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Cell Stress & Chaperones

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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
#1
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/28425050/oxidative-protein-modification-alters-proteostasis-under-acute-hypobaric-hypoxia-in-skeletal-muscles-a-comprehensive-in-vivo-study
#2
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...
April 19, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28409327/heat-shock-proteins-and-kidney-disease-perspectives-of-hsp-therapy
#3
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...
April 13, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28397086/structure-activity-relationship-of-piperine-and-its-synthetic-amide-analogs-for-therapeutic-potential-to-prevent-experimentally-induced-er-stress-in-vitro
#4
Ayat S Hammad, Sreenithya Ravindran, Ashraf Khalil, Shankar Munusamy
Endoplasmic reticulum (ER) is the key organelle involved in protein folding and maturation. Emerging studies implicate the role of ER stress in the development of chronic kidney disease. Thus, there is an urgent need for compounds that could ameliorate ER stress and prevent CKD. Piperine and its analogs have been reported to exhibit multiple pharmacological activities; however, their efficacy against ER stress in kidney cells has not been studied yet. Hence, the goal of this study was to synthesize amide-substituted piperine analogs and screen them for pharmacological activity to relieve ER stress using an in vitro model of tunicamycin-induced ER stress using normal rat kidney (NRK-52E) cells...
April 10, 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
#5
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
#6
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
#7
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/28337643/recombinant-heat-shock-protein-27-hsp27-hspb1-protects-against-cadmium-induced-oxidative-stress-and-toxicity-in-human-cervical-cancer-cells
#8
Daiana G Alvarez-Olmedo, Veronica S Biaggio, Geremy A Koumbadinga, Nidia N Gómez, Chunhua Shi, Daniel R Ciocca, Zarah Batulan, Mariel A Fanelli, Edward R O'Brien
Cadmium (Cd) is a carcinogen with several well-described toxicological effects in humans, but its molecular mechanisms are still not fully understood. Overexpression of heat shock protein 27 (HSP27/HSPB1)-a multifunctional protein chaperone-has been shown to protect cells from oxidative damage and apoptosis triggered by Cd exposure. The aims of this work were to investigate the potential use of extracellular recombinant HSP27 to prevent/counteract Cd-induced cellular toxicity and to evaluate if peroxynitrite was involved in the development of Cd-induced toxicity...
March 24, 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
#9
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
#10
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/28324352/the-six-tomato-yellow-leaf-curl-virus-genes-expressed-individually-in-tomato-induce-different-levels-of-plant-stress-response-attenuation
#11
Rena Gorovits, Adi Moshe, Linoy Amrani, Rotem Kleinberger, Ghandi Anfoka, Henryk Czosnek
Tomato yellow leaf curl virus (TYLCV) is a begomovirus infecting tomato plants worldwide. TYLCV needs a healthy host environment to ensure a successful infection cycle for long periods. Hence, TYLCV restrains its destructive effect and induces neither a hypersensitive response nor cell death in infected tomatoes. On the contrary, TYLCV counteracts cell death induced by other factors, such as inactivation of HSP90 functionality. Suppression of plant death is associated with the inhibition of the ubiquitin 26S proteasome degradation and with a deactivation of the heat shock transcription factor HSFA2 pathways (including decreased HSP17 levels)...
March 21, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28321764/protective-manifestation-of-bacoside-a-and-bromelain-in-terms-of-cholinesterases-gamma-amino-butyric-acid-serotonin-level-and-stress-proteins-in-the-brain-of-dichlorvos-intoxicated-mice
#12
Bharti Chaudhary, Renu Bist
The objective of the study was to evaluate the neuroprotective effects of bacoside A and bromelain against dichlorvos-incited toxicity. Healthy 6-8-week old, male Swiss mice were administered subacute doses of dichlorvos (40 mg/kg bw), bacoside A (5 mg/kg bw) and bromelain (70 mg/kg bw). AChE, BChE, GABA, serotonin and total protein content and their expressions were used for determination of toxic action of dichlorvos. Protective effects of bacoside A and bromelain were evaluated on the same parameters...
March 20, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28303510/enhanced-resistance-against-vibrio-harveyi-infection-by-carvacrol-and-its-association-with-the-induction-of-heat-shock-protein-72-in-gnotobiotic-artemia-franciscana
#13
Kartik Baruah, Parisa Norouzitallab, Ho Phuong Pham Duy Phong, Guy Smagghe, Peter Bossier
Induction of HSP72 is a natural response of stressed organisms that protects against many insults including bacterial diseases in farm (aquatic) animals. It would therefore be of great health benefit to search for natural compounds that are clinically safe yet able to induce HSP72 in animals. The phenolic compound carvacrol, an approved food component, had been shown in in vitro study to act as a co-inducer of HSP72, enhancing HSP72 production only in combination with a bona fide stress compared to the compound alone...
March 16, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28285429/hypothermia-decreased-the-expression-of-heat-shock-proteins-in-neonatal-rat-model-of-hypoxic-ischemic-encephalopathy
#14
Byong Sop Lee, Euiseok Jung, Yeonjoo Lee, Sung-Hoon Chung
Hypothermia (HT) is a well-established neuroprotective strategy against neonatal hypoxic ischemic encephalopathy (HIE). The overexpression of heat shock proteins (HSP) has been shown to provide neuroprotection in animal models of stroke. We aimed to investigate the effect of HT on HSP70 and HSP27 expression in a neonatal rat model of HIE. Seven-day-old rat pups were exposed to hypoxia for 90 min to establish the Rice-Vannucci model and were assigned to the following four groups: hypoxic injury (HI)-normothermia (NT, 36 °C), HI-HT (30 °C), sham-NT, and sham-HT...
March 11, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28283895/influence-of-the-pde5-inhibitor-tadalafil-on-redox-status-and-antioxidant-defense-system-in-c2c12-skeletal-muscle-cells
#15
Guglielmo Duranti, Roberta Ceci, Paolo Sgrò, Stefania Sabatini, Luigi Di Luigi
Phosphodiesterase type 5 inhibitors (PDE5Is), widely known for their beneficial effects onto male erectile dysfunction, seem to exert favorable effects onto metabolism as well. Tadalafil exposure increases oxidative metabolism of C2C12 skeletal muscle cells. A rise in fatty acid (FA) metabolism, requiring more oxygen, could induce a larger reactive oxygen species (ROS) release as a byproduct thus leading to a redox imbalance. The aim of this study was to determine how PDE5I tadalafil influences redox status in skeletal muscle cells to match the increasing oxidative metabolism...
March 11, 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
#16
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
#17
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/28261750/partial-dispensability-of-djp1-s-j-domain-in-peroxisomal-protein-import-in-saccharomyces-cerevisiae-results-from-genetic-redundancy-with-another-class-ii-j-protein-caj1
#18
Neha Dobriyal, Prerna Tripathi, Susrita Sarkar, Yogesh Tak, Amit K Verma, Chandan Sahi
J proteins are obligate co-chaperones of Hsp70s. Via their signature J domain, all J proteins interact with their partner Hsp70s and stimulate their weak ATPase activity, which is vital for Hsp70 functions. The dependency of J proteins on their J domain is such that mutations in critical amino acids in the J domain often results into a null phenotype for a particular J protein. Here, we show that the J domain of Djp1, a cytosolic J protein important for peroxisomal protein import in Saccharomyces cerevisiae, is partially dispensable...
March 6, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28258486/lea-proteins-are-involved-in-cyst-desiccation-resistance-and-other-abiotic-stresses-in-azotobacter-vinelandii
#19
Julieta Rodriguez-Salazar, Soledad Moreno, Guadalupe Espín
Late embryogenesis abundant (LEA) proteins constitute a large protein family that is closely associated with resistance to abiotic stresses in multiple organisms and protect cells against drought and other stresses. Azotobacter vinelandii is a soil bacterium that forms desiccation-resistant cysts. This bacterium possesses two genes, here named lea1 and lea2, coding for avLEA1 and avLEA2 proteins, both containing 20-mer motifs characteristic of eukaryotic plant LEA proteins. In this study, we found that disruption of the lea1 gene caused a loss of the cysts' viability after 3 months of desiccation, whereas at 6 months, wild-type or lea2 mutant strain cysts remained viable...
March 3, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28214988/an-alternative-splice-variant-of-human-%C3%AE-a-crystallin-modulates-the-oligomer-ensemble-and-the-chaperone-activity-of-%C3%AE-crystallins
#20
Waldemar Preis, Annika Bestehorn, Johannes Buchner, Martin Haslbeck
In humans, ten genes encode small heat shock proteins with lens αA-crystallin and αB-crystallin representing two of the most prominent members. The canonical isoforms of αA-crystallin and αB-crystallin collaborate in the eye lens to prevent irreversible protein aggregation and preserve visual acuity. α-Crystallins form large polydisperse homo-oligomers and hetero-oligomers and as part of the proteostasis system bind substrate proteins in non-native conformations, thereby stabilizing them. Here, we analyzed a previously uncharacterized, alternative splice variant (isoform 2) of human αA-crystallin with an exchanged N-terminal sequence...
February 18, 2017: Cell Stress & Chaperones
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