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https://www.readbyqxmd.com/read/28549213/binding-of-copper-and-cisplatin-to-atox1-is-mediated-by-glutathione-through-the-formation-of-metal-sulfur-clusters
#1
Nataliya V Dolgova, Corey Yu, John P Cvitkovic, Miroslav Hodak, Kurt Nienaber, Kelly Lynn Summers, Julien Cotelesage, Jerzy Bernholc, George A Kaminski, Ingrid J Pickering, Graham N George, Oleg Y Dmitriev
Copper is an essential nutrient required for many biological processes involved in primary metabolism, but free cop-per is toxic due to its ability to catalyze formation of free radicals. To prevent toxic effects, in the cell copper is bound to proteins and low molecular weight compounds, such as glutathione, at all times. The widely used chemotherapy agent cisplatin is known to bind to copper-transporting proteins, including copper chaperone Atox1. Cisplatin interac-tions with Atox1 and other copper transporters are linked to cancer resistance to platinum-based chemotherapy...
May 26, 2017: Biochemistry
https://www.readbyqxmd.com/read/28547133/hsf1-acetylation-decreases-its-transcriptional-activity-and-enhances-glucolipotoxicity-induced-apoptosis-in-rat-and-human-beta-cells
#2
Indri Purwana, Jun J Liu, Bernard Portha, Jean Buteau
AIMS/HYPOTHESIS: Heat shock factor protein 1 (HSF1) is a transcription factor that regulates the expression of key molecular chaperones, thereby orchestrating the cellular response to stress. This system was recently implicated in the control of insulin sensitivity and is therefore being scrutinised as a novel therapeutic avenue for type 2 diabetes. However, the regulation and biological actions of HSF1 in beta cells remain elusive. Herein, we sought to investigate the regulation of HSF1 in pancreatic beta cells and to study its potential role in cell survival...
May 25, 2017: Diabetologia
https://www.readbyqxmd.com/read/28546437/characterization-of-thermostable-cam-rubisco-activase-reveals-a-rubisco-interacting-surface-loop
#3
Devendra Shivhare, Oliver Mueller-Cajar
In order to maintain metabolic flux through the Calvin-Benson-Bassham (CBB) cycle in higher plants, dead-end inhibited complexes of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) must constantly be engaged and remodeled by the molecular chaperone Rubisco activase (Rca). In C3 plants the thermolability of Rca is responsible for the deactivation of Rubisco and reduction of photosynthesis at moderately elevated temperatures. We reasoned that CAM plants must possess thermostable Rca to support CBB flux during the day when stomata are closed...
May 25, 2017: Plant Physiology
https://www.readbyqxmd.com/read/28545881/high-fat-diet-and-saturated-fatty-acid-palmitate-inhibits-igf-1-function-in-chondrocytes
#4
Sumaiya A Nazli, Richard F Loeser, Susan Chubinskaya, Jeffrey S Willey, Raghunatha R Yammani
INTRODUCTION: Insulin-like growth factor-1 (IGF-1) promotes matrix synthesis and cell survival in cartilage. Chondrocytes from aged and osteoarthritic cartilage have a reduced response to IGF-1. The purpose of this study was to determine the effect of free fatty acids present in a high-fat diet on IGF-1 function in cartilage and the role of ER stress. METHODS: C57BL/6 male mice were maintained on either a high-fat (60% kcal from fat) or a low-fat (10% kcal from fat) diet for 4 months...
May 22, 2017: Osteoarthritis and Cartilage
https://www.readbyqxmd.com/read/28543811/the-structural-flexibility-of-the-human-copper-chaperone-atox1-insights-from-combined-pulsed-epr-studies-and-computations
#5
Ariel R Levy, Meital Turgeman, Lada Gevorkyan-Aiapetov, Sharon Ruthstein
Metallochaperones are responsible for shuttling metal ions to target proteins. Thus, a metallochaperone's structure must be sufficiently flexible both to hold onto its ion while traversing the cytoplasm and to transfer the ion to or from a partner protein. Here, we sought to shed light on the structure of Atox1, a metallochaperone involved in the human copper regulation system. Atox1 shuttles copper ions from the main copper transporter, Ctr1, to the ATP7b transporter in the Golgi apparatus. Conventional biophysical tools such as X-ray or NMR cannot always target the various conformational states of metallochaperones, owing to a requirement for crystallography or low sensitivity and resolution...
May 20, 2017: Protein Science: a Publication of the Protein Society
https://www.readbyqxmd.com/read/28542382/uv-b-induced-fibrillization-of-crystallin-protein-mixtures
#6
Sibel Cetinel, Valentyna Semenchenko, Jae-Young Cho, Mehdi Ghaffari Sharaf, Karim F Damji, Larry D Unsworth, Carlo Montemagno
Environmental factors, mainly oxidative stress and exposure to sunlight, induce the oxidation, cross-linking, cleavage, and deamination of crystallin proteins, resulting in their aggregation and, ultimately, cataract formation. Various denaturants have been used to initiate the aggregation of crystallin proteins in vitro. All of these regimens, however, are obviously far from replicating conditions that exist in vivo that lead to cataract formation. In fact, it is our supposition that only UV-B radiation may mimic the observed in vivo cause of crystallin alteration leading to cataract formation...
2017: PloS One
https://www.readbyqxmd.com/read/28542269/the-small-molecule-kinase-inhibitor-d11-counteracts-17-aag-mediated-up-regulation-of-hsp70-in-brain-cancer-cells
#7
Susanne Schaefer, Tina H Svenstrup, Barbara Guerra
Many types of cancer express high levels of heat shock proteins (HSPs) that are molecular chaperones regulating protein folding and stability ensuring protection of cells from potentially lethal stress. HSPs in cancer cells promote survival, growth and spreading even in situations of growth factors deprivation by associating with oncogenic proteins responsible for cell transformation. Hence, it is not surprising that the identification of potent inhibitors of HSPs, notably HSP90, has been the primary research focus, in recent years...
2017: PloS One
https://www.readbyqxmd.com/read/28542188/hsp90-inhibitors-potentiate-pgf2%C3%AE-induced-il-6-synthesis-via-p38-map-kinase-in-osteoblasts
#8
Kazuhiko Fujita, Haruhiko Tokuda, Gen Kuroyanagi, Naohiro Yamamoto, Shingo Kainuma, Tetsu Kawabata, Go Sakai, Rie Matsushima-Nishiwaki, Osamu Kozawa, Takanobu Otsuka
Heat shock protein 90 (HSP90) that is ubiquitously expressed in various tissues, is recognized to be a major molecular chaperone. We have previously reported that prostaglandin F2α (PGF2α), a potent bone remodeling mediator, stimulates the synthesis of interleukin-6 (IL-6) through p44/p42 mitogen-activated protein (MAP) kinase and p38 MAP kinase in osteoblast-like MC3T3-E1 cells, and that Rho-kinase acts at a point upstream of p38 MAP kinase. In the present study, we investigated the involvement of HSP90 in the PGF2α-stimulated IL-6 synthesis and the underlying mechanism in MC3T3-E1 cells...
2017: PloS One
https://www.readbyqxmd.com/read/28541519/reduced-sleep-during-social-isolation-leads-to-cellular-stress-and-induction-of-the-unfolded-protein-response-upr
#9
Marishka K Brown, Ewa Strus, Nirinjini Naidoo
Study Objectives: Social isolation has a multitude of negative consequences on human health including the ability to endure challenges to the immune system, sleep amount and efficiency, and general morbidity and mortality. These adverse health outcomes are conserved in other social species. In the fruit fly Drosophila melanogaster, social isolation leads to increased aggression, impaired memory and reduced amounts of daytime sleep. There is a correlation between molecules affected by social isolation and those implicated in sleep in Drosophila...
May 25, 2017: Sleep
https://www.readbyqxmd.com/read/28541049/synthesis-and-photophysical-and-photocatalytic-properties-of-a-highly-fluorinated-and-durable-phthalocyanine-peptide-bioconjugate-for-potential-theranostic-applications
#10
Erik N Carrión, Jenyffer Santiago, David Sabatino, Sergiu M Gorun
The functionalized, asymmetric fluoro-fluoroalkyl scaffold F48H7COOHPcZn (3) was used to prepare F48H7COOPcZn-6-amino-hexanoate-CTVALPGGYVRVC (5), a Pep42 peptide bioconjugate envisioned for photodynamic therapy, which can specifically target the GRP78 chaperone protein overexpressed and exclusively localized on some cancer cell surfaces. The analogous F48H7COOHPcCu (4) has also been prepared, and its single-crystal X-ray structure was elucidated. Despite reduced steric hindrance relative to the nonfunctionalized, single-site complexes of the F64Pc scaffold, no aggregation was detected in solution via UV-vis spectroscopy, for either 3, 4, or 5, consistent with the lack of π stacking observed for the crystalline 4...
May 25, 2017: Inorganic Chemistry
https://www.readbyqxmd.com/read/28539871/protein-quality-control-and-the-amyotrophic-lateral-sclerosis-frontotemporal-dementia-continuum
#11
Hamideh Shahheydari, Audrey Ragagnin, Adam K Walker, Reka P Toth, Marta Vidal, Cyril J Jagaraj, Emma R Perri, Anna Konopka, Jessica M Sultana, Julie D Atkin
Protein homeostasis, or proteostasis, has an important regulatory role in cellular function. Protein quality control mechanisms, including protein folding and protein degradation processes, have a crucial function in post-mitotic neurons. Cellular protein quality control relies on multiple strategies, including molecular chaperones, autophagy, the ubiquitin proteasome system, endoplasmic reticulum (ER)-associated degradation (ERAD) and the formation of stress granules (SGs), to regulate proteostasis. Neurodegenerative diseases are characterized by the presence of misfolded protein aggregates, implying that protein quality control mechanisms are dysfunctional in these conditions...
2017: Frontiers in Molecular Neuroscience
https://www.readbyqxmd.com/read/28539657/using-bicistronic-constructs-to-evaluate-the-chaperone-activities-of-heat-shock-proteins-in-cells
#12
Rebecca San Gil, Tracey Berg, Heath Ecroyd
Heat shock proteins (Hsps) are molecular chaperones that prevent the aggregation of client proteins by facilitating their refolding, or trafficking them for degradation. The chaperone activities of Hsps are dependent on dynamic protein-protein interactions, including their oligomerisation into large multi-subunit complexes. Thus, tagging Hsps with fluorescent proteins can interfere with their chaperone activity. To overcome this limitation, we have exploited bicistronic constructs for the concurrent expression of a non-tagged Hsp and fluorescent reporter from a single mRNA in cells...
May 24, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28539486/how-and-why-do-toxic-conformers-of-aberrant-proteins-accumulate-during-ageing
#13
REVIEW
Rebecca Josefson, Rebecca Andersson, Thomas Nyström
Ageing can be defined as a gradual decline in cellular and physical functions accompanied by an increased sensitivity to the environment and risk of death. The increased risk of mortality is causally connected to a gradual, intracellular accumulation of so-called ageing factors, of which damaged and aggregated proteins are believed to be one. Such aggregated proteins also contribute to several age-related neurodegenerative disorders e.g. Alzheimer's, Parkinson's, and Huntington's diseases, highlighting the importance of protein quality control (PQC) in ageing and its associated diseases...
May 24, 2017: Essays in Biochemistry
https://www.readbyqxmd.com/read/28539411/substrate-binding-by-the-yeast-hsp110-nucleotide-exchange-factor-and-molecular-chaperone-sse1-is-not-obligate-for-its-biological-activities
#14
Veronica M Garcia, Nadinath B Nillegoda, Bernd Bukau, Kevin A Morano
The highly conserved heat-shock protein 70 (Hsp70) is a ubiquitous molecular chaperone essential for maintaining cellular protein homeostasis. The related protein Hsp110 (Sse1/Sse2 in Saccharomyces cerevisiae) functions as a nucleotide exchange factor (NEF) to regulate the protein folding activity of Hsp70. Hsp110/Sse1 can additionally prevent protein aggregation in vitro via its substrate binding domain (SBD), but the cellular roles of this "holdase" activity remain poorly defined. We generated and characterized an Sse1 mutant that separates, for the first time, its nucleotide exchange and substrate binding functions...
May 24, 2017: Molecular Biology of the Cell
https://www.readbyqxmd.com/read/28539401/transmembrane-helix-hydrophobicity-is-an-energetic-barrier-during-the-retrotranslocation-of-integral-membrane-erad-substrates
#15
Christopher J Guerriero, Karl-Richard Reutter, Andrew A Augustine, G Michael Preston, Kurt F Weiberth, Timothy D Mackie, Hillary C Cleveland-Rubeor, Neville P Bethel, Keith M Callenberg, Kunio Nakatsukasa, Michael Grabe, Jeffrey L Brodsky
Integral membrane proteins fold inefficiently and are susceptible to turnover via the endoplasmic reticulum-associated degradation (ERAD) pathway. During ERAD, misfolded proteins are recognized by molecular chaperones, polyubiquitinated, and retrotranslocated to the cytoplasm for proteasomal degradation. Although many aspects of this pathway are defined, how transmembrane helices (TMHs) are removed from the membrane and into the cytoplasm prior to degradation is poorly understood. In this study, we asked whether the hydrophobic character of a TMH acts as an energetic barrier to retrotranslocation...
May 24, 2017: Molecular Biology of the Cell
https://www.readbyqxmd.com/read/28537572/understanding-nucleosome-dynamics-and-their-links-to-gene-expression-and-dna-replication
#16
REVIEW
William K M Lai, B Franklin Pugh
Advances in genomics technology have provided the means to probe myriad chromatin interactions at unprecedented spatial and temporal resolution. This has led to a profound understanding of nucleosome organization within the genome, revealing that nucleosomes are highly dynamic. Nucleosome dynamics are governed by a complex interplay of histone composition, histone post-translational modifications, nucleosome occupancy and positioning within chromatin, which are influenced by numerous regulatory factors, including general regulatory factors, chromatin remodellers, chaperones and polymerases...
May 24, 2017: Nature Reviews. Molecular Cell Biology
https://www.readbyqxmd.com/read/28537252/an-hsp90-co-chaperone-protein-in-yeast-is-functionally-replaced-by-site-specific-posttranslational-modification-in-humans
#17
Abbey D Zuehlke, Michael Reidy, Coney Lin, Paul LaPointe, Sarah Alsomairy, D Joshua Lee, Genesis M Rivera-Marquez, Kristin Beebe, Thomas Prince, Sunmin Lee, Jane B Trepel, Wanping Xu, Jill Johnson, Daniel Masison, Len Neckers
Heat shock protein 90 (Hsp90) is an essential eukaryotic molecular chaperone. To properly chaperone its clientele, Hsp90 proceeds through an ATP-dependent conformational cycle influenced by posttranslational modifications (PTMs) and assisted by a number of co-chaperone proteins. Although Hsp90 conformational changes in solution have been well-studied, regulation of these complex dynamics in cells remains unclear. Phosphorylation of human Hsp90α at the highly conserved tyrosine 627 has previously been reported to reduce client interaction and Aha1 binding...
May 24, 2017: Nature Communications
https://www.readbyqxmd.com/read/28536652/mesencephalic-astrocyte-derived-neurotrophic-factor-reduces-cell-apoptosis-via-upregulating-hsp70-in-shsy-5y-cells
#18
Hui Sun, Ming Jiang, Xing Fu, Qiong Cai, Jingxing Zhang, Yanxin Yin, Jia Guo, Lihua Yu, Yun Jiang, Yigang Liu, Liang Feng, Zhiyu Nie, Jianmin Fang, Lingjing Jin
BACKGROUND: Mesencephalic astrocyte-derived neurotrophic factor (MANF) is a new candidate growth factor for dopaminergic neurons against endoplasmic reticulum stress (ER stress). HSP70 family, a chaperon like heat shock protein family, was proved to be involved in the MANF induced survival pathway in 6-OHDA treated SHSY-5Y cells. However, the ER stress relative transcriptome, in MANF signaling cascades is still investigated. The involvement of HSP70, a 70kd member of HSP70 family, need further to be verified...
2017: Translational Neurodegeneration
https://www.readbyqxmd.com/read/28536390/showing-the-way-oncolytic-adenoviruses-as-chaperones-of-immunostimulatory-adjuncts
#19
REVIEW
Jing Li Huang, Christopher J LaRocca, Masato Yamamoto
Oncolytic adenoviruses (OAds) are increasingly recognized as vectors for immunotherapy in the treatment of various solid tumors. The myriads of advantages of using adenovirus include targeted specificity upon infection and selective replication, which lead to localized viral burst, exponential spread of OAds, and antitumor effect. OAds can also induce a strong immune reaction due to the massive release of tumor antigens upon cytolysis and the presence of viral antigens. This review will highlight recent advances in adenoviral vectors expressing immunostimulatory effectors, such as GM-CSF (granulocyte macrophage colony-stimulating factor), interferon-α, interleukin-12, and CD40L...
September 19, 2016: Biomedicines
https://www.readbyqxmd.com/read/28536268/endoplasmic-reticulum-stress-induced-degradation-of-dnajb12-stimulates-bok-accumulation-and-primes-cancer-cells-for-apoptosis
#20
Pattarawut Sopha, Hong Yu Ren, Diane E Grove, Douglas M Cyr
DNAJB12 (JB12) is an endoplasmic reticulum (ER)-associated Hsp40 family protein that recruits Hsp70 to the ER surface to coordinate the function of ER-associated and cytosolic chaperone systems in protein quality control. Hsp70 is stress inducible, but paradoxically, we report here that JB12 was degraded by the proteasome during severe ER stress. Destabilized JB12 was degraded by ER-associated degradation (ERAD) complexes that contained HERP, Sel1L, and gp78. JB12 was the only ER-associated chaperone that was destabilized by reductive stress...
May 23, 2017: Journal of Biological Chemistry
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