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[PMID]:28453954
[Au] Autor:Pakulska MM; Tator CH; Shoichet MS
[Ad] Endereço:Department of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, ON, M5S 3E5, Canada; Institute for Biomaterials and Biomedical Engineering, University of Toronto, Toronto, ON, M5S 3G9, Canada.
[Ti] Título:Local delivery of chondroitinase ABC with or without stromal cell-derived factor 1α promotes functional repair in the injured rat spinal cord.
[So] Source:Biomaterials;134:13-21, 2017 Jul.
[Is] ISSN:1878-5905
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Traumatic spinal cord injury (SCI) is a devastating event for which functional recovery remains elusive. Due to the complex nature of SCI pathology, a combination treatment strategy will likely be required for success. We hypothesized that tissue and functional repair would be achieved in a rat model of impact-compression SCI by combining degradation of the glial scar, using chondroitinase ABC (ChABC), with recruitment of endogenous neural precursor cells (NPCs), using stromal cell-derived factor 1α (SDF). To test this hypothesis, we designed a crosslinked methylcellulose hydrogel (XMC) for minimally invasive, localized, and sustained intrathecal drug delivery. ChABC was released from XMC using protein-peptide affinity interactions while SDF was delivered by electrostatic affinity interactions from polymeric nanoparticles embedded in XMC. Rats with SCI were treated acutely with a combination of SDF and ChABC, SDF alone, ChABC alone, or vehicle alone, and compared to injury only. Treatment with ChABC, both alone and in combination with SDF, resulted in faster and more sustained behavioural improvement over time than other groups. The significantly reduced chondroitin sulfate proteoglycan levels and greater distribution of NPCs throughout the spinal cord tissue with ChABC delivery, both alone and in combination with SDF, may explain the improved locomotor function. Treatment with SDF alone had no apparent effect on NPC number or distribution nor synergistic effect with ChABC delivery. Thus, in this model of SCI, tissue and functional repair is attributed to ChABC.
[Mh] Termos MeSH primário: Quimiocina CXCL12/química
Condroitina ABC Liase/metabolismo
Traumatismos da Medula Espinal/metabolismo
[Mh] Termos MeSH secundário: Animais
Quimiocina CXCL12/metabolismo
Quimiocina CXCL12/uso terapêutico
Condroitina ABC Liase/química
Proteoglicanas de Sulfatos de Condroitina/química
Ensaio de Imunoadsorção Enzimática
Feminino
Hidrogel de Polietilenoglicol-Dimetacrilato/química
Imuno-Histoquímica
Metilcelulose/química
Células-Tronco Neurais/citologia
Células-Tronco Neurais/efeitos dos fármacos
Ratos
Ratos Sprague-Dawley
Traumatismos da Medula Espinal/tratamento farmacológico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chemokine CXCL12); 0 (Chondroitin Sulfate Proteoglycans); 25852-47-5 (Hydrogel, Polyethylene Glycol Dimethacrylate); 9004-67-5 (Methylcellulose); EC 4.2.2.20 (Chondroitin ABC Lyase)
[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:170429
[St] Status:MEDLINE


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[PMID]:29228020
[Au] Autor:Carwardine D; Prager J; Neeves J; Muir EM; Uney J; Granger N; Wong LF
[Ad] Endereço:School of Veterinary Sciences, University of Bristol, Bristol, United Kingdom.
[Ti] Título:Transplantation of canine olfactory ensheathing cells producing chondroitinase ABC promotes chondroitin sulphate proteoglycan digestion and axonal sprouting following spinal cord injury.
[So] Source:PLoS One;12(12):e0188967, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Olfactory ensheathing cell (OEC) transplantation is a promising strategy for treating spinal cord injury (SCI), as has been demonstrated in experimental SCI models and naturally occurring SCI in dogs. However, the presence of chondroitin sulphate proteoglycans within the extracellular matrix of the glial scar can inhibit efficient axonal repair and limit the therapeutic potential of OECs. Here we have used lentiviral vectors to genetically modify canine OECs to continuously deliver mammalian chondroitinase ABC at the lesion site in order to degrade the inhibitory chondroitin sulphate proteoglycans in a rodent model of spinal cord injury. We demonstrate that these chondroitinase producing canine OECs survived at 4 weeks following transplantation into the spinal cord lesion and effectively digested chondroitin sulphate proteoglycans at the site of injury. There was evidence of sprouting within the corticospinal tract rostral to the lesion and an increase in the number of corticospinal axons caudal to the lesion, suggestive of axonal regeneration. Our results indicate that delivery of the chondroitinase enzyme can be achieved with the genetically modified OECs to increase axon growth following SCI. The combination of these two promising approaches is a potential strategy for promoting neural regeneration following SCI in veterinary practice and human patients.
[Mh] Termos MeSH primário: Axônios
Condroitina ABC Liase/biossíntese
Proteoglicanas de Sulfatos de Condroitina/metabolismo
Doenças do Cão/metabolismo
Mucosa Olfatória/transplante
Traumatismos da Medula Espinal/veterinária
[Mh] Termos MeSH secundário: Animais
Doenças do Cão/patologia
Cães
Mucosa Olfatória/citologia
Mucosa Olfatória/metabolismo
Traumatismos da Medula Espinal/metabolismo
Traumatismos da Medula Espinal/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chondroitin Sulfate Proteoglycans); EC 4.2.2.20 (Chondroitin ABC Lyase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180104
[Lr] Data última revisão:
180104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171212
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188967


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[PMID]:29216327
[Au] Autor:Kuboyama K; Tanga N; Suzuki R; Fujikawa A; Noda M
[Ad] Endereço:Division of Molecular Neurobiology, National Institute for Basic Biology (NIBB), Okazaki, Aichi, Japan.
[Ti] Título:Protamine neutralizes chondroitin sulfate proteoglycan-mediated inhibition of oligodendrocyte differentiation.
[So] Source:PLoS One;12(12):e0189164, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Chondroitin sulfate proteoglycans (CSPGs), which are enriched in demyelinating plaques in neurodegenerative diseases, such as multiple sclerosis (MS), impair remyelination by inhibiting the migration and differentiation of oligodendrocyte precursor cells (OPCs) in the central nervous system (CNS). We herein show that protamine (PRM, also known as a heparin antagonist) effectively neutralizes the inhibitory activities of CSPGs, thereby enhancing OPC differentiation and (re)myelination in mice. Cell-based assays using mouse OPC-like OL1 cells revealed that the PRM treatment exerted masking effects on extracellular CSPGs and improved oligodendrocyte differentiation on inhibitory CSPG-coated substrates. PRM also bound to the extracellular region of protein tyrosine phosphatase receptor type Z (PTPRZ), a membrane-spanning CSPG predominantly expressed in OPCs, and functioned as a ligand mimetic of PTPRZ, thereby suppressing its negative regulatory activity on oligodendrocyte differentiation. In primary cultures, the differentiation of OPCs from wild-type and Ptprz-deficient mice was equally enhanced by PRM. Moreover, the intranasal administration of PRM accelerated myelination in the developing mouse brain, and its intracerebroventricular administration stimulated remyelination after cuprizone-induced demyelination. These results indicate that PRM has CSPG-neutralizing activity which promotes oligodendrocyte differentiation under developmental and morbid conditions.
[Mh] Termos MeSH primário: Diferenciação Celular/efeitos dos fármacos
Proteoglicanas de Sulfatos de Condroitina/metabolismo
Oligodendroglia/citologia
Protaminas/farmacologia
[Mh] Termos MeSH secundário: Animais
Encéfalo/citologia
Encéfalo/efeitos dos fármacos
Camundongos
Bainha de Mielina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chondroitin Sulfate Proteoglycans); 0 (Protamines)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171226
[Lr] Data última revisão:
171226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171208
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189164


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[PMID]:28945172
[Au] Autor:Tsidulko AY; Kazanskaya GM; Kostromskaya DV; Aidagulova SV; Kiselev RS; Volkov AM; Kobozev VV; Gaitan AS; Krivoshapkin AL; Grigorieva EV
[Ad] Endereço:1 Institute of Molecular Biology and Biophysics, Novosibirsk, Russia.
[Ti] Título:Prognostic relevance of NG2/CSPG4, CD44 and Ki-67 in patients with glioblastoma.
[So] Source:Tumour Biol;39(9):1010428317724282, 2017 Sep.
[Is] ISSN:1423-0380
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Neuron-glial antigen 2 (NG2, also known as CSPG4) and hyaluronic acid receptor CD44 are chondroitin sulphate proteoglycans actively involved in brain development and its malignant transformation. Here, we aimed to compare prognostic significances of NG2, CD44 and Ki-67 expression in glioblastoma multiforme patients. Totally, 45 tissue samples and 83 paraffin-embedded tissues for 75 patients were analysed. The prognostic values of the genes were analysed using Kaplan-Meier survival curves. Grade III gliomas showed 2-fold difference in NG2 expression between anaplastic astrocytoma and oligoastrocytoma (10.1 ± 3.5 and 25.5 ± 14.5, respectively). For grade IV gliomas, upregulated NG2 expression (21.0 ± 6.8) was associated with poor glioblastoma multiforme prognosis (overall survival < 12 months) compared with glioblastoma multiforme patients with good prognosis (4.4 ± 3.2; overall survival > 12 months). Multivariate survival analysis using Cox proportional hazards model confirmed that high NG2 expression was associated with low survival of the patients (hazard ratio: 3.43; 95% confidence interval: 1.18-9.93; p = 0.02), whereas age (hazard ratio: 1.02; 95% confidence interval: 0.96-1.09; p = 0.42), tumour resection (hazard ratio: 1.03; 95% confidence interval: 0.98-1.08; p = 0.25) and sex (hazard ratio: 0.62; 95% confidence interval: 0.21-1.86; p = 0.40) did not show significant association with prognosis. Although the positive correlation was shown for NG2 and CD44 expression in the glioblastomas (Pearson coefficient = 0.954), Kaplan-Meier and multivariate survival analyses did not revealed a significant association of the increased CD44 expression (hazard ratio: 2.18; 95% confidence interval: 0.50-9.43; p = 0.30) or high Ki-67 proliferation index (hazard ratio: 1.10; 95% confidence interval: 1.02-1.20; p = 0.02) with the disease prognosis. The results suggest that upregulation of NG2/CSPG4 rather than changes in CD44 or Ki-67 expression is associated with low overall survival in glioblastoma multiforme patients, supporting NG2/CSPG4 as a potential prognostic marker in glioblastoma.
[Mh] Termos MeSH primário: Biomarcadores Tumorais/análise
Neoplasias Encefálicas/patologia
Proteoglicanas de Sulfatos de Condroitina/biossíntese
Glioblastoma/patologia
Receptores de Hialuronatos/biossíntese
Antígeno Ki-67/biossíntese
Proteínas de Membrana/biossíntese
[Mh] Termos MeSH secundário: Adolescente
Adulto
Idoso
Neoplasias Encefálicas/metabolismo
Neoplasias Encefálicas/mortalidade
Proteoglicanas de Sulfatos de Condroitina/análise
Feminino
Glioblastoma/metabolismo
Glioblastoma/mortalidade
Seres Humanos
Receptores de Hialuronatos/análise
Imuno-Histoquímica
Estimativa de Kaplan-Meier
Antígeno Ki-67/análise
Masculino
Proteínas de Membrana/análise
Meia-Idade
Reação em Cadeia da Polimerase
Prognóstico
Modelos de Riscos Proporcionais
Regulação para Cima
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (CD44 protein, human); 0 (CSPG4 protein, human); 0 (Chondroitin Sulfate Proteoglycans); 0 (Hyaluronan Receptors); 0 (Ki-67 Antigen); 0 (Membrane Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170926
[St] Status:MEDLINE
[do] DOI:10.1177/1010428317724282


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[PMID]:28842504
[Au] Autor:Gupta P; Zhang Z; Sugiman-Marangos SN; Tam J; Raman S; Julien JP; Kroh HK; Lacy DB; Murgolo N; Bekkari K; Therien AG; Hernandez LD; Melnyk RA
[Ad] Endereço:From Merck & Co., Inc., Kenilworth, New Jersey 07033.
[Ti] Título:Functional defects in TcdB toxin uptake identify CSPG4 receptor-binding determinants.
[So] Source:J Biol Chem;292(42):17290-17301, 2017 Oct 20.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:is a major nosocomial pathogen that produces two exotoxins, TcdA and TcdB, with TcdB thought to be the primary determinant in human disease. TcdA and TcdB are large, multidomain proteins, each harboring a cytotoxic glucosyltransferase domain that is delivered into the cytosol from endosomes via a translocation domain after receptor-mediated endocytosis of toxins from the cell surface. Although there are currently no known host cell receptors for TcdA, three cell-surface receptors for TcdB have been identified: CSPG4, NECTIN3, and FZD1/2/7. The sites on TcdB that mediate binding to each receptor are not defined. Furthermore, it is not known whether the combined repetitive oligopeptide (CROP) domain is involved in or required for receptor binding. Here, in a screen designed to identify sites in TcdB that are essential for target cell intoxication, we identified a region at the junction of the translocation and the CROP domains that is implicated in CSPG4 binding. Using a series of C-terminal truncations, we show that the CSPG4-binding site on TcdB extends into the CROP domain, requiring three short repeats for binding and for full toxicity on CSPG4-expressing cells. Consistent with the location of the CSPG4-binding site on TcdB, we show that the anti-TcdB antibody bezlotoxumab, which binds partially within the first three short repeats, prevents CSPG4 binding to TcdB. In addition to establishing the binding region for CSPG4, this work ascribes for the first time a role in TcdB CROPs in receptor binding and further clarifies the relative roles of host receptors in TcdB pathogenesis.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Toxinas Bacterianas/metabolismo
Proteoglicanas de Sulfatos de Condroitina/metabolismo
Clostridium difficile/enzimologia
Glucosiltransferases/metabolismo
Proteínas de Membrana/metabolismo
[Mh] Termos MeSH secundário: Animais
Anticorpos Monoclonais/química
Anticorpos Neutralizantes/química
Proteínas de Bactérias/antagonistas & inibidores
Proteínas de Bactérias/genética
Toxinas Bacterianas/antagonistas & inibidores
Toxinas Bacterianas/genética
Células CHO
Células CACO-2
Cercopithecus aethiops
Proteoglicanas de Sulfatos de Condroitina/genética
Clostridium difficile/genética
Clostridium difficile/patogenicidade
Cricetinae
Cricetulus
Glucosiltransferases/antagonistas & inibidores
Glucosiltransferases/genética
Células HEK293
Seres Humanos
Proteínas de Membrana/genética
Ligação Proteica
Domínios Proteicos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Antibodies, Neutralizing); 0 (Bacterial Proteins); 0 (Bacterial Toxins); 0 (CSPG4 protein, human); 0 (Chondroitin Sulfate Proteoglycans); 0 (Membrane Proteins); 0 (bezlotoxumab); 0 (toxB protein, Clostridium difficile); EC 2.4.1.- (Glucosyltransferases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170827
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.806687


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[PMID]:28594920
[Au] Autor:Dold L; Luda C; Schwarze-Zander C; Boesecke C; Hansel C; Nischalke HD; Lutz P; Mohr R; Wasmuth JC; Strassburg CP; Trebicka J; Rockstroh JK; Spengler U
[Ad] Endereço:Department of Internal Medicine I, Rheinische Friedrich-Wilhelms University Bonn, Bonn, Germany.
[Ti] Título:Genetic polymorphisms associated with fatty liver disease and fibrosis in HIV positive patients receiving combined antiretroviral therapy (cART).
[So] Source:PLoS One;12(6):e0178685, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hepatic steatosis can occur with any antiretroviral therapy (cART). Although single nucleotide polymorphisms (SNPs) have been identified to predispose to alcoholic and non-alcoholic fatty liver disease, their role for treatment-associated steatosis in HIV-positive patients remains unclear. We determined the frequency of PNPLA3 (rs738409), CSPG3/NCAN (rs2228603), GCKR (rs780094), PPP1R3B (rs4240624), TM6SF (rs8542926), LYPLAL1 (rs12137855) and MBOAT7 (rs626283) by RT-PCR in 117 HIV-positive patients on cART and stratified participants based on their "controlled attenuation parameter" (CAP) into probable (CAP: 215-300 dB/m) and definite (CAP >300 dB/m) hepatic steatosis. We analyzed CAP values and routine metabolic parameters according to the allele frequencies. Sixty-five (55.6%) and 13 (11.1%) patients were allocated to probable and definite steatosis. CAP values (p = 0.012) and serum triglycerides (p = 0.043) were increased in carriers of the GCKR (rs780094) A allele. Cox logistic regression identified triglycerides (p = 0.006), bilirubin (p = 0.021) and BMI (p = 0.068), but not the genetic parameters as risk factors for the occurrence of hepatic steatosis. Taken together, according to the limited sample size, this exploratory study generates the hypothesis that genetic polymorphisms seem to exert minor effects on the risk for fatty liver disease in HIV-positive patients on cART. Nevertheless, SNPs may modify metabolic complications once metabolic abnormalities have developed. Hence, subsequent analysis of a larger cohort is needed.
[Mh] Termos MeSH primário: Fígado Gorduroso/genética
Cirrose Hepática/genética
[Mh] Termos MeSH secundário: Aciltransferases/genética
Proteínas Adaptadoras de Transdução de Sinal/genética
Adulto
Idoso
Idoso de 80 Anos ou mais
Antirretrovirais/uso terapêutico
Bilirrubina/sangue
Índice de Massa Corporal
Proteoglicanas de Sulfatos de Condroitina/genética
Feminino
Predisposição Genética para Doença/genética
Soropositividade para HIV/tratamento farmacológico
Soropositividade para HIV/genética
Seres Humanos
Lipase/genética
Lisofosfolipase/genética
Masculino
Proteínas de Membrana/genética
Meia-Idade
Polimorfismo de Nucleotídeo Único/genética
Modelos de Riscos Proporcionais
Proteína Fosfatase 1/genética
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Triglicerídeos/sangue
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Anti-Retroviral Agents); 0 (CSPG4 protein, human); 0 (Chondroitin Sulfate Proteoglycans); 0 (GCKR protein, human); 0 (Membrane Proteins); 0 (Triglycerides); EC 2.3.- (Acyltransferases); EC 2.3.- (MBOAT7 protein, human); EC 3.1.1.3 (Lipase); EC 3.1.1.3 (adiponutrin, human); EC 3.1.1.5 (Lysophospholipase); EC 3.1.2.- (LYPLAL1 protein, human); EC 3.1.3.16 (PPP1R3B protein, human); EC 3.1.3.16 (Protein Phosphatase 1); RFM9X3LJ49 (Bilirubin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170919
[Lr] Data última revisão:
170919
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170609
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0178685


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[PMID]:28569157
[Au] Autor:Srisuthtayanont W; Pruksakorn D; Kongtawelert P; Pothacharoen P
[Ad] Endereço:Department of Biochemistry, Thailand Excellence Center for Tissue Engineering and Stem Cells, Faculty of Medicine, Chiang Mai University, 110 Intavaroros Road, Sripoom, Muang, Chiang Mai, 50200, Thailand.
[Ti] Título:Effects of sesamin on chondroitin sulfate proteoglycan synthesis induced by interleukin-1beta in human chondrocytes.
[So] Source:BMC Complement Altern Med;17(1):286, 2017 May 31.
[Is] ISSN:1472-6882
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Numerous studies have reported on the health benefits of sesamin, a major lignin found in sesame (S. indicum) seeds. Recently, sesamin was shown to have the ability to promote chondroitin sulfate proteoglycan synthesis in normal human chondrocytes. This study assesses the anti-inflammatory effect of sesamin on proteoglycans production in 3D chondrocyte cultures. METHODS: To evaluate the effects of sesamin on IL-1ß-treated human articular chondrocytes (HAC) pellets, the pellets were pre-treated with IL-1ß then cultured in the presence of various concentrations of sesamin for 21 days. During that period, the expression of IL-1ß, glycosaminoglycans (GAGs) content and Chondroitin sulfate proteoglycans (CSPGs) synthesis genes (ACAN, XT-1, XT-2, CHSY1 and ChPF) was measured. The GAGs accumulation in the extracellular matrix was determined on day 21 by histological analysis. RESULTS: There was clear evidence that sesamin upregulated expression of all the CSPGs synthesis genes, in contrast to the down-regulation of IL-1ß expression both in genes and in protein levels. The level of release and matrix accumulation of GAGs in IL-1ß pre-treated HAC pellets in the presence of sesamin was recovered. These results correlate with the histological examination which showed that sesamin enhanced matrix CSPGs accumulation. CONCLUSIONS: Sesamin enhances CSPGs synthesis, suppresses IL-1ß expression and ameliorates IL-1ß induced inflammation in human chondrocytes. Sesamin could have therapeutic benefits for treating inflammation in osteoarthritis.
[Mh] Termos MeSH primário: Condrócitos/efeitos dos fármacos
Proteoglicanas de Sulfatos de Condroitina/biossíntese
Dioxóis/farmacologia
Interleucina-1beta/metabolismo
Lignanas/farmacologia
[Mh] Termos MeSH secundário: Adulto
Agrecanas/genética
Agrecanas/metabolismo
Células Cultivadas
Condrócitos/metabolismo
Feminino
Seres Humanos
Masculino
Meia-Idade
N-Acetilgalactosaminiltransferases/genética
N-Acetilgalactosaminiltransferases/metabolismo
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ACAN protein, human); 0 (Aggrecans); 0 (Chondroitin Sulfate Proteoglycans); 0 (Dioxoles); 0 (Interleukin-1beta); 0 (Lignans); EC 2.4.1.- (N-Acetylgalactosaminyltransferases); EC 2.4.1.226 (CHSY1 protein, human); S7946O4P76 (sesamin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170821
[Lr] Data última revisão:
170821
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170602
[St] Status:MEDLINE
[do] DOI:10.1186/s12906-017-1805-1


  8 / 2876 MEDLINE  
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[PMID]:28424523
[Au] Autor:Busslinger GA; Stocsits RR; van der Lelij P; Axelsson E; Tedeschi A; Galjart N; Peters JM
[Ad] Endereço:Research Institute of Molecular Pathology (IMP), Vienna Biocenter (VBC), Campus-Vienna-Biocenter 1, A-1030 Vienna, Austria.
[Ti] Título:Cohesin is positioned in mammalian genomes by transcription, CTCF and Wapl.
[So] Source:Nature;544(7651):503-507, 2017 04 27.
[Is] ISSN:1476-4687
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mammalian genomes are spatially organized by CCCTC-binding factor (CTCF) and cohesin into chromatin loops and topologically associated domains, which have important roles in gene regulation and recombination. By binding to specific sequences, CTCF defines contact points for cohesin-mediated long-range chromosomal cis-interactions. Cohesin is also present at these sites, but has been proposed to be loaded onto DNA elsewhere and to extrude chromatin loops until it encounters CTCF bound to DNA. How cohesin is recruited to CTCF sites, according to this or other models, is unknown. Here we show that the distribution of cohesin in the mouse genome depends on transcription, CTCF and the cohesin release factor Wings apart-like (Wapl). In CTCF-depleted fibroblasts, cohesin cannot be properly recruited to CTCF sites but instead accumulates at transcription start sites of active genes, where the cohesin-loading complex is located. In the absence of both CTCF and Wapl, cohesin accumulates in up to 70 kilobase-long regions at 3'-ends of active genes, in particular if these converge on each other. Changing gene expression modulates the position of these 'cohesin islands'. These findings indicate that transcription can relocate mammalian cohesin over long distances on DNA, as previously reported for yeast cohesin, that this translocation contributes to positioning cohesin at CTCF sites, and that active genes can be freed from cohesin either by transcription-mediated translocation or by Wapl-mediated release.
[Mh] Termos MeSH primário: Proteínas de Ciclo Celular/metabolismo
Proteínas Cromossômicas não Histona/metabolismo
Cromossomos de Mamíferos/metabolismo
Genoma/genética
Proteínas/metabolismo
Proteínas Repressoras/metabolismo
Transcrição Genética/genética
[Mh] Termos MeSH secundário: Animais
Sítios de Ligação
Fator de Ligação a CCCTC
Proteínas de Ciclo Celular/deficiência
Proteínas de Ciclo Celular/genética
Células Cultivadas
Proteoglicanas de Sulfatos de Condroitina/deficiência
Proteoglicanas de Sulfatos de Condroitina/genética
Cromatina/genética
Cromatina/metabolismo
Proteínas Cromossômicas não Histona/deficiência
Proteínas Cromossômicas não Histona/genética
Cromossomos de Mamíferos/genética
DNA/genética
DNA/metabolismo
Feminino
Fibroblastos/citologia
Fibroblastos/metabolismo
Masculino
Camundongos
Transporte Proteico
Proteínas/genética
Proteínas Repressoras/deficiência
Proteínas Repressoras/genética
Sítio de Iniciação de Transcrição
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (CCCTC-Binding Factor); 0 (Cell Cycle Proteins); 0 (Chondroitin Sulfate Proteoglycans); 0 (Chromatin); 0 (Chromosomal Proteins, Non-Histone); 0 (Cspg6 protein, mouse); 0 (Ctcf protein, mouse); 0 (Proteins); 0 (Repressor Proteins); 0 (WAPL protein, mouse); 0 (cohesins); 9007-49-2 (DNA)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170421
[St] Status:MEDLINE
[do] DOI:10.1038/nature22063


  9 / 2876 MEDLINE  
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[PMID]:28408410
[Au] Autor:Fujita Y; Masuda K; Bando M; Nakato R; Katou Y; Tanaka T; Nakayama M; Takao K; Miyakawa T; Tanaka T; Ago Y; Hashimoto H; Shirahige K; Yamashita T
[Ad] Endereço:Department of Molecular Neuroscience, Graduate School of Medicine, Osaka University, Osaka 565-0871, Japan.
[Ti] Título:Decreased cohesin in the brain leads to defective synapse development and anxiety-related behavior.
[So] Source:J Exp Med;214(5):1431-1452, 2017 May 01.
[Is] ISSN:1540-9538
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Abnormal epigenetic regulation can cause the nervous system to develop abnormally. Here, we sought to understand the mechanism by which this occurs by investigating the protein complex cohesin, which is considered to regulate gene expression and, when defective, is associated with higher-level brain dysfunction and the developmental disorder Cornelia de Lange syndrome (CdLS). We generated conditional -knockout mice and observed greater dendritic complexity and larger numbers of immature synapses in the cerebral cortex of mice. mice also exhibited more anxiety-related behavior, which is a symptom of CdLS. Further, a gene ontology analysis after RNA-sequencing suggested the enrichment of immune processes, particularly the response to interferons, in the mice. Indeed, fewer synapses formed in their cortical neurons, and this phenotype was rescued by STAT1 knockdown. Thus, low levels of cohesin expression in the developing brain lead to changes in gene expression that in turn lead to a specific and abnormal neuronal and behavioral phenotype.
[Mh] Termos MeSH primário: Ansiedade/etiologia
Encéfalo/fisiopatologia
Proteínas de Ciclo Celular/deficiência
Proteínas Cromossômicas não Histona/deficiência
Sinapses/fisiologia
[Mh] Termos MeSH secundário: Animais
Ansiedade/fisiopatologia
Encéfalo/metabolismo
Química Encefálica/fisiologia
Proteínas de Ciclo Celular/fisiologia
Proteoglicanas de Sulfatos de Condroitina/fisiologia
Proteínas Cromossômicas não Histona/fisiologia
Feminino
Regulação da Expressão Gênica/fisiologia
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Cycle Proteins); 0 (Chondroitin Sulfate Proteoglycans); 0 (Chromosomal Proteins, Non-Histone); 0 (Cspg6 protein, mouse); 0 (cohesins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170415
[St] Status:MEDLINE
[do] DOI:10.1084/jem.20161517


  10 / 2876 MEDLINE  
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[PMID]:28368372
[Au] Autor:Chatzinikolaou G; Apostolou Z; Aid-Pavlidis T; Ioannidou A; Karakasilioti I; Papadopoulos GL; Aivaliotis M; Tsekrekou M; Strouboulis J; Kosteas T; Garinis GA
[Ad] Endereço:Institute of Molecular Biology and Biotechnology, Foundation for Research and Technology-Hellas, Nikolaou Plastira 100, 70013 Heraklion, Crete, Greece.
[Ti] Título:ERCC1-XPF cooperates with CTCF and cohesin to facilitate the developmental silencing of imprinted genes.
[So] Source:Nat Cell Biol;19(5):421-432, 2017 May.
[Is] ISSN:1476-4679
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Inborn defects in DNA repair are associated with complex developmental disorders whose causal mechanisms are poorly understood. Using an in vivo biotinylation tagging approach in mice, we show that the nucleotide excision repair (NER) structure-specific endonuclease ERCC1-XPF complex interacts with the insulator binding protein CTCF, the cohesin subunits SMC1A and SMC3 and with MBD2; the factors co-localize with ATRX at the promoters and control regions (ICRs) of imprinted genes during postnatal hepatic development. Loss of Ercc1 or exposure to MMC triggers the localization of CTCF to heterochromatin, the dissociation of the CTCF-cohesin complex and ATRX from promoters and ICRs, altered histone marks and the aberrant developmental expression of imprinted genes without altering DNA methylation. We propose that ERCC1-XPF cooperates with CTCF and cohesin to facilitate the developmental silencing of imprinted genes and that persistent DNA damage triggers chromatin changes that affect gene expression programs associated with NER disorders.
[Mh] Termos MeSH primário: Proteínas de Ciclo Celular/metabolismo
Proteínas Cromossômicas não Histona/metabolismo
Reparo do DNA
Proteínas de Ligação a DNA/metabolismo
Endonucleases/metabolismo
Inativação Gênica
Impressão Genômica
Proteínas Repressoras/metabolismo
[Mh] Termos MeSH secundário: Fatores Etários
Animais
Animais Recém-Nascidos
Fator de Ligação a CCCTC
Proteínas de Ciclo Celular/genética
Células Cultivadas
Proteoglicanas de Sulfatos de Condroitina/genética
Proteoglicanas de Sulfatos de Condroitina/metabolismo
Proteínas Cromossômicas não Histona/genética
Técnicas de Cocultura
Dano ao DNA
DNA Helicases/genética
DNA Helicases/metabolismo
Proteínas de Ligação a DNA/genética
Endonucleases/genética
Fibroblastos/enzimologia
Regulação da Expressão Gênica no Desenvolvimento
Genótipo
Histonas/metabolismo
Fígado/enzimologia
Camundongos da Linhagem 129
Camundongos Endogâmicos C57BL
Camundongos Transgênicos
Proteínas Nucleares/genética
Proteínas Nucleares/metabolismo
Fenótipo
Regiões Promotoras Genéticas
Proteínas Repressoras/genética
Proteína Nuclear Ligada ao X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CCCTC-Binding Factor); 0 (Cell Cycle Proteins); 0 (Chondroitin Sulfate Proteoglycans); 0 (Chromosomal Proteins, Non-Histone); 0 (Cspg6 protein, mouse); 0 (Ctcf protein, mouse); 0 (DNA-Binding Proteins); 0 (Histones); 0 (Mbd2 protein, mouse); 0 (Nuclear Proteins); 0 (Repressor Proteins); 0 (cohesins); 0 (structural maintenance of chromosome protein 1); 0 (xeroderma pigmentosum group F protein); EC 3.1.- (Endonucleases); EC 3.1.- (Ercc1 protein, mouse); EC 3.6.4.- (DNA Helicases); EC 3.6.4.12 (Atrx protein, mouse); EC 3.6.4.12 (X-linked Nuclear Protein)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170404
[St] Status:MEDLINE
[do] DOI:10.1038/ncb3499



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