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  1 / 24209 MEDLINE  
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[PMID]:29340527
[Au] Autor:Ribeiro LP; Freitas-Lima LC; Naumann GB; Meyrelles SS; Lunz W; Pires SF; Andrade HM; Carnielli JBT; Figueiredo SG
[Ad] Endereço:Departamento de Ciências Fisiológicas, Universidade Federal do Espírito Santo, Vitória, ES, Brasil.
[Ti] Título:Cardiac protein expression patterns are associated with distinct inborn exercise capacity in non-selectively bred rats.
[So] Source:Braz J Med Biol Res;51(3):e7033, 2018 Jan 11.
[Is] ISSN:1414-431X
[Cp] País de publicação:Brazil
[La] Idioma:eng
[Ab] Resumo:In the present study, we successfully demonstrated for the first time the existence of cardiac proteomic differences between non-selectively bred rats with distinct intrinsic exercise capacities. A proteomic approach based on two-dimensional gel electrophoresis coupled to mass spectrometry was used to study the left ventricle (LV) tissue proteome of rats with distinct intrinsic exercise capacity. Low running performance (LRP) and high running performance (HRP) rats were categorized by a treadmill exercise test, according to distance run to exhaustion. The running capacity of HRPs was 3.5-fold greater than LRPs. Protein profiling revealed 29 differences between HRP and LRP rats (15 proteins were identified). We detected alterations in components involved in metabolism, antioxidant and stress response, microfibrillar and cytoskeletal proteins. Contractile proteins were upregulated in the LVs of HRP rats (α-myosin heavy chain-6, myosin light chain-1 and creatine kinase), whereas the LVs of LRP rats exhibited upregulation in proteins associated with stress response (aldehyde dehydrogenase 2, α-crystallin B chain and HSPß-2). In addition, the cytoskeletal proteins desmin and α-actin were upregulated in LRPs. Taken together, our results suggest that the increased contractile protein levels in HRP rats partly accounted for their improved exercise capacity, and that proteins considered risk factors to the development of cardiovascular disease were expressed in higher amounts in LRP animals.
[Mh] Termos MeSH primário: Testes de Função Cardíaca/métodos
Miocárdio/metabolismo
Condicionamento Físico Animal/fisiologia
Proteínas/metabolismo
Corrida/fisiologia
[Mh] Termos MeSH secundário: Animais
Proteínas Contráteis/metabolismo
Proteínas do Citoesqueleto/metabolismo
Desmina/metabolismo
Eletroforese em Gel Bidimensional
Ventrículos do Coração/metabolismo
Proteínas de Choque Térmico/metabolismo
Masculino
Espectrometria de Massas
Tamanho do Órgão
Proteínas/isolamento & purificação
Proteômica
Ratos
Ratos Endogâmicos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Contractile Proteins); 0 (Cytoskeletal Proteins); 0 (Desmin); 0 (Heat-Shock Proteins); 0 (Proteins)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180301
[Lr] Data última revisão:
180301
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180118
[St] Status:MEDLINE


  2 / 24209 MEDLINE  
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[PMID]:29020644
[Au] Autor:Pradhan A; Olsson PE; Jass J
[Ad] Endereço:Biology, the Life Science Center, School of Science and Technology, Örebro University, SE-701 82 Örebro, Sweden. Electronic address: ajay.pradhan@oru.se.
[Ti] Título:Di(2-ethylhexyl) phthalate and diethyl phthalate disrupt lipid metabolism, reduce fecundity and shortens lifespan of Caenorhabditis elegans.
[So] Source:Chemosphere;190:375-382, 2018 Jan.
[Is] ISSN:1879-1298
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The widespread use of phthalates is of major concern as they have adverse effects on many different physiological functions, including reproduction, metabolism and cell differentiation. The aim of this study was to compare the toxicity of the widely-used di (2-ethydlhexyl) phthalate (DEHP) with its substitute, diethyl phthalate (DEP). We analyzed the toxicity of these two phthalates using Caenorhabditis elegans as a model system. Gene expression analysis following exposure during the L1 to young adult stage showed that DEHP and DEP alter the expression of genes involved in lipid metabolism and stress response. Genes associated with lipid metabolism, including fasn-1, pod-2, fat-5, acs-6 and sbp-1, and vitellogenin were upregulated. Among the stress response genes, ced-1 wah-1, daf-21 and gst-4 were upregulated, while ctl-1, cdf-2 and the heat shock proteins (hsp-16.1, hsp-16.48 and sip-1) were downregulated. Lipid staining revealed that DEHP significantly increased lipid content following 1 µM exposure, however, DEP required 10 µM exposure to elicit an effect. Both DEHP and DEP reduced the fecundity at 1 µM concentration. Lifespan analysis indicated that DEHP and DEP reduced the average lifespan from 14 days in unexposed worms to 13 and 12 days, respectively. Expression of lifespan associated genes showed a correlation to shortened lifespan in the exposed groups. As reported previously, our data also indicates that the banned DEHP is toxic to C. elegans, however its substitute DEP has not been previously tested in this model organism and our data revealed that DEP is equally potent as DEHP in regulating C. elegans physiological functions.
[Mh] Termos MeSH primário: Caenorhabditis elegans/efeitos dos fármacos
Dietilexilftalato/toxicidade
Fertilidade/efeitos dos fármacos
Metabolismo dos Lipídeos/efeitos dos fármacos
Longevidade/efeitos dos fármacos
Ácidos Ftálicos/toxicidade
[Mh] Termos MeSH secundário: Animais
Caenorhabditis elegans/metabolismo
Caenorhabditis elegans/fisiologia
Dietilexilftalato/farmacologia
Proteínas de Choque Térmico/genética
Metabolismo dos Lipídeos/genética
Ácidos Ftálicos/farmacologia
Reprodução/efeitos dos fármacos
Vitelogeninas/genética
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Heat-Shock Proteins); 0 (Phthalic Acids); 0 (Vitellogenins); 6O7F7IX66E (phthalic acid); C42K0PH13C (Diethylhexyl Phthalate); UF064M00AF (diethyl phthalate)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180228
[Lr] Data última revisão:
180228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171012
[St] Status:MEDLINE


  3 / 24209 MEDLINE  
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[PMID]:28464871
[Au] Autor:Aksoy MO; Kim V; Cornwell WD; Rogers TJ; Kosmider B; Bahmed K; Barrero C; Merali S; Shetty N; Kelsen SG
[Ad] Endereço:Department of Thoracic Medicine and Surgery, Temple University School of Medicine, Philadelphia, PA, 19140, USA. mark.aksoy@temple.edu.
[Ti] Título:Secretion of the endoplasmic reticulum stress protein, GRP78, into the BALF is increased in cigarette smokers.
[So] Source:Respir Res;18(1):78, 2017 May 02.
[Is] ISSN:1465-993X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Identification of biomarkers of cigarette smoke -induced lung damage and early COPD is an area of intense interest. Glucose regulated protein of 78 kD (i.e., GRP78), a multi-functional protein which mediates cell responses to oxidant stress, is increased in the lungs of cigarette smokers and in the serum of subjects with COPD. We have suggested that secretion of GRP78 by lung cells may explain the increase in serum GRP78 in COPD. To assess GRP78 secretion by the lung, we assayed GRP78 in bronchoalveolar lavage fluid (BALF) in chronic smokers and non-smokers. We also directly assessed the acute effect of cigarette smoke material on GRP78 secretion in isolated human airway epithelial cells (HAEC). METHODS: GRP78 was measured in BALF of smokers (S; n = 13) and non-smokers (NS; n = 11) by Western blotting. GRP78 secretion by HAEC was assessed by comparing its concentration in cell culture medium and cell lysates. Cells were treated for 24 h with either the volatile phase of cigarette smoke (cigarette smoke extract (CSE) or the particulate phase (cigarette smoke condensate (CSC)). RESULTS: GRP78 was present in the BALF of both NS and S but levels were significantly greater in S (p = 0.04). GRP78 was secreted constitutively in HAEC. CSE 15% X 24 h increased GRP78 in cell-conditioned medium without affecting its intracellular concentration. In contrast, CSC X 24 h increased intracellular GRP78 expression but did not affect GRP78 secretion. Brefeldin A, an inhibitor of classical Golgi secretion pathways, did not inhibit GRP78 secretion indicating that non-classical pathways were involved. CONCLUSION: The present study indicates that GRP78 is increased in BALF in cigarette smokers; that HAEC secrete GRP78; and that GRP78 secretion by HAEC is augmented by cigarette smoke particulates. Enhanced secretion of GRP78 by lung cells makes it a potential biomarker of cigarette smoke-induced lung injury.
[Mh] Termos MeSH primário: Líquido da Lavagem Broncoalveolar/química
Retículo Endoplasmático/secreção
Proteínas de Choque Térmico/secreção
Lesão Pulmonar/metabolismo
Fumar/metabolismo
[Mh] Termos MeSH secundário: Biomarcadores/análise
Biomarcadores/química
Feminino
Seres Humanos
Masculino
Meia-Idade
Reprodutibilidade dos Testes
Sensibilidade e Especificidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Heat-Shock Proteins); 0 (molecular chaperone GRP78)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1186/s12931-017-0561-6


  4 / 24209 MEDLINE  
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[PMID]:29346421
[Au] Autor:Higgins R; Kabbaj MH; Hatcher A; Wang Y
[Ad] Endereço:Department of Biomedical Sciences, College of Medicine, Florida State University, Tallahassee, Florida, United States of America.
[Ti] Título:The absence of specific yeast heat-shock proteins leads to abnormal aggregation and compromised autophagic clearance of mutant Huntingtin proteins.
[So] Source:PLoS One;13(1):e0191490, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The functionality of a protein depends on its correct folding, but newly synthesized proteins are susceptible to aberrant folding and aggregation. Heat shock proteins (HSPs) function as molecular chaperones that aid in protein folding and the degradation of misfolded proteins. Trinucleotide (CAG) repeat expansion in the Huntingtin gene (HTT) results in the expression of misfolded Huntingtin protein (Htt), which contributes to the development of Huntington's disease. We previously found that the degradation of mutated Htt with polyQ expansion (Htt103QP) depends on both ubiquitin proteasome system and autophagy. However, the role of heat shock proteins in the clearance of mutated Htt remains poorly understood. Here, we report that cytosolic Hsp70 (Ssa family), its nucleotide exchange factors (Sse1 and Fes1), and a Hsp40 co-chaperone (Ydj1) are required for inclusion body formation of Htt103QP proteins and their clearance via autophagy. Extended induction of Htt103QP-GFP leads to the formation of a single inclusion body in wild-type yeast cells, but mutant cells lacking these HSPs exhibit increased number of Htt103QP aggregates. Most notably, we detected more aggregated forms of Htt103QP in sse1Δ mutant cells using an agarose gel assay. Increased protein aggregates are also observed in these HSP mutants even in the absence Htt103QP overexpression. Importantly, these HSPs are required for autophagy-mediated Htt103QP clearance, but are less critical for proteasome-dependent degradation. These findings suggest a chaperone network that facilitates inclusion body formation of misfolded proteins and the subsequent autophagic clearance.
[Mh] Termos MeSH primário: Autofagia
Proteínas de Choque Térmico/metabolismo
Proteína Huntingtina/genética
Mutação
Proteínas de Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Repetições de Trinucleotídeos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Heat-Shock Proteins); 0 (Huntingtin Protein); 0 (Saccharomyces cerevisiae Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180223
[Lr] Data última revisão:
180223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180119
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191490


  5 / 24209 MEDLINE  
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[PMID]:28468249
[Au] Autor:Santos TG; Martins VR; Hajj GNM
[Ad] Endereço:International Research Center, A.C. Camargo Cancer Center, São Paulo 01508-010, Brazil. tsantos@cipe.accamargo.org.br.
[Ti] Título:Unconventional Secretion of Heat Shock Proteins in Cancer.
[So] Source:Int J Mol Sci;18(5), 2017 Apr 29.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Heat shock proteins (HSPs) are abundant cellular proteins involved with protein homeostasis. They have both constitutive and inducible isoforms, whose expression levels are further increased by stress conditions, such as temperature elevation, reduced oxygen levels, infection, inflammation and exposure to toxic substances. In these situations, HSPs exert a pivotal role in offering protection, preventing cell death and promoting cell recovery. Although the majority of HSPs functions are exerted in the cytoplasm and organelles, several lines of evidence reveal that HSPs are able to induce cell responses in the extracellular milieu. HSPs do not possess secretion signal peptides, and their secretion was subject to widespread skepticism until the demonstration of the role of unconventional secretion forms such as exosomes. Secretion of HSPs may confer immune system modulation and be a cell-to-cell mediated form of increasing stress resistance. Thus, there is a wide potential for secreted HSPs in resistance of cancer therapy and in the development new therapeutic strategies.
[Mh] Termos MeSH primário: Exossomos/metabolismo
Proteínas de Choque Térmico/metabolismo
Neoplasias/metabolismo
[Mh] Termos MeSH secundário: Animais
Exossomos/imunologia
Exossomos/patologia
Proteínas de Choque Térmico/análise
Proteínas de Choque Térmico/imunologia
Seres Humanos
Imunomodulação
Neoplasias/imunologia
Neoplasias/patologia
Neoplasias/terapia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Heat-Shock Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180221
[Lr] Data última revisão:
180221
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE


  6 / 24209 MEDLINE  
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[PMID]:29372801
[Au] Autor:Garbuz DG; Evgen'ev MB
[Ti] Título:[The evolution of heat shock genes and expression patterns of heat shock proteins in the species from temperature contrasting habitats].
[So] Source:Genetika;53(1):12-30, 2017 Jan.
[Is] ISSN:0016-6758
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:Heat shock genes are the most evolutionarily ancient among the systems responsible for adaptation of organisms to a harsh environment. The encoded proteins (heat shock proteins, Hsps) represent the most important factors of adaptation to adverse environmental conditions. They serve as molecular chaperones, providing protein folding and preventing aggregation of damaged cellular proteins. Structural analysis of the heat shock genes in individuals from both phylogenetically close and very distant taxa made it possible to reveal the basic trends of the heat shock gene organization in the context of adaptation to extreme conditions. Using different model objects and nonmodel species from natural populations, it was demonstrated that modulation of the Hsps expression during adaptation to different environmental conditions could be achieved by changing the number and structural organization of heat shock genes in the genome, as well as the structure of their promoters. It was demonstrated that thermotolerant species were usually characterized by elevated levels of Hsps under normal temperature or by the increase in the synthesis of these proteins in response to heat shock. Analysis of the heat shock genes in phylogenetically distant organisms is of great interest because, on one hand, it contributes to the understanding of the molecular mechanisms of evolution of adaptogenes and, on the other hand, sheds the light on the role of different Hsps families in the development of thermotolerance and the resistance to other stress factors.
[Mh] Termos MeSH primário: Ecossistema
Evolução Molecular
Regulação da Expressão Gênica/fisiologia
Proteínas de Choque Térmico
Temperatura Alta
Filogenia
[Mh] Termos MeSH secundário: Proteínas de Choque Térmico/biossíntese
Proteínas de Choque Térmico/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Heat-Shock Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180127
[St] Status:MEDLINE


  7 / 24209 MEDLINE  
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[PMID]:29304094
[Au] Autor:Wang HS; Tsai CL; Chang PY; Chao A; Wu RC; Chen SH; Wang CJ; Yen CF; Lee YS; Wang TH
[Ad] Endereço:Department of Obstetrics and Gynecology, LinKou Medical Center, Chang Gung Memorial Hospital and Chang Gung University, Taoyuan, Taiwan.
[Ti] Título:Positive associations between upregulated levels of stress-induced phosphoprotein 1 and matrix metalloproteinase-9 in endometriosis/adenomyosis.
[So] Source:PLoS One;13(1):e0190573, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Stress-induced phosphoprotein-1 (STIP1), an adaptor protein that coordinates the functions of HSP70 and HSP90 in protein folding, has been implicated in the development of human gynecologic malignancies. This case-control study investigates STIP1 serum levels and tissue expression in relation to endometriosis/adenomyosis in Taiwanese population. Female patients with surgically confirmed endometriosis/adenomyosis were compared with women free of endometriosis/adenomyosis. Serum STIP1 levels were measured using an enzyme-linked immunosorbent assay and surgical tissues were analyzed by immunohistochemistry. Both epithelial and stromal cells in surgical tissues of endometriosis and adenomyosis expressed STIP1 and MMP-9. Notably, MMP-9 expression was significantly decreased when STIP1 expression was knocked-down. In vitro experiments revealed that STIP1 was capable of binding to the MMP-9 promoter and enhanced its transcriptional expression. The preoperative serum STIP1 levels of patients with endometriosis/adenomyosis were significantly higher than those of the controls. In brief, our data suggest an association between STIP1 levels and endometriosis/adenomyosis.
[Mh] Termos MeSH primário: Endometriose/enzimologia
Proteínas de Choque Térmico/metabolismo
Metaloproteinase 9 da Matriz/metabolismo
Regulação para Cima
[Mh] Termos MeSH secundário: Adulto
Estudos de Casos e Controles
Linhagem Celular Tumoral
Ensaio de Imunoadsorção Enzimática
Feminino
Proteínas de Choque Térmico/sangue
Proteínas de Choque Térmico/genética
Seres Humanos
Imuno-Histoquímica
Metaloproteinase 9 da Matriz/genética
Regiões Promotoras Genéticas
Taiwan
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Heat-Shock Proteins); 0 (STIP1 protein, human); EC 3.4.24.35 (Matrix Metalloproteinase 9)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180106
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190573


  8 / 24209 MEDLINE  
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[PMID]:29284056
[Au] Autor:Bento M; Pereira SG; Viegas W; Silva M
[Ad] Endereço:Linking Landscape, Environment, Agriculture and Food (LEAF), Instituto Superior de Agronomia, Universidade de Lisboa, Lisboa, Portugal.
[Ti] Título:Durum wheat diversity for heat stress tolerance during inflorescence emergence is correlated to TdHSP101C expression in early developmental stages.
[So] Source:PLoS One;12(12):e0190085, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The predicted world population increase along with climate changes threatens sustainable agricultural supply in the coming decades. It is therefore vital to understand crops diversity associated to abiotic stress response. Heat stress is considered one of the major constrains on crops productivity thus it is essential to develop new approaches for a precocious and rigorous evaluation of varietal diversity regarding heat tolerance. Plant cell membrane thermostability (CMS) is a widely used method for wheat thermotolerance assessment although its limitations require complementary solutions. In this work we used CMS assay and explored TdHSP101C genes as an additional tool for durum wheat screening. Genomic and transcriptomic analyses of TdHSP101C genes were performed in varieties with contrasting CMS results and further correlated with heat stress tolerance during fertilization and seed development. Although the durum wheat varieties studied presented a very high homology on TdHSP101C genes (>99%) the transcriptomic assessment allowed the discrimination between varieties with good CMS results and its correlation with differential impacts of heat treatment during inflorescence emergence and seed development on grain yield. The evidences here reported indicate that TdHSP101C transcription levels induced by heat stress in fully expanded leaves may be a promising complementary screening tool to discriminate between durum wheat varieties identified as thermotolerant through CMS.
[Mh] Termos MeSH primário: Adaptação Fisiológica
Temperatura Alta
Inflorescência
Triticum/fisiologia
[Mh] Termos MeSH secundário: Proteínas de Choque Térmico/genética
Triticum/classificação
Triticum/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Heat-Shock Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171229
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190085


  9 / 24209 MEDLINE  
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[PMID]:29178343
[Au] Autor:Moriya C; Taniguchi H; Nagatoishi S; Igarashi H; Tsumoto K; Imai K
[Ad] Endereço:Center for Antibody and Vaccine Therapy, Research Hospital, The Institute of Medical Science, The University of Tokyo, Tokyo, Japan.
[Ti] Título:PRDM14 directly interacts with heat shock proteins HSP90α and glucose-regulated protein 78.
[So] Source:Cancer Sci;109(2):373-383, 2018 Feb.
[Is] ISSN:1349-7006
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:PRDM14 is overexpressed in various cancers and can regulate cancer phenotype under certain conditions. Inhibiting PRDM14 expression in breast and pancreatic cancers has been reported to reduce cancer stem-like phenotypes, which are associated with aggressive tumor properties. Therefore, PRDM14 is considered a promising target for cancer therapy. To develop a pharmaceutical treatment, the mechanism and interacting partners of PRDM14 need to be clarified. Here, we identified the proteins interacting with PRDM14 in triple-negative breast cancer (TNBC) cells, which do not express the three most common types of receptor (estrogen receptors, progesterone receptors, and HER2). We obtained 13 candidates that were pulled down with PRDM14 in TNBC HCC1937 cells and identified them by mass spectrometry. Two candidates-glucose-regulated protein 78 (GRP78) and heat shock protein 90-α (HSP90α)-were confirmed in immunoprecipitation assay in two TNBC cell lines (HCC1937 and MDA-MB231). Surface plasmon resonance analysis using GST-PRDM14 showed that these two proteins directly interacted with PRDM14 and that the interactions required the C-terminal region of PRDM14, which includes zinc finger motifs. We also confirmed the interactions in living cells by NanoLuc luciferase-based bioluminescence resonance energy transfer (NanoBRET) assay. Moreover, HSP90 inhibitors (17DMAG and HSP990) significantly decreased breast cancer stem-like CD24  CD44 and side population (SP) cells in HCC1937 cells, but not in PRDM14 knockdown HCC1937 cells. The combination of the GRP78 inhibitor HA15 and PRDM14 knockdown significantly decreased cell proliferation and SP cell number in HCC1937 cells. These results suggest that HSP90α and GRP78 interact with PRDM14 and participate in cancer regulation.
[Mh] Termos MeSH primário: Proteínas de Choque Térmico HSP90/metabolismo
Proteínas de Choque Térmico/metabolismo
Proteínas Repressoras/metabolismo
Neoplasias de Mama Triplo Negativas/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Proliferação Celular
Feminino
Regulação Neoplásica da Expressão Gênica
Células HEK293
Seres Humanos
Espectrometria de Massas
Domínios Proteicos
Mapeamento de Interação de Proteínas
Proteínas Repressoras/química
Ressonância de Plasmônio de Superfície
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (HSP90 Heat-Shock Proteins); 0 (HSP90alpha protein, human); 0 (Heat-Shock Proteins); 0 (PRDM14 protein, human); 0 (Repressor Proteins); 0 (molecular chaperone GRP78)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.1111/cas.13458


  10 / 24209 MEDLINE  
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[PMID]:29247649
[Au] Autor:Park KY; Kim WT; Kim EY
[Ad] Endereço:Department of Systems Biology, College of Life Sciences and Biotechnology, Yonsei University, Seoul 03722, South Korea.
[Ti] Título:The proper localization of RESPONSIVE TO DESICCATION 20 in lipid droplets depends on their biogenesis induced by STRESS-RELATED PROTEINS in vegetative tissues.
[So] Source:Biochem Biophys Res Commun;495(2):1885-1889, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Arabidopsis LD surface proteins, SRPs are found only in higher plants and are important for LD biogenesis and abiotic stress signaling. However, the cellular mechanism of SRPs is still unclear. To investigate molecular functions of SRPs, we used tobacco transient expression system. Transient expression of SRPs was sufficient and synergistic for LD biogenesis, and SRPs participated in the formation step of LD in tobacco leaves. RESPONSIVE TO DESICCATION 20 (RD20), a known LD-localizing peroxygenase, localized to LD in the presence of an SRP, and its peroxygenase activity correlated with proper localization of RD20 to LD. Our data suggest that Arabidopsis SRPs play roles as positive factors for LD biogenesis to provide a proper localization of LD-localizing proteins in vegetative tissues.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/biossíntese
Arabidopsis/metabolismo
Proteínas de Ligação ao Cálcio/biossíntese
Regulação da Expressão Gênica de Plantas/fisiologia
Proteínas de Choque Térmico/metabolismo
Gotículas Lipídicas/metabolismo
Frações Subcelulares/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Calcium-Binding Proteins); 0 (Heat-Shock Proteins); 0 (RD20 protein, Arabidopsis)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171217
[St] Status:MEDLINE



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