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Pesquisa : D12.776.860.300.250.400.550 [Categoria DeCS]
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[PMID]:27568096
[Au] Autor:Barrett DW; David AL; Thrasivoulou C; Mata A; Becker DL; Engels AC; Deprest JA; Chowdhury TT
[Ad] Endereço:Institute of Bioengineering, School of Engineering and Materials Science, Queen Mary University of London, London, UK.
[Ti] Título:Connexin 43 is overexpressed in human fetal membrane defects after fetoscopic surgery.
[So] Source:Prenat Diagn;36(10):942-952, 2016 Oct.
[Is] ISSN:1097-0223
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: We examined whether surgically induced membrane defects elevate connexin 43 (Cx43) expression in the wound edge of the amniotic membrane (AM) and drives structural changes in collagen that affects healing after fetoscopic surgery. METHOD: Cell morphology and collagen microstructure was investigated by scanning electron microscopy and second harmonic generation in fetal membranes taken from women who underwent fetal surgery. Immunofluoresence and real-time quantitative polymerase chain reaction was used to examine Cx43 expression in control and wound edge AM. RESULTS: Scanning electron microscopy showed dense, helical patterns of collagen fibrils in the wound edge of the fetal membrane. This arrangement changed in the fibroblast layer with evidence of collagen fibrils that were highly polarised along the wound edge but not in control membranes. Cx43 was increased by 112.9% in wound edge AM compared with controls (p < 0.001), with preferential distribution in the fibroblast layer compared with the epithelial layer (p < 0.01). In wound edge AM, mesenchymal cells had a flattened morphology, and there was evidence of poor epithelial migration across the defect. Cx43 and COX-2 expression was significantly increased in wound edge AM compared with controls (p < 0.001). CONCLUSION: Overexpression of Cx43 in the AM after fetal surgery induces morphological and structural changes in the collagenous matrix that may interfere with normal healing mechanisms. © 2016 The Authors. Prenatal Diagnosis published by John Wiley & Sons, Ltd.
[Mh] Termos MeSH primário: Âmnio/metabolismo
Conexina 43/genética
Ciclo-Oxigenase 2/genética
Fetoscopia
RNA Mensageiro/metabolismo
[Mh] Termos MeSH secundário: Adulto
Âmnio/lesões
Âmnio/ultraestrutura
Estudos de Casos e Controles
Conexina 43/metabolismo
Ciclo-Oxigenase 2/metabolismo
Matriz Extracelular
Feminino
Transfusão Feto-Fetal/cirurgia
Colágenos Associados a Fibrilas
Imunofluorescência
Idade Gestacional
Hérnias Diafragmáticas Congênitas/cirurgia
Seres Humanos
Microscopia Eletrônica de Varredura
Gravidez
Reação em Cadeia da Polimerase em Tempo Real
Cicatrização
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Connexin 43); 0 (Fibril-Associated Collagens); 0 (GJA1 protein, human); 0 (RNA, Messenger); EC 1.14.99.1 (Cyclooxygenase 2); EC 1.14.99.1 (PTGS2 protein, human)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160829
[St] Status:MEDLINE
[do] DOI:10.1002/pd.4917


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[PMID]:26930474
[Au] Autor:Tsuzuki T; Kajiya H; T-Goto K; Tsutsumi T; Nemoto T; Okabe K; Takahashi Y
[Ad] Endereço:Department of Oral Rehabilitation, Fukuoka Dental College, Fukuoka 8140193, Japan.
[Ti] Título:Hyperocclusion stimulates the expression of collagen type XII in periodontal ligament.
[So] Source:Arch Oral Biol;66:86-91, 2016 Jun.
[Is] ISSN:1879-1506
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:OBJECTIVES: It is known that excessive mechanical force exerted by hyperocclusion induces occlusal trauma. However, the mechanism of the process remains unclear. In the present study, we employed an in vivo hyperocclusion rodent model to examine morphological and biological mechanisms of occlusal trauma in periodontal ligament tissue. DESIGN: To investigate alveolar bone resorption, tooth sections were stained to detect osteoclasts. To investigate the relationship between hyperocclusion and the regeneration of the cell matrix, we examined the effect of hyperocclusal force on the expression of collagens using immunohistochemistry and quantitative PCR methods. RESULTS: The arrangement of collagen fibers in the furcation area of the teeth was undisturbed before hyperocclusion (control). Type I collagen was localized in the extracellular area at the furcation and there was faint expression and localization of type XII collagen in the periodontal ligament. The number of osteoclasts significantly increased in the furcation and lingual cervical regions on day 4 after hyperocclusion was induced. Type XII collagens were gradually up-regulated following the induction of hyperocclusion, in a time-dependent manner. Although type I collagen mRNA expression was stable before and after hyperocclusion, type XII collagen mRNA was significantly up-regulated on day 2 and day 4 after hyperocclusion treatment. CONCLUSIONS: Our findings indicate that hyperocclusal force predominantly up-regulates the expression of type XII collagen in periodontal tissue, but not type I collagen, suggesting that there is a mechanism for regeneration of periodontal tissues as a response to occlusal trauma.
[Mh] Termos MeSH primário: Colágeno Tipo XII/biossíntese
Oclusão Dentária
Ligamento Periodontal/metabolismo
[Mh] Termos MeSH secundário: Perda do Osso Alveolar/patologia
Animais
Fenômenos Biomecânicos
Força de Mordida
Colágeno/biossíntese
Colágeno Tipo I/metabolismo
Colágenos Associados a Fibrilas/biossíntese
Colágenos Fibrilares/biossíntese
Camundongos
Osteoclastos/metabolismo
Ligamento Periodontal/citologia
Ratos
Ratos Wistar
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Collagen Type I); 0 (Collagen Type XII); 0 (Fibril-Associated Collagens); 0 (Fibrillar Collagens); 9007-34-5 (Collagen)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170208
[Lr] Data última revisão:
170208
[Sb] Subgrupo de revista:D; IM
[Da] Data de entrada para processamento:160302
[St] Status:MEDLINE


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[PMID]:26902645
[Au] Autor:Blum KM; Novak T; Watkins L; Neu CP; Wallace JM; Bart ZR; Voytik-Harbin SL
[Ad] Endereço:Weldon School of Biomedical Engineering, College of Engineering, Purdue University, West Lafayette, IN 47907, USA. harbins@purdue.edu.
[Ti] Título:Acellular and cellular high-density, collagen-fibril constructs with suprafibrillar organization.
[So] Source:Biomater Sci;4(4):711-23, 2016 Apr.
[Is] ISSN:2047-4849
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Collagen is used extensively for tissue engineering due to its prevalence in connective tissues and its role in defining tissue biophysical and biological signalling properties. However, traditional collagen-based materials fashioned from atelocollagen and telocollagen have lacked collagen densities, multi-scale organization, mechanical integrity, and proteolytic resistance found within tissues in vivo. Here, highly interconnected low-density matrices of D-banded fibrils were created from collagen oligomers, which exhibit fibrillar as well as suprafibrillar assembly. Confined compression then was applied to controllably reduce the interstitial fluid while maintaining fibril integrity. More specifically, low-density (3.5 mg mL(-1)) oligomer matrices were densified to create collagen-fibril constructs with average concentrations of 12.25 mg mL(-1) and 24.5 mg mL(-1). Control and densified constructs exhibited nearly linear increases in ultimate stress, Young's modulus, and compressive modulus over the ranges of 65 to 213 kPa, 400 to 1.26 MPa, and 20 to 150 kPa, respectively. Densification also increased construct resistance to collagenase degradability. Finally, this process was amenable to creating high-density cellularized tissues; all constructs maintained high cell viability (at least 97%) immediately following compression as well as after 1 day and 7 days of culture. This method, which integrates the suprafibrillar assembly capacity of oligomers and controlled fluid reduction by confined compression, supports the rational and scalable design of a broad range of collagen-fibril materials and cell-encapsulated tissue constructs for tissue engineering applications.
[Mh] Termos MeSH primário: Colágeno/química
Matriz Extracelular/química
Colágenos Associados a Fibrilas/química
Engenharia Tecidual
[Mh] Termos MeSH secundário: Fenômenos Biomecânicos
Colágeno/fisiologia
Matriz Extracelular/fisiologia
Colágenos Associados a Fibrilas/fisiologia
Teste de Materiais/métodos
Modelos Biológicos
Pressão
Estresse Mecânico
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fibril-Associated Collagens); 9007-34-5 (Collagen)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170215
[Lr] Data última revisão:
170215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160224
[St] Status:MEDLINE
[do] DOI:10.1039/c5bm00443h


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[PMID]:26621838
[Au] Autor:Oudart JB; Doué M; Vautrin A; Brassart B; Sellier C; Dupont-Deshorgue A; Monboisse JC; Maquart FX; Brassart-Pasco S; Ramont L
[Ad] Endereço:Université de Reims Champagne-Ardenne, CNRS UMR 7369 (Matrice Extracellulaire et Dynamique Cellulaire, MEDyC), Reims, France.
[Ti] Título:The anti-tumor NC1 domain of collagen XIX inhibits the FAK/ PI3K/Akt/mTOR signaling pathway through αvß3 integrin interaction.
[So] Source:Oncotarget;7(2):1516-28, 2016 Jan 12.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Type XIX collagen is a minor collagen associated with basement membranes. It was isolated for the first time in a human cDNA library from rhabdomyosarcoma and belongs to the FACITs family (Fibril Associated Collagens with Interrupted Triple Helices). Previously, we demonstrated that the NC1 domain of collagen XIX (NC1(XIX)) exerts anti-tumor properties on melanoma cells by inhibiting their migration and invasion. In the present work, we identified for the first time the integrin αvß3 as a receptor of NC1(XIX). Moreover, we demonstrated that NC1(XIX) inhibits the FAK/PI3K/Akt/mTOR pathway, by decreasing the phosphorylation and activity of the major proteins involved in this pathway. On the other hand, NC1(XIX) induced an increase of GSK3ß activity by decreasing its degree of phosphorylation. Treatments targeting this central signaling pathway in the development of melanoma are promising and new molecules should be developed. NC1(XIX) seems to have the potential for the design of new anti-cancer drugs.
[Mh] Termos MeSH primário: Colágeno/metabolismo
Colágenos Associados a Fibrilas/metabolismo
Quinase 1 de Adesão Focal/metabolismo
Integrina alfaVbeta3/metabolismo
Melanoma/enzimologia
Fragmentos de Peptídeos/metabolismo
Fosfatidilinositol 3-Quinase/metabolismo
Proteínas Proto-Oncogênicas c-akt/metabolismo
Transdução de Sinais
Neoplasias Cutâneas/enzimologia
Serina-Treonina Quinases TOR/metabolismo
[Mh] Termos MeSH secundário: Proteínas Quinases Dependentes de 3-Fosfoinositídeo/metabolismo
Antineoplásicos/farmacologia
Linhagem Celular Tumoral
Colágeno/farmacologia
Colágenos Associados a Fibrilas/farmacologia
Glicogênio Sintase Quinase 3 beta/metabolismo
Seres Humanos
Integrina alfaVbeta3/efeitos dos fármacos
Melanoma/tratamento farmacológico
Melanoma/patologia
Terapia de Alvo Molecular
Fragmentos de Peptídeos/farmacologia
Fosforilação
Domínios Proteicos
Transdução de Sinais/efeitos dos fármacos
Neoplasias Cutâneas/tratamento farmacológico
Neoplasias Cutâneas/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Fibril-Associated Collagens); 0 (Integrin alphaVbeta3); 0 (Peptide Fragments); 0 (collagen XIX protein, human); 9007-34-5 (Collagen); EC 2.7.1.1 (MTOR protein, human); EC 2.7.1.1 (TOR Serine-Threonine Kinases); EC 2.7.1.137 (Phosphatidylinositol 3-Kinase); EC 2.7.10.2 (Focal Adhesion Kinase 1); EC 2.7.10.2 (PTK2 protein, human); EC 2.7.11.1 (3-Phosphoinositide-Dependent Protein Kinases); EC 2.7.11.1 (GSK3B protein, human); EC 2.7.11.1 (Glycogen Synthase Kinase 3 beta); EC 2.7.11.1 (PDPK1 protein, human); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151202
[St] Status:MEDLINE
[do] DOI:10.18632/oncotarget.6399


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[PMID]:25312736
[Au] Autor:Osidak MS; Osidak EO; Akhmanova MA; Domogatsky SP; Domogatskaya AS
[Ti] Título:Fibrillar, fibril-associated and basement membrane collagens of the arterial wall: architecture, elasticity and remodeling under stress.
[So] Source:Curr Pharm Des;21(9):1124-33, 2015.
[Is] ISSN:1873-4286
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The ability of a human artery to pass through 150 million liters of blood sustaining 2 billion pulsations of blood pressure with minor deterioration depends on unique construction of the arterial wall. Viscoelastic properties of this construction enable to re-seal the occuring damages apparently without direct immediate participance of the constituent cells. Collagen structures are considered to be the elements that determine the mechanoelastic properties of the wall in parallel with elastin responsible for elasticity and resilience. Collagen scaffold architecture is the function-dependent dynamic arrangement of a dozen different collagen types composing three distinct interacting forms inside the extracellular matrix of the wall. Tightly packed molecules of collagen types I, III, V provide high tensile strength along collagen fibrils but toughness of the collagen scaffold as a whole depends on molecular bonds between distinct fibrils. Apart of other macromolecules in the extracellular matrix (ECM), collagen-specific interlinks involve microfilaments of collagen type VI, meshwork-organized collagen type VIII, and FACIT collagen type XIV. Basement membrane collagen types IV, XV, XVIII and cell-associated collagen XIII enable transmission of mechanical signals between cells and whole artery matrix. Collagen scaffold undergoes continuous remodeling by decomposition promoted with MMPs and reconstitution from newly produced collagen molecules. Pulsatile stress-strain load modulates both collagen synthesis and MMP-dependent collagen degradation. In this way the ECM structure becomes adoptive to mechanical challenges. The mechanoelastic properties of the arterial wall are changed in atherosclerosis concomitantly with collagen turnover both type-specific and dependent on the structure. Improving the feedback could be another approach to restore sufficient blood circulation.
[Mh] Termos MeSH primário: Artérias/fisiologia
Aterosclerose/fisiopatologia
Membrana Basal/fisiologia
Elasticidade/fisiologia
Colágenos Associados a Fibrilas/fisiologia
Colágenos Fibrilares/fisiologia
Remodelação Vascular/fisiologia
[Mh] Termos MeSH secundário: Artérias/anatomia & histologia
Artérias/patologia
Aterosclerose/patologia
Matriz Extracelular/fisiologia
Seres Humanos
Metaloproteinases da Matriz/sangue
Estresse Mecânico
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Fibril-Associated Collagens); 0 (Fibrillar Collagens); EC 3.4.24.- (Matrix Metalloproteinases)
[Em] Mês de entrada:1509
[Cu] Atualização por classe:150107
[Lr] Data última revisão:
150107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141015
[St] Status:MEDLINE


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[PMID]:25092217
[Au] Autor:Rinck-Junior JA; Oliveira C; Lourenço GJ; Sagarra RA; Derchain SF; Segalla JG; Lima CS
[Ad] Endereço:Clinical Oncology Service, Department of Internal Medicine, Faculty of Medical Sciences, University of Campinas, Rua Alexander Fleming 181, Cidade Universitária "Zeferino Vaz", Distrito de Barão Geraldo, Campinas, São Paulo, CEP: 13083-970, Brazil.
[Ti] Título:Vascular endothelial growth factor (VEGF) polymorphism and increased risk of epithelial ovarian cancer.
[So] Source:J Cancer Res Clin Oncol;141(1):69-73, 2015 Jan.
[Is] ISSN:1432-1335
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION: Angiogenesis (AG) is essential for epithelial ovarian cancer (EOC) development. Vascular endothelial growth factor (VEGF), encoded by the VEGF gene, and endostatin, the product of the COL18A1 gene, act as a potent promoter and an inhibitor of AG, respectively. In the present study, we tested whether VEGF C936T and COL18A1 D104N polymorphisms alter the risk of EOC. METHODS: Genomic DNA from 131 EOC patients and 137 controls were analyzed by polymerase chain reaction and restriction fragment length polymorphism methods. The differences between groups were analyzed by χ (2) or Fisher's exact test and logistic regression analysis. RESULTS: The frequency of the VEGF 936CC genotype was higher in patients than in controls (84.8% vs. 75.3%, P = 0.03). Individuals with respective genotypes had a 1.98 (95% CI 1.04-3.78)-fold increased risk of EOC than those with the remaining genotypes. An excess of VEGF 936CC plus COL18A1 DN genotype was seen in patients when compared to controls (48.6% vs. 30.5%); however, only a tendency toward a statistically significant difference in genotype frequencies was found in the study (P = 0.06), reflecting a trend toward an increased risk of 2.44 for EOC in carriers of the combined genotype. CONCLUSION: Our data present, for the first time, preliminary evidence that VEGF C936T alone or combined with the COL18A1 D104N polymorphism of AG constitutes an important inherited EOC determinant.
[Mh] Termos MeSH primário: Biomarcadores Tumorais/genética
Colágenos Associados a Fibrilas/genética
Neoplasias Ovarianas/genética
Polimorfismo Genético/genética
Fator A de Crescimento do Endotélio Vascular/genética
[Mh] Termos MeSH secundário: Adenocarcinoma de Células Claras/genética
Adenocarcinoma de Células Claras/patologia
Adenocarcinoma Mucinoso/genética
Adenocarcinoma Mucinoso/patologia
Adulto
Idoso
Idoso de 80 Anos ou mais
Carcinoma de Células de Transição/genética
Carcinoma de Células de Transição/patologia
Estudos de Casos e Controles
Cistadenocarcinoma Seroso/genética
Cistadenocarcinoma Seroso/patologia
Neoplasias do Endométrio/genética
Neoplasias do Endométrio/patologia
Feminino
Seguimentos
Seres Humanos
Masculino
Meia-Idade
Gradação de Tumores
Estadiamento de Neoplasias
Neoplasias Ovarianas/patologia
Reação em Cadeia da Polimerase
Polimorfismo de Fragmento de Restrição
Prognóstico
Regiões Promotoras Genéticas
Fatores de Risco
Adulto Jovem
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (COL19A1 protein, human); 0 (Fibril-Associated Collagens); 0 (VEGFA protein, human); 0 (Vascular Endothelial Growth Factor A)
[Em] Mês de entrada:1503
[Cu] Atualização por classe:171007
[Lr] Data última revisão:
171007
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140806
[St] Status:MEDLINE
[do] DOI:10.1007/s00432-014-1786-0


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[PMID]:25775860
[Au] Autor:Ivanova VP; Krivchenko AI
[Ti] Título:[A current viewpoint on structure and evolution of collagens. II. The fibril-associated collagens with interrupted triple helices].
[So] Source:Zh Evol Biokhim Fiziol;50(4):245-54, 2014 Jul-Aug.
[Is] ISSN:0044-4529
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:Fibril-associated collagens with interrupted triple helices (FACITs) form one of the subfamilies of collagen family. Being minor components of connective tissues in multicellular animals, FACITs play an important role in structurization of extracellular matrix whose peculiarities determine differences among tissues. FACITs take part in regulation of the sizes of banded collagen fibrils and are also a link between diverse components of extracellular matrix and cells in different tissues. The functional characteristics of FACIT molecules are determined by peculiarities of α-chain structure (interruptions in collagenous domains and module structure of N-terminal noncollagenous regions), trimeric molecules (trimerization domains), and supramolecular assemblies (mainly, association with banded fibrils and inability to form homopolymeric suprastructural aggregates). The evolution of FACITs is also discussed. A hypothetical model of structural changes leading to formation of FACIT subfamily is propounded.
[Mh] Termos MeSH primário: Evolução Molecular
Colágenos Associados a Fibrilas/química
[Mh] Termos MeSH secundário: Animais
Colágenos Associados a Fibrilas/genética
Colágenos Associados a Fibrilas/metabolismo
Seres Humanos
Estrutura Terciária de Proteína
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Fibril-Associated Collagens)
[Em] Mês de entrada:1504
[Cu] Atualização por classe:150317
[Lr] Data última revisão:
150317
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150318
[St] Status:MEDLINE


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[PMID]:24801612
[Au] Autor:Chiquet M; Birk DE; Bönnemann CG; Koch M
[Ad] Endereço:Department of Orthodontics and Dentofacial Orthopedics, School of Dental Medicine, University of Bern, Bern, Switzerland. Electronic address: matthias.chiquet@zmk.unibe.ch.
[Ti] Título:Collagen XII: Protecting bone and muscle integrity by organizing collagen fibrils.
[So] Source:Int J Biochem Cell Biol;53:51-4, 2014 Aug.
[Is] ISSN:1878-5875
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Collagen XII, largest member of the fibril-associated collagens with interrupted triple helix (FACIT) family, assembles from three identical α-chains encoded by the COL12A1 gene. The molecule consists of three threadlike N-terminal noncollagenous NC3 domains, joined by disulfide bonds and a short interrupted collagen triple helix toward the C-terminus. Splice variants differ considerably in size and properties: "small" collagen XIIB (220 kDa subunit) is similar to collagen XIV, whereas collagen XIIA (350 kDa) has a much larger NC3 domain carrying glycosaminoglycan chains. Collagen XII binds to collagen I-containing fibrils via its collagenous domain, whereas its large noncollagenous arms interact with other matrix proteins such as tenascin-X. In dense connective tissues and bone, collagen XII is thought to regulate organization and mechanical properties of collagen fibril bundles. Accordingly, recent findings show that collagen XII mutations cause Ehlers-Danlos/myopathy overlap syndrome associated with skeletal abnormalities and muscle weakness in mice and humans.
[Mh] Termos MeSH primário: Autoantígenos/genética
Colágeno Tipo XII/genética
Desenvolvimento Muscular/genética
Colágenos não Fibrilares/genética
Osteogênese/genética
[Mh] Termos MeSH secundário: Animais
Autoantígenos/metabolismo
Colágeno Tipo XII/metabolismo
Contratura/genética
Contratura/patologia
Síndrome de Ehlers-Danlos/genética
Síndrome de Ehlers-Danlos/patologia
Colágenos Associados a Fibrilas/genética
Colágenos Associados a Fibrilas/metabolismo
Seres Humanos
Camundongos
Músculos/patologia
Distrofias Musculares/congênito
Distrofias Musculares/genética
Distrofias Musculares/patologia
Colágenos não Fibrilares/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, N.I.H., INTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Autoantigens); 0 (COL12A1 protein, human); 0 (Collagen Type XII); 0 (Fibril-Associated Collagens); 0 (Non-Fibrillar Collagens); 0 (collagen type XVII)
[Em] Mês de entrada:1503
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140508
[St] Status:MEDLINE


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[PMID]:24731707
[Au] Autor:Zimmermann EA; Gludovatz B; Schaible E; Busse B; Ritchie RO
[Ad] Endereço:Materials Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
[Ti] Título:Fracture resistance of human cortical bone across multiple length-scales at physiological strain rates.
[So] Source:Biomaterials;35(21):5472-81, 2014 Jul.
[Is] ISSN:1878-5905
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:While most fracture-mechanics investigations on bone have been performed at low strain rates, physiological fractures invariably occur at higher loading rates. Here, at strain rates from 10(-5) to 10(-1) s(-1), we investigate deformation and fracture in bone at small length-scales using in situ small-angle x-ray scattering (SAXS) to study deformation in the mineralized collagen fibrils and at the microstructural level via fracture-mechanics experiments to study toughening mechanisms generating toughness through crack-tip shielding. Our results show diminished bone toughness at increasing strain rates as cracks penetrate through the osteons at higher strain rates instead of deflecting at the cement lines, which is a prime toughening mechanism in bone at low strain rates. The absence of crack deflection mechanisms at higher strain rates is consistent with lower intrinsic bone matrix toughness. In the SAXS experiments, higher fibrillar strains at higher strain rates suggest less inelastic deformation and thus support a lower intrinsic toughness. The increased incidence of fracture induced by high strain rates can be associated with a loss in toughness in the matrix caused by a strain rate induced stiffening of the fibril ductility, i.e., a "locking-up" of the viscous sliding and sacrificial bonding mechanisms, which are the origin of inelastic deformation (and toughness) in bone at small length-scales.
[Mh] Termos MeSH primário: Matriz Óssea/diagnóstico por imagem
Fraturas Ósseas/diagnóstico por imagem
Difração de Raios X/métodos
[Mh] Termos MeSH secundário: Fenômenos Biomecânicos
Matriz Óssea/fisiologia
Colágenos Associados a Fibrilas/química
Seres Humanos
Masculino
Microscopia Eletrônica de Varredura
Meia-Idade
Radiografia
Espalhamento a Baixo Ângulo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Fibril-Associated Collagens)
[Em] Mês de entrada:1412
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140416
[St] Status:MEDLINE


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[PMID]:24443029
[Au] Autor:Mienaltowski MJ; Birk DE
[Ad] Endereço:Departments of Molecular Pharmacology & Physiology and Orthopaedics & Sports Medicine, University of South Florida, Morsani College of Medicine, 12901 Bruce B. Downs Blvd., MDC8, Tampa, FL, 33612, USA.
[Ti] Título:Mouse models in tendon and ligament research.
[So] Source:Adv Exp Med Biol;802:201-30, 2014.
[Is] ISSN:0065-2598
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mutant mouse models are valuable resources for the study of tendon and ligament biology. Many mutant mouse models are used because their manifested phenotypes mimic clinical pathobiology for several heritable disorders, such as Ehlers-Danlos Syndrome and Osteogenesis Imperfecta. Moreover, these models are helpful for discerning roles of specific genes in the development, maturation, and repair of musculoskeletal tissues. There are several categories of genes with essential roles in the synthesis and maintenance of tendon and ligament structures. The form and function of these tissues depend highly upon fibril-forming collagens, the primary extracellular macromolecules of tendons and ligaments. Models for these fibril-forming collagens, as well as for regulatory molecules like FACITs and SLRPs, are important for studying fibril assembly, growth, and maturation. Additionally, mouse models for growth factors and transcription factors are useful for defining regulation of cell proliferation, cell differentiation, and cues that stimulate matrix synthesis. Models for membrane-bound proteins assess the roles of cell-cell communication and cell-matrix interaction. In some cases, special considerations need to be given to spatio-temporal control of a gene in a model. Thus, conditional and inducible mouse models allow for specific regulation of genes of interest. Advances in mouse models have provided valuable tools for gaining insight into the form and function of tendons and ligaments.
[Mh] Termos MeSH primário: Colágeno/genética
Síndrome de Ehlers-Danlos/genética
Colágenos Associados a Fibrilas/genética
Ligamentos/metabolismo
Osteogênese Imperfeita/genética
Tendões/metabolismo
[Mh] Termos MeSH secundário: Animais
Modelos Animais de Doenças
Síndrome de Ehlers-Danlos/metabolismo
Síndrome de Ehlers-Danlos/patologia
Fibrilinas
Seres Humanos
Peptídeos e Proteínas de Sinalização Intercelular/genética
Ligamentos/patologia
Camundongos
Camundongos Transgênicos
Proteínas dos Microfilamentos/genética
Osteogênese Imperfeita/metabolismo
Osteogênese Imperfeita/patologia
Isoformas de Proteínas/genética
Tendões/patologia
Fatores de Transcrição/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fibril-Associated Collagens); 0 (Fibrillins); 0 (Intercellular Signaling Peptides and Proteins); 0 (Microfilament Proteins); 0 (Protein Isoforms); 0 (Transcription Factors); 9007-34-5 (Collagen)
[Em] Mês de entrada:1405
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140121
[St] Status:MEDLINE
[do] DOI:10.1007/978-94-007-7893-1_13



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