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  1 / 574 MEDLINE  
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[PMID]:29254293
[Au] Autor:Di Spigna G; Iannone M; Ladogana P; Salzano S; Ventre M; Covelli B; De Marinis E; Postiglione L
[Ad] Endereço:Department of Translational Medical Sciences, University of Naples “Federico II”, Naples, Italy.
[Ti] Título:Human cardiac multipotent adult stem cells in 3D matrix: new approach of tissue engineering in cardiac regeneration post-infarction.
[So] Source:J Biol Regul Homeost Agents;31(4):911-921, 2017 Oct-Dec.
[Is] ISSN:0393-974X
[Cp] País de publicação:Italy
[La] Idioma:eng
[Ab] Resumo:Myocardial infarction is the leading cause of morbidity and mortality in developed countries. It causes a left ventricular dysfunction, mainly due to the loss of functional tissue, resulting in heart failure. New therapies are being developed, using a tissue engineering approach, with the ultimate goal of restoring cardiac function by regenerating and repairing the damaged myocardium. In the present study we investigated the behaviour of a specific population of c-kit positive human cardiac stem cells, called Multipotent Adult Stem Cells (MASCs), grown within three-dimensional collagen scaffolds (3D), to establish whether they could be used in post-infarction cardiac regeneration. We also evaluated the expression levels of the Granulocyte Macrophage-Colony Stimulating Factor Receptor (GM-CSFR) and endoglin, a component of the Transforming Growth Factor beta (TGF-ß) receptor complex. Finally, we also evaluated the expression of the α2ß1integrin. MASCs cultured within 3D collagen matrices are able to proliferate and migrate even in the absence of chemotactic agents and express high levels of factors involved in cell proliferation and migration, such as GM-CSFRα chain and integrins. They therefore represent a promising approach to tissue engineering aimed to restore cardiac function. Our results also suggest a role of GM-CSF in cell proliferation, while TGF-ß does not seem to be relevant.
[Mh] Termos MeSH primário: Células-Tronco Adultas/citologia
Células-Tronco Multipotentes/citologia
Engenharia Tecidual/métodos
Tecidos Suporte
[Mh] Termos MeSH secundário: Células-Tronco Adultas/metabolismo
Técnicas de Cultura de Células
Movimento Celular
Proliferação Celular
Separação Celular
Colágeno/química
Endoglina/genética
Endoglina/metabolismo
Expressão Gênica
Seres Humanos
Integrina alfa2beta1/genética
Integrina alfa2beta1/metabolismo
Células-Tronco Multipotentes/metabolismo
Infarto do Miocárdio
Receptores de Fator Estimulador das Colônias de Granulócitos e Macrófagos/genética
Receptores de Fator Estimulador das Colônias de Granulócitos e Macrófagos/metabolismo
Fator de Crescimento Transformador beta/genética
Fator de Crescimento Transformador beta/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ENG protein, human); 0 (Endoglin); 0 (Integrin alpha2beta1); 0 (Receptors, Granulocyte-Macrophage Colony-Stimulating Factor); 0 (Transforming Growth Factor beta); 9007-34-5 (Collagen)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171220
[St] Status:MEDLINE


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[PMID]:28704418
[Au] Autor:Parkin JD; San Antonio JD; Persikov AV; Dagher H; Dalgleish R; Jensen ST; Jeunemaitre X; Savige J
[Ad] Endereço:From the University of Melbourne Department of Medicine (Northern Health), Melbourne, VIC, Australia.
[Ti] Título:The collαgen III fibril has a "flexi-rod" structure of flexible sequences interspersed with rigid bioactive domains including two with hemostatic roles.
[So] Source:PLoS One;12(7):e0175582, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Collagen III is critical to the integrity of blood vessels and distensible organs, and in hemostasis. Examination of the human collagen III interactome reveals a nearly identical structural arrangement and charge distribution pattern as for collagen I, with cell interaction domains, fibrillogenesis and enzyme cleavage domains, several major ligand-binding regions, and intermolecular crosslink sites at the same sites. These similarities allow heterotypic fibril formation with, and substitution by, collagen I in embryonic development and wound healing. The collagen III fibril assumes a "flexi-rod" structure with flexible zones interspersed with rod-like domains, which is consistent with the molecule's prominence in young, pliable tissues and distensible organs. Collagen III has two major hemostasis domains, with binding motifs for von Willebrand factor, α2ß1 integrin, platelet binding octapeptide and glycoprotein VI, consistent with the bleeding tendency observed with COL3A1 disease-causing sequence variants.
[Mh] Termos MeSH primário: Colágeno Tipo III/química
Colágeno Tipo III/metabolismo
Hemostasia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sítios de Ligação
Colágeno Tipo III/genética
Seres Humanos
Integrina alfa2beta1/metabolismo
Glicoproteínas da Membrana de Plaquetas/metabolismo
Ligação Proteica
Mapas de Interação de Proteínas
Estabilidade Proteica
Fator de von Willebrand/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Collagen Type III); 0 (Integrin alpha2beta1); 0 (Platelet Membrane Glycoproteins); 0 (platelet membrane glycoprotein VI); 0 (von Willebrand Factor)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170920
[Lr] Data última revisão:
170920
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170714
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0175582


  3 / 574 MEDLINE  
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[PMID]:28704364
[Au] Autor:Eble JA; McDougall M; Orriss GL; Niland S; Johanningmeier B; Pohlentz G; Meier M; Karrasch S; Estevão-Costa MI; Martins Lima A; Stetefeld J
[Ad] Endereço:Institute of Physiological Chemistry and Pathobiochemistry, University of Münster, Münster, Germany.
[Ti] Título:Dramatic and concerted conformational changes enable rhodocetin to block α2ß1 integrin selectively.
[So] Source:PLoS Biol;15(7):e2001492, 2017 Jul.
[Is] ISSN:1545-7885
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The collagen binding integrin α2ß1 plays a crucial role in hemostasis, fibrosis, and cancer progression amongst others. It is specifically inhibited by rhodocetin (RC), a C-type lectin-related protein (CLRP) found in Malayan pit viper (Calloselasma rhodostoma) venom. The structure of RC alone reveals a heterotetramer arranged as an αß and γδ subunit in a cruciform shape. RC specifically binds to the collagen binding A-domain of the integrin α2 subunit, thereby blocking collagen-induced platelet aggregation. However, until now, the molecular basis for this interaction has remained unclear. Here, we present the molecular structure of the RCγδ-α2A complex solved to 3.0 Å resolution. Our findings show that RC undergoes a dramatic structural reorganization upon binding to α2ß1 integrin. Besides the release of the nonbinding RCαß tandem, the RCγ subunit interacts with loop 2 of the α2A domain as result of a dramatic conformational change. The RCδ subunit contacts the integrin α2A domain in the "closed" conformation through its helix C. Combined with epitope-mapped antibodies, conformationally locked α2A domain mutants, point mutations within the α2A loop 2, and chemical modifications of the purified toxin protein, this molecular structure of RCγδ-α2A complex explains the inhibitory mechanism and specificity of RC for α2ß1 integrin.
[Mh] Termos MeSH primário: Venenos de Crotalídeos/química
Integrina alfa2beta1/química
[Mh] Termos MeSH secundário: Venenos de Crotalídeos/farmacologia
Cristalografia por Raios X
Integrina alfa2beta1/antagonistas & inibidores
Modelos Moleculares
Ligação Proteica
Estrutura Terciária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Crotalid Venoms); 0 (Integrin alpha2beta1); 0 (rhodocetin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171003
[Lr] Data última revisão:
171003
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170714
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pbio.2001492


  4 / 574 MEDLINE  
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[PMID]:28326736
[Au] Autor:Yingzhu K; Shujuan G; Chengcheng L; Yi D
[Ad] Endereço:State Key Laboratory of Oral Diseases, Dept. of Periodontics, West China Hospital of Stomatology, Sichuan University, Chengdu 610041, China.
[Ti] Título:[Research progression of the relationship between integrin α2ß1 and drug-induced gingival overgrowth].
[So] Source:Hua Xi Kou Qiang Yi Xue Za Zhi;35(1):99-103, 2017 Feb 01.
[Is] ISSN:1000-1182
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:Drug-induced gingival overgrowth (DIGO) is characterized by fibrous gingival hyperplasia and increased gingival volume. DIGO is histologically associated with proliferation of cells and deposition of extracellular matrices, particularly collagen. Integrin α2ß1 is related to collagen phagocytosis and involved in the occurrence and progression of DIGO. This paper reviews the progress of research on the relationship between integrin α2ß1 and DIGO.
[Mh] Termos MeSH primário: Crescimento Excessivo da Gengiva
[Mh] Termos MeSH secundário: Colágeno
Gengiva
Seres Humanos
Integrina alfa2beta1
Fagocitose
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Integrin alpha2beta1); 9007-34-5 (Collagen)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170412
[Lr] Data última revisão:
170412
[Sb] Subgrupo de revista:D; IM
[Da] Data de entrada para processamento:170323
[St] Status:MEDLINE
[do] DOI:10.7518/hxkq.2017.01.016


  5 / 574 MEDLINE  
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[PMID]:28251149
[Au] Autor:Hong J; Chu M; Qian L; Wang J; Guo Y; Xu D
[Ad] Endereço:Department of Cardiology, Geriatric Medicine, The First Affiliated Hospital of Nanjing Medical University, Nanjing, China.
[Ti] Título:Fibrillar Type I Collagen Enhances the Differentiation and Proliferation of Myofibroblasts by Lowering 2 1 Integrin Expression in Cardiac Fibrosis.
[So] Source:Biomed Res Int;2017:1790808, 2017.
[Is] ISSN:2314-6141
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Many studies have shown that 2 1 integrin plays an important role in the development of cardiac fibrosis. However, the mechanism of how 2 1 integrin regulates the differentiation and proliferation of myofibroblasts in cardiac fibrosis through fibrillar collagen (FC) remains uncertain. We established that FC mimicked the 3-dimensional extracellular matrix (ECM) of fibroblasts from post-myocardial infarction (MI) patients in vivo. This allowed us to explore the differentiation and proliferation of cardiac fibroblasts on FC. Here, we report that low expression of 2 1 integrin increased protein kinase B (AKT) activation and -smooth muscle actin ( -SMA) expression. This occurred due to the instability of phosphatase and tensin homolog (PTEN) in myofibroblasts on FC. We also demonstrated that FC reduced protein phosphatase type 2A (PP2A) activity of myofibroblasts, which was coincident with low 2 1 integrin expression and activation of AKT, but not mitogen-activated protein kinase (ERK). In addition, knock-down of both 1 integrin and PP2A in fibroblasts promoted differentiation and proliferation via AKT activation and increased -SMA expression. In summary, our study demonstrated that low 2 1 integrin expression regulated its downstream targets PTEN and AKT via crosstalk with PP2A, a critical cell signaling pathway that permits aberrant differentiation and proliferation of myofibroblasts on FC.
[Mh] Termos MeSH primário: Diferenciação Celular/efeitos dos fármacos
Colágeno Tipo I/farmacologia
Integrina alfa2beta1/metabolismo
Miocárdio/patologia
Miofibroblastos/patologia
[Mh] Termos MeSH secundário: Animais
Proliferação Celular/efeitos dos fármacos
Fibrose
Técnicas de Silenciamento de Genes
Camundongos Endogâmicos C57BL
Miocárdio/metabolismo
Miofibroblastos/efeitos dos fármacos
Miofibroblastos/metabolismo
PTEN Fosfo-Hidrolase/metabolismo
Proteína Fosfatase 2/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Collagen Type I); 0 (Integrin alpha2beta1); EC 3.1.3.16 (Protein Phosphatase 2); EC 3.1.3.67 (PTEN Phosphohydrolase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170313
[Lr] Data última revisão:
170313
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170303
[St] Status:MEDLINE
[do] DOI:10.1155/2017/1790808


  6 / 574 MEDLINE  
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[PMID]:28004990
[Au] Autor:Liu H; Wang Y; Zheng J; Li G; Chen T; Lei J; Mao Y; Wang J; Liu W; Zhao G; Tacey M; Yan B
[Ad] Endereço:1 Department of Neurology, the Second Clinical Medical College of North Sichuan Medical College & Nanchong Central Hospital, Nanchong, P R China.
[Ti] Título:Platelet glycoprotein gene Ia C807T, HPA-3, and Ibα VNTR polymorphisms are associated with increased ischemic stroke risk: Evidence from a comprehensive meta-analysis.
[So] Source:Int J Stroke;12(1):46-70, 2017 Jan.
[Is] ISSN:1747-4949
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Background/aims Platelet glycoproteins play a crucial role in the initial stage of thrombus formation and may contribute to the pathophysiology of atherosclerosis. Polymorphisms in glycoprotein genes alter the function of the protein, possibly leading to increased risk of ischemic stroke. However, previous genetic association studies that examined the relationship between glycoprotein genes polymorphisms and ischemic stroke have yielded inconsistent results. This study aimed to evaluate the association between glycoprotein genes and ischemic stroke by the application of meta-analysis. Methods Relevant studies were identified by an extensive search through databases. The quality of included studies was assessed independently using the Newcastle-Ottawa Scale. Allele and genotype frequencies for each included study were extracted. The odds ratio (OR) with 95% confidence interval (95%CI) was calculated using a random-effects or fixed-effects model. Q statistic was used to evaluate homogeneity, and a meta-regression model was used to explore the study-level variables and to describe the heterogeneity in included studies. Egger's test and funnel plot were used to assess publication bias. Results A total of 60 studies (9 polymorphisms) were included and identified in the current meta-analysis. The Newcastle-Ottawa Scale scores ranged from 7 to 9 except for two studies with Newcastle-Ottawa Scale scores of 6. The T allele or TT genotype of the glycoprotein Ia C807T polymorphism were associated with an increased susceptibility to ischemic stroke in combined population (807T allele: OR, 95%CI: 1.24, 1.03-1.50, p = 0.02) or Asian populations (807T allele: OR, 95%CI: 1.31, 1.10-1.54, p = 0.002 and 807TT genotype: OR, 95%CI: 1.53, 1.13-2.08, p = 0.006, respectively), and the Ser allele of HPA-3 was associated with increased risk of ischemic stroke in combined population or in Asians (OR, 95%CI: 1.21, 1.04-1.40, p = 0.01 or 1.54, 1.18-2.01, p = 0.001). Of note, the Ser/Ser genotype was more common in Asians (OR, 95%CI: 2.09, 1.40-3.13, p < 0.001). For glycoprotein Ibα variable number tandem repeat, only B allele showed a mild significant association with ischemic stroke risk in combined population or in Caucasians (OR, 95%CI: 2.17, 1.04-4.55, p = 0.04 or 1.79, 1.02-3.13, p = 0.04). There was no significant association between HPA-1, HPA-2, HPA-4, HPA-5, glycoprotein Ibα-5 T/C as well as Ia G873A polymorphisms and increased risk of ischemic stroke. Conclusions We found that glycoprotein Ia C807T T allele or the TT genotype, the Ser-allele of HPA-3 and B allele of glycoprotein Ibα variable number tandem repeat polymorphisms were associated with increased risk for ischemic stroke. Future studies with larger sample sizes will be necessary to confirm the results. In addition, analyses of ischemic stroke subtypes and gene-gene and gene-environment interactions are warranted.
[Mh] Termos MeSH primário: Isquemia Encefálica/genética
Predisposição Genética para Doença
Integrina alfa2beta1/genética
Repetições Minissatélites
Complexo Glicoproteico GPIb-IX de Plaquetas/genética
Glicoproteína IIb da Membrana de Plaquetas/genética
Acidente Vascular Cerebral/genética
[Mh] Termos MeSH secundário: Seres Humanos
Polimorfismo Genético
[Pt] Tipo de publicação:JOURNAL ARTICLE; META-ANALYSIS; REVIEW
[Nm] Nome de substância:
0 (Integrin alpha2beta1); 0 (Platelet Glycoprotein GPIb-IX Complex); 0 (Platelet Membrane Glycoprotein IIb)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161223
[St] Status:MEDLINE
[do] DOI:10.1177/1747493016672085


  7 / 574 MEDLINE  
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[PMID]:27915017
[Au] Autor:Bax DV; Davidenko N; Gullberg D; Hamaia SW; Farndale RW; Best SM; Cameron RE
[Ad] Endereço:Department of Materials Science and Metallurgy, University of Cambridge, 27 Charles Babbage Road, Cambridge CB3 0FS, United Kingdom; Department of Biochemistry, University of Cambridge, Downing Site, Cambridge CB2 1QW, United Kingdom. Electronic address: dvb24@cam.ac.uk.
[Ti] Título:Fundamental insight into the effect of carbodiimide crosslinking on cellular recognition of collagen-based scaffolds.
[So] Source:Acta Biomater;49:218-234, 2017 Feb.
[Is] ISSN:1878-7568
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Research on the development of collagen constructs is extremely important in the field of tissue engineering. Collagen scaffolds for numerous tissue engineering applications are frequently crosslinked with 1-ethyl-3-(3-dimethylaminopropyl-carbodiimide hydrochloride (EDC) in the presence of N-hydroxy-succinimide (NHS). Despite producing scaffolds with good biocompatibility and low cellular toxicity the influence of EDC/NHS crosslinking on the cell interactive properties of collagen has been overlooked. Here we have extensively studied the interaction of model cell lines with collagen I-based materials after crosslinking with different ratios of EDC in relation to the number of carboxylic acid residues on collagen. Divalent cation-dependent cell adhesion, via integrins α ß , α ß , α ß and α ß , were sensitive to EDC crosslinking. With increasing EDC concentration, this was replaced with cation-independent adhesion. These results were replicated using purified recombinant I domains derived from integrin α and α subunits. Integrin α ß -mediated cell spreading, apoptosis and proliferation were all heavily influenced by EDC crosslinking of collagen. Data from this rigorous study provides an exciting new insight that EDC/NHS crosslinking is utilising the same carboxylic side chain chemistry that is vital for native-like integrin-mediated cell interactions. Due to the ubiquitous usage of EDC/NHS crosslinked collagen for biomaterials fabrication this data is essential to have a full understanding in order to ensure optimized collagen-based material performance. STATEMENT OF SIGNIFICANCE: Carbodiimide stabilised collagen is employed extensively for the fabrication of biologically active materials. Despite this common usage, the effect of carbodiimide crosslinking on cell-collagen interactions is unclear. Here we have found that carbodiimide crosslinking of collagen inhibits native-like, whilst increasing non-native like, cellular interactions. We propose a mechanistic model in which carbodiimide modifies the carboxylic acid groups on collagen that are essential for cell binding. As such we feel that this research provides a crucial, long awaited, insight into the bioactivity of carbodiimide crosslinked collagen. Through the ubiquitous use of collagen as a cellular substrate we feel that this is fundamental to a wide range of research activity with high impact across a broad range of disciplines.
[Mh] Termos MeSH primário: Colágeno/química
Reagentes para Ligações Cruzadas/química
Etildimetilaminopropil Carbodi-Imida/química
Tecidos Suporte/química
[Mh] Termos MeSH secundário: Animais
Cátions
Bovinos
Adesão Celular
Linhagem Celular
Proliferação Celular
Sobrevivência Celular
Seres Humanos
Integrina alfa2beta1/metabolismo
Camundongos
Domínios Proteicos
Solubilidade
Succinimidas
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cations); 0 (Cross-Linking Reagents); 0 (Integrin alpha2beta1); 0 (Succinimides); 9007-34-5 (Collagen); MJE3791M4T (N-hydroxysuccinimide); RJ5OZG6I4A (Ethyldimethylaminopropyl Carbodiimide)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161205
[St] Status:MEDLINE


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[PMID]:27548579
[Au] Autor:Yan Z; Pan Y; Wang S; Cheng M; Kong H; Sun C; Hu K; Chen T; Dong Q; Chen J
[Ad] Endereço:*The Second Affiliated Hospital of Soochow University, Suzhou, China †State Key Laboratory of Cell Biology, CAS Center for Excellence in Molecular Cell Science, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China.
[Ti] Título:Static Compression Induces ECM Remodeling and Integrin α2ß1 Expression and Signaling in a Rat Tail Caudal Intervertebral Disc Degeneration Model.
[So] Source:Spine (Phila Pa 1976);42(8):E448-E458, 2017 Apr 15.
[Is] ISSN:1528-1159
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:STUDY DESIGN: A three-level rat tail caudal intervertebral disc (IVD) degeneration (IVDD) model was established to study effects of static compression on extracellular matrix (ECM) remodeling and integrin signaling in IVDs during IVDD. OBJECTIVE: The aim of this study was to investigate the effect of compression force on ECM remodeling and integrin signaling in IVDs during IVDD. SUMMARY OF BACKGROUND DATA: Integrins sense mechanical environment alteration via binding to ECM ligands and trigger intracellular signaling for pathological ECM remodeling during IVDD. However, the role of compression force in ECM remodeling and integrin signaling during IVDD remains elusive. METHODS: Compared with the classical one-level rat tail IVDD model that exerts axial stress on the 8th to 9th caudal vertebral bodies, a three-level model was established by using an Ilizarov-type apparatus to exert stress on the 7th to 10th caudal vertebral bodies in rat tails for four weeks. To exclude side effects from surgical stab injury on manipulated discs, intact coccygeal (Co) disc Co8-9 was analyzed. RESULTS: In three-level IVDD model, significant degeneration of the Co8-9 disc was observed. Quantitative real-time polymerase chain reaction (qRT-PCR) showed elevated mRNA expression of collagen types I, III, and V; matrix metalloproteinases (MMPs) 2, 3, 9, 13, 14; and decreased mRNA expression of collagen type II in Co8-9 disc. Compression loading altered the expression of integrin α2ß1 (upregulated) and α10ß1 (downregulated) in NP cells, and activated integrin downstream signaling. By contrast, one-level model showed more severe disc degeneration and ECM remodeling. Integrin α1, α2, α11, and ß1 were upregulated, whereas α10 was downregulated. Similar activation of integrin signaling was observed. CONCLUSION: Static compression altered collagen and MMP expression, and promoted ß1 integrin expression and signaling in IVD. Compared with one-level rat tail IVDD model, three-level model showed milder effects on disc degeneration, ECM remodeling, and integrin expression, suggesting one-level model might involve other causes that induce IVDD via mechanisms independent of compression force. LEVEL OF EVIDENCE: N/A.
[Mh] Termos MeSH primário: Matriz Extracelular/metabolismo
Integrina alfa2beta1/biossíntese
Degeneração do Disco Intervertebral/metabolismo
Disco Intervertebral/metabolismo
[Mh] Termos MeSH secundário: Animais
Colágeno/biossíntese
Modelos Animais de Doenças
Matriz Extracelular/patologia
Integrinas/biossíntese
Disco Intervertebral/diagnóstico por imagem
Disco Intervertebral/patologia
Degeneração do Disco Intervertebral/diagnóstico por imagem
Degeneração do Disco Intervertebral/patologia
Imagem por Ressonância Magnética
Masculino
Metaloproteinases da Matriz/biossíntese
RNA Mensageiro/biossíntese
Ratos
Ratos Sprague-Dawley
Transdução de Sinais
Estresse Mecânico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Integrin alpha2beta1); 0 (Integrins); 0 (RNA, Messenger); 9007-34-5 (Collagen); EC 3.4.24.- (Matrix Metalloproteinases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160823
[St] Status:MEDLINE
[do] DOI:10.1097/BRS.0000000000001856


  9 / 574 MEDLINE  
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[PMID]:27997897
[Au] Autor:Zhang L; Kong D; Meng H; Han C; Zhu J; Qiao J; He Y; Wang T; Li X; Zhang F; Jin X
[Ad] Endereço:Department of Pathology, Basic Medical Science College, Harbin Medical University, Harbin, China.
[Ti] Título:Plasma Gelsolin Promotes Proliferation of Mesangial Cell in IgA Nephropathy.
[So] Source:Cell Physiol Biochem;40(6):1473-1486, 2016.
[Is] ISSN:1421-9778
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIMS: Plasma gelsolin (pGSN) is an actin-binding protein that plays a critical role in the pathogenesis of rheumatoid arthritis. However, whether pGSN is involved in other immunological diseases remains unknown. This study focused on the relationship between pGSN and immunoglobulin A (IgA) nephropathy (IgAN). METHODS: Two hundred patients with IgAN, 200 patients each with several other types of nephropathy and healthy controls (HCs) who underwent kidney biopsies between 2000 and 2014 were enrolled in the study. The Oxford classification system was used to predict the risk of disease progression. Serum and renal tissue were used to detect pGSN, and the correlations between pGSN and IgA, galactose-deficient IgA1 (Gd-IgA1), transforming growth factor beta1 (TGF-ß1), fibronectin (FN) content, clinical symptoms, and kidney function were analyzed. RESULTS: We found that the pGSN levels were significantly decreased in sera from IgAN patients compared to sera from patients with other forms of glomerular nephritis and HCs. Furthermore, the serum pGSN levels were negatively correlated with the serum IgA1, FN, and TGF-ß1 levels, and positively correlated with the estimated glomerular filtration rate. Conversely, the glomerular pGSN content was significantly elevated in the IgAN patients and was positively correlated with TGF-ß1 and FN levels. In renal tissue, the pGSN levels were significantly higher in IgAN patients with M1 and S1 compared to patients with M0 and S0 (p < 0.05). Meanwhile, pGSN promoted human mesangial cell (HMC) proliferation by facilitating cell mitosis in vitro. pGSN also promoted integrin α2ß1 expression in HMCs and enhanced the integrin α2ß1-pGSN interaction. CONCLUSION: Our study suggested that pGSN may play an important role in the development of IgAN by promoting the proliferation of mesangial cells and that serum and glomerular pGSN levels may be new markers for predicting IgAN progression and prognosis.
[Mh] Termos MeSH primário: Gelsolina/sangue
Glomerulonefrite por IGA/sangue
Glomerulonefrite por IGA/patologia
Células Mesangiais/metabolismo
Células Mesangiais/patologia
[Mh] Termos MeSH secundário: Adulto
Western Blotting
Estudos de Casos e Controles
Proliferação Celular
Ensaio de Imunoadsorção Enzimática
Feminino
Fibronectinas/sangue
Seres Humanos
Imunoglobulina A/sangue
Integrina alfa2beta1/metabolismo
Glomérulos Renais/metabolismo
Glomérulos Renais/patologia
Mitose
Fator de Crescimento Transformador beta1/sangue
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fibronectins); 0 (Gelsolin); 0 (Immunoglobulin A); 0 (Integrin alpha2beta1); 0 (Transforming Growth Factor beta1)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170208
[Lr] Data última revisão:
170208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161221
[St] Status:MEDLINE
[do] DOI:10.1159/000453199


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[PMID]:27639165
[Au] Autor:Ghatak S; Niland S; Schulz JN; Wang F; Eble JA; Leitges M; Mauch C; Krieg T; Zigrino P; Eckes B
[Ad] Endereço:Department of Dermatology, University of Cologne, Cologne, Germany.
[Ti] Título:Role of Integrins α1ß1 and α2ß1 in Wound and Tumor Angiogenesis in Mice.
[So] Source:Am J Pathol;186(11):3011-3027, 2016 Nov.
[Is] ISSN:1525-2191
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Integrins are transmembrane receptors composed of one α subunit and one ß subunit and are involved in cellular growth, differentiation, and apoptosis. The collagen-binding integrins α1ß1 and α2ß1 have been shown to regulate wound and tumor vascularization by different mechanisms. In this study, we assessed wound and tumor vascularization in mice with genetic ablation of both integrin subunits α1 and α2, which resulted in loss of integrins α1ß1 and α2ß1. Wound angiogenesis was investigated in excisional wounds that were inflicted on the back skin of control and mice lacking integrin α1ß1 and α2ß1. Mutant mice displayed reduced wound angiogenesis, which correlated with decreased macrophage numbers at 3 and 7 days after injury, and showed significantly attenuated vascularization of sponge implants. Angiogenesis induced by tumors arising from intradermal injection of B16 F1 melanoma cells was also reduced in comparison to controls 7 days after injection. This reduction in angiogenesis correlated with increased levels and activity of circulating matrix metalloproteinase 9 and elevated angiostatin levels in plasma of mutant mice, which reduced endothelial cell proliferation. Ex vivo mutant aortic ring explants developed significantly fewer and thinner aortic sprouts with fewer branch points than controls because of impaired endothelial cell proliferation. In conclusion, the loss of integrins α1ß1 and α2ß1 in mice results in reduced wound and tumor angiogenesis by cell-autonomous and extrinsic mechanisms.
[Mh] Termos MeSH primário: Integrina alfa1beta1/metabolismo
Integrina alfa2beta1/metabolismo
Neoplasias/irrigação sanguínea
Cicatrização/fisiologia
Ferimentos e Lesões/patologia
[Mh] Termos MeSH secundário: Animais
Modelos Animais de Doenças
Feminino
Fibroblastos/metabolismo
Fibroblastos/patologia
Seres Humanos
Integrina alfa1beta1/genética
Integrina alfa2beta1/genética
Melanoma/irrigação sanguínea
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Neoplasias/etiologia
Neoplasias/patologia
Neovascularização Patológica
Pele/irrigação sanguínea
Pele/lesões
Pele/metabolismo
Pele/patologia
Neoplasias Cutâneas/irrigação sanguínea
Ferimentos e Lesões/etiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Integrin alpha1beta1); 0 (Integrin alpha2beta1)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170827
[Lr] Data última revisão:
170827
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:160918
[St] Status:MEDLINE



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