RESUMEN
The hypothesis that physiological changes in women can affect periodontal tissues is the subject of this study, and inflammatory markers such as matrix metalloproteinase-8 can measure susceptibility to inflammation. The study aimed to analyze MMP-8 levels in periodontal sites of postpartum women and women without a history of pregnancy, comparing health parameters and periodontal disease. This is a case-control study with 40 participants, 20 cases (women in the postpartum period) and 20 controls (women without any pregnancy), who underwent clinical periodontal examination and the collection of crevicular gingival fluid. The ELISA test was used to detect MMP-8 levels. Postpartum women had worse periodontal parameters, such as bleeding index on probing, number of sites with CAL ≥ 3, and fewer teeth present. In the group of women without a history of pregnancy, a significantly lower MMP-8 level was observed in healthy sites and a higher one was observed in periodontal pockets (p < 0.01). In contrast, in postpartum women, MMP-8 levels were elevated in both healthy sites and periodontal pockets (p > 0.01). The MMP-8 levels in gingival fluid appear to be related to periodontal clinical parameters and may be a possible marker of enzymatic changes involved in periodontal tissue destruction in postpartum women.
Asunto(s)
Líquido del Surco Gingival , Metaloproteinasa 8 de la Matriz , Periodo Posparto , Humanos , Femenino , Metaloproteinasa 8 de la Matriz/metabolismo , Metaloproteinasa 8 de la Matriz/análisis , Adulto , Estudios de Casos y Controles , Líquido del Surco Gingival/enzimología , Embarazo , Enfermedades Periodontales/enzimología , Biomarcadores/metabolismo , Adulto JovenRESUMEN
Periodontitis are infectious diseases characterized by immune-mediated destruction of periodontal supporting tissues and tooth loss. Matrix metalloproteinases (MMPs) are key proteases involved in destructive periodontal diseases. The study and interest in MMP has been fuelled by emerging evidence demonstrating the broad spectrum of molecules that can be cleaved by them and the myriad of biological processes that they can potentially regulate. The huge complexity of MMP functions within the 'protease web' is crucial for many physiologic and pathologic processes, including immunity, inflammation, bone resorption, and wound healing. Evidence points out that MMPs assemble in activation cascades and besides their classical extracellular matrix substrates, they cleave several signalling molecules-such as cytokines, chemokines, and growth factors, among others-regulating their biological functions and/or bioavailability during periodontal diseases. In this review, we provide an overview of emerging evidence of MMPs as regulators of periodontal inflammation.
Asunto(s)
Inflamación/enzimología , Metaloproteinasas de la Matriz/metabolismo , Enfermedades Periodontales/enzimología , Activación Enzimática , Humanos , Modelos Biológicos , Transducción de SeñalRESUMEN
La Fosfatasa Alcalina Ósea (FAO) es una isoforma de la Fosfatasa Alcalina (FAL). La medición de su actividad en saliva es una medida indirecta del proceso de formación ósea, más sensible y específica que la FAL. La catepsina K es la principal colagenasa del proceso de resorción ósea, es capaz de degradar al colágeno tipo I en varios sitios dando lugar a pequeños péptidos N- y C- terminales. El telopéptido C-terminal (CTx) es el marcador más sensible y específico en el aumento de la resorción ósea, ya que el colágeno tipo I constituye más del 90 por ciento de la matriz orgánica del hueso...
Asunto(s)
Humanos , Biomarcadores , Remodelación Ósea/fisiología , Enfermedades Periodontales/fisiopatología , Catepsina K/fisiología , Enfermedades Periodontales/enzimología , Enfermedades Periodontales/inmunología , Fosfatasa Alcalina/análisis , Matriz Ósea/fisiología , Resorción Ósea/fisiopatología , Saliva/enzimologíaRESUMEN
Molecular mechanisms responsible for periodontal disease (PD) and its worsening in type 1 Diabetes Mellitus (DM1) remain unknown. Cytokine profile and expression levels of collagenases, Mmp14, and tissue inhibitors were determined, as were the numbers of neutrophils and macrophages in combined streptozotocin-induced DM1 and ligature-induced PD models. Increased IL-23 (80-fold) and Mmp8 expression (25-fold) was found in DM1. Ligature resulted in an IL-1ß/IL-6 profile, increased expression of Mmp8, Mmp13, and Mmp14 (but not Mmp1), and transient expression of Timp1 and Reck in non-diabetics. PD in DM1 involved IL-1ß (but not IL-6) and IL-23/IL-17, reduced IL-6 and IL-10, sustained Mmp8 and Mmp14, increased Mmp13 and reduced Reck expression in association with 20-fold higher counts of neutrophils and macrophages. IL-23 and Mmp8 expression are hallmarks of DM1. In association with the IL-1/IL-6 (Th1) response in PD, one found a secondary IL-17 (Th17) pathway in non-diabetic rats. Low IL-6/TNF-α suggest that the Th1 response was compromised in DM1, while IL-17 indicates a prevalence of the Th17 pathway, resulting in high neutrophil recruitment. Mmp8, Mmp13, and Mmp14 expression seems important in the tissue destruction during PD in DM1. PD-associated IL-1/IL-6 (Th1), IL-10, and Reck expression are associated with the acute-to-chronic inflammation transition, which is lost in DM1. In conclusion, IL-23/IL-17 are associated with the PD progression in DM1.
Asunto(s)
Diabetes Mellitus Experimental/complicaciones , Diabetes Mellitus Tipo 1/complicaciones , Encía/enzimología , Encía/inmunología , Mediadores de Inflamación/metabolismo , Interleucina-17/metabolismo , Interleucina-23/metabolismo , Metaloproteinasa 14 de la Matriz/metabolismo , Metaloproteinasa 8 de la Matriz/metabolismo , Enfermedades Periodontales/complicaciones , Pérdida de Hueso Alveolar/enzimología , Pérdida de Hueso Alveolar/etiología , Pérdida de Hueso Alveolar/inmunología , Animales , Diabetes Mellitus Experimental/enzimología , Diabetes Mellitus Experimental/genética , Diabetes Mellitus Experimental/inmunología , Diabetes Mellitus Tipo 1/enzimología , Diabetes Mellitus Tipo 1/genética , Diabetes Mellitus Tipo 1/inmunología , Progresión de la Enfermedad , Proteínas Ligadas a GPI/metabolismo , Interleucina-10/metabolismo , Interleucina-1beta/metabolismo , Interleucina-6/metabolismo , Ligadura , Macrófagos/inmunología , Masculino , Metaloproteinasa 13 de la Matriz/metabolismo , Metaloproteinasa 14 de la Matriz/genética , Metaloproteinasa 8 de la Matriz/genética , Diente Molar/cirugía , Infiltración Neutrófila , Neutrófilos/inmunología , Enfermedades Periodontales/enzimología , Enfermedades Periodontales/genética , Enfermedades Periodontales/inmunología , ARN Mensajero/metabolismo , Ratas , Ratas Wistar , Células Th17/inmunología , Factores de Tiempo , Proteínas Supresoras de Tumor/metabolismo , Regulación hacia ArribaRESUMEN
OBJECTIVE: Evaluate expression of MMP-13 during the course of two models experimentally induced periodontal disease in rats. DESIGN: Expression of MMP-13 at mRNA and protein levels was studied, respectively, by reverse transcription polymerase chain reaction (RT-PCR) and Western blotting. Two experimental models were used: LPS injections and ligature placement. 30mug of LPS from Eschericia coli was injected twice a week into the palatal aspect of upper molars. Ligatures were placed at the gingival margin around lower first molars. Controls received injections of PBS vehicle and no ligatures on lower molars. Samples were collected 5, 15 and 30 days after initiation of periodontal disease and processed for extraction of total RNA, total protein, and routinely processed for histology. RESULTS: Both experimental models produced a significant increase on the inflammatory infiltrate that paralleled elevated levels of MMP-13 mRNA and protein at 5 and 15 days. The LPS model was associated with a sustained level of inflammation and increased MMP-13 mRNA throughout the 30 days, whereas the ligature model showed a decrease on the severity of inflammation and MMP-13 mRNA at the 30-day period. Interestingly, MMP-13 protein levels were diametrically contrary to the mRNA levels. CONCLUSION: MMP-13 expression during LPS- and ligature-induced experimental periodontal disease follows the increase on severity of inflammation at the earliest periods. At 30 days, there is a decrease on the severity of inflammation on the ligature model associated with decreased MMP-13 mRNA. There is a lack of transcription-translation coupling of MMP-13 gene in both experimental models.
Asunto(s)
Metaloproteinasa 13 de la Matriz/análisis , Enfermedades Periodontales/enzimología , Animales , Western Blotting , Modelos Animales de Enfermedad , Epitelio/enzimología , Epitelio/patología , Escherichia coli , Regulación Enzimológica de la Expresión Génica/genética , Encía/lesiones , Gingivitis/enzimología , Gingivitis/etiología , Gingivitis/patología , Ligadura/instrumentación , Lipopolisacáridos/efectos adversos , Masculino , Metaloproteinasa 13 de la Matriz/genética , Diente Molar , Enfermedades Periodontales/etiología , Enfermedades Periodontales/patología , Periodontitis/enzimología , Periodontitis/etiología , Periodontitis/patología , ARN Mensajero/análisis , Ratas , Ratas Wistar , Reacción en Cadena de la Polimerasa de Transcriptasa Inversa , Factores de Tiempo , Transcripción Genética/genéticaRESUMEN
The immunopathologic and inflammatory mechanisms involved in periodontal disease (PD) include the participation of host resident, inflammatory cells and chemical mediators. Metalloproteinases (MMPs) and nitric oxide (NO) play essential role in extracellular matrix turnover of periodontal tissue destruction. In this study, by means of RT-PCR through semi-quantitative densitometric scanning methods, the expression of MMPs -2 and -9 and inducible NO synthase (iNOS) was temporally and spatially investigated during the destructive mechanisms of experimentally induced PD in rats. Samples from different periods were microscopically analyzed and compared with the contralateral side (control). Our results showed significant expression of MMP-9 and iNOS in tissues affected by PD, as compared with controls, three days after PD induction, simultaneously with the beginning of alveolar bone loss. At 7 days post induction, only the MMP-9 mRNA presented a significantly higher expression, as compared with the respective controls. Thus, in the rat ligature-induced PD, MMP-9 and iNOS might importantly participate in the early stages of the disease, including inflammatory cell migration, tissue destruction and alveolar bone resorption. Also, we may suggest that the exuberant presence of PMNs may be related to the important expression of iNOS and MMP-9 found at 3 days post induction.
Asunto(s)
Metaloproteinasa 2 de la Matriz/metabolismo , Metaloproteinasa 9 de la Matriz/metabolismo , Óxido Nítrico/metabolismo , Enfermedades Periodontales/enzimología , Animales , Modelos Animales de Enfermedad , Regulación Enzimológica de la Expresión Génica , Masculino , Metaloproteinasa 2 de la Matriz/genética , Metaloproteinasa 9 de la Matriz/genética , Óxido Nítrico Sintasa de Tipo II/genética , Óxido Nítrico Sintasa de Tipo II/metabolismo , Enfermedades Periodontales/patología , ARN Mensajero/genética , ARN Mensajero/metabolismo , Ratas , Ratas WistarRESUMEN
BACKGROUND AND OBJECTIVE: Periodontal disease corresponds to a group of lesions that affect the tooth-supporting tissues present in the dental follicle. Although bacterial plaque is important, the immune response also contributes to the destruction of periodontal tissues. Diabetes mellitus is closely associated with the development, progression and severity of periodontal disease because it not only affects extracellular matrix organization but also the tissue response to inflammation. The objective of the present investigation was to study the influence of diabetes on experimental periodontal disease by evaluating the degradation of extracellular matrix through the analysis of matrix metalloproteinase (MMP)-2 and MMP-9 expression and activity, using immunofluorescence, zymography and real-time reverse transcription-polymerase chain reaction. MATERIAL AND METHODS: Wistar rats were divided into normal and diabetic groups and evaluated 0, 15 and 30 d after the induction of periodontal disease by ligature. RESULTS: MMP-2 and -9 were detected in epithelial cells, in the blood vessel endothelium and in connective tissue cells. The same profile of enzymatic expression of MMP-2 and -9 was observed in normal and diabetic animals, with a peak in activity at day 15 of inflammation. However, in diabetic animals, MMP-2 gelatinolytic activity was reduced after the inflammatory stimulus, whereas that of MMP-9 was increased. MMP-2 gene expression decreased with inflammation in both normal groups and groups with diabetes. In contrast, MMP-9 expression increased in normal animals and decreased in diabetic animals after inflammation. CONCLUSION: The results suggest the involvement of MMP-2 and -9 in the dynamics of periodontal disease and that variation in their expression levels results in differences in tissue organization and wound healing in normal and diabetic animals.
Asunto(s)
Diabetes Mellitus Tipo 1/enzimología , Metaloproteinasa 2 de la Matriz/metabolismo , Metaloproteinasa 9 de la Matriz/metabolismo , Enfermedades Periodontales/enzimología , Animales , Diabetes Mellitus Experimental/enzimología , Diabetes Mellitus Tipo 1/complicaciones , Masculino , Metaloproteinasa 2 de la Matriz/análisis , Metaloproteinasa 9 de la Matriz/análisis , ARN/análisis , Ratas , Ratas Wistar , Factores de TiempoRESUMEN
This review focuses specifically on matrix metalloproteinases (MMPs) and their role in physiological and pathological extracellular matrix (ECM) remodeling and degradation processes in the oral environment. A group of enzymes capable of degrading almost all ECM proteins, MMPs contribute to both normal and pathological tissue remodeling. The expression of different MMPs may be upregulated in pathological conditions such as inflammation and tumor invasion. The balance between activated MMPs and tissue inhibitors of metalloproteinases (TIMPs) controls the extent of ECM remodeling. Prior to mineralization, MMPs may participate in the organization of enamel and dentin organic matrix, or they may regulate mineralization by controlling the proteoglycan turnover. There is evidence indicating that MMPs could be involved in the etiology of enamel fluorosis and amelogenesis imperfecta. They seem to play a part in dentinal caries progression, since they have a crucial role in dentin collagen breakdown in caries lesions. MMPs have been identified in pulpal and periapical inflammation and are strongly correlated with periodontal diseases, since they are the major players in collagen breakdown during periodontal tissue destruction. The use of MMP inhibitors could help the prevention and treatment of many MMP-related oral diseases.
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Matriz Extracelular/enzimología , Metaloproteinasas de la Matriz/fisiología , Enfermedades Periodontales/enzimología , Caries Dental/enzimología , Esmalte Dental/enzimología , Pulpa Dental/enzimología , Dentina/enzimología , Proteínas Ligadas a GPI , Humanos , Metaloproteinasas de la Matriz/química , Glicoproteínas de Membrana/metabolismo , Inhibidores Tisulares de Metaloproteinasas/química , Desmineralización Dental/enzimologíaRESUMEN
For many years the diagnosis of Periodontal Disease has been based on clinical and radiographic methods. Other more recent methods have the objective of studying the inflammatory response of the host. That way, immunologic and biological methods determine the free mediators in the periodontal infection. The components of the gingivo-crevicular liquid or fluid are used to identify or to diagnose the active disease, to anticipate the risk of acquiring the disease and to determine its progress. For it to be clinically useful important changes should be registered the way a specific site turns active or that a previously disease affected site improves its conditions as a result of periodontal therapy. The response of the neutrophillic granulocytes play an important role in the detection of Periodontal Disease. The unspecific defense system in the gingivo-crevicular fluid can be determined through cytokines and/or interleukines that serve to identify sites at risk on the patient. In Periodontal Disease, the cytokines are not only defense mediators of the gingival sulcus fluid, but are also an indicator of tissue destruction. The liberation of high levels of lysosomal enzymes by neutrophils, proteolytic enzymes as the collagenases, or intercytoplasmatic enzymes as dehydrogenase lactate and aspartate amino transferase can equally help monitor the progress of the Periodontal Disease.
Asunto(s)
Enfermedades Periodontales/diagnóstico , Biomarcadores/análisis , Enzimas/análisis , Enzimas/fisiología , Líquido del Surco Gingival/química , Líquido del Surco Gingival/citología , Líquido del Surco Gingival/inmunología , Humanos , Enfermedades Periodontales/enzimología , Enfermedades Periodontales/inmunología , Ligamento PeriodontalRESUMEN
In this study, A. actinomycetemcomitans, B. forsythus, P. gingivalis and F. nucleatum were identified from subgingival plaque from 50 periodontal patients and 50 healthy subjects. Subgingival clinical samples were collected with sterilized paper points and transported in VMGA III. From all the diluted clinical samples (1:10), DNA was obtained by boiling, and after centrifugation the supernatant was used as template. Specific primers for each bacterial species were used in PCR. PCR amplification was sensitive to identify these organisms. PCR products from each species showed a single band and can be used to identify periodontal organisms from clinical specimens. PCR detection odds ratio values for A. actinomycetemcomitans and B. forsythus were significantly associated with disease showing a higher OR values for B. forsythus (2.97, 95 percent CI 1.88 - 4.70). These results suggest a strong association among the studied species and the periodontal lesion.
Asunto(s)
Enfermedades Periodontales/enzimología , Enfermedades Periodontales/patología , Técnicas In Vitro , Patógenos Transmitidos por la Sangre/aislamiento & purificación , Reacción en Cadena de la Polimerasa/métodos , MétodosRESUMEN
La bioquímica clínica en relacíon con la enfermedad periodontal puede proporcionarmos una valiosa información acerca de los episódios de actividad que presenta esta enfermedad. Los autores han centrado esta revisón em la actividad enzimática presente en el fluido gingival, como resultado de la destrucción tisular. La aplicación de métodos, ampliamente utilizados en Medicina tienen gran importancia en el diagnóstico y tratamiento de los pacientes con alto riesgo de padecer enfermedad periodontal
Asunto(s)
Humanos , Masculino , Femenino , Enfermedades Periodontales/enzimología , EncíaRESUMEN
Neste trabalho, estudamos a concentraçäo das enzimas: protease, desidrogenase lática, fosfatase alcalina, transaminase glutâmico-oxaloacético (GOT), transaminase glutâmico-pirúvico (GPT) e creatina fosfotransferase (CPK) em extratos teciduais de gengivas obtidas de pacientes com diferentes graus de doença periodontal inflamatória. Também realizamos o estudo do perfil proteico dos extratos teciduais através de eletroforese em gel de poliacrilamida em pH 8,6, pH 4,0 e contendo SDS. Para este propósito, selecionamos 81 pacientes de sexo masculino, com idade variando entre 14 e 51 anos, previamente classificados de acordo com os índices: gengival de Loe e Silness e de Ramfjord, além do exame radiográfico da área em estudo. Os pacientes foram divididos em sete grupos, distribuídos da seguinte maneira: Normal 10, Gengivite I 12, Gengivite II 12, Gengivite III 11, Periodontite I 10, Periodontite II 15 e Periodontite III 11. A análise dos nossos estudos mostraram os seguintes resultados: - A concentraçäo da protease é maior no grupo da periodontite grau I. A média da concentraçäo da enzima no grupo da gengivite é menor que no grupo normal. A média da concentraçäo da enzima no grupo da periodontite é ligeiramente superior à média no grupo normal. - A concentraçäo da desidrogenase lática é maior no grupo da gengivite grau II. A concentraçäo da enzima em UE/g de tecido é maior que o grupo normal na gengivite II e III. A média da concentraçäo da enzima no grupo da gengivite é maior do que o valor do grupo normal. A média no grupo da periodontite é inferior à média no grupo normal. - A concentraçäo da fosfatase alcalina em UE/mg de proteína apresentou valores maiores que o grupo normal nos grupos da gengivite II e III e periodontite I, II e III. A concentraçäo da fosfatase alcalina em UE/g de tecido apresentou valores maiores que o grupo normal, nos grupos da gengivite III e periodontite II e III. A média da concentraçäo da fosfatase alcalina foi crescente na seguinte ordem: normal, gengivite e periodontite...