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https://www.readbyqxmd.com/read/27908666/molecular-cloning-and-expression-analysis-of-five-heat-shock-protein-70-hsp70-family-members-in-lateolabrax-maculatus-with-vibrio-harveyi-infection
#1
Ying-Li Han, Cong-Cong Hou, Chen Du, Jun-Quan Zhu
Heat shock proteins 70 (HSP70s) are molecular chaperones that aid in protection against environmental stress. In this study, we cloned and characterized five members of the HSP70 family (designated as HSPa1a, HSC70-1, HSC70-2, HSPa4 and HSPa14) from Lateolabrax maculatus using rapid amplification cDNA ends (RACE). Multiple sequence alignment and structural analysis revealed that all members of the HSP70 family had a conserved domain architecture, with some distinguishing features unique to each HSP70. Quantitative real-time (qPCR) analysis revealed that all members of the HSP70 family were ubiquitously and differentially expressed in all major types of tissues, including testicular tissue...
November 28, 2016: Fish & Shellfish Immunology
https://www.readbyqxmd.com/read/27894884/modulation-of-the-heat-shock-response-is-associated-with-acclimation-to-novel-temperatures-but-not-adaptation-to-climatic-variation-in-the-ants-aphaenogaster-picea-and-a-rudis
#2
Sara Helms Cahan, Andrew D Nguyen, John Stanton-Geddes, Clint A Penick, Yainna Hernáiz-Hernández, Bernice B DeMarco, Nicholas J Gotelli
Ecological diversification into thermally divergent habitats can push species toward their physiological limits, requiring them to accommodate temperature extremes through plastic or evolutionary changes that increase persistence under the local thermal regime. One way to withstand thermal stress is to increase production of heat shock proteins, either by maintaining higher baseline abundance within cells or by increasing the magnitude of induction in response to heat stress. We evaluated whether environmental variation was associated with expression of three heat shock protein genes in two closely-related species of woodland ant, Aphaenogaster picea and A...
November 25, 2016: Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology
https://www.readbyqxmd.com/read/27859498/the-srl-peptide-of-rhesus-rotavirus-vp4-protein-governs-cholangiocyte-infection-and-the-murine-model-of-biliary-atresia
#3
Sujit K Mohanty, Bryan Donnelly, Inna Lobeck, Ashley Walther, Phylicia Dupree, Abigail Coots, Jaroslaw Meller, Monica McNeal, Karol Sestak, Greg Tiao
: Biliary atresia (BA) is a neonatal obstructive cholangiopathy which progresses to end stage liver disease, often requiring transplantation. The murine model of BA, employing rhesus rotavirus (RRV), parallels human disease and has been used to elucidate mechanistic aspects of a virus induced biliary cholangiopathy. We previously reported that RRV VP4 gene plays an integral role in activating the immune system and induction of BA. Utilizing rotavirus binding and blocking assays, this study elucidated how RRV VP4 protein governs cholangiocyte susceptibility to infection both in vitro and in vivo in the murine model of BA...
November 17, 2016: Hepatology: Official Journal of the American Association for the Study of Liver Diseases
https://www.readbyqxmd.com/read/27852853/coat-protein-regulation-by-ck2-cpip-hsp70-and-chip-is-required-for-potato-virus-a-replication-and-coat-protein-accumulation
#4
Andres Lõhmus, Anders Hafrén, Kristiina Mäkinen
: We demonstrate here that coat protein (CP) phosphorylation by protein kinase CK2 and a chaperone system formed by two heat-shock proteins, CP-interacting protein (CPIP) and HSP70, are both essential for Potato virus A (PVA; genus Potyvirus) replication and that all of these host proteins have the capacity to contribute to the level of PVA CP accumulation. An E3 ubiquitin ligase called carboxyl terminus Hsc70-interacting protein (CHIP), which may participate in the CPIP-HSP70-mediated CP degradation, is also needed for robust PVA gene expression...
November 16, 2016: Journal of Virology
https://www.readbyqxmd.com/read/27835608/pc-1-works-in-conjunction-with-e3-ligase-chip-to-regulate-androgen-receptor-stability-and-activity
#5
Jian Wang, Hui Zhang, Xiaoqing Zhang, Peng Wang, Hongtao Wang, Fang Huang, Chenyan Zhou, Jianguang Zhou, Shanhu Li
The androgen receptor (AR) is not only a ligand-dependent transcription factor, but also functions as a licensing factor, a component of DNA replication, which is degraded during mitosis. Furthermore, the deregulation of AR activity is involved in the initiation of prostate cancer and contributes to castration resistant prostate cancer (CRPC). While AR degradation is known to occur primarily through a proteasome-mediated pathway, very little is known about how this process is regulated, especially in M phase...
November 9, 2016: Oncotarget
https://www.readbyqxmd.com/read/27833127/two-dimensional-gel-electrophoresis-based-proteomic-analysis-reveals-n-terminal-truncation-of-the-hsc70-protein-in-cotton-fibers-in-vivo
#6
Chengcheng Tao, Xiang Jin, Liping Zhu, Hongbin Li
On two-dimensional electrophoresis gels, six protein spots from cotton ovules and fibers were identified as heat shock cognate 70 kD protein (Hsc70). Three spots corresponded to an experimental molecular weight (MW) of 70 kD (spots 1, 2 and 3), and the remaining three spots corresponded to an experimental MW slightly greater than 45 kD (spots 4, 5 and 6). Protein spots 1, 2 and 3 were abundant on gels of 0-day (the day of anthesis) wild-type (WT) ovules, 0-day fuzzless-lintless mutant ovules and 10-day WT ovules but absent from gels of 10-day WT fibers...
November 11, 2016: Scientific Reports
https://www.readbyqxmd.com/read/27807229/evidence-that-hsc70-is-associated-with-cnv-particles-and-plays-a-role-in-cnv-particle-disassembly
#7
Syed Benazir Alam, D'Ann Rochon
: Uncoating of a virus particle to expose its nucleic acid is a critical aspect of the viral multiplication cycle as it is essential for the establishment of infection. In the present study, we investigated the role of plant HSP70 homologs in the uncoating process of Cucumber necrosis virus (CNV), a non-enveloped (+)ssRNA virus having a T=3 icosahedral capsid. We have found through Western blot analysis and mass spectrometry that the HSP70 homolog, Hsc70-2, copurifies with CNV particles...
November 2, 2016: Journal of Virology
https://www.readbyqxmd.com/read/27783273/hsp70-in-human-polymorphonuclear-and-mononuclear-leukocytes-comparison-of-the-protein-content-and-transcriptional-activity-of-hspa-genes
#8
Anna A Boyko, Tatyana L Azhikina, Maria A Streltsova, Alexander M Sapozhnikov, Elena I Kovalenko
Cell-type specific variations are typical for the expression of different members of the HSP70 family. In circulating immune cells, HSP70 proteins interact with units of signaling pathways involved in the immune responses and may promote cell survival in sites of inflammation. In this work, we compared basal HSP70 expression and stress-induced HSP70 response in polymorphonuclear and mononuclear human leukocytes. The intracellular content of inducible and constitutive forms of HSP70 was analyzed in relation to the transcriptional activity of HSPA genes...
October 25, 2016: Cell Stress & Chaperones
https://www.readbyqxmd.com/read/27757073/a-decade-of-boon-or-burden-what-has-the-chip-ever-done-for-cellular-protein-quality-control-mechanism-implicated-in-neurodegeneration-and-aging
#9
Vibhuti Joshi, Ayeman Amanullah, Arun Upadhyay, Ribhav Mishra, Amit Kumar, Amit Mishra
Cells regularly synthesize new proteins to replace old and abnormal proteins for normal cellular functions. Two significant protein quality control pathways inside the cellular milieu are ubiquitin proteasome system (UPS) and autophagy. Autophagy is known for bulk clearance of cytoplasmic aggregated proteins, whereas the specificity of protein degradation by UPS comes from E3 ubiquitin ligases. Few E3 ubiquitin ligases, like C-terminus of Hsc70-interacting protein (CHIP) not only take part in protein quality control pathways, but also plays a key regulatory role in other cellular processes like signaling, development, DNA damage repair, immunity and aging...
2016: Frontiers in Molecular Neuroscience
https://www.readbyqxmd.com/read/27709416/-1-h-15-n-and-13-c-resonance-assignments-for-free-and-ieevd-peptide-bound-forms-of-the-tetratricopeptide-repeat-domain-from-the-human-e3-ubiquitin-ligase-chip
#10
Huaqun Zhang, Cameron McGlone, Matthew M Mannion, Richard C Page
The ubiquitin ligase CHIP catalyzes covalent attachment of ubiquitin to unfolded proteins chaperoned by the heat shock proteins Hsp70/Hsc70 and Hsp90. CHIP interacts with Hsp70/Hsc70 and Hsp90 by binding of a C-terminal IEEVD motif found in Hsp70/Hsc70 and Hsp90 to the tetratricopeptide repeat (TPR) domain of CHIP. Although recruitment of heat shock proteins to CHIP via interaction with the CHIP-TPR domain is well established, alterations in structure and dynamics of CHIP upon binding are not well understood...
October 5, 2016: Biomolecular NMR Assignments
https://www.readbyqxmd.com/read/27706239/spatial-and-temporal-resolution-of-global-protein-synthesis-during-hsv-infection-using-bioorthogonal-precursors-and-click-chemistry
#11
Catherine Su Hui Teo, Remigiusz A Serwa, Peter O'Hare
We used pulse-labeling with the methionine analogue homopropargylglycine (HPG) to investigate spatiotemporal aspects of protein synthesis during herpes simplex virus (HSV) infection. In vivo incorporation of HPG enables subsequent selective coupling of fluorochrome-capture reagents to newly synthesised proteins. We demonstrate that HPG labeling had no effect on cell viability, on accumulation of test early or late viral proteins, or on overall virus yields. HPG pulse-labeling followed by SDS-PAGE analysis confirmed incorporation into newly synthesised proteins, while parallel processing by in situ cycloaddition revealed new insight into spatiotemporal aspects of protein localisation during infection...
October 2016: PLoS Pathogens
https://www.readbyqxmd.com/read/27706135/the-epichaperome-is-an-integrated-chaperome-network-that-facilitates-tumour-survival
#12
Anna Rodina, Tai Wang, Pengrong Yan, Erica DaGama Gomes, Mark P S Dunphy, Nagavarakishore Pillarsetty, John Koren, John F Gerecitano, Tony Taldone, Hongliang Zong, Eloisi Caldas-Lopes, Mary Alpaugh, Adriana Corben, Matthew Riolo, Brad Beattie, Christina Pressl, Radu I Peter, Chao Xu, Robert Trondl, Hardik J Patel, Fumiko Shimizu, Alexander Bolaender, Chenghua Yang, Palak Panchal, Mohammad F Farooq, Sarah Kishinevsky, Shanu Modi, Oscar Lin, Feixia Chu, Sujata Patil, Hediye Erdjument-Bromage, Pat Zanzonico, Clifford Hudis, Lorenz Studer, Gail J Roboz, Ethel Cesarman, Leandro Cerchietti, Ross Levine, Ari Melnick, Steven M Larson, Jason S Lewis, Monica L Guzman, Gabriela Chiosis
Transient, multi-protein complexes are important facilitators of cellular functions. This includes the chaperome, an abundant protein family comprising chaperones, co-chaperones, adaptors, and folding enzymes-dynamic complexes of which regulate cellular homeostasis together with the protein degradation machinery. Numerous studies have addressed the role of chaperome members in isolation, yet little is known about their relationships regarding how they interact and function together in malignancy. As function is probably highly dependent on endogenous conditions found in native tumours, chaperomes have resisted investigation, mainly due to the limitations of methods needed to disrupt or engineer the cellular environment to facilitate analysis...
October 5, 2016: Nature
https://www.readbyqxmd.com/read/27702574/cell-free-analysis-of-polyq-dependent-protein-aggregation-and-its-inhibition-by-chaperone-proteins
#13
Kodai Machida, Tomoaki Shigeta, Ayano Kobayashi, Ai Masumoto, Yuna Hidaka, Hiroaki Imataka
Protein misfolding and aggregation is one of the major causes of neurodegenerative disorders such as Alzheimer's disease, Parkinson's disease and Huntington's disease. So far protein aggregation related to these diseases has been studied using animals, cultured cells or purified proteins. In this study, we show that a newly synthesized polyglutamine protein implicated in Huntington's disease forms large aggregates in HeLa cells, and successfully recapitulate the process of this aggregation using a translation-based system derived from HeLa cell extracts...
October 1, 2016: Journal of Biotechnology
https://www.readbyqxmd.com/read/27699616/backbone-and-methyl-resonance-assignments-of-the-42%C3%A2-kda-human-hsc70-nucleotide-binding-domain-in-the-adp-state
#14
Erik R P Zuiderweg, Jason E Gestwicki
Hsc70 is the constitutively expressed mammalian heat shock 70 kDa (Hsp70) cytosolic chaperone. It plays a central role in cellular proteostasis and protein trafficking. Here, we present the backbone and methyl group assignments for the 386-residue nucleotide binding domain of the human protein. This domain controls the chaperone's allostery, binds multiple co-chaperones and is the target of several classes of known chemical Hsp70 inhibitors. The NMR assignments are based on common triple resonance experiments with triple labeled protein, and on several (15)N and (13)C-resolved 3D NOE experiments with methyl-reprotonated samples...
October 3, 2016: Biomolecular NMR Assignments
https://www.readbyqxmd.com/read/27659529/induction-of-anti-egfr-immune-response-with-mimotopes-identified-from-a-phage-display-peptide-library-by-panitumumab
#15
Aidong Wang, Ming Cui, Hong Qu, Jiabo Di, Zaozao Wang, Jiadi Xing, Fan Wu, Wei Wu, Xicheng Wang, Lin Shen, Beihai Jiang, Xiangqian Su
The epidermal growth factor receptor (EGFR) is overexpressed in several epithelial tumors. Anti-EGFR humanized monoclonal antibodies, cetuximab and panitumumab, in combination with chemotherapy have improved the prognosis for patients with wild-type RAS tumors. To identify mimotopes of EGFR and develop mimotope-based EGFR vaccines, we screened a phage display peptide library with panitumumab. Two EGFR mimotopes P19 and P26, which could be recognized by panitumumab specifically, were isolated. To enhance the immune responses, we generated recombinant proteins of P19 or P26 fused to a heat-shock cognate protein 70 (Hsc70), and evaluated the efficacy of Hsc70-P19 and Hsc70-P26 as vaccines in vivo...
September 21, 2016: Oncotarget
https://www.readbyqxmd.com/read/27651462/a-small-stem-loop-structure-of-the-ebola-virus-trailer-is-essential-for-replication-and-interacts-with-heat-shock-protein-a8
#16
Joanna Sztuba-Solinska, Larissa Diaz, Mia R Kumar, Gaëlle Kolb, Michael R Wiley, Lucas Jozwick, Jens H Kuhn, Gustavo Palacios, Sheli R Radoshitzky, Stuart F J Le Grice, Reed F Johnson
Ebola virus (EBOV) is a single-stranded negative-sense RNA virus belonging to the Filoviridae family. The leader and trailer non-coding regions of the EBOV genome likely regulate its transcription, replication, and progeny genome packaging. We investigated the cis-acting RNA signals involved in RNA-RNA and RNA-protein interactions that regulate replication of eGFP-encoding EBOV minigenomic RNA and identified heat shock cognate protein family A (HSC70) member 8 (HSPA8) as an EBOV trailer-interacting host protein...
November 16, 2016: Nucleic Acids Research
https://www.readbyqxmd.com/read/27639943/cloning-of-heat-shock-protein-genes-hsp70-hsc70-and-hsp90-and-their-expression-in-response-to-larval-diapause-and-thermal-stress-in-the-wheat-blossom-midge-sitodiplosis-mosellana
#17
Weining Cheng, Dan Li, Yue Wang, Yang Liu, Keyan Zhu-Salzman
Sitodiplosis mosellana Géhin, one of the most important pests of wheat, undergoes obligatory diapause as a larva to survive unfavorable temperature extremes during hot summers and cold winters. To explore the potential roles of heat shock proteins (hsp) in this process, we cloned full-length cDNAs of hsp70, hsc70 and hsp90 from S. mosellana larvae, and examined their expression in response to diapause and short-term temperature stresses. Three hsps included all signature sequences of corresponding protein family and EEVD motifs...
December 2016: Journal of Insect Physiology
https://www.readbyqxmd.com/read/27633857/regulation-of-osteoblast-development-by-bcl-2-associated-athanogene-1-bag-1
#18
Joanna Greenhough, Emmanouil S Papadakis, Ramsey I Cutress, Paul A Townsend, Richard O C Oreffo, Rahul S Tare
BCL-2-associated athanogene-1 (BAG-1) is expressed by osteoblast-lineage cells; early embryonic lethality in Bag-1 null mice, however, has limited the investigation of BAG-1 function in osteoblast development. In the present study, bone morphogenetic protein-2/BMP-2-directed osteogenic differentiation of bone marrow stromal cells (BMSCs) of Bag-1(+/-) (heterozygous) female mice was decreased significantly. Genes crucial for osteogenic differentiation, bone matrix formation and mineralisation were expressed at significantly lower levels in cultures of Bag-1(+/-) BMSCs supplemented with BMP-2, while genes with roles in inhibition of BMP-2-directed osteoblastogenesis were significantly upregulated...
September 16, 2016: Scientific Reports
https://www.readbyqxmd.com/read/27633855/effect-of-chaperones-on-prion-protein-prp23-98-aggregation-in-vitro
#19
Noriyuki Shiraishi, Yoshiaki Hirano
Recent studies have indicated that PrP23-98, an N-terminal portion of PrP, polymerizes into amyloid-like and proteinase K (PK)-resistant aggregates in the presence of NADPH with copper ions [19], and then that CRT suppressed aggregation of PrP23-98 and also promoted solubilization of the aggregates [18]. As it is interesting to find out whether other chaperones can inhibit aggregation of PrP23-98 in vitro similar to CRT, this study was conducted to determine whether BiP, Grp94, PDI Grp58 and heat shock cognate protein70 (Hsc70) can inhibit aggregation of PrP23-98 in vitro...
September 9, 2016: Protein and Peptide Letters
https://www.readbyqxmd.com/read/27620487/glucolipotoxicity-diminishes-cardiomyocyte-tfeb-and-inhibits-lysosomal-autophagy-during-obesity-and-diabetes
#20
Purvi C Trivedi, Jordan J Bartlett, Lester J Perez, Keith R Brunt, Jean Francois Legare, Ansar Hassan, Petra C Kienesberger, Thomas Pulinilkunnil
Impaired cardiac metabolism in the obese and diabetic heart leads to glucolipotoxicity and ensuing cardiomyopathy. Glucolipotoxicity causes cardiomyocyte injury by increasing energy insufficiency, impairing proteasomal-mediated protein degradation and inducing apoptosis. Proteasome-evading proteins are degraded by autophagy in the lysosome, whose metabolism and function are regulated by master regulator transcription factor EB (TFEB). Limited studies have examined the impact of glucolipotoxicity on intra-lysosomal signaling proteins and their regulators...
September 9, 2016: Biochimica et Biophysica Acta
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