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[PMID]:29028811
[Au] Autor:Fan W; Fan SS; Feng J; Xiao D; Fan S; Luo J
[Ad] Endereço:Department of Neurology, The Third Hospital of Changsha, Changsha, Hunan, China.
[Ti] Título:Elevated expression of HSP10 protein inhibits apoptosis and associates with poor prognosis of astrocytoma.
[So] Source:PLoS One;12(10):e0185563, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Astrocytoma is the most common type of primary malignant brain tumor, with pretty lowly 5-year survival rate in patients. Although extended surgical removal of the tumor and postoperative chemotherapy/radiotherapy executed, still there is large recurrence rate, mainly because diffuse glioma tumor cells ubiquitously infiltrate into normal parenchyma. So it becomes a priority to hunt novel molecular and signaling pathway targets to suppress astrocyma progression. HSP10, an important member of Heat shock proteins (Hsps) family, classically works as molecular chaperone folding or degradating of target proteins. Evolutionarily, HSP10 is also reported to be involved in immunomodulation and tumor progression. Poly (ADP-ribose) polymerase (PARP), important in DNA repair, is one of the main cleavage targets of caspase. And cleaved PARP (c-PARP) can serve as a marker of cells undergoing apoptosis. So far, whether the expression of HSP10 or c-PARP is associated with clinicopathologic implication for astrocytoma has not been reported. Meanwhile, it is unclear about the relationship between HSP10 and cell apoptosis. The purpose of this research is to elucidate the association between the expression of HSP10 and c-PARP and clinicopathological characteristics of astrocytoma by immunohistochemistry. The results showed that positive percentage of high HSP10 expression in astrocytoma 42/103, 40.8%) was significantly higher than that in the non-tumor control brain tissues (8/43, 18.6%) (P = 0.01). While no apparent difference of high c-PARP expression existed between astrocytoma and non-tumor control brain tissues. Furthermore, elevated expression of HSP10 was negative related to low expression of c-PARP (r = -0.224, P = 0.023), indicating high expression of HSP10 in astrocytoma inhibited apoptosis process effectively. And overexpression of HSP10 was proved to be the independent poor prognostic factor for astrocytoma by multivariate analysis. Taken together, our results suggest that elevated expression of HSP10 protein inhibits apoptosis and associates with poor prognosis of astrocytoma.
[Mh] Termos MeSH primário: Apoptose
Astrocitoma/diagnóstico
Astrocitoma/metabolismo
Neoplasias Encefálicas/diagnóstico
Neoplasias Encefálicas/metabolismo
Chaperonina 10/metabolismo
Regulação para Cima
[Mh] Termos MeSH secundário: Adolescente
Adulto
Idoso
Astrocitoma/patologia
Neoplasias Encefálicas/patologia
Criança
Feminino
Seres Humanos
Estimativa de Kaplan-Meier
Masculino
Meia-Idade
Poli(ADP-Ribose) Polimerases/metabolismo
Prognóstico
Proteólise
Estudos Retrospectivos
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chaperonin 10); EC 2.4.2.30 (Poly(ADP-ribose) Polymerases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171014
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185563


  2 / 1203 MEDLINE  
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[PMID]:28662100
[Au] Autor:Pfeiffer D; Roßmanith E; Lang I; Falkenhagen D
[Ad] Endereço:Institute of Cell Biology, Histology and Embryology, Medical University Graz, Graz, Austria.
[Ti] Título:miR-146a, miR-146b, and miR-155 increase expression of IL-6 and IL-8 and support HSP10 in an In vitro sepsis model.
[So] Source:PLoS One;12(6):e0179850, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:microRNAs (miRNAs) play an essential role in inflammation processes including sepsis. This study aimed to identify miRNAs as candidates for therapies that are involved in the innate immune response and to assess their potential functions in the activation of the endothelium. We stimulated THP-1 monocytes with 10 ng/ml LPS for 4 h and used the supernatant for the stimulation of human umbilical vein endothelial cells (HUVEC) or human pulmonary microvascular endothelial cells (HPMEC) for 16 h. miRNA array analysis (of 1,891 miRNAs) identified a 1.5-fold upregulation of miR-146a, miR-146b, and miR-155 in stimulated endothelial cells. HUVEC were transfected with miRNA inhibitors for miR-146a, miR-146b, and miR-155 to investigate the function of these miRNAs in endothelial inflammatory pathways. Inhibition of miR-146a resulted in a diminished release of interleukin (IL)-6 and IL-8 by respective 68% and 55% (P<0.001). Inhibition of miR-146b reduced the expression of IL-6 by 49% (P<0.001). Inhibition of miR-155 reduced the expression of IL-6 and IL-8 by respective 31% (P<0.001) and 14%. The inhibition of miR-146a, miR-146b, and miR-155 reduced the release of HSP10 by 50%, 35%, and 69% (P<0.05), respectively, but did not influence the expression of HSP27 or TXA2. In conclusion, miR-146a, miR-146b, and miR-155 are exerting anti-inflammatory properties by down-regulating IL-6 and IL-8, and influencing the expression of HSP10 in the activated endothelium. We provide evidence for the central role of selected miRNAs in sepsis and their use in the development of small interfering RNA therapeutics to target immune cells and sepsis pathways.
[Mh] Termos MeSH primário: Chaperonina 10/metabolismo
Interleucina-6/metabolismo
Interleucina-8/metabolismo
MicroRNAs/fisiologia
Sepse/metabolismo
[Mh] Termos MeSH secundário: Células Cultivadas
Meios de Cultivo Condicionados
Seres Humanos
Técnicas In Vitro
Sepse/genética
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chaperonin 10); 0 (Culture Media, Conditioned); 0 (Interleukin-6); 0 (Interleukin-8); 0 (MIRN146 microRNA, human); 0 (MIRN155 microRNA, human); 0 (MicroRNAs)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170928
[Lr] Data última revisão:
170928
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170630
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0179850


  3 / 1203 MEDLINE  
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[PMID]:28651912
[Au] Autor:Jacobsen MT; Erickson PW; Kay MS
[Ad] Endereço:Department of Biochemistry, University of Utah School of Medicine, 15 North Medical Drive East, Room 4100, Salt Lake City, UT 84112-5650, United States.
[Ti] Título:Aligator: A computational tool for optimizing total chemical synthesis of large proteins.
[So] Source:Bioorg Med Chem;25(18):4946-4952, 2017 Sep 15.
[Is] ISSN:1464-3391
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The scope of chemical protein synthesis (CPS) continues to expand, driven primarily by advances in chemical ligation tools (e.g., reversible solubilizing groups and novel ligation chemistries). However, the design of an optimal synthesis route can be an arduous and fickle task due to the large number of theoretically possible, and in many cases problematic, synthetic strategies. In this perspective, we highlight recent CPS tool advances and then introduce a new and easy-to-use program, Aligator (Automated Ligator), for analyzing and designing the most efficient strategies for constructing large targets using CPS. As a model set, we selected the E. coli ribosomal proteins and associated factors for computational analysis. Aligator systematically scores and ranks all feasible synthetic strategies for a particular CPS target. The Aligator script methodically evaluates potential peptide segments for a target using a scoring function that includes solubility, ligation site quality, segment lengths, and number of ligations to provide a ranked list of potential synthetic strategies. We demonstrate the utility of Aligator by analyzing three recent CPS projects from our lab: TNFα (157 aa), GroES (97 aa), and DapA (312 aa). As the limits of CPS are extended, we expect that computational tools will play an increasingly important role in the efficient execution of ambitious CPS projects such as production of a mirror-image ribosome.
[Mh] Termos MeSH primário: Biologia Computacional/métodos
Proteínas/síntese química
Software
[Mh] Termos MeSH secundário: Chaperonina 10/síntese química
Chaperonina 10/química
Chaperonina 60/síntese química
Chaperonina 60/química
Escherichia coli/metabolismo
Proteínas/química
Proteínas Ribossômicas/síntese química
Proteínas Ribossômicas/química
Fator de Necrose Tumoral alfa/síntese química
Fator de Necrose Tumoral alfa/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Chaperonin 10); 0 (Chaperonin 60); 0 (Proteins); 0 (Ribosomal Proteins); 0 (Tumor Necrosis Factor-alpha)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171009
[Lr] Data última revisão:
171009
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170628
[St] Status:MEDLINE


  4 / 1203 MEDLINE  
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[PMID]:28396349
[Au] Autor:Illingworth M; Hooppaw AJ; Ruan L; Fisher DJ; Chen L
[Ad] Endereço:Department of Molecular and Cellular Biochemistry, Indiana University, Bloomington, Indiana, USA.
[Ti] Título:Biochemical and Genetic Analysis of the Chlamydia GroEL Chaperonins.
[So] Source:J Bacteriol;199(12), 2017 Jun 15.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Chaperonins are essential for cellular growth under normal and stressful conditions and consequently represent one of the most conserved and ancient protein classes. The paradigm chaperonin, EcGroEL, and its cochaperonin, EcGroES, assist in the folding of proteins via an ATP-dependent mechanism. In addition to the presence of and homologs, paralogs are found in many bacteria, including pathogens, and have evolved poorly understood species-specific functions. spp., which are obligate intracellular bacteria, have reduced genomes that nonetheless contain three genes, ( ), , and We hypothesized that ChGroEL is the bona fide chaperonin and that the paralogs perform novel -specific functions. To test our hypothesis, we investigated the biochemical properties of ChGroEL and its cochaperonin, ChGroES, and queried the essentiality of the three genes through targeted mutagenesis in ChGroEL hydrolyzed ATP at a rate 25% of that of EcGroEL and bound with high affinity to ChGroES, and the ChGroEL-ChGroES complex could refold malate dehydrogenase (MDH). The chlamydial ChGroEL was selective for its cognate cochaperonin, ChGroES, while EcGroEL could function with both EcGroES and ChGroES. A P35T ChGroES mutant (ChGroESP35T) reduced ChGroEL-ChGroES interactions and MDH folding activities but was tolerated by EcGroEL. Both ChGroEL-ChGroES and EcGroEL-ChGroESP35T could complement an EcGroEL-EcGroES mutant. Finally, we successfully inactivated both paralogs but not , leading to minor growth defects in cell culture that were not exacerbated by heat stress. Collectively, our results support novel functions for the paralogs and solidify ChGroEL as a bona fide chaperonin that is biochemically distinct from EcGroEL. is an important cause of human diseases, including pneumonia, sexually transmitted infections, and trachoma. The chlamydial chaperonin ChGroEL and chaperonin paralog ChGroEL2 have been associated with survival under stress conditions, and ChGroEL is linked with immunopathology elicited by chlamydial infections. However, their exact roles in bacterial survival and disease remain unclear. Our results further substantiate the hypotheses that ChGroEL is the primary chlamydial chaperonin and that the paralogs play specialized roles during infection. Furthermore, ChGroEL and the mitochondrial GroEL only functioned with their cochaperonin, in contrast to the promiscuous nature of GroEL from and , which might indicate a divergent evolution of GroEL during the transition from a free-living organism to an obligate intracellular lifestyle.
[Mh] Termos MeSH primário: Chaperonina 10/genética
Chaperonina 10/metabolismo
Chaperonina 60/genética
Chaperonina 60/metabolismo
Chlamydia trachomatis/genética
Chlamydia trachomatis/metabolismo
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Técnicas de Inativação de Genes
Genes Essenciais
Hidrólise
Malato Desidrogenase/metabolismo
Ligação Proteica
Dobramento de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chaperonin 10); 0 (Chaperonin 60); 8L70Q75FXE (Adenosine Triphosphate); EC 1.1.1.37 (Malate Dehydrogenase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171126
[Lr] Data última revisão:
171126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170412
[St] Status:MEDLINE


  5 / 1203 MEDLINE  
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[PMID]:28011268
[Au] Autor:Yamamoto S; Okamoto T; Ogasawara N; Hashimoto S; Shiraishi T; Sato T; Yamamoto K; Tsutsumi H; Takano K; Himi T; Itoh H; Yokota SI
[Ad] Endereço:Department of Microbiology, Sapporo Medical University School of Medicine, Sapporo, Japan.
[Ti] Título:NIP-SNAP-1 and -2 mitochondrial proteins are maintained by heat shock protein 60.
[So] Source:Biochem Biophys Res Commun;483(3):917-922, 2017 Feb 12.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:NIP-SNAP-1 and -2 are ubiquitous proteins thought to be associated with maintenance of mitochondrial function, neuronal transmission, and autophagy. However, their physiological functions remain largely unknown. To elucidate their functional importance, we screened for proteins that interact with NIP-SNAP-1 and -2, resulting in identification of HSP60 and P62/SQSTM1 as binding proteins. NIP-SNAP-1 and -2 localized in the mitochondrial inner membrane space, whereas HSP60 localized in the matrix. Native gel electrophoresis and filter trap assays revealed that human HSP60 prevented aggregation of newly synthesized NIP-SNAP-2 in an in vitro translation system. Moreover, expression levels of NIP-SNAP-1 and -2 in cells were decreased by knockdown of HSP60, but not HSP10. These findings indicate that HSP60 promotes folding and maintains the stability of NIP-SNAP-1 and -2.
[Mh] Termos MeSH primário: Chaperonina 60/metabolismo
Proteínas de Membrana/metabolismo
Proteínas Mitocondriais/metabolismo
Fosfoproteínas/metabolismo
Proteínas/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular
Chaperonina 10/antagonistas & inibidores
Chaperonina 10/genética
Chaperonina 10/metabolismo
Chaperonina 60/antagonistas & inibidores
Chaperonina 60/genética
Técnicas de Silenciamento de Genes
Seres Humanos
Proteínas de Membrana/química
Proteínas de Membrana/genética
Membranas Mitocondriais/metabolismo
Proteínas Mitocondriais/antagonistas & inibidores
Proteínas Mitocondriais/química
Proteínas Mitocondriais/genética
Fosfoproteínas/química
Fosfoproteínas/genética
Ligação Proteica
Dobramento de Proteína
Mapas de Interação de Proteínas
Estabilidade Proteica
Proteínas/química
Proteínas/genética
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Proteína Sequestossoma-1/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chaperonin 10); 0 (Chaperonin 60); 0 (GBAS protein, human); 0 (HSPD1 protein, human); 0 (Membrane Proteins); 0 (Mitochondrial Proteins); 0 (NIPSNAP1 protein, human); 0 (Phosphoproteins); 0 (Proteins); 0 (Recombinant Proteins); 0 (SQSTM1 protein, human); 0 (Sequestosome-1 Protein)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170606
[Lr] Data última revisão:
170606
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161225
[St] Status:MEDLINE


  6 / 1203 MEDLINE  
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[PMID]:27993580
[Au] Autor:Chu S; Wen Q; Qing Z; Luo J; Wang W; Chen L; Feng J; Xu L; Zang H; Fan S
[Ad] Endereço:Department of Pathology, The Second Xiangya Hospital, Central South University, Changsha, Hunan 410011, China.
[Ti] Título:High expression of heat shock protein 10 correlates negatively with estrogen/progesterone receptor status and predicts poor prognosis in invasive ductal breast carcinoma.
[So] Source:Hum Pathol;61:173-180, 2017 Mar.
[Is] ISSN:1532-8392
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Heat shock proteins (HSPs) usually are associated with stress response and tolerance. HSP10 is a co-chaperone for HSP60, which is involved in the mitochondrial protein-folding machinery. To the best of our knowledge, the expression of HSP10 in invasive ductal breast carcinoma (IDBC) has never been reported. In the present study, HSP10 expression in 242 cases of IDBC and 46 cases of noncancerous breast tissues was detected by immunohistochemistry staining. High expression was significantly more common in IDBC than in noncancerous breast tissues (P<.001). Also, high expression was significantly more common in poorly differentiated than in well- and moderately differentiated IDBC (P=.023). Furthermore, high expression correlated negatively with estrogen receptor and progesterone receptor expression (P=.031 and P=.042, respectively). The most interesting result of the study was that high expression of HSP10 was significantly associated with shorter overall survival by both univariate and multivariate analyses (P=.013 and P=.036, respectively). In conclusion, we report for the first time that high expression of HSP10 is negatively associated with estrogen receptor/progesterone receptor status and might be a novel independent biomarker for poor prognosis in IDBC.
[Mh] Termos MeSH primário: Biomarcadores Tumorais/análise
Neoplasias da Mama/química
Carcinoma Ductal de Mama/química
Chaperonina 10/análise
Receptores Estrogênicos/análise
Receptores de Progesterona/análise
[Mh] Termos MeSH secundário: Biópsia
Neoplasias da Mama/mortalidade
Neoplasias da Mama/patologia
Neoplasias da Mama/terapia
Carcinoma Ductal de Mama/mortalidade
Carcinoma Ductal de Mama/patologia
Carcinoma Ductal de Mama/terapia
Diferenciação Celular
Distribuição de Qui-Quadrado
Intervalo Livre de Doença
Feminino
Seres Humanos
Imuno-Histoquímica
Estimativa de Kaplan-Meier
Meia-Idade
Análise Multivariada
Invasividade Neoplásica
Modelos de Riscos Proporcionais
Fatores de Risco
Fatores de Tempo
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (Chaperonin 10); 0 (Receptors, Estrogen); 0 (Receptors, Progesterone)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170828
[Lr] Data última revisão:
170828
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161221
[St] Status:MEDLINE


  7 / 1203 MEDLINE  
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[PMID]:27860532
[Au] Autor:Hammerstad SS; Stefan M; Blackard J; Owen RP; Lee HJ; Concepcion E; Yi Z; Zhang W; Tomer Y
[Ad] Endereço:Department of Endocrinology, Morbid Obesity and Preventive Medicine, Oslo University Hospital, Aker, 0586 Oslo, Norway.
[Ti] Título:Hepatitis C Virus E2 Protein Induces Upregulation of IL-8 Pathways and Production of Heat Shock Proteins in Human Thyroid Cells.
[So] Source:J Clin Endocrinol Metab;102(2):689-697, 2017 Feb 01.
[Is] ISSN:1945-7197
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Context: Thyroiditis is one of the most common extrahepatic manifestations of hepatitis C virus (HCV) infection. By binding to surface cell receptor CD81, HCV envelope glycoprotein E2 mediates entry of HCV into cells. Studies have shown that different viral proteins may individually induce host responses to infection. We hypothesized that HCV E2 protein binding to CD81 expressed on thyroid cells activates a cascade of inflammatory responses that can trigger autoimmune thyroiditis in susceptible individuals. Setting: Human thyroid cell lines ML-1 and human thyrocytes in primary cell culture were treated with HCV recombinant E2 protein. The expression of major proinflammatory cytokines was measured at the messenger RNA and protein levels. Next-generation transcriptome analysis was used to identify early changes in gene expression in thyroid cells induced by E2. Results: HCV envelope protein E2 induced strong inflammatory responses in human thyrocytes, resulting in production of interleukin (IL)-8, IL-6, and tumor necrosis factor-α. Furthermore, the E2 protein induced production of several heat shock proteins including HSP60, HSP70p12A, and HSP10, in human primary thyrocytes. In thyroid cell line ML-1, RNA sequencing identified upregulation of molecules involved in innate immune pathways with high levels of proinflammatory cytokines and chemokines and increased expression of costimulatory molecules, specifically CD40, known to be a major thyroid autoimmunity gene. Conclusion: Our data support a key role for HCV envelope protein E2 in triggering thyroid autoimmunity through activation of cytokine pathways by bystander mechanisms.
[Mh] Termos MeSH primário: Autoimunidade/imunologia
Perfilação da Expressão Gênica/métodos
Proteínas de Choque Térmico/metabolismo
Interleucina-8/metabolismo
Células Epiteliais da Tireóide/imunologia
Proteínas do Envelope Viral/imunologia
[Mh] Termos MeSH secundário: Linhagem Celular
Células Cultivadas
Chaperonina 10/metabolismo
Chaperonina 60/metabolismo
Expressão Gênica
Proteínas de Choque Térmico HSP70/metabolismo
Seres Humanos
Interleucina-6/metabolismo
Células Epiteliais da Tireóide/metabolismo
Fator de Necrose Tumoral alfa/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chaperonin 10); 0 (Chaperonin 60); 0 (HSP70 Heat-Shock Proteins); 0 (Heat-Shock Proteins); 0 (IL6 protein, human); 0 (IL8 protein, human); 0 (Interleukin-6); 0 (Interleukin-8); 0 (Tumor Necrosis Factor-alpha); 0 (Viral Envelope Proteins); 157184-61-7 (glycoprotein E2, Hepatitis C virus)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170719
[Lr] Data última revisão:
170719
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:161119
[St] Status:MEDLINE
[do] DOI:10.1210/jc.2016-3403


  8 / 1203 MEDLINE  
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[PMID]:27539923
[Au] Autor:Kameda H; Usugi S; Kobayashi M; Fukui N; Lee S; Hongo K; Mizobata T; Sekiguchi Y; Masaki Y; Kobayashi A; Oroguchi T; Nakasako M; Takayama Y; Yamamoto M; Kawata Y
[Ad] Endereço:Department of Chemistry and Biotechnology, Graduate School of Engineering, and Department of Biomedical Science, Institute of Regenerative Medicine and Biofunction, Graduate School of Medical Science, Tottori University, Koyama-Minami, Tottori 680-8552, Japan.
[Ti] Título:Common structural features of toxic intermediates from α-synuclein and GroES fibrillogenesis detected using cryogenic coherent X-ray diffraction imaging.
[So] Source:J Biochem;161(1):55-65, 2017 Jan.
[Is] ISSN:1756-2651
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The aggregation and deposition of α-synuclein (αSyn) in neuronal cells is correlated to pathogenesis of Parkinson's disease. Although the mechanism of αSyn aggregation and fibril formation has been studied extensively, the structural hallmarks that are directly responsible for toxicity toward cells are still under debate. Here, we have compared the structural characteristics of the toxic intermediate molecular species of αSyn and similar toxic species of another protein, GroES, using coherent X-ray diffraction analysis. Using coherent X-ray free electron laser pulses of SACLA, we analysed αSyn and GroES fibril intermediate species and characterized various aggregate structures. Unlike previous studies where an annular oligomeric form of αSyn was identified, particle reconstruction from scattering traces suggested that the specific forms of the toxic particles were varied, with the sizes of the particles falling within a specific range. We did however discover a common structural feature in both αSyn and GroES samples; the edges of the detected particles were nearly parallel and produced a characteristic diffraction pattern in the diffraction experiments. The presence of parallel-edged particles in toxic intermediates of αSyn and GroES fibrillogenesis pointed towards a plausible common molecular interface that leads to the formation of mature fibrils.
[Mh] Termos MeSH primário: Chaperonina 10/química
Agregados Proteicos
Agregação Patológica de Proteínas
alfa-Sinucleína/química
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Chaperonina 10/farmacologia
Seres Humanos
Camundongos
Doença de Parkinson/metabolismo
Difração de Raios X
alfa-Sinucleína/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chaperonin 10); 0 (Protein Aggregates); 0 (alpha-Synuclein)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170130
[Lr] Data última revisão:
170130
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160820
[St] Status:MEDLINE
[do] DOI:10.1093/jb/mvw052


  9 / 1203 MEDLINE  
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[PMID]:28275270
[Au] Autor:Rajtar-Ciosek A; Wyroba J; Kacalska-Jansen O; Zmaczynski A; Figula J; Babczyk D; Jach R
[Ad] Endereço:Clinic of Gynecological Endocrynology, Jagiellonian University Medical College, Kraków, Poland.
[Ti] Título:Markers of implantation in ectopic and high-risk early eutopic pregnancies.
[So] Source:Folia Med Cracov;56(3):41-50, 2016.
[Is] ISSN:0015-5616
[Cp] País de publicação:Poland
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION: This study focused on the assessment of HSP-10, HSP-27 and PSG-11 which are one of the first detectable serum pregnancy proteins. Contrary to ultrasound imaging, biochemical methods allow to clarify the pathogenesis and pathomechanism of high-risk pregnancies, fetal anomalies, and abnormal fetal implantation. Early serum concentration estimation of HSP-10, HSP-27 and PSG-11 may be very useful not only in prognosis of pregnancies of unknown localization (PUL), but also as markers of ectopic pregnancies. OBJECTIVES: The aim of the study was to evaluate the expression of HSP-10, HSP-27, PSG-11 implantation proteins in ectopic and eutopic pregnancies, and their mutual correlations. PATIENTS AND METHODS: The study involved 42 healthy women who were hospitalized, due to symptoms of imminent miscarriage, risk of spontaneous abortion, or the diagnosis of an ectopic pregnancy. The subjects were subdivided into two equal groups of 21 women who consented to participate in this clinical trial. Biochemical assays were performed involving PSG-11, HSP-27, and HSP-10 serum concentration. RESULTS: Serum concentration levels of HSP-10, HSP-27, and PSG-11 were significantly higher in pregnancies at risk of spontaneous abortion as compared to ectopic pregnancies. CONCLUSIONS: The results of the study indicate high value of PSG-11, HSP-27 and HSP-10 serum concentrations as predictors of correct implantation site. This may be very useful in prognosis of pregnancies of unknown localization (PUL) and early conservative/surgical ectopic pregnancies treatment if necessary to preserve maximum fertility.
[Mh] Termos MeSH primário: Chaperonina 10/sangue
Glicoproteínas/sangue
Proteínas de Choque Térmico HSP27/sangue
Primeiro Trimestre da Gravidez/sangue
Gravidez Ectópica/diagnóstico
[Mh] Termos MeSH secundário: Biomarcadores/sangue
Feminino
Seres Humanos
Gravidez
Glicoproteínas beta 1 Específicas da Gravidez
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Chaperonin 10); 0 (Glycoproteins); 0 (HSP27 Heat-Shock Proteins); 0 (Pregnancy-Specific beta 1-Glycoproteins); 0 (pregnancy-specific beta-1-glycoprotein 12)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170706
[Lr] Data última revisão:
170706
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170310
[St] Status:MEDLINE


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[PMID]:27874025
[Au] Autor:Alsultan AM; Chin DY; Howard CB; de Bakker CJ; Jones ML; Mahler SM
[Ad] Endereço:Australian Institute for Bioengineering and Nanotechnology (AIBN), University of Queensland (UQ), Brisbane, QLD 4072, Australia.
[Ti] Título:Beyond Antibodies: Development of a Novel Protein Scaffold Based on Human Chaperonin 10.
[So] Source:Sci Rep;5:37348, 2016 11 22.
[Is] ISSN:2045-2322
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Human Chaperonin 10 (hCpn10) was utilised as a novel scaffold for presenting peptides of therapeutic and diagnostic significance. Molecular dynamic simulations and protein sizing analyses identified a peptide linker (P1) optimal for the formation of the quarternary hCpn10 heptamer structure. hCpn10 scaffold displaying peptides targeting Factor VIIa (CE76 ) and CD44 (CP7) were expressed in E. coli. Functional studies of CE76 indicated nanomolar affinity for Factor VIIa (3 nM) similar to the E-76 peptide (6 nM), with undetectable binding to Factor X. CE76 was a potent inhibitor of FX activity (via inhibition of Factor VIIa) and prolonged clot formation 4 times longer than achieved by E-76 peptide as determined by prothrombin time (PT) assays. This improvement in clotting function by CE76 , highlights the advantages of a heptamer-based scaffold for improving avidity by multiple peptide presentation. In another example of hCPn10 utility as a scaffold, CP7 bound to native CD44 overexpressed on cancer cells and bound rCD44 with high affinity (K 9.6 nM). The ability to present various peptides through substitution of the hCpn10 mobile loop demonstrates its utility as a novel protein scaffold.
[Mh] Termos MeSH primário: Chaperonina 10/química
Fator VIIa/farmacologia
Receptores de Hialuronatos/metabolismo
Peptídeos/química
Peptídeos/farmacologia
Proteínas da Gravidez/química
Fatores Supressores Imunológicos/química
[Mh] Termos MeSH secundário: Sítios de Ligação
Coagulação Sanguínea/efeitos dos fármacos
Seres Humanos
Modelos Moleculares
Simulação de Dinâmica Molecular
Biblioteca de Peptídeos
Ligação Proteica
Estrutura Quaternária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CD44 protein, human); 0 (Chaperonin 10); 0 (Hyaluronan Receptors); 0 (Peptide Library); 0 (Peptides); 0 (Pregnancy Proteins); 0 (Suppressor Factors, Immunologic); 0 (early pregnancy factor); EC 3.4.21.21 (Factor VIIa)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161123
[St] Status:MEDLINE
[do] DOI:10.1038/srep37348



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