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Cell Stress & Chaperones

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https://www.readbyqxmd.com/read/28220454/the-remarkable-multivalency-of-the-hsp70-chaperones
#1
REVIEW
Erik R P Zuiderweg, Lawrence E Hightower, Jason E Gestwicki
Hsp70 proteins are key to maintaining intracellular protein homeostasis. To carry out this task, they employ a large number of cochaperones and adapter proteins. Here, we review what is known about the interaction between the chaperones and partners, with a strong slant toward structural biology. Hsp70s in general, and Hsc70 (HSPA8) in particular, display an amazing array of interfaces with their protein cofactors. We also review the known interactions between Hsp70s with lipids and with active compounds that may become leads toward Hsp70 modulation for treatment of a variety of diseases...
February 20, 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
#2
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
https://www.readbyqxmd.com/read/28181153/an-interaction-study-in-mammalian-cells-demonstrates-weak-binding-of-hspb2-to-bag3-which-is-regulated-by-hspb3-and-abrogated-by-hspb8
#3
Federica F Morelli, Laura Mediani, Lonneke Heldens, Jessika Bertacchini, Ilaria Bigi, Arianna Dorotea Carrà, Jonathan Vinet, Serena Carra
The ten mammalian small heat shock proteins (sHSPs/HSPBs) show a different expression profile, although the majority of them are abundant in skeletal and cardiac muscles. HSPBs form hetero-oligomers and homo-oligomers by interacting together and complexes containing, e.g., HSPB2/HSPB3 or HSPB1/HSPB5 have been documented in mammalian cells and muscles. Moreover, HSPB8 associates with the Hsc70/Hsp70 co-chaperone BAG3, in mammalian, skeletal, and cardiac muscle cells. Interaction of HSPB8 with BAG3 regulates its stability and function...
February 8, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28160209/increased-expression-of-microrna-378a-5p-in-acute-ethanol-exposure-of-rat-cardiomyocytes
#4
Zhongkai Wang, Jingwen Song, Liang Zhang, Songqun Huang, Lizhi Bao, Feng Chen, Xianxian Zhao
Alcohol abuse is a risk factor for a distinct form of congestive heart failure, known as alcoholic cardiomyopathy (ACM). Here, we investigate how microRNAs may participate in the induction of cardiomyocyte apoptosis associated with ethanol exposure in vitro. Increasing the concentrations of ethanol to primary rat cardiomyocytes resulted in elevated apoptosis assessed by annexin V and propidium iodide staining, and reduced expression of an enzyme for alcohol detoxification aldehyde dehydrogenase 2 (ALDH2). These ethanol effects were accompanied by a substantial elevation of miR-378a-5p...
February 3, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28155127/attenuation-of-exercise-induced-heat-shock-protein-72-expression-blunts-improvements-in-whole-body-insulin-resistance-in-rats-with-type-2-diabetes
#5
Takamasa Tsuzuki, Hiroyuki Kobayashi, Toshinori Yoshihara, Ryo Kakigi, Noriko Ichinoseki-Sekine, Hisashi Naito
Heat shock proteins (HSPs) play an important role in insulin resistance and improve the cellular stress response via HSP induction by exercise to treat type 2 diabetes. In this study, the effects of exercise-induced HSP72 expression levels on whole-body insulin resistance in type 2 diabetic rats were investigated. Male 25-week-old Otsuka Long-Evans Tokushima Fatty rats were divided into three groups: sedentary (Sed), trained in a thermal-neutral environment (NTr: 25 °C), and trained in a cold environment (CTr: 4 °C)...
February 2, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28144778/mammalian-hspb1-hsp27-is-a-molecular-sensor-linked-to-the-physiology-and-environment-of-the-cell
#6
REVIEW
André-Patrick Arrigo
Constitutively expressed small heat shock protein HspB1 regulates many fundamental cellular processes and plays major roles in many human pathological diseases. In that regard, this chaperone has a huge number of apparently unrelated functions that appear linked to its ability to recognize many client polypeptides that are subsequently modified in their activity and/or half-life. A major parameter to understand how HspB1 is dedicated to interact with particular clients in defined cellular conditions relates to its complex oligomerization and phosphorylation properties...
January 31, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28130664/chaperone-activity-of-human-small-heat-shock-protein-gst-fusion-proteins
#7
Hannah Arbach, Caley Butler, Kathryn A McMenimen
Small heat shock proteins (sHsps) are a ubiquitous part of the machinery that maintains cellular protein homeostasis by acting as molecular chaperones. sHsps bind to and prevent the aggregation of partially folded substrate proteins in an ATP-independent manner. sHsps are dynamic, forming an ensemble of structures from dimers to large oligomers through concentration-dependent equilibrium dissociation. Based on structural studies and mutagenesis experiments, it is proposed that the dimer is the smallest active chaperone unit, while larger oligomers may act as storage depots for sHsps or play additional roles in chaperone function...
January 27, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28120291/role-of-shsps-in-organizing-cytosolic-protein-aggregation-and-disaggregation
#8
REVIEW
Axel Mogk, Bernd Bukau
Small heat shock proteins (sHsps) exhibit an ATP-independent chaperone activity to prevent the aggregation of misfolded proteins in vitro. The seemingly conflicting presence of sHsps in insoluble protein aggregates in cells obstructs a precise definition of sHsp function in proteostasis networks. Recent findings specify sHsp activities in protein quality control systems. The sHsps of yeast, Hsp42 and Hsp26, interact with early unfolding intermediates of substrates, keeping them in a ready-to-refold conformation close to the native state...
January 24, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28116619/hdac6-regulates-sensitivity-to-cell-death-in-response-to-stress-and-post-stress-recovery
#9
Hyun-Wook Ryu, Hye-Rim Won, Dong Hoon Lee, So Hee Kwon
Histone deacetylase 6 (HDAC6) plays an important role in stress responses such as misfolded protein-induced aggresomes, autophagy, and stress granules. However, precisely how HDAC6 manages response during and after cellular stress remains largely unknown. This study aimed to investigate the effect of HDAC6 on various stress and post-stress recovery responses. We showed that HIF-1α protein levels were reduced in HDAC6 knockout (KO) MEFs compared to wild-type (WT) MEFs in hypoxia. Furthermore, under hypoxia, HIF-1α levels were also reduced following rescue with either a catalytically inactive or a ubiqiutin-binding mutant HDAC6...
January 23, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28074336/small-heat-shock-proteins-in-ageing-and-age-related-diseases
#10
REVIEW
Nikolaos Charmpilas, Emmanouil Kyriakakis, Nektarios Tavernarakis
Small heat shock proteins (sHSPs) are gatekeepers of cellular homeostasis across species, preserving proteome integrity under stressful conditions. Nonetheless, recent evidence suggests that sHSPs are more than molecular chaperones with merely auxiliary role. In contrast, sHSPs have emerged as central lifespan determinants, and their malfunction has been associated with the manifestation of neurological disorders, cardiovascular disease and cancer malignancies. In this review, we focus on the role of sHSPs in ageing and age-associated diseases and highlight the most prominent paradigms, where impairment of sHSP function has been implicated in human pathology...
January 10, 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28028759/the-expression-of-damp-proteins-hsp70-and-cancer-testis-antigen-spag9-in-peripheral-blood-of-patients-with-hcc-and-lung-cancer
#11
Biqiong Ren, Shudi Luo, Fei Xu, Guoying Zou, Guofeng Xu, Junyu He, Yiran Huang, Haowen Zhu, Yong Li
There are different views of how the immune system participates in the reaction to cancer. Here, we evaluated expression of DAMP proteins HSP70 and cancer-testis antigen SPAG9 in patients with hepatocellular carcinoma (HCC) and lung cancer to explore tumor immunity. Our analysis showed that levels of HSP70 and SPAG9 antibody were significantly higher in the serum of lung cancer and HCC patients than in the serum of healthy subjects (P < 0.001), but there were no differences in levels of HSP70 antibody in patients and controls...
December 27, 2016: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28000086/interaction-of-small-heat-shock-proteins-with-light-component-of-neurofilaments-nfl
#12
Victoria V Nefedova, Maria V Sudnitsyna, Nikolai B Gusev
The interaction of human small heat shock protein HspB1, its point mutants associated with distal hereditary motor neuropathy, and three other small heat shock proteins (HspB5, HspB6, HspB8) with the light component of neurofilaments (NFL) was analyzed by differential centrifugation, analytical ultracentrifugation, and fluorescent spectroscopy. The wild-type HspB1 decreased the quantity of NFL in pellets obtained after low- and high-speed centrifugation and increased the quantity of NFL remaining in the supernatant after high-speed centrifugation...
December 20, 2016: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/27988888/the-cellular-stress-response-of-the-scleractinian-coral-goniopora-columna-during-the-progression-of-the-black-band-disease
#13
Davide Seveso, Simone Montano, Melissa Amanda Ljubica Reggente, Davide Maggioni, Ivan Orlandi, Paolo Galli, Marina Vai
Black band disease (BBD) is a widespread coral pathology caused by a microbial consortium dominated by cyanobacteria, which is significantly contributing to the loss of coral cover and diversity worldwide. Since the effects of the BBD pathogens on the physiology and cellular stress response of coral polyps appear almost unknown, the expression of some molecular biomarkers, such as Hsp70, Hsp60, HO-1, and MnSOD, was analyzed in the apparently healthy tissues of Goniopora columna located at different distances from the infection and during two disease development stages...
December 17, 2016: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/27987076/hop-expression-is-regulated-by-p53-and-ras-and-characteristic-of-a-cancer-gene-signature
#14
Stacey A Mattison, Gregory L Blatch, Adrienne L Edkins
The Hsp70/Hsp90 organising protein (HOP) is a co-chaperone essential for client protein transfer from Hsp70 to Hsp90 within the Hsp90 chaperone machine. Although HOP is upregulated in various cancers, there is limited information from in vitro studies on how HOP expression is regulated in cancer. The main objective of this study was to identify the HOP promoter and investigate its activity in cancerous cells. Bioinformatic analysis of the -2500 to +16 bp region of the HOP gene identified a large CpG island and a range of putative cis-elements...
December 16, 2016: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/27975204/a-disulfide-bonded-dnak-dimer-is-maintained-in-an-atp-bound-state
#15
Qingdai Liu, Hongtao Li, Ying Yang, Xueli Tian, Jiayue Su, Lei Zhou, Qinglian Liu
DnaK, a major Hsp70 molecular chaperones in Escherichia coli, is a widely used model for studying Hsp70s. We recently solved a crystal structure of DnaK in complex with ATP and showed that DnaK was packed as a dimer in the crystal structure. Our previous biochemical studies supported the formation of a specific DnaK dimer as observed in the crystal structure in solution in the presence of ATP and suggested an important role of this dimer in efficient interaction with Hsp40 co-chaperones. In this study, we dissected the biochemical properties of this DnaK dimer...
December 14, 2016: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/27975203/loss-of-malin-but-not-laforin-results-in-compromised-autophagic-flux-and-proteasomal-dysfunction-in-cells-exposed-to-heat-shock
#16
Navodita Jain, Anupama Rai, Rohit Mishra, Subramaniam Ganesh
Heat stress to a cell leads to the activation of heat shock response, which is required for the management of misfolded and unfolded proteins. Macroautophagy and proteasome-mediated degradation are the two cellular processes that degrade polyubiquitinated, misfolded proteins. Contrasting pieces of evidence exist on the effect of heat stress on the activation of the above-mentioned degradative pathways. Laforin phosphatase and malin E3 ubiquitin ligase, the two proteins defective in Lafora neurodegenerative disorder, are involved in cellular stress response pathways and are required for the activation of heat shock transcription factor - the heat shock factor 1 (HSF1) - and, consequently, for cellular protection under heat shock...
December 14, 2016: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/27966060/components-of-a-mammalian-protein-disaggregation-refolding-machine-are-targeted-to-nuclear-speckles-following-thermal-stress-in-differentiated-human-neuronal-cells
#17
Catherine A S Deane, Ian R Brown
Heat shock proteins (Hsps) are a set of highly conserved proteins involved in cellular repair and protective mechanisms. They counter protein misfolding and aggregation that are characteristic features of neurodegenerative diseases. Hsps act co-operatively in disaggregation/refolding machines that assemble at sites of protein misfolding and aggregation. Members of the DNAJ (Hsp40) family act as "holdases" that detect and bind misfolded proteins, while members of the HSPA (Hsp70) family act as "foldases" that refold proteins to biologically active states...
December 13, 2016: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/27933579/oligomerization-and-chaperone-like-activity-of-drosophila-melanogaster-small-heat-shock-protein-dmhsp27-and-three-arginine-mutants-in-the-alpha-crystallin-domain
#18
Mohamed Taha Moutaoufik, Geneviève Morrow, Halim Maaroufi, Céline Férard, Stéphanie Finet, Robert M Tanguay
The small Hsp DmHsp27 from Drosophila melanogaster is one of the few small heat shock proteins (sHsps) found within the nucleus. We report that its dimerization is independent of disulfide bond formation and seems to rely on salt bridges. Unlike metazoan sHsps, DmHsp27 forms two populations of oligomers not in equilibrium. Mutations at highly conserved arginine residues in mammalian sHsps have been reported to be associated with protein conformational defects and intracellular aggregation. Independent mutation of three highly conserved arginines (R122, R131, and R135) to glycine in DmHsp27 results in only one population of higher molecular weight form...
December 8, 2016: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/28054181/susan-lee-lindquist-1949-2016-it-is-personal
#19
EDITORIAL
Lawrence E Hightower
No abstract text is available yet for this article.
January 2017: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/27966061/ubl-bag-domain-co-chaperones-cause-cellular-stress-upon-overexpression-through-constitutive-activation-of-hsf1
#20
Esben G Poulsen, Caroline Kampmeyer, Franziska Kriegenburg, Jens V Johansen, Kay Hofmann, Christian Holmberg, Rasmus Hartmann-Petersen
As a result of exposure to stress conditions, mutations, or defects during synthesis, cellular proteins are prone to misfold. To cope with such partially denatured proteins, cells mount a regulated transcriptional response involving the Hsf1 transcription factor, which drives the synthesis of molecular chaperones and other stress-relieving proteins. Here, we show that the fission yeast Schizosaccharomyces pombe orthologues of human BAG-1, Bag101, and Bag102, are Hsp70 co-chaperones that associate with 26S proteasomes...
January 2017: Cell Stress & Chaperones
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