Base de dados : LILACS
Pesquisa : D08.811.277.656.300.480.525.700.200 [Categoria DeCS]
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Silva, Léa Assed Bezerra da
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Id: biblio-888652
Autor: Küchler, Erika Calvano; Barreiros, Driely; Silva, Raphaela Oliveira da; Abreu, Júlia Guimarães Barcellos de; Teixeira, Ellen Cardoso; Silva, Raquel Assed Bezerra da; Silva, Lea Assed Bezerra da; Nelson Filho, Paulo; Romano, Fábio Lourenço; Granjeiro, José Mauro; Antunes, Lívia Azeredo Alves; Antunes, Leonardo Santos.
Título: Genetic Polymorphism in MMP9 May Be Associated With Anterior Open Bite in Children
Fonte: Braz. dent. j;28(3):277-280, May-June 2017. tab.
Idioma: en.
Projeto: CNPq; . FAPERJ; . FAPESP.
Resumo: Abstract Anterior open bite (AOB) has a multifactorial etiology caused by the interaction of sucking habits and genetic factors. The aim of this study was to evaluate the association between AOB and polymorphisms in genes that encode Matrix metalloproteinases (MMPs) and their tissue inhibitors (TIMPs). Four hundred and seventy-two children that presented at least one sucking habit were evaluated. Children were examined clinically for the presence of AOB. Genomic DNA was extracted from saliva. Genotyping of the selected polymorphisms in MMP2, MMP3, MMP9, TIMP1 and TIMP2 was carried out by real-time PCR using the TaqMan method. Allele and genotype frequencies were compared between the groups with and without AOB using the PLINK® software in a free and in a recessive model using a chi-square test. Logistic regression analysis was implemented (p≤0.05). Two hundred nineteen children had AOB while 253 did not. The polymorphism rs17576 in MMP9 was significantly associated with AOB (p=0.009). In a recessive model GG genotype was a protective factor for AOB (p=0.014; OR 4.6, 95%CI 1.3-16.2). In the logistic regression analysis, none of the genes was associated with AOB. In conclusion, the polymorphism rs17576 (glutamine for arginine substitution) in MMP9 was a protective factor for AOB.

Resumo A mordida aberta anterior apresenta uma etiologia multifatorial causada pela interação entre hábitos de sucção e fatores genéticos. O objetivo deste estudo foi avaliar a associação entre mordida aberta anterior e polimorfismo nos genes que codificam as metaloproteinases da matriz (MMPs) e seus inibidores teciduais (TIMPs). Foram avaliadas 472 crianças que apresentvam pelo menos um hábito de sucção. As crianças foram clinicamente examinadas para avaliar a presença de mordida aberta anterior. DNA genômico foi extraído da saliva. A genotipagem dos polimorfismos selecionados em MMP2, MMP3, MMP9, TIMP1 e TIMP2 foi realizada por PCR em tempo real, usando o método de TaqMan. As frequências alélicas e genotípicas foram comparadas entre os grupos com e sem mordida aberta anterior usando o software PLINK®. Duzentas e dezenove crianças apresentavam mordida aberta anterior enquanto 253 não a apresentavam. O polimorfismo rs17576 em MMP9 estava significativamente associado com mordida aberta anterior (p=0,009). No modelo recessivo (GG versus AG+AA) o genótipo GG foi um fator protetor para mordida aberta anterior (p=0,014; OR 4,6; 95%CI 1,3- 16,2). Concluindo, o polimorfismo rs17576 (substituição de glutamina por arginina) em MMP9 está associado com mordida aberta anterior. Os resultados obtidos suportam a hipótese de que fatores genéticos estão envolvidos com a etiologia da mordida aberta anterior.
Descritores: Metaloproteinase 9 da Matriz/genética
Polimorfismo de Nucleotídeo Único
Mordida Aberta/etiologia
-Metaloproteinase 3 da Matriz/genética
Inibidor Tecidual de Metaloproteinase-1/genética
Inibidor Tecidual de Metaloproteinase-2/genética
Metaloproteinase 2 da Matriz/genética
Mordida Aberta/genética
Reação em Cadeia da Polimerase em Tempo Real
Sucção de Dedo
Frequência do Gene
Genótipo
Modelos Genéticos
Limites: Seres Humanos
Masculino
Feminino
Pré-Escolar
Criança
Responsável: BR1.1 - BIREME


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Id: biblio-910864
Autor: Poonja, PA; Sattur, AP; Burde, KN; Hiremath, SV.
Título: A study on genetic polymorphism in Matrix Metalloproteinases-3 in oral submucous fibrosis patients and in healthy individuals
Fonte: Appl. cancer res;37:1-12, 2017. tab, ilus.
Idioma: en.
Resumo: Background: OSF is a potentially malignant condition affecting the oral cavity and oropharynx. MMP-3 also known as Stromelysin -I is a key member of the MMP family which is responsible for degradation of collagen type II,IV,V,IX and X, proteoglycans, gelatins, fibronectin, laminin and elastin. It plays an important role in activation of pro MMP-1 into the active form of MMP-1 in malignant tissues. MMP-3 expression is low in normal tissues but it is altered during tumour formation, where remodeling of ECM is required. Purpose of the study: To assess the association of single-nucleotide polymorphisms, Adenosine (Insertion/Deletion) in -1171 5A > 6A in the MMP-3 promoter regions of patients with oral submucous fibrosis and in healthy individuals (controls). Methods: Thirty cases of OSF were categorized according to Khanna et al classification into four groups and Twenty age and sex matched controls were included in the study. Blood samples were collected in EDTA coated vacutainers and PCR restriction analysis was done. A statistical analysis was done using Chi-square test and Fisher's exact test to assess the frequency and association of the alleles in the case-control group. Results: The result showed a statistical significance difference between the duration of habit and disease severity with polymorphisms. The result also showed a higher frequency of the 5A allele in the study group as compared to the controls. Conclusion: A long-term follow up of these patients is mandatory to see the prognosis and their susceptibility to malignancy. The positive outcome of an association of the disease with polymorphisms would result in the development of potential diagnostic and therapeutic possibilities in potentially malignant and malignant lesions (AU)
Descritores: Metaloproteinase 3 da Matriz
Boca
Fibrose Oral Submucosa
Orofaringe
Polimorfismo Genético
Limites: Seres Humanos
Masculino
Feminino
Responsável: BR30.1 - Biblioteca


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Id: biblio-875864
Autor: Munhoz, Francielle Boçon de Araujo; Nogara, Paula Regina Bach; Costa Junior, Francisco Rafael da Costa; Branco, Filipe Polese; Santos, Maria Cristina Leme Godoy dos.
Título: Analysis of MMP-3 polymorphism in osseointegrated implant failure
Fonte: Braz. j. oral sci;15(4):304-307, Oct.-Dec. 2016. tab.
Idioma: en.
Resumo: Polymorphisms in matrix metalloproteinases (MMPs) genes have been associated with several pathologies, including dental implant loss. MMP-3 is crucial to the connective tissue remodeling process. The objective of this study was to investigate the possible relationship between -1612 MMP-3 polymorphism and the early implant failure. A sample of 240 non-smokers was divided: test group 120 patients with one or more early failed implants and control group 120 patients with one or more healthy implants. Genomic DNA from oral mucosa was analyzed by PCR-RFLP. No association of early implant loss with genotypes and alleles of the -1612 polymorphism in MMP-3 were found by the Chi-squared test. Only the presence of the -1612 polymorphism of MMP-3 is not a genetic risk factor for early loss of implants (AU)
Descritores: Metaloproteinase 3 da Matriz
Metaloproteases
Polimorfismo Genético
Fatores de Risco
-Implantes Dentários
Limites: Seres Humanos
Masculino
Feminino
Adolescente
Adulto
Responsável: BR218.1 - Biblioteca Carlos Henrique Robertson Liberalli


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Id: biblio-839285
Autor: Wang, CC; Guo, L; Tian, FD; An, N; Luo, L; Hao, RH; Wang, B; Zhou, ZH.
Título: Naringenin regulates production of matrix metalloproteinases in the knee-joint and primary cultured articular chondrocytes and alleviates pain in rat osteoarthritis model
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;50(4):e5714, 2017. tab, graf.
Idioma: en.
Resumo: Inflammation of cartilage is a primary symptom for knee-joint osteoarthritis. Matrix metalloproteinases (MMPs) are known to play an important role in the articular cartilage destruction related to osteoarthritis. Naringenin is a plant-derived flavonoid known for its anti-inflammatory properties. We studied the effect of naringenin on the transcriptional expression, secretion and enzymatic activity of MMP-3 in vivo in the murine monosodium iodoacetate (MIA) osteoarthritis model. The assessment of pain behavior was also performed in the MIA rats. The destruction of knee-joint tissues was analyzed microscopically. Moreover, the effect of naringenin was also studied in vitro in IL-1β activated articular chondrocytes. The transcriptional expression of MMP-3, MMP-1, MMP-13, thrombospondin motifs (ADAMTS-4) and ADAMTS-5 was also studied in primary cultured chondrocytes of rats. Naringenin caused significant reduction in pain behavior and showed marked improvement in the tissue morphology of MIA rats. Moreover, a significant inhibition of MMP-3 expression in MIA rats was observed upon treatment with naringenin. In the in vitro tests, naringenin caused a significant reduction in the transcriptional expression, secretion and enzymatic activity of the studied degradative enzymes. The NF-κB pathway was also found to be inhibited upon treatment with naringenin in vitro. Overall, the study suggests that naringenin alleviated pain and regulated the production of matrix-metalloproteinases via regulation of NF-κB pathway. Thus, naringenin could be a potent therapeutic option for the treatment of osteoarthritis.
Descritores: Anti-Inflamatórios/farmacologia
Artralgia/enzimologia
Condrócitos/enzimologia
Flavanonas/farmacologia
Articulação do Joelho/enzimologia
Metaloproteinase 3 da Matriz/biossíntese
Osteoartrite do Joelho/enzimologia
-Artralgia/tratamento farmacológico
Western Blotting
Proliferação Celular/efeitos dos fármacos
Células Cultivadas
Condrócitos/efeitos dos fármacos
Modelos Animais de Doenças
Expressão Gênica
Interleucina-1beta/análise
Interleucina-1beta/efeitos dos fármacos
Interleucina-1beta/metabolismo
Articulação do Joelho/patologia
Metaloproteinase 3 da Matriz/análise
NF-kappa B/análise
NF-kappa B/efeitos dos fármacos
Inibidor de NF-kappaB alfa/análise
Inibidor de NF-kappaB alfa/efeitos dos fármacos
Osteoartrite do Joelho/tratamento farmacológico
Osteoartrite do Joelho/patologia
Distribuição Aleatória
Ratos Wistar
Reprodutibilidade dos Testes
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Fatores de Tempo
Resultado do Tratamento
Limites: Animais
Masculino
Tipo de Publ: Estudos de Avaliação
Responsável: BR1.1 - BIREME


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Id: lil-186121
Autor: Pardo, A; Selman, M.
Título: Matrix metalloproteinases and lung injury
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;29(9):1109-15, Sept. 1996.
Idioma: en.
Conferência: Apresentado em: Brazilian Symposium on Extracellular Matrix, 4, Angra dos Reis, Sept. 8-11, 1996.
Resumo: The dynamic equilibrium of extracellular matrix (ECM) under different physiological conditions is a consequence of the balance between the regulation of synthesis and degradation of ECM components. Matrix metalloproteinases (MMPs), a family of structurally related zinc-dependent endopeptidases, are the physiological mediators of matrix remodeling. The expression and activity of these enzymes are highly regulated at several intra- and extracellular levels, so that in vivo enzymatic activity is the final result of a complex series of events including gene expression, zymogen activation, matrix binding, and enzymatic inhibition. MMPs are expressed at low levels in normal adult tissues, and their upregulation appears to play an important role in the development of a number of pathological processes. In acute lung injury, a disorder characterized by a severe disruption of the gas exchange alveolo-capillary structures, the upregulation of interstitial collagenase and gelatinases A and B strongly suggests that MMPs contribute to acute lung damage by facilitating the migration of inflammatory cells, as well as to the disruption of basement membrane components and extracellular matrix remodeling.
Descritores: Matriz Extracelular/enzimologia
Técnicas In Vitro
Pneumopatias/enzimologia
Metaloproteases/metabolismo
-Colagenases/química
Gelatinases/química
Metaloproteinase 3 da Matriz/química
Metaloproteases/classificação
Limites: Seres Humanos
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: BR1.1 - BIREME



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