apoptosis-in-a-rat-model-of-sepsis-by-promoting-expression-of-heat-shock-protein-90
#20
Wanxia Li, Shaoyu Tao, Qinghua Wu, Tao Wu, Ran Tao, Jun Fan
BACKGROUND: Myocardial cell injury and cardiac myocyte apoptosis are associated with sepsis. Glutamine (Gln) has been reported to repair myocardial cell injury. The aim of this study was to explore the role of Gln on cardiac myocytes in a cecal ligation and puncture (CLP) model of sepsis in Wistar rats. MATERIALS AND METHODS: Following induction of sepsis in a CLP rat model, viral encoding heat shock protein 90 (Hsp90) gene and Hsp90dsDNA were designed to express and knockdown Hsp90, respectively...
December 2017: Journal of Surgical Research
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