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Cell Stress & Chaperones

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https://www.readbyqxmd.com/read/28512729/protective-effects-of-nebivolol-against-interleukin-1%C3%AE-il-1%C3%AE-induced-type-ii-collagen-destruction-mediated-by-matrix-metalloproteinase-13-mmp-13
#1
Zhigang Li, Baoyi Liu, Dewei Zhao, BenJie Wang, Yupeng Liu, Yao Zhang, Fengde Tian, Borui Li
The pathological progression of osteoarthritis (OA) involves degradation of articular cartilage matrix. Type II collagen is the main component of cartilage matrix, which is degraded by pro-inflammatory cytokines such as IL-1β mediated by MMP-13. Nebivolol, a licensed drug used for the treatment of hypertension in clinics, displays its anti-inflammatory capacity in various conditions. However, whether Nebivolol has a protective effect on cartilage matrix degradation has not been reported before. In this study, we investigated the effects of Nebivolol on regulating the expression of MMP-13 and degradation of type II collagen...
May 17, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28484965/the-protective-role-of-small-heat-shock-proteins-in-cardiac-diseases-key-role-in-atrial-fibrillation
#2
Xu Hu, Denise M S Van Marion, Marit Wiersma, Deli Zhang, Bianca J J M Brundel
Atrial fibrillation (AF) is the most common tachyarrhythmia which is associated with increased morbidity and mortality. AF usually progresses from a self-terminating paroxysmal to persistent disease. It has been recognized that AF progression is driven by structural remodeling of cardiomyocytes, which results in electrical and contractile dysfunction of the atria. We recently showed that structural remodeling is rooted in derailment of proteostasis, i.e., homeostasis of protein production, function, and degradation...
May 8, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28474205/chaperone-co-inducer-bgp-15-inhibits-histone-deacetylases-and-enhances-the-heat-shock-response-through-increased-chromatin-accessibility
#3
Marek A Budzyński, Tim Crul, Samu V Himanen, Noemi Toth, Ferenc Otvos, Lea Sistonen, Laszlo Vigh
Defects in cellular protein homeostasis are associated with many severe and prevalent pathological conditions such as neurodegenerative diseases, muscle dystrophies, and metabolic disorders. One way to counteract these defects is to improve the protein homeostasis capacity through induction of the heat shock response. Despite numerous attempts to develop strategies for chemical activation of the heat shock response by heat shock transcription factor 1 (HSF1), the underlying mechanisms of drug candidates' mode of action are poorly understood...
May 4, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28470624/%C3%AE-b-crystallin-is-a-sensor-for-assembly-intermediates-and-for-the-subunit-topology-of-desmin-intermediate-filaments
#4
Sarika Sharma, Gloria M Conover, Jayne L Elliott, Ming Der Perng, Harald Herrmann, Roy A Quinlan
Mutations in the small heat shock protein chaperone CRYAB (αB-crystallin/HSPB5) and the intermediate filament protein desmin, phenocopy each other causing cardiomyopathies. Whilst the binding sites for desmin on CRYAB have been determined, desmin epitopes responsible for CRYAB binding and also the parameters that determine CRYAB binding to desmin filaments are unknown. Using a combination of co-sedimentation centrifugation, viscometric assays and electron microscopy of negatively stained filaments to analyse the in vitro assembly of desmin filaments, we show that the binding of CRYAB to desmin is subject to its assembly status, to the subunit organization within filaments formed and to the integrity of the C-terminal tail domain of desmin...
May 3, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28470623/erratum-to-association-of-heat-stress-protein-90-and-70-gene-polymorphism-with-adaptability-traits-in-indian-sheep-ovis-aries
#5
K M Singh, S Singh, I Ganguly, Raja K Nachiappan, A Ganguly, R Venkataramanan, A Chopra, H K Narula
No abstract text is available yet for this article.
May 3, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28466152/suppression-of-heat-shock-protein-70-by-sirna-enhances-the-antitumor-effects-of-cisplatin-in-cultured-human-osteosarcoma-cells
#6
Yuki Mori, Ryu Terauchi, Toshiharu Shirai, Shinji Tsuchida, Naoki Mizoshiri, Yuji Arai, Tsunao Kishida, Hiroyoshi Fujiwara, Osam Mazda, Toshikazu Kubo
Although advances in chemotherapy have improved the prognosis for osteosarcoma, some patients do not respond sufficiently to treatment. Heat shock protein 70 (Hsp70) is expressed at high levels in cancer cells and attenuates the therapeutic efficacy of anticancer agents, resulting in a poorer prognosis. This study investigated whether small interfering RNA (siRNA)-mediated inhibition of Hsp70 expression in an osteosarcoma cell line would enhance sensitivity to cisplatin. The expression of Hsp70 with cisplatin treatment was observed by using Western blotting and real-time reverse transcription polymerase chain reaction (RT-PCR)...
May 2, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28455613/polymyxin-b-inhibits-the-chaperone-activity-of-plasmodium-falciparum-hsp70
#7
Tawanda Zininga, Ofentse J Pooe, Pertunia B Makhado, Lebogang Ramatsui, Earl Prinsloo, Ikechukwu Achilonu, Heinrich Dirr, Addmore Shonhai
Heat shock protein 70 (Hsp70) is a molecular chaperone that plays an important role in cellular proteostasis. Hsp70s are also implicated in the survival and pathogenicity of malaria parasites. The main agent of malaria, Plasmodium falciparum, expresses six Hsp70s. Of these, two (PfHsp70-1 and PfHsp70-z) localize to the parasite cytosol. Previously conducted gene knockout studies suggested that PfHsp70-z is essential, and it has been demonstrated that small-molecule inhibitors targeting PfHsp70-1 cause parasite death...
April 28, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28455612/hsp90-inhibitors-radicicol-and-geldanamycin-have-opposing-effects-on-leishmania-aha1-dependent-proliferation
#8
Katharina Bartsch, Antje Hombach-Barrigah, Joachim Clos
Hsp90 and its co-chaperones are essential for the medically important parasite Leishmania donovani, facilitating life cycle control and intracellular survival. Activity of Hsp90 is regulated by co-chaperones of the Aha1 and P23 families. In this paper, we studied the expression of L. donovani Aha1 in two life cycle stages, its interaction with Hsp90 and the phenotype of Aha1 null mutants during the insect stage and inside infected macrophages. This study provides a detailed in vitro analysis of the function of Aha1 in Leishmania parasites and the first instance of a reverse genetic analysis of Aha1 in a protozoan parasite...
April 28, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28451878/differential-expression-of-myocardial-heat-shock-proteins-in-rats-acutely-exposed-to-fluoride
#9
Lakshmikanthan Panneerselvam, Azhwar Raghunath, Ekambaram Perumal
Acute fluoride (F(-)) toxicity is known to cause severe cardiac complications and leads to sudden heart failure. Previously, we reported that increased myocardial oxidative damage, apoptosis, altered cytoskeleton and AMPK signaling proteins associated with energy deprivation in acute F(-) induced cardiac dysfunction. The present study was aimed to decipher the status of myocardial heat shock proteins (Hsps-Hsp27, Hsp32, Hsp40, Hsp60, Hsp70, Hsp90) and heat shock transcription factor 1 (Hsf1) in acute F(-)-intoxicated rats...
April 27, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28447215/interplay-between-recombinant-hsp70-and-proteasomes-proteasome-activity-modulation-and-ubiquitin-independent-cleavage-of-hsp70
#10
Alexey V Morozov, Tatiana M Astakhova, David G Garbuz, George S Krasnov, Natalia V Bobkova, Olga G Zatsepina, Vadim L Karpov, Michail B Evgen'ev
The heat shock protein 70 (Hsp70, human HSPA1A) plays indispensable roles in cellular stress responses and protein quality control (PQC). In the framework of PQC, it cooperates with the ubiquitin-proteasome system (UPS) to clear damaged and dysfunctional proteins in the cell. Moreover, Hsp70 itself is rapidly degraded following the recovery from stress. It was demonstrated that its fast turnover is mediated via ubiquitination and subsequent degradation by the 26S proteasome. At the same time, the effect of Hsp70 on the functional state of proteasomes has been insufficiently investigated...
April 26, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28425051/upregulation-and-phosphorylation-of-hspb1-hsp25-and-hspb5-%C3%AE-b-crystallin-after-transient-middle-cerebral-artery-occlusion-in-rats
#11
Britta Bartelt-Kirbach, Alexander Slowik, Cordian Beyer, Nikola Golenhofen
Ischemic stroke leads to cellular dysfunction, cell death, and devastating clinical outcomes. The cells of the brain react to such a cellular stress by a stress response with an upregulation of heat shock proteins resulting in activation of endogenous neuroprotective capacities. Several members of the family of small heat shock proteins (HspBs) have been shown to be neuroprotective. However, yet no systematic study examined all HspBs during cerebral ischemia. Here, we performed a comprehensive comparative study comprising all HspBs in an animal model of stroke, i...
April 20, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28391594/the-functional-roles-of-the-unstructured-n-and-c-terminal-regions-in-%C3%AE-b-crystallin-and-other-mammalian-small-heat-shock-proteins
#12
John A Carver, Aidan B Grosas, Heath Ecroyd, Roy A Quinlan
Small heat-shock proteins (sHsps), such as αB-crystallin, are one of the major classes of molecular chaperone proteins. In vivo, under conditions of cellular stress, sHsps are the principal defence proteins that prevent large-scale protein aggregation. Progress in determining the structure of sHsps has been significant recently, particularly in relation to the conserved, central and β-sheet structured α-crystallin domain (ACD). However, an understanding of the structure and functional roles of the N- and C-terminal flanking regions has proved elusive mainly because of their unstructured and dynamic nature...
April 8, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28389817/oligomeric-structure-and-chaperone-like-activity-of-drosophila-melanogaster-mitochondrial-small-heat-shock-protein-hsp22-and-arginine-mutants-in-the-alpha-crystallin-domain
#13
Afrooz Dabbaghizadeh, Stéphanie Finet, Genevieve Morrow, Mohamed Taha Moutaoufik, Robert M Tanguay
The structure and chaperone function of DmHsp22WT, a small Hsp of Drosophila melanogaster localized within mitochondria were examined. Mutations of conserved arginine mutants within the alpha-crystallin domain (ACD) domain (R105G, R109G, and R110G) were introduced, and their effects on oligomerization and chaperone function were assessed. Arginine to glycine mutations do not induce significant changes in tryptophan fluorescence, and the mutated proteins form oligomers that are of equal or smaller size than the wild-type protein...
April 7, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28364346/the-growing-world-of-small-heat-shock-proteins-from-structure-to-functions
#14
REVIEW
Serena Carra, Simon Alberti, Patrick A Arrigo, Justin L Benesch, Ivor J Benjamin, Wilbert Boelens, Britta Bartelt-Kirbach, Bianca J J M Brundel, Johannes Buchner, Bernd Bukau, John A Carver, Heath Ecroyd, Cecilia Emanuelsson, Stephanie Finet, Nikola Golenhofen, Pierre Goloubinoff, Nikolai Gusev, Martin Haslbeck, Lawrence E Hightower, Harm H Kampinga, Rachel E Klevit, Krzysztof Liberek, Hassane S Mchaourab, Kathryn A McMenimen, Angelo Poletti, Roy Quinlan, Sergei V Strelkov, Melinda E Toth, Elizabeth Vierling, Robert M Tanguay
Small heat shock proteins (sHSPs) are present in all kingdoms of life and play fundamental roles in cell biology. sHSPs are key components of the cellular protein quality control system, acting as the first line of defense against conditions that affect protein homeostasis and proteome stability, from bacteria to plants to humans. sHSPs have the ability to bind to a large subset of substrates and to maintain them in a state competent for refolding or clearance with the assistance of the HSP70 machinery. sHSPs participate in a number of biological processes, from the cell cycle, to cell differentiation, from adaptation to stressful conditions, to apoptosis, and, even, to the transformation of a cell into a malignant state...
March 31, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28337642/the-small-heat-shock-proteins-%C3%AE-b-crystallin-hspb5-and-hsp27-hspb1-inhibit-the-intracellular-aggregation-of-%C3%AE-synuclein
#15
Dezerae Cox, Heath Ecroyd
Protein homeostasis, or proteostasis, is the process of maintaining the conformational and functional integrity of the proteome. Proteostasis is preserved in the face of stress by a complex network of cellular machinery, including the small heat shock molecular chaperone proteins (sHsps), which act to inhibit the aggregation and deposition of misfolded protein intermediates. Despite this, the pathogenesis of several neurodegenerative diseases has been inextricably linked with the amyloid fibrillar aggregation and deposition of α-synuclein (α-syn)...
March 23, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28332148/ph-dependent-structural-modulation-is-conserved-in-the-human-small-heat-shock-protein-hsbp1
#16
Amanda F Clouser, Rachel E Klevit
The holdase activity and oligomeric propensity of human small heat shock proteins (sHSPs) are regulated by environmental factors. However, atomic-level details are lacking for the mechanisms by which stressors alter sHSP responses. We previously demonstrated that regulation of HSPB5 is mediated by a single conserved histidine over a physiologically relevant pH range of 6.5-7.5. Here, we demonstrate that HSPB1 responds to pH via a similar mechanism through pH-dependent structural changes that are induced via protonation of the structurally analogous histidine...
March 22, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28275944/fine-tuning-of-actin-dynamics-by-the-hspb8-bag3-chaperone-complex-facilitates-cytokinesis-and-contributes-to-its-impact-on-cell-division
#17
Alice Anaïs Varlet, Margit Fuchs, Carole Luthold, Herman Lambert, Jacques Landry, Josée N Lavoie
The small heat shock protein HSPB8 and its co-chaperone BAG3 are proposed to regulate cytoskeletal proteostasis in response to mechanical signaling in muscle cells. Here, we show that in dividing cells, the HSPB8-BAG3 complex is instrumental to the accurate disassembly of the actin-based contractile ring during cytokinesis, a process required to allow abscission of daughter cells. Silencing of HSPB8 markedly decreased the mitotic levels of BAG3 in HeLa cells, supporting its crucial role in BAG3 mitotic functions...
March 8, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28265807/association-of-heat-stress-protein-90-and-70-gene-polymorphism-with-adaptability-traits-in-indian-sheep-ovis-aries
#18
K M Singh, S Singh, I Ganguly, Raja K Nachiappan, A Ganguly, R Venkataramanan, A Chopra, H K Narula
Heat stress proteins assist cellular proteins in the acquisition of native structure. The present research was conducted to study how thermo-tolerance is modulated by HSP90 and HSP70 gene polymorphism and its association with hemato-physio-biochemical parameters, supported by their expression profiles in Chokla, Magra, Marwari, and Madras Red sheep breeds. Least square analysis revealed significant effect (P < 0.05) of season and breed on all the physiological parameters, i.e., temperature, respiratory rate, and pulse rate (a...
March 6, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28425050/oxidative-protein-modification-alters-proteostasis-under-acute-hypobaric-hypoxia-in-skeletal-muscles-a-comprehensive-in-vivo-study
#19
Akanksha Agrawal, Richa Rathor, Geetha Suryakumar
While numerous maladies are associated with hypobaric hypoxia, muscle protein loss is an important under studied topic. Hence, the present study was designed to investigate the mechanism of muscle protein loss at HH. SD rats were divided into normoxic rats, while remaining rats were exposed to simulated hypoxia equivalent to 282-torr pressure (equal to an altitude of 7620 m, 8% oxygen), at 25 °C for 6, 12, and 24 h. Post-exposure rats were sacrificed and analysis was performed. Ergo, muscle loss-related changes were observed at 12 and 24 h post-HH exposure...
May 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28409327/heat-shock-proteins-and-kidney-disease-perspectives-of-hsp-therapy
#20
REVIEW
Natalia Chebotareva, Irina Bobkova, Evgeniy Shilov
Heat shock proteins (HSPs) mediate a diverse range of cellular functions, prominently including folding and regulatory processes of cellular repair. A major property of these remarkable proteins, dependent on intracellular or extracellular location, is their capacity for immunoregulation that optimizes immune activity while avoiding hyperactivated inflammation. In this review, recent investigations are described, which examine roles of HSPs in protection of kidney tissue from various traumatic influences and demonstrate their potential for clinical management of nephritic disease...
May 2017: Cell Stress & Chaperones
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