HSF1 and HSPA6 As Functional Candidate Genes Associated with Heat Tolerance in Angus Cattle
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At Elevated Temperatures, Heat Shock Protein Genes Show Altered Ratios Of
EXPERIMENTAL AND THERAPEUTIC MEDICINE 22: 900, 2021 At elevated temperatures, heat shock protein genes show altered ratios of different RNAs and expression of new RNAs, including several novel HSPB1 mRNAs encoding HSP27 protein isoforms XIA GAO1,2, KEYIN ZHANG1,2, HAIYAN ZHOU3, LUCAS ZELLMER4, CHENGFU YUAN5, HAI HUANG6 and DEZHONG JOSHUA LIAO2,6 1Department of Pathology, Guizhou Medical University Hospital; 2Key Lab of Endemic and Ethnic Diseases of The Ministry of Education of China in Guizhou Medical University; 3Clinical Research Center, Guizhou Medical University Hospital, Guiyang, Guizhou 550004, P.R. China; 4Masonic Cancer Center, University of Minnesota, Minneapolis, MN 55455, USA; 5Department of Biochemistry, China Three Gorges University, Yichang, Hubei 443002; 6Center for Clinical Laboratories, Guizhou Medical University Hospital, Guiyang, Guizhou 550004, P.R. China Received December 16, 2020; Accepted May 10, 2021 DOI: 10.3892/etm.2021.10332 Abstract. Heat shock proteins (HSP) serve as chaperones genes may engender multiple protein isoforms. These results to maintain the physiological conformation and function of collectively suggested that, besides increasing their expres‑ numerous cellular proteins when the ambient temperature is sion, certain HSP and associated genes also use alternative increased. To determine how accurate the general assumption transcription start sites to produce multiple RNA transcripts that HSP gene expression is increased in febrile situations is, and use alternative splicing of a transcript to produce multiple the RNA levels of the HSF1 (heat shock transcription factor 1) mature RNAs, as important mechanisms for responding to an gene and certain HSP genes were determined in three cell increased ambient temperature in vitro. lines cultured at 37˚C or 39˚C for three days. -
Whole-Exome Sequencing of Metastatic Cancer and Biomarkers of Treatment Response
Supplementary Online Content Beltran H, Eng K, Mosquera JM, et al. Whole-exome sequencing of metastatic cancer and biomarkers of treatment response. JAMA Oncol. Published online May 28, 2015. doi:10.1001/jamaoncol.2015.1313 eMethods eFigure 1. A schematic of the IPM Computational Pipeline eFigure 2. Tumor purity analysis eFigure 3. Tumor purity estimates from Pathology team versus computationally (CLONET) estimated tumor purities values for frozen tumor specimens (Spearman correlation 0.2765327, p- value = 0.03561) eFigure 4. Sequencing metrics Fresh/frozen vs. FFPE tissue eFigure 5. Somatic copy number alteration profiles by tumor type at cytogenetic map location resolution; for each cytogenetic map location the mean genes aberration frequency is reported eFigure 6. The 20 most frequently aberrant genes with respect to copy number gains/losses detected per tumor type eFigure 7. Top 50 genes with focal and large scale copy number gains (A) and losses (B) across the cohort eFigure 8. Summary of total number of copy number alterations across PM tumors eFigure 9. An example of tumor evolution looking at serial biopsies from PM222, a patient with metastatic bladder carcinoma eFigure 10. PM12 somatic mutations by coverage and allele frequency (A) and (B) mutation correlation between primary (y- axis) and brain metastasis (x-axis) eFigure 11. Point mutations across 5 metastatic sites of a 55 year old patient with metastatic prostate cancer at time of rapid autopsy eFigure 12. CT scans from patient PM137, a patient with recurrent platinum refractory metastatic urothelial carcinoma eFigure 13. Tracking tumor genomics between primary and metastatic samples from patient PM12 eFigure 14. -
Senescence Inhibits the Chaperone Response to Thermal Stress
SUPPLEMENTAL INFORMATION Senescence inhibits the chaperone response to thermal stress Jack Llewellyn1, 2, Venkatesh Mallikarjun1, 2, 3, Ellen Appleton1, 2, Maria Osipova1, 2, Hamish TJ Gilbert1, 2, Stephen M Richardson2, Simon J Hubbard4, 5 and Joe Swift1, 2, 5 (1) Wellcome Centre for Cell-Matrix Research, Oxford Road, Manchester, M13 9PT, UK. (2) Division of Cell Matrix Biology and Regenerative Medicine, School of Biological Sciences, Faculty of Biology, Medicine and Health, Manchester Academic Health Science Centre, University of Manchester, Manchester, M13 9PL, UK. (3) Current address: Department of Biomedical Engineering, University of Virginia, Box 800759, Health System, Charlottesville, VA, 22903, USA. (4) Division of Evolution and Genomic Sciences, School of Biological Sciences, Faculty of Biology, Medicine and Health, Manchester Academic Health Science Centre, University of Manchester, Manchester, M13 9PL, UK. (5) Correspondence to SJH ([email protected]) or JS ([email protected]). Page 1 of 11 Supplemental Information: Llewellyn et al. Chaperone stress response in senescence CONTENTS Supplemental figures S1 – S5 … … … … … … … … 3 Supplemental table S6 … … … … … … … … 10 Supplemental references … … … … … … … … 11 Page 2 of 11 Supplemental Information: Llewellyn et al. Chaperone stress response in senescence SUPPLEMENTAL FIGURES Figure S1. A EP (passage 3) LP (passage 16) 200 µm 200 µm 1.5 3 B Mass spectrometry proteomics (n = 4) C mRNA (n = 4) D 100k EP 1.0 2 p < 0.0001 p < 0.0001 LP p < 0.0001 p < 0.0001 ) 0.5 1 2 p < 0.0001 p < 0.0001 10k 0.0 0 -0.5 -1 Cell area (µm Cell area fold change vs. EP fold change vs. -
Cellular and Molecular Adaptation of Arabian Camel to Heat Stress
fgene-10-00588 June 18, 2019 Time: 16:2 # 1 REVIEW published: 19 June 2019 doi: 10.3389/fgene.2019.00588 Cellular and Molecular Adaptation of Arabian Camel to Heat Stress Abdullah Hoter1,2, Sandra Rizk3 and Hassan Y. Naim2* 1 Department of Biochemistry and Chemistry of Nutrition, Faculty of Veterinary Medicine, Cairo University, Giza, Egypt, 2 Department of Physiological Chemistry, University of Veterinary Medicine Hannover, Hanover, Germany, 3 School of Arts and Sciences, Lebanese American University, Beirut, Lebanon To cope with the extreme heat stress and drought of the desert, the Arabian camel (Camelus dromedarius) has developed exceptional physiological and biochemical particularities. Previous reports focused mainly on the physiological features of Arabian camel and neglected its cellular and molecular characteristics. Heat shock proteins are suggested to play a key role in the protein homeostasis and thermotolerance. Therefore, we aim by this review to elucidate the implication of camel HSPs in its physiological adaptation to heat stress and compare them with HSPs in related mammalian species. Correlation of these molecules to the adaptive mechanisms in Edited by: Pamela Burger, camel is of special importance to expand our understanding of the overall camel University of Veterinary Medicine physiology and homeostasis. Vienna, Austria Keywords: Arabian camel, heat shock proteins, heat stress, chaperones, desert, adaptation Reviewed by: Pablo Orozco-terWengel, Cardiff University, United Kingdom Ajamaluddin Malik, INTRODUCTION King Saud University, Saudi Arabia *Correspondence: Arabian camel (Camelus dromedarius), also known as the one humped camel, is a unique large Hassan Y. Naim animal belonging to the Camelidae family. This creature is well adapted to endure extreme levels [email protected] of heat stress and arid conditions of the desert. -
Prognostic and Functional Significant of Heat Shock Proteins (Hsps)
biology Article Prognostic and Functional Significant of Heat Shock Proteins (HSPs) in Breast Cancer Unveiled by Multi-Omics Approaches Miriam Buttacavoli 1,†, Gianluca Di Cara 1,†, Cesare D’Amico 1, Fabiana Geraci 1 , Ida Pucci-Minafra 2, Salvatore Feo 1 and Patrizia Cancemi 1,2,* 1 Department of Biological Chemical and Pharmaceutical Sciences and Technologies (STEBICEF), University of Palermo, 90128 Palermo, Italy; [email protected] (M.B.); [email protected] (G.D.C.); [email protected] (C.D.); [email protected] (F.G.); [email protected] (S.F.) 2 Experimental Center of Onco Biology (COBS), 90145 Palermo, Italy; [email protected] * Correspondence: [email protected]; Tel.: +39-091-2389-7330 † These authors contributed equally to this work. Simple Summary: In this study, we investigated the expression pattern and prognostic significance of the heat shock proteins (HSPs) family members in breast cancer (BC) by using several bioinfor- matics tools and proteomics investigations. Our results demonstrated that, collectively, HSPs were deregulated in BC, acting as both oncogene and onco-suppressor genes. In particular, two different HSP-clusters were significantly associated with a poor or good prognosis. Interestingly, the HSPs deregulation impacted gene expression and miRNAs regulation that, in turn, affected important bio- logical pathways involved in cell cycle, DNA replication, and receptors-mediated signaling. Finally, the proteomic identification of several HSPs members and isoforms revealed much more complexity Citation: Buttacavoli, M.; Di Cara, of HSPs roles in BC and showed that their expression is quite variable among patients. In conclusion, G.; D’Amico, C.; Geraci, F.; we elaborated two panels of HSPs that could be further explored as potential biomarkers for BC Pucci-Minafra, I.; Feo, S.; Cancemi, P. -
De Novo and Rare Mutations in the HSPA1L Heat
Takahashi et al. Genome Medicine (2017) 9:8 DOI 10.1186/s13073-016-0394-9 RESEARCH Open Access De novo and rare mutations in the HSPA1L heat shock gene associated with inflammatory bowel disease Shinichi Takahashi1,2†, Gaia Andreoletti3†, Rui Chen1, Yoichi Munehira4,5, Akshay Batra6, Nadeem A. Afzal6, R. Mark Beattie6, Jonathan A. Bernstein7, Sarah Ennis3* and Michael Snyder1* Abstract Background: Inflammatory bowel disease (IBD) is a chronic, relapsing inflammatory disease of the gastrointestinal tract which includes ulcerative colitis and Crohn's disease. Genetic risk factors for IBD are not well understood. Methods: We performed a family-based whole exome sequencing (WES) analysis on a core family (Family A) to identify potential causal mutations and then analyzed exome data from a Caucasian pediatric cohort (136 patients and 106 controls) to validate the presence of mutations in the candidate gene, heat shock 70 kDa protein 1-like (HSPA1L). Biochemical assays of the de novo and rare (minor allele frequency, MAF < 0.01) mutation variant proteins further validated the predicted deleterious effects of the identified alleles. Results: In the proband of Family A, we found a heterozygous de novo mutation (c.830C > T; p.Ser277Leu) in HSPA1L. Through analysis of WES data of 136 patients, we identified five additional rare HSPA1L mutations (p.Gly77Ser, p.Leu172del, p.Thr267Ile, p.Ala268Thr, p.Glu558Asp) in six patients. In contrast, rare HSPA1L mutations were not observed in controls, and were significantly enriched in patients (P = 0.02). Interestingly, we did not find non-synonymous rare mutations in the HSP70 isoforms HSPA1A and HSPA1B. Biochemical assays revealed that all six rare HSPA1L variant proteins showed decreased chaperone activity in vitro. -
Characterization of the Dual Functional Effects of Heat Shock Proteins (Hsps
Zhang et al. Genome Medicine (2020) 12:101 https://doi.org/10.1186/s13073-020-00795-6 RESEARCH Open Access Characterization of the dual functional effects of heat shock proteins (HSPs) in cancer hallmarks to aid development of HSP inhibitors Zhao Zhang1†, Ji Jing2†, Youqiong Ye1, Zhiao Chen1, Ying Jing1, Shengli Li1, Wei Hong1, Hang Ruan1, Yaoming Liu1, Qingsong Hu3, Jun Wang4, Wenbo Li1, Chunru Lin3, Lixia Diao5*, Yubin Zhou2* and Leng Han1* Abstract Background: Heat shock proteins (HSPs), a representative family of chaperone genes, play crucial roles in malignant progression and are pursued as attractive anti-cancer therapeutic targets. Despite tremendous efforts to develop anti-cancer drugs based on HSPs, no HSP inhibitors have thus far reached the milestone of FDA approval. There remains an unmet need to further understand the functional roles of HSPs in cancer. Methods: We constructed the network for HSPs across ~ 10,000 tumor samples from The Cancer Genome Atlas (TCGA) and ~ 10,000 normal samples from Genotype-Tissue Expression (GTEx), and compared the network disruption between tumor and normal samples. We then examined the associations between HSPs and cancer hallmarks and validated these associations from multiple independent high-throughput functional screens, including Project Achilles and DRIVE. Finally, we experimentally characterized the dual function effects of HSPs in tumor proliferation and metastasis. Results: We comprehensively analyzed the HSP expression landscape across multiple human cancers and revealed a global disruption of the co-expression network for HSPs. Through analyzing HSP expression alteration and its association with tumor proliferation and metastasis, we revealed dual functional effects of HSPs, in that they can simultaneously influence proliferation and metastasis in opposite directions. -
Regulation of Antimicrobial Pathways by Endogenous Heat Shock Proteins in Gastrointestinal Disorders
Review Regulation of Antimicrobial Pathways by Endogenous Heat Shock Proteins in Gastrointestinal Disorders Emma Finlayson-Trick 1 , Jessica Connors 2, Andrew Stadnyk 1,2 and Johan Van Limbergen 1,2,* 1 Department of Microbiology & Immunology, Dalhousie University, 5850 College Street, Room 7-C, Halifax, NS B3H 4R2, Canada; emma.fi[email protected] (E.F.-T.); [email protected] (A.S.) 2 Division of Pediatric Gastroenterology and Nutrition, Department of Pediatrics, Dalhousie University, IWK Health Centre, 5850/5980 University Avenue, Halifax, NS B3K 6R8, Canada; [email protected] * Correspondence: [email protected]; Tel.: +902-470-8746; Fax: +902-470-7249 Received: 31 August 2018; Accepted: 26 September 2018; Published: 28 September 2018 Abstract: Heat shock proteins (HSPs) are essential mediators of cellular homeostasis by maintaining protein functionality and stability, and activating appropriate immune cells. HSP activity is influenced by a variety of factors including diet, microbial stimuli, environment and host immunity. The overexpression and down-regulation of HSPs is associated with various disease phenotypes, including the inflammatory bowel diseases (IBD) such as Crohn’s disease (CD). While the precise etiology of CD remains unclear, many of the putative triggers also influence HSP activity. The development of different CD phenotypes therefore may be a result of the disease-modifying behavior of the environmentally-regulated HSPs. Understanding the role of bacterial and endogenous HSPs in host homeostasis and disease will help elucidate the complex interplay of factors. Furthermore, discerning the function of HSPs in CD may lead to therapeutic developments that better reflect and respond to the gut environment. -
Heat Shock Proteins in Infection
Clinica Chimica Acta 498 (2019) 90–100 Contents lists available at ScienceDirect Clinica Chimica Acta journal homepage: www.elsevier.com/locate/cca Review Heat shock proteins in infection T ⁎ Azam Bolhassania, , Elnaz Agib a Department of Hepatitis and AIDS, Pasteur Institute of Iran, Tehran, Iran b Iranian Comprehensive Hemophilia Care Center, Tehran, Iran ARTICLE INFO ABSTRACT Keywords: Heat shock proteins (HSPs) are constitutively expressed under physiological conditions in most organisms but Heat shock protein their expression can significantly enhance in response to four types of stimuli including physical (e.g., radiation Infectious disease or heat shock), chemical and microbial (e.g., pathogenic bacteria, viruses, parasites and fungi) stimuli, and also Chaperone dietary. These proteins were identified for their role in protecting cells from high temperature and other forms of Immunity stress. HSPs control physiological activities or virulence through interaction with various regulators of cellular Apoptosis signaling pathways. Several roles were determined for HSPs in the immune system including intracellular roles (e.g., antigen presentation and expression of innate receptors) as well as extracellular roles (e.g., tumor im- munosurveillance and autoimmunity). It was observed that exogenously administered HSPs induced various immune responses in immunotherapy of cancer, infectious diseases, and autoimmunity. Moreover, virus inter- action with HSPs as molecular chaperones showed important roles in regulating viral infections including cell entry and nuclear import, viral replication and gene expression, folding/assembly of viral protein, apoptosis regulation, and host immunity. Viruses could regulate host HSPs at different levels such as transcription, translation, post-translational modification and cellular localization. In this review, we attempt to overview the roles of HSPs in a variety of infectious diseases. -
Prognostic Value of Members of the HSP70 Family in Hepatocellular Carcinoma
Prognostic value of members of the HSP70 family in Hepatocellular Carcinoma Haixing Jiang ( [email protected] ) Guangxi Medical University First Aliated Hospital https://orcid.org/0000-0002-0582-221X Ziyu Liang Guangxi Medical University First Aliated Hospital Shanyu Qin Guangxi Medical University First Aliated Hospital Kang Liu Guangxi Medical University First Aliated Hospital Research article Keywords: hepatocellular carcinoma, heat shock protein 70, Kaplan-Meier plotter, prognosis, database Posted Date: May 27th, 2020 DOI: https://doi.org/10.21203/rs.3.rs-30115/v1 License: This work is licensed under a Creative Commons Attribution 4.0 International License. Read Full License Page 1/21 Abstract BACKGROUND: Despite multiple functions in the disease, the prognosis of the heat shock protein (HSP) 70 family in Hepatocellular Carcinoma (HCC) remains unclear. METHODS: The UALCAN database has provided information about the expression level of HSP70 family members in both HCC and in normal tissues. Overall survival (OS) was conducted by Kaplan-Meier plotter (KM plotter). Gene ontology (GO) and KEGG pathway enrichment analyses were accomplished by DAVID database. GeneMANIA and STRING were applied to construct gene-gene and protein-protein interaction (PPI) networks. RESULTS: From the UALCAN database, we found that the expression levels of eight members of the HSP70 family in HCC patients were higher than in normal liver tissues. These eight members were, namely, HSPA1A, HSPA1B, HSPA1L, HSPA2, HSPA5, HSPA6, HSPA8 and HSPA9. From KM plotter database, high expression of HSPA1A, HSPA1B, HSPA6 and HSPA8 has been observed to be associated with worse OS in patients with HCC (hazard ratio [HR] =1.49, 95% condence interval [CI]: 1.03-2.15, P=0.031; HR=1.49, 95%CI: 1.05-2.12, P=0.026; HR=1.53, 95%CI: 1.06-2.2, P=0.021 and HR=1.81, 95%CI: 1.21-2.71, P=0.0036, respectively). -
Impact of Heat Shock Protein 90 Inhibition on the Proteomic Profile
cells Article Impact of Heat Shock Protein 90 Inhibition on the Proteomic Profile of Lung Adenocarcinoma as Measured by Two-Dimensional Electrophoresis Coupled with Mass Spectrometry Ángela Marrugal 1 , Irene Ferrer 1,2, Maria Dolores Pastor 3, Laura Ojeda 1 , 4 2,3 2,3, , Álvaro Quintanal-Villalonga , Amancio Carnero , Sonia Molina-Pinelo * y and 1,2,5,6, , Luis Paz-Ares * y 1 H12O-CNIO Lung Cancer Clinical Research Unit, Instituto de Investigación Hospital 12 de Octubre & Centro Nacional de Investigaciones Oncológicas (CNIO), 28029 Madrid, Spain 2 CIBERONC, 28029 Madrid, Spain 3 Instituto de Biomedicina de Sevilla (IBIS) (HUVR, CSIC, Universidad de Sevilla), 41013 Sevilla, Spain 4 Program in Molecular Pharmacology, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA 5 Medical Oncology Department, Hospital Universitario Doce de Octubre, 28041 Madrid, Spain 6 Medical School, Universidad Complutense, 28040 Madrid, Spain * Correspondence: [email protected] (S.M.-P.); [email protected] (L.P.-A.) These authors contributed equally to this work. y Received: 24 June 2019; Accepted: 30 July 2019; Published: 31 July 2019 Abstract: Heat shock protein 90 (HSP90) is an important chaperone in lung adenocarcinoma, with relevant protein drivers such as EGFR (epidermal growth factor receptor) and EML4-ALK (echinoderm microtubule-associated protein-like protein4 fused to anaplastic lymphoma kinase) depending on it for their correct function, therefore HSP90 inhibitors show promise as potential treatments for lung adenocarcinoma. To study responses to its inhibition, HSP90 was pharmacologically interrupted by geldanamycin and resorcinol derivatives or with combined inhibition of HSP90 plus HSP70 in lung adenocarcinoma cell lines. -
Crystal Structures of the Atpase Domains of Four Human Hsp70 Isoforms: HSPA1L/Hsp70-Hom, HSPA2/Hsp70-2, HSPA6/Hsp70b’, and HSPA5/Bip/GRP78
Crystal Structures of the ATPase Domains of Four Human Hsp70 Isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B’, and HSPA5/BiP/GRP78 Magdalena Wisniewska, Tobias Karlberg, Lari Lehtio¨ ¤, Ida Johansson, Tetyana Kotenyova, Martin Moche, Herwig Schu¨ ler* Structural Genomics Consortium, Karolinska Institutet, Stockholm, Sweden Abstract The 70-kDa heat shock proteins (Hsp70) are chaperones with central roles in processes that involve polypeptide remodeling events. Hsp70 proteins consist of two major functional domains: an N-terminal nucleotide binding domain (NBD) with ATPase activity, and a C-terminal substrate binding domain (SBD). We present the first crystal structures of four human Hsp70 isoforms, those of the NBDs of HSPA1L, HSPA2, HSPA5 and HSPA6. As previously with Hsp70 family members, all four proteins crystallized in a closed cleft conformation, although a slight cleft opening through rotation of subdomain IIB was observed for the HSPA5-ADP complex. The structures presented here support the view that the NBDs of human Hsp70 function by conserved mechanisms and contribute little to isoform specificity, which instead is brought about by the SBDs and by accessory proteins. Enhanced version: This article can also be viewed as an enhanced version in which the text of the article is integrated with interactive 3D representations and animated transitions. Please note that a web plugin is required to access this enhanced functionality. Instructions for the installation and use of the web plugin are available in Text S1. Citation: Wisniewska M, Karlberg T, Lehtio¨ L, Johansson I, Kotenyova T, et al. (2010) Crystal Structures of the ATPase Domains of Four Human Hsp70 Isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B’, and HSPA5/BiP/GRP78.