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Cell Stress & Chaperones

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
Lawrence E Hightower
No abstract text is available yet for this article.
January 4, 2017: Cell Stress & Chaperones
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
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
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
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
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
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
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...
December 14, 2016: Cell Stress & Chaperones
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
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
Vladimir S Shavva, Alexandra M Bogomolova, Artemy A Nikitin, Ella B Dizhe, Galina N Oleinikova, Ivan A Lapikov, Dmitry A Tanyanskiy, Andrej P Perevozchikov, Sergey V Orlov
Reactive oxygen species damage various cell components including DNA, proteins, and lipids, and these impairments could be a reason for severe human diseases including atherosclerosis. Forkhead box O1 (FOXO1), an important metabolic transcription factor, upregulates antioxidant and proapoptotic genes during oxidative stress. Apolipoprotein A-I (ApoA-I) forms high density lipoprotein (HDL) particles that are responsible for cholesterol transfer from peripheral tissues to liver for removal in bile in vertebrates...
November 28, 2016: Cell Stress & Chaperones
Susana Gomez-Escalante, Peter W Piper, Stefan H Millson
Folding of the myosin head often requires the joint actions of Hsp90 and a dedicated UNC45, Cro1, She4 (UCS) domain-containing cochaperone protein. Relatively weak sequence conservation exists between the single UCS protein of simple eukaryotes (She4 in budding yeast) and the two UCS proteins of higher organisms (the general cell and smooth muscle UNC45s; UNC45-GC and UNC45-SM respectively). In vertebrates, UNC45-GC facilitates cytoskeletal function whereas the 55% identical UNC45-SM assists in the assembly of the contractile apparatus of cardiac and skeletal muscles...
November 25, 2016: Cell Stress & Chaperones
Marcelo Sartori Grunwald, Rodrigo Ligabue-Braun, Cristiane Santos Souza, Luana Heimfarth, Hugo Verli, Daniel Pens Gelain, José Cláudio Fonseca Moreira
Extracellular heat shock protein 70 (HSP70) is recognized by receptors on the plasma membrane, such as Toll-like receptor 4 (TLR4), TLR2, CD14, and CD40. This leads to activation of nuclear factor-kappa B (NF-κB), release of pro-inflammatory cytokines, enhancement of the phagocytic activity of innate immune cells, and stimulation of antigen-specific responses. However, the specific characteristics of HSP70 binding are still unknown, and all HSP70 receptors have not yet been described. Putative models for HSP70 complexation to the receptor for advanced glycation endproducts (RAGEs), considering both ADP- and ATP-bound states of HSP70, were obtained through molecular docking and interaction energy calculations...
November 17, 2016: Cell Stress & Chaperones
Ana Claudia Silva Braga, Bruno Moreira Carneiro, Mariana Nogueira Batista, Mônica Mayumi Akinaga, Paula Rahal
Hepatitis C (HCV) is a viral disease affecting millions of people worldwide, and persistent HCV infection can lead to progressive liver disease with the development of liver cirrhosis and hepatocellular carcinoma. During treatment for hepatitis C, the occurrence of viral resistance is common. To reduce the occurrence of resistance, new viral treatments should target both viral and cellular factors. Many interactions occur between viral and host proteins during the HCV replication cycle and might be used for the development of new therapies against hepatitis C...
November 17, 2016: Cell Stress & Chaperones
Krishnamoorthy Srikanth, Anam Kwon, Eunjin Lee, Hoyoung Chung
This study aimed to investigate the genes and pathways that respond to heat stress in Holstein bull calves exposed to severe ranges of temperature and humidity. A total of ten animals from 4 to 6 months of age were subjected to heat stress at 37 °C and 90 % humidity for 12 h. Skin and rectal temperatures were measured before and after heat stress; while no correlation was found between them before heat stress, a moderate correlation was detected after heat stress, confirming rectal temperature to be a better barometer for monitoring heat stress...
November 16, 2016: Cell Stress & Chaperones
Feifei Xu, You Wang, Tianqi Tao, Dandan Song, Xiuhua Liu
Recent work reveals that actin acetylation modification has been linked to different normal and disease processes and the effects associated with metabolic and environmental stressors. Herein, we highlight the effects of calreticulin on actin acetylation and cell injury induced by microwave radiation in human microvascular endothelial cell (HMEC). HMEC injury was induced by high-power microwave of different power density (10, 30, 60, 100 mW/cm(2), for 6 min) with or without exogenous recombinant calreticulin...
November 4, 2016: Cell Stress & Chaperones
Dig B Mahat, John T Lis
Heat shock response (HSR) maintains and restores protein homeostasis when cells are exposed to proteotoxic heat stress. Heat shock (HS) triggers a rapid and robust change in genome-wide transcription, protein synthesis, and chaperone activity; and therefore, the HSR has been widely used as a model system in these studies. The conventional method of performing instantaneous HS in the laboratory uses heated fresh media to induce HSR when added to cells. However, addition of fresh media to cells may evoke additional cellular responses and signaling pathways...
November 3, 2016: Cell Stress & Chaperones
Bai-Liu Ya, Hong-Fang Li, Hai-Ying Wang, Fei Wu, Qing Xin, Hong-Ju Cheng, Wen-Juan Li, Na Lin, Zai-Hua Ba, Ru-Juan Zhang, Qian Liu, Ya-Nan Li, Bo Bai, Feng Ge
Recent studies have shown 5-hydroxymethyl-2-furfural (5-HMF) has favorable biological effects, and its neuroprotection in a variety of neurological diseases has been noted. Our previous study showed that treatment of 5-HMF led to protection against permanent global cerebral ischemia. However, the underlying mechanisms in cerebral ischemic injury are not fully understood. This study was conducted to investigate the neuroprotective effect of 5-HMF and elucidate the nuclear factor erythroid 2-related factor 2 (Nrf2)/antioxidant response element (ARE) signaling pathway mechanism in the striatum after transient global cerebral ischemia...
November 3, 2016: Cell Stress & Chaperones
Zou Lin, Zhang Guichun, Liu Lifeng, Chen Chen, Cao Xuecheng, Cai Jinfang
Oxidative stress represents a major cause of cellular damage and death in the process of osteoporosis. Antimycin A (AMA) has been shown to stimulate mitochondrial superoxide anions and reactive oxygen species (ROS). α-Lipoic acid (α-LA) is a naturally occurring essential coenzyme in mitochondrial multienzyme complexes and acts as a key player in mitochondrial energy production. However, whether α-LA affects the cytotoxicity of AMA in osteoblastic cells is unknown. In this study, we investigated the protective effects of α-LA against AMA-induced cytotoxicity using the MC3T3-E1 osteoblast-like cell line...
October 30, 2016: Cell Stress & Chaperones
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