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[PMID]:28905442
[Au] Autor:Kielty CM
[Ad] Endereço:Wellcome Trust Centre for Cell-Matrix Research, School of Biological Sciences, Faculty of Biology, Medicine and Health, University of Manchester, Manchester, UK.
[Ti] Título:Fell-Muir Lecture: Fibrillin microfibrils: structural tensometers of elastic tissues?
[So] Source:Int J Exp Pathol;98(4):172-190, 2017 Aug.
[Is] ISSN:1365-2613
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Fibrillin microfibrils are indispensable structural elements of connective tissues in multicellular organisms from early metazoans to humans. They have an extensible periodic beaded organization, and support dynamic tissues such as ciliary zonules that suspend the lens. In tissues that express elastin, including blood vessels, skin and lungs, microfibrils support elastin deposition and shape the functional architecture of elastic fibres. The vital contribution of microfibrils to tissue form and function is underscored by the heritable fibrillinopathies, especially Marfan syndrome with severe elastic, ocular and skeletal tissue defects. Research since the early 1990s has advanced our knowledge of biology of microfibrils, yet understanding of their mechanical and homeostatic contributions to tissues remains far from complete. This review is a personal reflection on key insights, and puts forward the conceptual hypothesis that microfibrils are structural 'tensometers' that direct cells to monitor and respond to altered tissue mechanics.
[Mh] Termos MeSH primário: Tecido Elástico/patologia
Matriz Extracelular/patologia
Fibrilinas/metabolismo
Síndrome de Marfan/patologia
Microfibrilas/patologia
Proteínas dos Microfilamentos/metabolismo
[Mh] Termos MeSH secundário: Animais
Tecido Elástico/metabolismo
Matriz Extracelular/metabolismo
Seres Humanos
Síndrome de Marfan/metabolismo
Microfibrilas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Fibrillins); 0 (Microfilament Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170915
[St] Status:MEDLINE
[do] DOI:10.1111/iep.12239


  2 / 1410 MEDLINE  
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[PMID]:28165551
[Au] Autor:Kowalczyk K; Franik G; Kowalczyk D; Pluta D; Blukacz L; Madej P
[Ad] Endereço:Department of Gynaecological Endocrinology, Medical Faculty in Katowice, Medical University of Silesia, Katowice, Poland. karolina.kowalczyk74@gmail.com.
[Ti] Título:Thyroid disorders in polycystic ovary syndrome.
[So] Source:Eur Rev Med Pharmacol Sci;21(2):346-360, 2017 Jan.
[Is] ISSN:2284-0729
[Cp] País de publicação:Italy
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: Thyroid disorders, especially Hashimoto's thyroiditis (HT), are observed significantly more often in patients with polycystic ovary syndrome (PCOS) than in the general population - approximately 27% and 8%, respectively. This is extremely important in young women, because both disorders are connected with fertility problems. As HT and PCOS occur together, fertility problems may become a serious clinical issue in these patients. MATERIALS AND METHODS: A systematic literature review in PubMed of PCOS- and HT-related articles in English, published until December 2015 was conducted. RESULTS: The reasons for joint prevalence still remain unclear. Genetic and autoimmune backgrounds are recognized to be possible common etiological factors. Three genetic polymorphisms have been described to play a role in PCOS as well as in HT. They are polymorphism of the gene for fibrillin 3 (FBN3) regulating the activity of transforming growth factor-b (TGF-b) and regulatory T cell levels, gonadotropin-releasing hormone receptor (GnRHR) polymorphism and CYP1B1 polymorphism standing for estradiol hydroxylation. High estrogen-to-progesterone ratios owing to anovulatory cycles, as well as high estrogen levels during prenatal life, disrupt development of the thymus and its function in maintaining immune tolerance, and are suspected to enhance autoimmune response in PCOS. Vitamin D deficiency could be also involved in the pathogenesis of HT and PCOS. CONCLUSIONS: The above-mentioned common etiological factors associated with fertility problems in HT and PCOS require further research.
[Mh] Termos MeSH primário: Doença de Hashimoto/epidemiologia
Síndrome do Ovário Policístico/epidemiologia
[Mh] Termos MeSH secundário: Citocromo P-450 CYP1B1/genética
Feminino
Fibrilinas/genética
Seres Humanos
Receptores LHRH/genética
Fator de Crescimento Transformador beta/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (FBN3 protein, human); 0 (Fibrillins); 0 (GNRHR protein, human); 0 (Receptors, LHRH); 0 (Transforming Growth Factor beta); EC 1.14.14.1 (CYP1B1 protein, human); EC 1.14.14.1 (Cytochrome P-450 CYP1B1)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170724
[Lr] Data última revisão:
170724
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170207
[St] Status:MEDLINE


  3 / 1410 MEDLINE  
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[PMID]:27455822
[Au] Autor:Penpattharakul W; Pithukpakorn M
[Ti] Título:Revised Ghent Criteria is Comparable to Original Diagnostic Criteria for Marfan Syndrome with Increased Ability to Clinically Diagnose Related Disorders.
[So] Source:J Med Assoc Thai;99(1):34-9, 2016 Jan.
[Is] ISSN:0125-2208
[Cp] País de publicação:Thailand
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Marfan syndrome (MFS) is an autosomal dominant connective tissue disorder with major features in cardiovascular ocular and skeletal systems. Due to its genetic heterogeneity and variable expressivity, Ghent nosology was established for clinical diagnosis of MFS. In 2010, Ghent diagnostic criteria were revised to better diagnose MS and categorize its related disorders. There is no previous clinical comparison between the original and revised Ghent criteria for diagnosis of MFS in Thai patients. OBJECTIVE: To compare application and efficacy of Ghent and revised Ghent criteria in adult Thai patients with clinical suspicion of MFS. MATERIAL AND METHOD: This study was a retrospective analysis of patients with clinical suspicion of MFS who attended the Medical Genetics Clinic, Siriraj Hospital between January 2003 and December 2013. Patients were clinically examined for diagnosis of MFS using both the Ghent and revised Ghent criteria. Multidisciplinary data, including physical examination, echocardiography, slit-lamp examination, and genetic testing, were analyzed. RESULTS: Clinical and genetic data of 138 (77 males and 61 females) individuals with clinical suspicion of MFS were reviewed The most common presentation was cardiovascular manifestation. Of 92 patients diagnosed as MFS by original Ghent nosology 70 of those patients (76.1%) were also diagnosed as MFS by revised Ghent criteria. Forty-eight of 138 patients (34.8%) had undergone genetic testing, with FBN1 mutations detected in 23 patients. Twenty-two patients with detectable FBN1 mutations fulfilled both the Ghent and revised Ghent criteria. Of 22 patients whose diagnoses were not fulfilled by revised Ghent nosology, most were due to inadequate systemic score (SS). The use of revised Ghent nosology also facilitated improved diagnosis of MFS-related disorders. CONCLUSION: Revised Ghent nosology has further differentiated MFS from other MFS-related disorders and has further expanded the classification of MFS-related disorders. Genetic testing of FBN1 helps physicians to more accurately diagnose patients with MFS and related disorders.
[Mh] Termos MeSH primário: Ectopia do Cristalino/diagnóstico
Síndrome de Marfan/diagnóstico
Prolapso da Valva Mitral/diagnóstico
Miopia/diagnóstico
Dermatopatias/diagnóstico
[Mh] Termos MeSH secundário: Adolescente
Adulto
Idoso
Feminino
Fibrilina-1
Fibrilinas
Testes Genéticos
Seres Humanos
Masculino
Síndrome de Marfan/genética
Proteínas dos Microfilamentos/genética
Meia-Idade
Mutação
Exame Físico
Estudos Retrospectivos
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (FBN1 protein, human); 0 (Fibrillin-1); 0 (Fibrillins); 0 (Microfilament Proteins)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160727
[St] Status:MEDLINE


  4 / 1410 MEDLINE  
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[PMID]:27455564
[Au] Autor:Rudoi AS; Moskalev AV; Sboitchakov VB
[Ti] Título:[THE ROLE OF TRANSFORMING GROWTH FACTOR-B IN IMMUNOPATHOGENESIS OF DISEASES OF CONNECTIVE TISSUE].
[So] Source:Klin Lab Diagn;61(2):103-6, 2016 Feb.
[Is] ISSN:0869-2084
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:The recent studies of molecular physiology of fibrillin and pathophysiology of inherent disorders of structure and function of connective tissue such as dissection and aneurysm of aorta, myxomatously altered cusps and prolapses of mitral valve, syndrome of hyper-mobility of joints, demonstrated that important role in development of these malformations play alterations of transfer of signals by growth factors and matrix cellular interaction. These conditions under manifesting Marfan's syndrome can be a consequence of anomalies of fibrillin-1 which deficiency unbrakes process of activation of transforming growth factor-ß (TGFß). The involvement of TGFß in pathogenesis of Marfan's syndrome permits consider antagonists of angiotensin-transforming enzymes as potential pharmaceuticals in therapy of this disease. The article presents analysis of publications' data related to this problem.
[Mh] Termos MeSH primário: Aneurisma Dissecante/imunologia
Aneurisma Aórtico/imunologia
Instabilidade Articular/imunologia
Síndrome de Marfan/imunologia
Prolapso da Valva Mitral/imunologia
Fator de Crescimento Transformador beta/imunologia
[Mh] Termos MeSH secundário: Aneurisma Dissecante/tratamento farmacológico
Aneurisma Dissecante/genética
Aneurisma Dissecante/patologia
Inibidores da Enzima Conversora de Angiotensina/uso terapêutico
Aneurisma Aórtico/tratamento farmacológico
Aneurisma Aórtico/genética
Aneurisma Aórtico/patologia
Tecido Conjuntivo/efeitos dos fármacos
Tecido Conjuntivo/imunologia
Tecido Conjuntivo/patologia
Fibrilina-1
Fibrilinas
Regulação da Expressão Gênica
Seres Humanos
Instabilidade Articular/tratamento farmacológico
Instabilidade Articular/genética
Instabilidade Articular/patologia
Síndrome de Marfan/tratamento farmacológico
Síndrome de Marfan/genética
Síndrome de Marfan/patologia
Proteínas dos Microfilamentos/genética
Proteínas dos Microfilamentos/imunologia
Prolapso da Valva Mitral/tratamento farmacológico
Prolapso da Valva Mitral/genética
Prolapso da Valva Mitral/patologia
Peptidil Dipeptidase A/genética
Peptidil Dipeptidase A/imunologia
Transdução de Sinais
Fator de Crescimento Transformador beta/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Angiotensin-Converting Enzyme Inhibitors); 0 (FBN1 protein, human); 0 (Fibrillin-1); 0 (Fibrillins); 0 (Microfilament Proteins); 0 (Transforming Growth Factor beta); EC 3.4.15.1 (ACE protein, human); EC 3.4.15.1 (Peptidyl-Dipeptidase A)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160727
[St] Status:MEDLINE


  5 / 1410 MEDLINE  
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[PMID]:27252363
[Au] Autor:Robertson IB; Rifkin DB
[Ad] Endereço:Departments of Cell Biology, New York University School of Medicine, New York, New York 10016.
[Ti] Título:Regulation of the Bioavailability of TGF-ß and TGF-ß-Related Proteins.
[So] Source:Cold Spring Harb Perspect Biol;8(6), 2016 06 01.
[Is] ISSN:1943-0264
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The bioavailability of members of the transforming growth factor ß (TGF-ß) family is controlled by a number of mechanisms. Bona fide TGF-ß is sequestered into the matrix in a latent state and must be activated before it can bind to its receptors. Here, we review the molecules and mechanisms that regulate the bioavailability of TGF-ß and compare these mechanisms with those used to regulate other TGF-ß family members. We also assess the physiological significance of various latent TGF-ß activators, as well as other extracellular modulators of TGF-ß family signaling, by examining the available in vivo data from knockout mouse models and other biological systems.
[Mh] Termos MeSH primário: Disponibilidade Biológica
Proteínas de Ligação a TGF-beta Latente/metabolismo
Transdução de Sinais/fisiologia
Fator de Crescimento Transformador beta/fisiologia
[Mh] Termos MeSH secundário: Animais
Proteínas de Transporte/metabolismo
Matriz Extracelular/metabolismo
Fibrilinas/metabolismo
Glicosilação
Seres Humanos
Camundongos
Camundongos Knockout
Filogenia
Domínios Proteicos
Multimerização Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; REVIEW
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Fibrillins); 0 (Latent TGF-beta Binding Proteins); 0 (Transforming Growth Factor beta)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170809
[Lr] Data última revisão:
170809
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160603
[St] Status:MEDLINE


  6 / 1410 MEDLINE  
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[PMID]:27222596
[Au] Autor:Bastian NA; Bayne RA; Hummitzsch K; Hatzirodos N; Bonner WM; Hartanti MD; Irving-Rodgers HF; Anderson RA; Rodgers RJ
[Ad] Endereço:Discipline of Obstetrics and GynaecologySchool of Medicine, Robinson Research Institute, The University of Adelaide, Adelaide, South Australia, Australia.
[Ti] Título:Regulation of fibrillins and modulators of TGFß in fetal bovine and human ovaries.
[So] Source:Reproduction;152(2):127-37, 2016 Aug.
[Is] ISSN:1741-7899
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Fibrillins 1-3 are stromal extracellular matrix proteins that play important roles in regulating TGFß activity, which stimulates fibroblasts to proliferate and synthesize collagen. In the developing ovary, the action of stroma is initially necessary for the formation of ovigerous cords and subsequently for the formation of follicles and the surface epithelium of the ovary. FBN3 is highly expressed only in early ovarian development and then it declines. In contrast, FBN1 and 2 are upregulated in later ovarian development. We examined the expression of FBN1-3 in bovine and human fetal ovaries. We used cell dispersion and monolayer culture, cell passaging and tissue culture. Cells were treated with growth factors, hormones or inhibitors to assess the regulation of expression of FBN1-3 When bovine fetal ovarian tissue was cultured, FBN3 expression declined significantly. Treatment with TGFß-1 increased FBN1 and FBN2 expression in bovine fibroblasts, but did not affect FBN3 expression. Additionally, in cultures of human fetal ovarian fibroblasts (9-17weeks gestational age), the expression of FBN1 and FBN2 increased with passage, whereas FBN3 dramatically decreased. Treatment with activin A and a TGFß family signaling inhibitor, SB431542, differentially regulated the expression of a range of modulators of TGFß signaling and of other growth factors in cultured human fetal ovarian fibroblasts suggesting that TGFß signaling is differentially involved in the regulation of ovarian fibroblasts. Additionally, since the changes in FBN1-3 expression that occur in vitro are those that occur with increasing gestational age in vivo, we suggest that the fetal ovarian fibroblasts mature in vitro.
[Mh] Termos MeSH primário: Ativinas/metabolismo
Feto/metabolismo
Fibrilinas/metabolismo
Regulação da Expressão Gênica
Ovário/metabolismo
Fator de Crescimento Transformador beta/metabolismo
[Mh] Termos MeSH secundário: Animais
Bovinos
Células Cultivadas
Feminino
Feto/citologia
Fibrilina-1/metabolismo
Fibrilina-2/metabolismo
Fibroblastos/citologia
Fibroblastos/metabolismo
Seres Humanos
Ovário/citologia
Gravidez
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (FBN1 protein, human); 0 (FBN2 protein, human); 0 (FBN3 protein, human); 0 (Fibrillin-1); 0 (Fibrillin-2); 0 (Fibrillins); 0 (Transforming Growth Factor beta); 0 (activin A); 104625-48-1 (Activins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171025
[Lr] Data última revisão:
171025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160526
[St] Status:MEDLINE
[do] DOI:10.1530/REP-16-0172


  7 / 1410 MEDLINE  
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[PMID]:27026396
[Au] Autor:Jensen SA; Handford PA
[Ad] Endereço:Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, U.K.
[Ti] Título:New insights into the structure, assembly and biological roles of 10-12 nm connective tissue microfibrils from fibrillin-1 studies.
[So] Source:Biochem J;473(7):827-38, 2016 Apr 01.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The 10-12 nm diameter microfibrils of the extracellular matrix (ECM) impart both structural and regulatory properties to load-bearing connective tissues. The main protein component is the calcium-dependent glycoprotein fibrillin, which assembles into microfibrils at the cell surface in a highly regulated process involving specific proteolysis, multimerization and glycosaminoglycan interactions. In higher metazoans, microfibrils act as a framework for elastin deposition and modification, resulting in the formation of elastic fibres, but they can also occur in elastin-free tissues where they perform structural roles. Fibrillin microfibrils are further engaged in a number of cell matrix interactions such as with integrins, bone morphogenetic proteins (BMPs) and the large latent complex of transforming growth factor-ß (TGFß). Fibrillin-1 (FBN1) mutations are associated with a range of heritable connective disorders, including Marfan syndrome (MFS) and the acromelic dysplasias, suggesting that the roles of 10-12 nm diameter microfibrils are pleiotropic. In recent years the use of molecular, cellular and whole-organism studies has revealed that the microfibril is not just a structural component of the ECM, but through its network of cell and matrix interactions it can exert profound regulatory effects on cell function. In this review we assess what is known about the molecular properties of fibrillin that enable it to assemble into the 10-12 nm diameter microfibril and perform such diverse roles.
[Mh] Termos MeSH primário: Tecido Conjuntivo/metabolismo
Nanismo/metabolismo
Síndrome de Marfan/metabolismo
Microfibrilas/metabolismo
Proteínas dos Microfilamentos/metabolismo
Mutação
Osteocondrodisplasias/metabolismo
[Mh] Termos MeSH secundário: Animais
Tecido Conjuntivo/patologia
Nanismo/genética
Nanismo/patologia
Matriz Extracelular/genética
Matriz Extracelular/metabolismo
Fibrilina-1
Fibrilinas
Seres Humanos
Síndrome de Marfan/genética
Síndrome de Marfan/patologia
Microfibrilas/genética
Microfibrilas/patologia
Proteínas dos Microfilamentos/genética
Osteocondrodisplasias/genética
Osteocondrodisplasias/patologia
Fator de Crescimento Transformador beta/genética
Fator de Crescimento Transformador beta/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (FBN1 protein, human); 0 (Fibrillin-1); 0 (Fibrillins); 0 (Microfilament Proteins); 0 (Transforming Growth Factor beta)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160331
[St] Status:MEDLINE
[do] DOI:10.1042/BJ20151108


  8 / 1410 MEDLINE  
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[PMID]:27003297
[Au] Autor:Uriarte JJ; Meirelles T; Gorbenko Del Blanco D; Nonaka PN; Campillo N; Sarri E; Navajas D; Egea G; Farré R
[Ad] Endereço:Unitat Biofísica i Bioenginyeria, Facultat de Medicina, Universitat de Barcelona, Barcelona, Spain.
[Ti] Título:Early Impairment of Lung Mechanics in a Murine Model of Marfan Syndrome.
[So] Source:PLoS One;11(3):e0152124, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Early morbidity and mortality in patients with Marfan syndrome (MFS) -a connective tissue disease caused by mutations in fibrillin-1 gene- are mainly caused by aorta aneurysm and rupture. However, the increase in the life expectancy of MFS patients recently achieved by reparatory surgery promotes clinical manifestations in other organs. Although some studies have reported respiratory alterations in MFS, our knowledge of how this connective tissue disease modifies lung mechanics is scarce. Hence, we assessed whether the stiffness of the whole lung and of its extracellular matrix (ECM) is affected in a well-characterized MFS mouse model (FBN1C1039G/+). The stiffness of the whole lung and of its ECM were measured by conventional mechanical ventilation and atomic force microscopy, respectively. We studied 5-week and 9-month old mice, whose ages are representative of early and late stages of the disease. At both ages, the lungs of MFS mice were significantly more compliant than in wild type (WT) mice. By contrast, no significant differences were found in local lung ECM stiffness. Moreover, histopathological lung evaluation showed a clear emphysematous-like pattern in MFS mice since alveolar space enlargement was significantly increased compared with WT mice. These data suggest that the mechanism explaining the increased lung compliance in MFS is not a direct consequence of reduced ECM stiffness, but an emphysema-like alteration in the 3D structural organization of the lung. Since lung alterations in MFS are almost fully manifested at an early age, it is suggested that respiratory monitoring could provide early biomarkers for diagnosis and/or follow-up of patients with the Marfan syndrome.
[Mh] Termos MeSH primário: Pulmão/patologia
Síndrome de Marfan/patologia
[Mh] Termos MeSH secundário: Animais
Modelos Animais de Doenças
Matriz Extracelular/genética
Matriz Extracelular/patologia
Fibrilina-1
Fibrilinas
Síndrome de Marfan/genética
Camundongos
Camundongos Endogâmicos C57BL
Proteínas dos Microfilamentos/genética
Mutação/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fbn1 protein, mouse); 0 (Fibrillin-1); 0 (Fibrillins); 0 (Microfilament Proteins)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160323
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0152124


  9 / 1410 MEDLINE  
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[PMID]:26969163
[Au] Autor:Raynaud S; Ragel P; Rojas T; Mérida Á
[Ad] Endereço:From the Instituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas, University of Sevilla, Avenida Américo Vespucio 49, 41092 Sevilla, Spain.
[Ti] Título:The N-terminal Part of Arabidopsis thaliana Starch Synthase 4 Determines the Localization and Activity of the Enzyme.
[So] Source:J Biol Chem;291(20):10759-71, 2016 May 13.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Starch synthase 4 (SS4) plays a specific role in starch synthesis because it controls the number of starch granules synthesized in the chloroplast and is involved in the initiation of the starch granule. We showed previously that SS4 interacts with fibrillins 1 and is associated with plastoglobules, suborganelle compartments physically attached to the thylakoid membrane in chloroplasts. Both SS4 localization and its interaction with fibrillins 1 were mediated by the N-terminal part of SS4. Here we show that the coiled-coil region within the N-terminal portion of SS4 is involved in both processes. Elimination of this region prevents SS4 from binding to fibrillins 1 and alters SS4 localization in the chloroplast. We also show that SS4 forms dimers, which depends on a region located between the coiled-coil region and the glycosyltransferase domain of SS4. This region is highly conserved between all SS4 enzymes sequenced to date. We show that the dimerization seems to be necessary for the activity of the enzyme. Both dimerization and the functionality of the coiled-coil region are conserved among SS4 proteins from phylogenetically distant species, such as Arabidopsis and Brachypodium This finding suggests that the mechanism of action of SS4 is conserved among different plant species.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/enzimologia
Sintase do Amido/metabolismo
[Mh] Termos MeSH secundário: Arabidopsis/genética
Proteínas de Arabidopsis/química
Proteínas de Arabidopsis/genética
Brachypodium/enzimologia
Brachypodium/genética
Sequência Conservada
Fibrilinas/metabolismo
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Proteínas de Plantas/química
Proteínas de Plantas/genética
Proteínas de Plantas/metabolismo
Plantas Geneticamente Modificadas
Domínios e Motivos de Interação entre Proteínas
Multimerização Proteica
Amido/biossíntese
Sintase do Amido/química
Sintase do Amido/genética
Tilacoides/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Fibrillins); 0 (Peptide Fragments); 0 (Plant Proteins); 9005-25-8 (Starch); EC 2.4.1.21 (Starch Synthase); EC 2.4.1.21 (starch synthase IV, Arabidopsis)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:170513
[Lr] Data última revisão:
170513
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160313
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.698332


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[PMID]:26945878
[Au] Autor:Schiavinato A; Keene DR; Wohl AP; Corallo D; Colombatti A; Wagener R; Paulsson M; Bonaldo P; Sengle G
[Ad] Endereço:Center for Biochemistry, Medical Faculty, University of Cologne, Cologne, Germany; Department of Molecular Medicine, University of Padova, Padova, Italy.
[Ti] Título:Targeting of EMILIN-1 and EMILIN-2 to Fibrillin Microfibrils Facilitates their Incorporation into the Extracellular Matrix.
[So] Source:J Invest Dermatol;136(6):1150-60, 2016 Jun.
[Is] ISSN:1523-1747
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Elastin microfibril interface-located proteins (EMILINs) 1 and 2 belong to a family of structurally related extracellular glycoproteins with unique functions in the extracellular space, such as modulation of pro-transforming growth factor-ß processing, activation of the extrinsic apoptotic pathway, and regulation of Hedgehog and Wnt ligand bioavailability. However, little is known about how EMILINs may exert their extracellular functions. We therefore investigated the spatiotemporal localization and deposition of EMILIN-1 and -2 within the extracellular space. By using immunoelectron and immunofluorescence microscopy together with biochemical extraction, we showed that EMILIN-1 and -2 are targeted to fibrillin microfibrils in the skin. In addition, during skin wound healing and in vitro matrix fiber assembly by primary dermal fibroblasts, EMILIN-1 and -2 are deposited on and coregulated with fibrillin. Analysis of wounds and mouse embryonic fibroblast cultures showed that EMILIN-1 and -2 network formation also requires the presence of fibronectin. Disruption of microfibrils in fibrillin-1-deficient mice leads to fragmentation of the EMILIN-1 and -2 networks, suggesting an involvement of EMILINs in fibrillin-related skin disorders. The addition of EMILINs to the ligand repertoire of fibrillin strengthens the concept of fibrillin microfibrils as extracellular scaffolds integrating cellular force transmission and growth factor bioactivity.
[Mh] Termos MeSH primário: Matriz Extracelular/metabolismo
Fibroblastos/metabolismo
Glicoproteínas/metabolismo
Glicoproteínas de Membrana/metabolismo
Ferimentos e Lesões/patologia
[Mh] Termos MeSH secundário: Animais
Biomarcadores/metabolismo
Células Cultivadas
Modelos Animais de Doenças
Fibrilina-1/genética
Fibrilinas/metabolismo
Fibroblastos/citologia
Camundongos
Camundongos Mutantes
RNA Mensageiro/metabolismo
Reação em Cadeia da Polimerase em Tempo Real/métodos
Pele/lesões
Cicatrização/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Emilin2 protein, mouse); 0 (Fbn1 protein, mouse); 0 (Fibrillin-1); 0 (Fibrillins); 0 (Glycoproteins); 0 (Membrane Glycoproteins); 0 (RNA, Messenger); 0 (elastin microfibril interface located protein)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170913
[Lr] Data última revisão:
170913
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160307
[St] Status:MEDLINE



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