Relevant bibliographies by topics / MMPZ

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Academic literature on the topic 'MMPZ'

Author: Grafiati
Published: 4 June 2021
Last updated: 17 February 2022

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Journal articles on the topic "MMPZ"

1

Lenglet, Sébastien, Fabrizio Montecucco, François Mach, Karl Schaller, Yvan Gasche, and Jean-Christophe Copin. "Analysis of the expression of nine secreted matrix metalloproteinases and their endogenous inhibitors in the brain of mice subjected to ischaemic stroke." Thrombosis and Haemostasis 112, no. 08 (2014): 363–78. http://dx.doi.org/10.1160/th14-01-0007.

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SummaryMatrix metalloproteinases (MMPs) are a family of more than twenty secreted and cell-surface endopeptidases. Among them, MMP2, MMP3 and MMP9 are involved in blood-brain barrier injury and neuronal death after cerebral ischaemia. On the other hand, very little is known about the expression of the other secreted MMPs. Herein, we compared the global changes in MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP12 and MMP13, and their endogenous inhibitors TIMP1 and TIMP2, both at the mRNA and protein levels, during the hyperacute (6 h), acute (24 h) and subacute (72 h) stages following transient focal cerebral ischaemia and treatment with recombinant tissue plasminogen activator (rtPA). We observed a significant increase in MMP1, MMP2, MMP9, MMP10, MMP13 and TIMP1 levels during the acute stage of reperfusion, which was further amplified during the subacute stage for MMP1, MMP2, MMP10 and TIMP1. In general, no change of MMP3, MMP7, MMP8, MMP12 and TIMP2 was observed. However, rtPA treatment induced a rapid increase in MMP1/TIMP2, MMP2/TIMP2, MMP8/TIMP2 and MMP9/TIMP2 ratios during the hyperacute stage of reperfusion compared to saline treatment, which may have potential implications in the early disruption of the blood-brain barrier after rtPA treatment.
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Balasa, Rodica, Ciurba Bianca, Voidezan Septimiu, Simu Iunius, Hutanu Adina, Andone Sebastian, Romaniuc Andreea, Motataianu Anca, and Maier Smaranda. "The Matrix Metalloproteinases Panel in Multiple Sclerosis Patients Treated with Natalizumab: A Possible Answer to Natalizumab Non- Responders." CNS & Neurological Disorders - Drug Targets 17, no. 6 (August 28, 2018): 464–72. http://dx.doi.org/10.2174/1871527317666180703102536.

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Background: In the lymphocyte migration across the blood-brain barrier (BBB) in multiple sclerosis (MS), matrix metalloproteinases (MMPs) play an important role in the degradation of the basal membrane. Natalizumab (NAT), a monoclonal antibody, binds to the alpha-4 (α4) integrin leading to BBB impermeability. Approximately 30% of NAT-treated patients show clinical or MRI signs of BBB disruption. Objective: To determine whether NAT significantly influences the MMPs serum levels and to what extent these could be used as biomarkers in relapsing-remitting MS (RRMS) patients. Materials and Methods: This prospective study over a period of 8 months of NAT treatment, included 30 RRMS patients (mean age 38 ± 6 years; mean MS duration 12 ± 5 years), of which ten were initially naive to NAT and 15 were healthy controls. We determined the serum levels of the MMPs Panel (MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP12, and MMP13) quantified by a multiplex method at the beginning and end of the study. Results: After 8 months of NAT treatment, a statistically significant decrease was found in MMP9, MMP2, MMP3, MMP8, and MMP10 levels. Relapses during the study were correlated with a variation of MMP12 and MMP13 serum levels. MMP9 had the most numerous correlations with the EDSS score, Rio score, and duration of NAT treatment. MMPs signature (the sum of all MMPs) and the MMP9/MMP2 ratio significantly decreased during the study. Conclusion: 1. The serum level of MMP9 significantly decreased by NAT treatment and correlates with MS activity; 2. After eight months of NAT treatment, the MMPs signature and the MMP9/MMP2 ratio decreased; 3. MMP9 might be used as a biomarker in MS patients treated with NAT.
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Sakowicz, Agata, Michalina Lisowska, Lidia Biesiada, Magda Rybak-Krzyszkowska, Agnieszka Gach, Bartosz Sakowicz, Mariusz Grzesiak, Hubert Huras, and Tadeusz Pietrucha. "Association of Maternal and Fetal Single-Nucleotide Polymorphisms in Metalloproteinase (MMP1, MMP2, MMP3, and MMP9) Genes with Preeclampsia." Disease Markers 2018 (2018): 1–10. http://dx.doi.org/10.1155/2018/1371425.

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Background. Metalloproteinases (MMPs) play a pivotal role during the process of trophoblast invasion and placentation. The appearance of five functional single-nucleotide polymorphisms (SNP) in the genes of the metalloproteinases most commonly implicated in the implantation process may influence the development of preeclampsia. Methods. Blood samples were collected from 86 mothers and 86 children after preeclampsia and 85 mothers and 85 children with uncomplicated pregnancies. The distribution of genotypes for −1607 1G/2G MMP1, −735 C/T MMP2, −1306 C/T MMP2, −1171 5A/6A MMP3, and −1562C/T MMP9 polymorphisms was determined by RFLP-PCR. Results. The occurrence of 1G/1G MMP1 or 5A/5A MMP3 genotype in the mother or 1G/1G MMP1 or 5A/6A MMP3 genotype in the child is associated with preeclampsia development. Moreover, simultaneous maternal and fetal 1G/1G homozygosity increases the risk of preeclampsia development 2.39-fold and the set of maternal 5A/5A and fetal 5A/6A MMP3 genotypes by over 4.5 times. No association between the carriage of studied MMP2 or MMP9 polymorphisms and the predisposition to preeclampsia was found. Conclusion. The maternal 1G/1G MMP1 and 5A/5A MMP3 and fetal 1G/1G MMP1 and 5A/6A MMP3 gene polymorphisms may be strong genetic markers of preeclampsia, occurring either individually or together.
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Decock, J., W. Hendrickx, M. Drijkoningen, H. Wildiers, P. Neven, A. Smeets, and R. Paridaens. "Matrix Metalloproteinase Expression Patterns in Luminal A Type Breast Carcinomas." Disease Markers 23, no. 3 (2007): 189–96. http://dx.doi.org/10.1155/2007/281727.

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Objective:Aberrant expression of individual matrix metalloproteinases has been associated with poor prognosis in various human carcinomas. The current study aimed at defining an RNA expression profile of various MMPs in breast cancer and correlating their expression with clinicopathological parameters.Methods:The RNA expression patterns of 6 MMPs (MMP2, MMP8, MMP9, MMP10, MMP11, MMP13) were determined in 25 breast carcinomas using quantitative RT-PCR and correlated with clinicopathological parameters, including menopausal status, tumor size and grade, and lymph node involvement.Results:We observed high MMP2 levels more frequently in premenopausal than in postmenopausal women (p= 0.02). Analysis of luminal A type invasive ductal carcinomas (19/25), revealed an even stronger association of MMP2 with menopausal status (p= 0.005). Within this subgroup, we also found a correlation between MMP11 and menopausal status (p= 0.02). No correlation was found between MMP expressions and other clinicopathological parameters. In co-expression analyses MMP2-MMP10 and MMP8-MMP9 showed a weak correlation of their expression.Conclusions:Although this is a pilot study, our findings indicate that luminal A invasive ductal carcinomas commonly express high MMP2 and MMP11 levels in premenopausal breast cancer patients and suggest a co-regulation of MMP2-MMP10 and MMP8-MMP9.
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Sorrell, David A., Malgorzata Szymanowska, Marion Boutinaud, Claire Robinson, Richard WE Clarkson, Torsten Stein, David J. Flint, and Andreas F. Kolb. "Regulation of genes encoding proteolytic enzymes during mammary gland development." Journal of Dairy Research 72, no. 4 (July 14, 2005): 433–41. http://dx.doi.org/10.1017/s0022029905001202.

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The mammary gland undergoes extensive tissue remodelling during each lactation cycle. During pregnancy, the epithelial compartment of the gland is vastly expanded (Benaud et al. 1998). At the end of lactation the epithelial cells undergo apoptosis and adipocyte differentiation is induced (Lilla et al. 2002). Ductal and alveolar growth during puberty and pregnancy, and the involution process require the action of proteolytic enzymes (including matrix metalloproteinases, plasminogen and membrane-peptidases) and the corresponding genes are activated during these periods (Benaud et al. 1998; Alexander et al. 2001). Matrix metalloproteinases (MMP) are expressed in several cell types of the mammary gland including stromal fibroblasts (e.g., MMP3, MMP2), epithelial cells (e.g., MMP7 or MMP9), adipocytes (e.g., MMP2) and lymphoid cells (e.g., MMP9) (Crawford et al. 1996; Lund et al. 1996; Wiseman et al. 2003). A number of knock-out mice, which are deficient for individual MMP genes (e.g., MMP2, MMP3) or plasminogen, display alterations to mammary gland structure and impairment of lactation (Lund et al. 1999; Wiseman et al. 2003).
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Yang, Hui, Carlos E. Bueso-Ramos, Sherry A. Pierce, Yue Wei, Zhihong Fang, Martin Nguyen, Michael Fernadez, Marylou Cardenas-Turanzas, Hagop M. Kantarjian, and Guillermo Garcia-Manero. "Expression Profiles of Matrix Metalloproteinases (MMPs) and Tissue Inhibitors of Metalloproteinases (TIMPs) in Myelodysplastic Syndromes (MDS): Level of MMP-9 Is Associated with Improved Prognosis in MDS Patients." Blood 120, no. 21 (November 16, 2012): 3845. http://dx.doi.org/10.1182/blood.v120.21.3845.3845.

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Abstract Abstract 3845 Introduction: Matrix metalloproteinases (MMPs) belong to a unique family of zinc dependent endopeptidases, they are strictly regulated by their endogenous inhibitors called tissue inhibitor of MMPs (TIMPs). MMPs have been associated with tumorigenesis. In addition to their role in extracellular matrix turnover and cancer cell migration, MMPs regulate signaling pathways that control cell growth, inflammation, or angiogenesis and may even work in nonproteolytic manner. MMPs play a key role during invasion and metastasizing of cancer cells and they have been shown to be associated to invasive phenotype and poor prognosis in several solid tumors. Little is known about their role in MDS. A total of 23 different human MMPs and 4 TIMPs have been identified. To better understand the role of MMPs in MDS, we performed an expression profile screen study by QPCR to detect the expression level of all MMP and TIMP family members, except MMP23, in CD34+ cells from a cohort (N=10) of newly diagnosed, untreated patients with MDS, and compared the expression level with CD34+ cells from 5 normal donors. Of these 26 genes, we identified MMP2, MMP8, MMP9, MMP25, MMP28, TIMP1, TIMP2 and TIMP3 as aberrantly up-regulated genes in MDS and expanded the study to a larger cohort of patients to correlate with clinical features and clinical outcomes. Methods: CD34+ cells from 98 newly diagnosed patients with MDS and 5 normal donors were evaluated for MMP2, MMP8, MMP9, MMP25, MMP28, TIMP1, TIMP2 and TIMP3 expression profiling. CD34+ cells were sorted from patients and normal donor bone marrow. Total cellular RNA was isolated using Trizol, cDNA was obtained by using TaqMan reverse transcription reagent (Applied Biosystems). For real-time PCR, all assays were purchased from Applied Biosystems and analyzed with an Applied Biosystems Prism 7500 Sequencing detection system. GAPDH was used as internal control. Immunohistochemistry was used to detect MMP9 protein level in cytospin from CD34+ cells. MMP9 abtibody was obtained from R&D systems, MMP9 ELISA kit (R&D systems) was used to detect the MMP9 protein level in bone marrow plasma. Results: For the 98 MDS patients studied, 78% were older than 60 years; by IPSS score, 17 (17.3%) low risk, 35 (35.7%) INT-1, 24 (24.5%) INT-2, 10 (10.2%) high risk, 12 (12.2%) not available. By Cytogenetics, diploid 44 (45%), 20q- 7(7%), −5/5q- 7 (7%), −7/7q- 7 (7%), −5/5q- and −7/7q- 6 (6%), 8+ 6 (6%), IM 6 (6%), MISC 14 (14%). By QPCR and comparing MDS CD34+ cells with normal CD34+ cells, aberrant up-regulation (fold>2) of MMP2, MMP8, MMP9, MMP25, MMP28, TIMP1, TIMP2 and TIMP3 was detected in 40%, 93.8%, 94%, 84%, 15.6%, 45%, 21% and 27% of patients respectively. Up-regulation of MMP8, MMP9 and MMP25 were significant with a mean fold value 350.7 (0–3363.7), 1112.4 (0–15641) and 143.8 (0–1017.9) respectively. We performed MMP9 immunohistochemistry of MDS CD34+ cytospins from 16 pts with higher and lower MMP9 RNA relative expression level and found consistent protein expression level in cytoplasm. No elevated MMP9 protein levels were detected in bone marrow plasma. We then performed an analysis of associations with clinical variables and observed that relative expression value of MMP9 was associated with lower bone marrow blast (p=0.001) and longer survival (p=0.02) (figure 1). We did not found association between survival and the other 7 up-regulated genes. Conclusions: Bone marrow CD34+ cells from patients with MDS have abnormal up-regulation of MMP2, MMP8, MMP9, MMP25, MMP28, TIMP1, TIMP2 and TIMP3. MMP9 up-regulation is associated with longer survival. Our results suggest that MMP-9 could be a useful prognostic indicator for MDS and that this family of proteins needs further study in MDS. Disclosures: No relevant conflicts of interest to declare.
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Wieczorek, Edyta, Michal Galicki, Bartlomiej Tomasik, Magdalena Krol, Ewa Jablonska, Wojciech Fendler, Jolanta Gromadzinska, Zbigniew Morawiec, Wojciech Wasowicz, and Edyta Reszka. "Expression of MMP and TIMP mRNA in Peripheral Blood Leukocytes of Patients with Invasive Ductal Carcinoma of the Breast." International Journal of Biological Markers 31, no. 3 (July 2016): 309–16. http://dx.doi.org/10.5301/jbm.5000203.

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Purpose An imbalance between matrix metalloproteinases (MMPs) and tissue inhibitors of MMPs (TIMPs) appears critical for tumor progression and metastasis. This study aimed to determine whether gene expression of MMP1, MMP2, MMP9, TIMP1 and TIMP3 and the MMP/TIMP expression ratio in peripheral blood leukocytes (PBLs) and the MMP1 and TIMP1 contents or MMP1/TIMP1 ratio in plasma were associated with clinicopathological characteristics in invasive ductal carcinoma (IDC) of the breast. Materials and methods Blood samples were collected from women newly diagnosed with IDC who had not received prior treatment (n = 102). Gene expression in PBLs was analyzed by quantitative real-time polymerase chain reaction. Concentrations of MMP1 and TIMP1 in plasma were measured using ELISA. Results In univariate analysis the expression levels of MMP2 and TIMP1 mRNA were significantly higher in premenopausal compared to postmenopausal patients (p<0.001 and p = 0.014, respectively). MMP2 mRNA expression negatively correlated with age (p<0.001, r = -0.43). We found that the MMP2/TIMP3 expression ratio was significantly higher in women after menopause (p = 0.007). The MMP2/TIMP1 expression ratio was higher in human epidermal growth factor receptor 2 (HER2)-positive patients (p = 0.022). Low-grade tumors had significantly lower MMP1/TIMP1 and MMP2/TIMP1 expression ratios (p = 0.047 and p = 0.048, respectively). TIMP1 plasma concentration was significantly higher in small tumors compared with T2-T3 tumors (p = 0.013). Conclusions These findings reveal an important association between tumor characteristics and expression ratios of MMP1/TIMP1 and MMP2/TIMP1 in PBLs and TIMP1 concentration in plasma. Menopausal status may influence the mRNA expression levels of MMP2 and TIMP1 as well as the MMP2/TIMP3 expression ratio in IDC of the breast.
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Dvornyk, Volodymyr, Irina Ponomarenko, Oksana Minyaylo, Evgeny Reshetnikov, and Mikhail Churnosov. "Association of the functionally significant polymorphisms of the MMP9 gene with H. pylori-positive gastric ulcer in the Caucasian population of Central Russia." PLOS ONE 16, no. 9 (September 7, 2021): e0257060. http://dx.doi.org/10.1371/journal.pone.0257060.

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Background and purpose The study analyzed the association of functionally significant polymorphisms of matrix metalloproteinases (MMPs) genes with the development of gastric ulcer (GU) in Caucasians from Central Russia. Methods The 781 participants, including 434 patients with GU (196 Helicobacter pylori (H. pylori)-positive and 238 H. pylori-negative) and 347 controls (all H. pylori-negative) were recruited for the study. Ten SNPs of the MMP1 (rs1799750), MMP2 (rs243865), MMP3 (rs679620), MMP8 (rs1940475), and MMP9 (rs3918242, rs3918249, rs3787268, rs17576, rs17577, and rs2250889) genes were considered for association with GU using multiple logistic regression. The SNPs associated with GU and loci linked (r2≥0.8) to them were analyzed in silico for their functional assignments. Results The SNPs of the MMP9 gene were associated with H. pylori-positive GU: alleles C of rs3918249 (OR = 2.02, pperm = 0.008) and A of rs3787268 (OR = 1.60–1.82, pperm ≤ 0.016), and eight haplotypes of all studied MMP9 gene SNPs (OR = 1.85–2.04, pperm ≤ 0.016) increased risk for H. pylori-positive GU. None of the analyzed SNPs was independently associated with GU and H. pylori-negative GU. Two haplotypes of the MMP9 gene (contributed by rs3918242, rs3918249, rs17576, and rs3787268) increased risk for GU (OR = 1.62–1.65, pperm ≤ 0.006). Six loci of the MMP9 gene, which are associated with H. pylori-positive GU, and 65 SNPs linked to them manifest significant epigenetic effects, have pronounced eQTL (17 genes) and sQTL (6 genes) values. Conclusion SNPs of the MMP9 were associated with H. pylori-positive GU but not with H. pylori-negative GU in Caucasians of Central Russia.
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Bates, Amber, Carol Fischer, Vrushali Abhyankar, Georgia Johnson, Janet Guthmiller, Ann Progulske-Fox, and Kim Brogden. "Matrix Metalloproteinase Response of Dendritic Cell, Gingival Epithelial Keratinocyte, and T-Cell Transwell Co-Cultures Treated with Porphyromonas gingivalis Hemagglutinin-B." International Journal of Molecular Sciences 19, no. 12 (December 7, 2018): 3923. http://dx.doi.org/10.3390/ijms19123923.

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Matrix metalloproteinases (MMPs) are enzymes involved in periodontal tissue destruction. Hemagglutinin B (HagB) from the periodontal pathogen Porphyromonas gingivalis induces an elevated MMP response in dendritic cells, but responses from cultures of single-cell types do not reflect the local tissue environment. The objective of this study was to measure HagB-induced MMP responses in a transwell co-culture system containing dendritic cells, gingival epithelial (GE) keratinocytes, and CD4+ T-cells. Transwell co-cultures were assembled and treated with or without HagB. Immunoassays were used to determine production of MMP1, MMP7, MMP9, and MMP12 in response to HagB up to 64 h. Control responses were subtracted from HagB-induced responses. A two-way fixed effect ANOVA was fit to log-transformed concentrations and pairwise group comparisons were conducted (p < 0.05). At 64 h, dendritic cells produced elevated MMP1 and MMP9 responses, which were attenuated in the 3-cell co-culture (p < 0.05). There were also significant differences in MMP7 and MMP12 production between single-cell cultures and co-cultures. These results support the need to use multiple cell types in culture models to evaluate a more representative response to proinflammatory agonists. This three-cell transwell co-culture model may help us better understand the inflammatory process in periodontal disease and test novel therapeutic approaches.
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Durmanova, Vladimira, Juraj Javor, Zuzana Parnicka, Gabriel Minarik, Agata Ocenasova, Barbora Vaseckova, Veronika Reznakova, Maria Kralova, Tomas Hromadka, and Ivana Shawkatova. "Impact of MMP2 rs243865 and MMP3 rs3025058 Polymorphisms on Clinical Findings in Alzheimer’s Disease Patients." Mediators of Inflammation 2021 (April 19, 2021): 1–9. http://dx.doi.org/10.1155/2021/5573642.

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Alzheimer’s disease (AD) is a chronic neurodegenerative disease of the central nervous system with higher prevalence in elderly people. Despite numerous research studies, the etiopathogenesis of AD remains unclear. Matrix metalloproteinases (MMPs) are endopeptidases involved in the cleavage of extracellular matrix proteins and basement membrane compounds. In the brain, the pathological role of MMPs includes the disruption of the blood-brain barrier leading to the induction of neuroinflammation. Among various MMPs, MMP-2 and MMP-3 belong to candidate molecules related to AD pathology. In our study, we aimed to evaluate the association of MMP2 rs243865 and MMP3 rs3025058 polymorphisms with AD susceptibility and their influence on age at onset and MoCA score in patients from Slovakia. Both MMP gene promoter polymorphisms were genotyped in 171 AD patients and 308 controls by the PCR-RFLP method. No statistically significant differences in the distribution of MMP2 rs243865 (-1306 C>T) and MMP3 rs3025058 (-1171 5A>6A) alleles/genotypes were found between AD patients and the control group. However, correlation with clinical findings revealed later age at disease onset in MMP2 rs243865 CC carriers in the dominant model as compared to T allele carriers (CC vs. CT+TT: 78.44 ± 6.28 vs. 76.36 ± 6.39 , p = 0.036 ). The results of MMP3 rs3025058 analysis revealed that 5A/6A carriers in the overdominant model tended to have earlier age at disease onset as compared to other MMP3 genotype carriers (5A/6A vs. 5A/5A+6A/6A: 76.61 ± 5.88 vs. 78.57 ± 6.79 , p = 0.045 ). In conclusion, our results suggest that MMP2 rs243865 and MMP3 rs3025058 promoter polymorphisms may have influence on age at onset in AD patients.
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Dissertations / Theses on the topic "MMPZ"

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Planello, Aline Cristiane 1980. "Analise de polimorfismos no promotor dos genes MMP1, MMP3 e MMP9 na desordem da articulação temporomandibular." [s.n.], 2010. http://repositorio.unicamp.br/jspui/handle/REPOSIP/288534.

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Orientador: Ana Paula de Souza Pardo
Dissertação (mestrado) - Universidade Estadual de Campinas, Faculdade de Odontologia de Piracicaba
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Resumo: Objetivo: As Metaloproteinases da Matriz ( MMPs) são enzimas que degradam a matriz extracelular (MEC) e tem sido associadas às desordens temporomandibulares (DTM). Nós investigamos a freqüência dos -1607 1G/2G MMP1 polimorfismo (rs1799750), -1171 6A/5A MMP3 polimorfismo (rs3025058) e -1562 C/T MMP9 polimorfismo (rs3918242) em indivíduos com sinais de degeneração da ATM, diagnosticados por exame de imagem, a fim de analisar a associação desses polimorfismos e a DTM. Métodos: A população estudada foi composta por 115 indivíduos diagnosticados por exame de imagem (grupo DTM) e 117 controles. Os polimorfismos genéticos foram determinados por PCR/RFLP. Resultados: A freqüência do genótipo 2G/2G no gene MMP1 foi significantemente mais alta no grupo DTM do que no grupo Controle (p = 0.008). O genótipo 2G/2G no grupo DTM mostrou um risco aumentado para a DTM com um OR = 2.25 ( 95% IC = 1.26 - 3.99) quando comparado com os genótipo 1G/2G e 1G/1G. A freqüência dos alelos do gene MMP1 não mostrou diferença significativa entre os grupos (p > 0.05). A distribuição dos genótipos e alelos dos genes MMP3 e MMP9 não mostrou diferença significativa (p > 0.05). Conclusão: Nossos resultados mostram a associação entre o polimorfismo -1607 MMP1 e a suscetibilidade à DTM
Abstract: Objective. Matrix metalloproteinases (MMPs) degrade extracellular matrix components and have been implicated to play an important role in temporomandibular joint disorder (TMD). We investigated the frequency of -1607 1G/2G MMP1 polymorphism (rs1799750), -1171 6A/5A MMP3 polymorphism (rs3025058) and -1562 C/T MMP9 polymorphism (rs3918242) in individuals with TMJ degeneration diagnosed by image exam in order to analyze the association of these MMPs polymorphisms and TMD. Methods. The studied population comprised 115 TMD individuals diagnosed by image exam and 117 healthy controls. Genotypes were determined using polymerase chain reaction/Restriction fragment length polymorphism PCR/RFLP. Results. The MMP1 2G/2G genotype was significantly higher in the TMD group than in the Control group (p = 0.008). The genotype 2G/2G in the TMD group showed an increased risk to TMD with an OR = 2.25 (95% CI = 1.26 - 3.99) when compared with 1G/2G and 1G/1G genotypes. Analysis of MMP1 allele frequencies showed no significant difference (p > 0.05). The MMP3 and MMP9 genotypes distribution and alleles frequency did not differ between the groups (p > 0.05). Conclusion. Our results report the association of -1607 MMP1 gene polymorphism and increased risk to TMD
Mestrado
Histologia e Embriologia
Mestre em Biologia Buco-Dental
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Mendes, Odete Rodrigues. "Role of MMP2, MMP3 and MMP9 in the development of breast cancer brain and lung metastasis in a syngeneic rat model." Texas A&M University, 2005. http://hdl.handle.net/1969.1/2645.

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In order to study the expression of MMP2, MMP 3 and MMP9 in breast cancer brain and lung metastasis, we used a syngeneic rat model of distant metastasis of ENU1564, a carcinogen-induced mammary adenocarcinoma cell line. At six weeks post inoculation we observed development of micro-metastasis in the brain and lung. Immunohistochemistry and Western blotting analyses showed that MMP 2, -3 and -9 protein expression is consistently significantly higher in neoplastic brain tissue compared to normal brain tissue. Lung metastases express abundant MMP2, -3 and -9 in neoplastic cell cytoplasm. In situ zymography revealed gelatinase activity within the brain metastasis. Gel zymography showed an increase in MMP2 and MMP3 activity in brain metastasis. Furthermore, we were able to significantly decrease the development of breast cancer brain and lung metastasis in animals by treatment with PD 166793, a selective synthetic MMP inhibitor. In addition, PD 166793 decreased the in vitro invasive cell behavior of ENU1546. TIMP2 overexpression also decreased the development of breast cancer lung metastasis in our model. Our results suggest that MMP2, -3 and -9 may be involved in the process of metastasis of breast cancer to the brain and lung. Because astrocytes have been associated with breast cancer brain metastasis we evaluated the role of astrocytes and ERK2 pathway in MMP2 up-regulation in BC brain metastasis. A significant decrease in brain metastases development, and orthotopic tumor size and weight were observed in animals inoculated with ENU1564-TIMP2 cells. These were associated with decreased MMP2 activity, as demonstrated by gel zymography. Rat astrocyte-conditioned media increased expression of MMP2 in ENU15645 cells and increased in vitro cell invasion of ENU1564 and ENU1564-TIMP2 cells. Blockage of ERK1/2 phosphorylation by treatment with PD98059 decreased the expression of MMP2 in cancer cells grown in rat astrocyte-conditioned media. We determine that MMP2 plays a role in in vivo development of breast cancer brain metastases. Additionally, we conclude that astrocytes are associated with expression of MMP2 in cancer cells via ERK1/2 signaling pathway.
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Santos, Raphaela Paulo dos. "Análise de polimorfismos nos genes HSD17B1, MMP2 e MMP9 em pacientes com endometriose." Niterói, 2013. https://app.uff.br/riuff/handle/1/4736.

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Universidade Federal Fluminense. Hospital Universitário Antonio Pedro. Centro de Ciências Médicas
A endometriose é definida pela presença de tecido endometrial (glândula e/ou estroma) fora da cavidade uterina, a patologia afeta 10-15% das mulheres em idade reprodutiva, além disso, os sintomas álgicos da doença implicam em impactos econômicos e sociais. A doença apresenta diagnóstico tardio e sua etiologia ainda não foi completamente elucidada, porém, sabe-se que a endometriose possui caráter poligênico e multifatorial. O objetivo do estudo foi avaliar se os polimorfismos no gene HSD17β1 (rs605059), envolvido na síntese de estrogênio, e nos genes MMP2 (rs243865) e MMP9 (rs17576), que atuam no remodelamento da matriz extracelular, estão associados com a endometriose quanto ao risco e o grau de severidade da doença. O estudo do tipo caso-controle foi composto por 231 mulheres, sendo 97 casos e 134 controles. Todas as pacientes do grupo caso possuíam diagnóstico histopatológico para a endometriose. O DNA genômico foi extraído a partir de saliva, e o polimorfismo no gene HSD17β1 foi detectado pela técnica de PCR- Nested seguido de digestão do produto de PCR pela enzima BstUI, os genes MMP2 e MMP9 foram genotipados pela técnica de PCR em Tempo Real. Não foi encontrada diferença estatisticamente significante entre as distribuições genotípicas e alélicas dos genes analisados entre os grupos estudados (p>0,05). Do mesmo modo não foi observada diferença significativa na frequência dos genótipos e alelos entre os diferentes estágios da doença (p>0,05). Os resultados do presente estudo sugerem que os polimorfismos nos genes HSD17β1 (rs605059), MMP2 (rs243865) e MMP9 (rs17576), não estão associado com a endometriose em pacientes brasileiras, mesmo quando avaliado as relações entre graus de severidade variados
Endometriosis is defined by the presence of endometrial tissue (glands and / or stroma) outside the uterine cavity, this condition affects 10-15% of women of reproductive age, in addition, the pain symptoms of the disease involves economic and social impacts. The disease presents late diagnosis and its etiology has not been fully elucidated, but it is known that endometriosis has multifactorial and polygenic character. The aim of the study was to assess whether the polymorphisms in the HSD17β1 (rs605059), involved in estrogen synthesis, and MMP2 genes (rs243865) and MMP9 (rs17576), which act in extracellular matrix remodeling are associated with endometriosis as the risk and severity of the disease. The case-control study consisted of 231 women, with 97 cases and 134 controls. All patients in the case group had histopathological diagnosis for endometriosis. Genomic DNA was extracted from saliva, and HSD17β1 gene polymorphism was detected by Nested-PCR followed by digestion of the PCR product by the enzyme BstUI, MMP2 and MMP9 genes were genotyped by Real Time-PCR. There was no statistically significant difference between the genotypic and allelic distributions of genes analyzed between groups (p> .05). Similarly there was no significant difference in the frequency of genotypes and alleles between different stages of the disease (p> .05). The results of this study suggest that polymorphisms in genes HSD17β1 (rs605059), MMP2 (rs243865) and MMP9 (rs17576), are not associated with endometriosis in Brazilian patients, even when the relations between different degrees of severity were evaluated
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Peres, Juliana Alves. "Avaliação histométrica do reparo de defeito ósseo em calvária de rato após implante de rhMMP-2 ligada à monoleína." Universidade de São Paulo, 2012. http://www.teses.usp.br/teses/disponiveis/58/58137/tde-18092012-154340/.

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As metaloproteinases da matriz (MMPs) são enzimas proteolíticas dependentes de zinco que degradam componentes da matriz extracelular, facilitando a remodelação tecidual e a migração celular. MMPs secretadas por osteoclastos exercem papel central na absorção óssea fisiológica e estão também associadas a processos de degradação patológica do osso. No entanto, o papel essencialmente degradador de osso das MMPs, particularmente da MMP-2, vem sendo questionado em anos recentes por estudos que evidenciam sua importância na diferenciação de células da linhagem osteoblástica e na formação de tecido ósseo em cultura. Neste sentido, é possível que a MMP-2 exerça um papel importante na formação de tecido ósseo em processo de reparação. O objetivo do presente trabalho foi investigar a pretensa ação osteo-estimulatória da rhMMP-2 ligada à monoleína (usada como carreador) implantada em defeito confeccionado na calvária de ratos. Foram confeccionados defeitos ósseos unilaterais de 4 mm de diâmetro na calvária de ratos adultos; nos animais controles o defeito ósseo foi mantido com o preenchimento natural de coágulo sanguíneo e nos animais implantados o defeito foi preenchido com monoleína ou com rhMMP-2 ligada à monoleína. Os animais foram eutanasiados após 2 e 4 semanas e a taxa de neoformação óssea foi estimada em cortes histológicos por um método histométrico de contagem diferencial de pontos. A taxa de neoformação óssea foi semelhante nos animais dos grupos controle e monoleína e significativamente maior nos animais do grupo MMP-2, em ambos os períodos analisados. Os resultados permitem concluir que a monoleína não interferiu com o processo reparacional e pareceu eficaz como carreador da rhMMP-2, e adicionam evidências á hipótese da importância da atividade da MMP-2 para a formação óssea, em um modelo experimental in vivo de reparo ósseo.
Matrix metalloproteinases (MMPs) are zinc-dependent proteolytic enzymes that degrade extracellular matrix components, facilitating cell migration and tissue remodeling. MMPs secreted by osteclasts are important in the physiological bone resorption as in pathological bone degradation. However, the essentially bone absorbing hole of MMPs, particularly of the MMP-2, has been questioned in recent years by studies that show its importance in osteoblastic cells differentiation and in vitro bone formation. Therefore, the MMP-2 may have also an important hole in reparational bone formation. The purpose of the present study was to investigate the pretense osteostimulatory effect of the rhMMP-2 linked to monoolein (used as a carrier) implanted into rat calvarial defects. Bone defects of 4mm in diameter were created unilaterally in rats calvaria and filled with natural blood clot (control), monoolein or rhMMP-2 linked to monoolein. The animals were killed 2 and 4 weeks postoperatively and the rate of new bone formation was estimated in histological sections by a histometric differential point-counting method. The rate of reparational bone formation was similar in the animals from control and monoolein groups and was significantly greater in the MMP-2 group, in both periods. From the results it may be concluded that monoolein did not interfere with the reparacional process and seemed effective as a rhMMP-2 carrier. In addition, the results add evidence to the importance of MMP-2 activity for bone formation, in an in vivo bone healing experimental model.
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Khvaramze, Shaverdashvili. "MT1-MMP REGULATES MELANOMA METASTASIS THROUGH ACTIVATION OF MMP2/RAC1 AXIS AND INHIBITION OF TUMOR SUPPRESSOR GENE SPRY4." Case Western Reserve University School of Graduate Studies / OhioLINK, 2015. http://rave.ohiolink.edu/etdc/view?acc_num=case1438809026.

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Meffert-Laschinski, Philipp [Verfasser], Fabian Alexander [Akademischer Betreuer] Kari, and Matthias [Akademischer Betreuer] Siepe. "Die Charakterisierung von MMP2- und MMP9- Serumspiegeln als prognostische Biomarker bei Aneurysmen der Aorta ascendens." Freiburg : Universität, 2016. http://d-nb.info/1136862838/34.

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Meffert-Laschinski, Philipp [Verfasser], Matthias [Akademischer Betreuer] Siepe, and Fabian Alexander [Akademischer Betreuer] Kari. "Die Charakterisierung von MMP2- und MMP9- Serumspiegeln als prognostische Biomarker bei Aneurysmen der Aorta ascendens." Freiburg : Universität, 2016. http://d-nb.info/1122743033/34.

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Stott, Holly Rosannah. "MMP-12 activity during vascular remodelling." Thesis, University of Edinburgh, 2017. http://hdl.handle.net/1842/23609.

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Matrix metalloproteinases (MMPs) are required for tissue remodelling processes, including angiogenesis. MMP activity is generally proangiogenic but MMP-12 is suggested to be antiangiogenic and its precise role is still unclear. The work in this thesis describes the synthesis of an MMP-12 inhibitor and activity probe to address the hypothesis that MMP-12 inhibits angiogenesis. An inhibitor, synthesised in-house, selectively inhibited MMP-12 in in vitro recombinant enzyme assays. An activity probe, also synthesised in-house, was selective for MMP-12 in in vitro recombinant enzyme assays. The function of MMP-12 during angiogenesis was assessed using murine models of angiogenesis; the in vivo sponge implantation, and the ex vivo aortic ring assays. Angiogenesis and MMP activity were imaged in vivo in sponges in C57Bl6/J mice over 7 − 21 days (D) using commercial probes (MMPSense™ and AngioSense™). MMP-12 protein concentration and activity were higher in sponges during early angiogenesis (D 3 − 7) when gene expression of vascular endothelial growth factor (a proangiogenic marker) was also high. Gene expression for MMP-12 and platelet-derived growth factor receptor (a marker of vascular maturation) were both higher on D 21 as angiogenesis started to stabilise. The MMP-12 activity probe was unsuccessful in selectively detecting MMP-12 activity in sponge lysate mixtures from D 7 − 21. Administration of an MMP-12 inhibitor did not increase angiogenesis in the sponges in vivo. Additionally, sponges implanted in MMP-12-/- mice did not exhibit significant changes in angiogenesis or MMP activity when imaged in vivo using commercial probes (MMPSense™ and AngioSense™) on D 7. Supporting this, histological analysis of the sponges (removed on D 21) showed that deletion of MMP-12 also did not increase angiogenesis within the sponges.
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Segarra, Blasco Marta. "Regulació de la Producció de Gelatinases (MMP2 i MMP9) pels Limfòcits. Implicació en Malalties Inflamatòries i Síndromes Limfoproliferatives." Doctoral thesis, Universitat de Barcelona, 2006. http://hdl.handle.net/10803/2200.

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Les metal·loproteïnases de matriu (MMPs) són uns enzims de gran rellevància biològica en totes les accions relacionades amb la reorganització de la matriu extracel·lular i també en la regulació de molts processos cel·lulars.
Els limfòcits produeixen petites quantitats de gelatinases (MMP2 i MMP9) que són essencials en la migració a través dels teixits, tant en situacions fisiològiques com en els fenòmens patològics d'inflamació i disseminació tumoral.
Prèviament vam demostrar que la interacció amb proteïnes de la matriu extracel·lular a través de receptors integrina era un dels mecanismes més efectius no només en la producció sinó també en l'activació de gelatinases en cèl·lules limfoïdes T. No obstant, els mecanismes que modulen la producció de MMPs a través d'integrines en els limfòcits no estaven identificats. En el conjunt d'aquests treballs hem volgut aprofundir en diferents aspectes de la producció de gelatinases pels limfòcits derivada del contacte cel·lular. Primerament hem estudiat les vies de transducció de senyals involucrades en aquest procés i després hem analitzat les seves implicacions en dos processos fisiopatològics que tenen un vincle important amb el microentorn matricial: una malaltia inflamatòria invasiva (arteritis de cèl·lules gegants) i una patologia neoplàsica (síndromes limfoproliferatives).
Els resultats obtinguts en aquests treballs ens han permès arribar a les següents conclusions:

1. La senyalització a través d'integrines en resposta a estímuls del microentorn (proteïnes de la matriu extracel·lular, concretament fibronectina) és un mecanisme molt eficient per a la producció i activació de gelatinases (MMP2 i MMP9) i MMP14 pels limfòcits T i B.

2. La unió a fibronectina provoca un alliberament post-transcripcional ràpid de gelatinases en aquestes cèl·lules. La secreció d'aquests enzims és necessària per al procés d'invasió.

3. Els mecanismes de senyalització integrina estan modulats per FAK i la seva interacció amb Src. FAK, a través de l'acoblament de senyals duals, coordina l'alliberament de gelatinases i els processos d'adhesió cíclica necessaris per a la migració, suggerint que FAK adaptaria la secreció pulsàtil de gelatinases als canvis del citoesquelet en el procés invasiu limfocitari.

4. La inflamació de les artèries de pacients d'arteritis de cèl·lules gegants s'acompanya d'un increment en l'expressió i activació de gelatinases i es troba en relació topogràfica amb l'expressió d'integrines leucocitàries. Aquest fet suggereix que la progressió de l'infiltrat limfocitari està relacionat amb l'expressió i l'activació de les gelatinases, les quals a més contribuirien a la destrucció de l'estructura arterial. El tractament amb corticoids s'acompanya d'una disminució en l'expressió de MMPs.

5. La talidomida redueix la producció de gelatinases induïda per fibronectina en cèl·lules limfoïdes B interferint amb diferents vies de senyalització mitjançada per integrines. Aquest podria ser un dels mecanismes d'acció d'aquest fàrmac que explicaria la seva eficàcia en el tractament del mieloma múltiple en el microentorn medul·lar.

Com a conclusió general, les integrines leucocitàries poden coordinar la producció de gelatinases amb els mecanismes de migració cel·lular, afavorint el procés d'invasió cel·lular. Els processos inflamatoris i tumorals utilitzen aquest mecanisme, i la seva disrupció podria beneficiar l'evolució terapèutica d'aquestes patologies.
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Barreiros, Driely. "Aspectos moleculares da gênese e progressão de lesões periapicais induzidas experimentalmente em camundongos." Universidade de São Paulo, 2017. http://www.teses.usp.br/teses/disponiveis/58/58135/tde-01092017-093300/.

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O conhecimento dos eventos biológicos que ocorrem no periápice dos dentes com necrose pulpar se torna importante para compreender o desenvolvimento das lesões periapicais. Muitas são as moléculas e mediadores que participam na instalação da lesão periapical, a partir da infecção bacteriana que ocorre no interior dos canais radiculares. Assim, o objetivo do presente trabalho foi avaliar moléculas do sistema imune inato, da osteoclastogênese e metaloproteinases em lesões periapicais (LP) induzidas experimentalmente em camundongos knockout e wild type. Para esse objetivo, o presente estudo foi dividido em dois trabalhos distintos. O primeiro teve como objetivo avaliar a expressão de metaloproteinase 2 (MMP2) e metaloproteinase 9 (MMP9) durante a progressão da LP em camundongos knockout para TLR2 (TLR2 KO) e MyD88 (MyD88 KO), em comparação com camundongos wild type (WT). O segundo estudo avaliou a correlação da expressão gênica e imunomarcação de RANK, RANKL, OPG, TLR2 e MyD88 durante a progressão da LP em camundongos WT. No primeiro estudo lesões periapicais foram induzidas em molares inferiores de 54 camundongos TLR2 KO, MyD88 KO e WT (n=18/grupo). Após 7, 21 e 42 dias, os animais foram eutanaziados e as mandíbulas foram dissecadas e submetidas a processamento histotécnico. Os cortes histológicos foram submetidos a imunohistoquímica e posteriormente foi avaliada presença ou ausência de MMP2 e MMP9 nos diferentes grupos. No segundo estudo, 35 camundongos WT foram utilizados. As lesões periapicais foram induzidas nos primeiros molares inferiores de ambos os lados. Após 0 (G0), 7 (G7), 21 (G21) e 42 (G42) dias, os animais foram anestesiados e eutanasiados para que as mandíbulas fossem dissecadas e divididas ao meio.O lado direito das mandíbulas foi para o processamento histotécnico, para posterior marcação de RANK, RANKL, OPG, TLR2 e MyD88, por meio da imuno-histoquímica do lado esquerdo da mandíbula foi utilizado para a extração de RNA, para a determinação da expressão gênica de RANK (Tnfrsf11a), RANKL (Tnfrsf11), OPG (Tnfrsf11b), TLR2 (Tlr2) e MyD88 (Myd88) utilizando quantificação em Tempo Real da Reação da Polimerase em Cadeia (qRT-PCR). Para ambos os estudos, testes paramétricos e não paramétricos foram realizados com nível de significância de 5%. Foi possível observar, no primeiro estudo, que nos períodos iniciais da progressão da lesão periapical, houve um aumento na imunomarcação de MMP9 nos camundongos TLR2 KO e MyD88 KO, quando comparados aos WT, diferente da MMP2 que não se observou nenhum aumento na imunomarcação. No entanto, aos 42 dias observou-se uma redução da imunomarcação de MMP2 e um aumento da MMP9 nos camundongos TLR2 KO. Adicionalmente, no segundo estudo, foi possível observar um aumento da imunomarcação para RANK, RANKL, OPG, TLR2 e MyD88 durante a progressão da lesão periapical (p<0,05). O aumento da expressão de Tnfrsf11 foi diferente entre os grupos G0 e G42, e G21 e G42 (p=0,006). No entanto, a expressão de Tnfrsf11b foi diferente entre os grupos G0 e G7, G7, G21 e G42, sendo possível observar uma diminuição dessa expressão ao longo do tempo (p<0,001). Tlr2 foi mais expresso entre os grupos G0 e G42 (p=0,03). E a expressão da molécula Myd88 foi estatisticamente significante entre os grupos G0 e G7, G21 e G42 (p=0,01). A razão Tnfrsf11/Tnfrsf11b aumentou durante a progressão da lesão periapical (p=0,002). Também foi possível observar uma correlação moderada entre Myd88 e Rankl (r=0,42; p=0,03) e entre Myd88 e Tlr2 (r=0,48; p<0,0001). Após as metodologias empregadas e os dados analisados, concluímos que a produção de MMP2 e MMP9 foi modulada por TLR2 e Myd88 durante a progressão da lesão periapical. Alem disso, podemos sugerir que existe uma correlação positiva entre o sistema RANK/RANKL/OPG e as proteínas do sistema imune inato, TLR2 e MyD88, durante a perda óssea decorrente da infecção bacteriana dos canais radiculares e posterior progressão da lesão periapical.
Knowledge of the biological events occurring inteeth apex with pulp necrosis becomes important to understand the development of periapical lesions. There are manymolecules and mediators that participate in the installation of the periapical lesion, from the bacterial infection that occurs inside the root canals. Thus, the aim of the present study was to evaluate molecules of the innate immune system, osteoclastogenesis and metalloproteinases in experimentally apical periodontitis (AP) induced in knockout and wild type mice. For this purpose, the present study was divided into two distinct studies. The first one aimed to evaluate the expression of metalloproteinases 2 (MMP2) and metalloproteinases 9 (MMP9) during the progression of AP in TLR2 knockout mice (TLR2 KO) and MyD88 knockout mice (MyD88 KO), compared to wild type mice (WT). The second study evaluated the correlation of gene expression and immunostaining of RANK, RANKL, OPG, TLR2 and MyD88 during LP progression in WT mice. In the first study AP were induced in lower molars of 54 TLR2 KO, MyD88 KO and WT mice (n = 18 / group). After 7, 21 and 42 days, the animals were euthanized and the jaws were dissected and submitted to histotechnical processing. The histological sections were submitted to immunohistochemistry and subsequently the presence or absence of MMP2 and MMP9 in the different groups was evaluated. In the second study, 35 WT mice were used. Periapical lesions were induced in the lower first molars on both sides. After 0 (G0) to 7 (G7), 21 (G21) and 42 (G42) days, the animals were anesthetized and euthanized so that the jaws were dissected and divided in half. The right side of the jaws was for the histotechnic processing, for subsequent imunostaining of RANK, RANKL, OPG, TLR2 and MyD88, through immunohistochemistry and the left side of the jaws was used for the extraction of RNA, for the determination of expression of RANK (Tnfrsf11a), RANKL (Tnfrsf11), OPG (Tnfrsf11b), TLR2 (Tlr2) and MyD88 (Myd88) using Quantification Real Time of Polymerase Chain Reaction (qRT-PCR). For both studies, parametric and non-parametric tests were performed with significance level of 5%. It was possible to observe in the first study that in the initial periods of AP progression there was an increase in MMP9 immunostaining in TLR2 KO and MyD88 KO mice when compared to WT, different from MMP2 that no increase in immunostaining was observed. However, at 42 days there was a reduction in MMP2 immunostaining and an increase of MMP9 in TLR2 KO mice was observed. Additionally, in the second study, it was possible to observe an increase in the immunostaining for RANK, RANKL, OPG, TLR2 and MyD88 during periapical lesion progression (p <0.05). The increase in Tnfrsf11 expression was different between groups G0 and G42, and G21 and G42 (p = 0.006). However, the expression of Tnfrsf11b was different between the G0 and G7, G7, G21 and G42 groups, and a decrease in expression over time (p <0.001) was observed. Tlr2 was more expressed between the G0 and G42 groups (p = 0.03). And the expression of the Myd88 molecule was statistically significant between the G0 and G7, G21 and G42 groups (p = 0.01). The Tnfrsf11 / Tnfrsf11b ratio increased during the AP progression (p = 0.002). It was also possible to observe a moderate correlation between Myd88 and Rankl (r = 0.42, p = 0.03) and between Myd88 and Tlr2 (r = 0.48, p <0.0001). After the methodologies used and the data analyzed, we conclude that the production of MMP2 and MMP9 was modulated by TLR2 and Myd88 during the AP progression. In addition, we can suggest that there is a positive correlation between the RANK / RANKL / OPG system and the proteins of the innate immune system, TLR2 and MyD88, during bone loss due to bacterial infection of the root canals and subsequent progression of the apical periodontitis.
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Books on the topic "MMPZ"

1

Hathaway, Starke R. MMPI-2. [Minneapolis, MN]: University of Minnesota Press, 1989.

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L, Greene Roger, ed. The MMPI-2/MMPI: An interpretive manual. Boston: Allyn and Bacon, 1991.

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Greene, Roger L. The MMPI-2 / MMPI: An Interpretive Manual. Boston: Allyn and Bacon, 1991.

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Butcher, James Neal. Essentials of MMPI-2 and MMPI-A interpretation. 2nd ed. Minneapolis: University of Minnesota Press, 2000.

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Butcher, James Neal. Essentials of MMPI-2 and MMPI-A interpretation. Minneapolis: University of Minnesota Press, 1992.

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Radhika, Krishnamurthy, and Jacobson Jody M, eds. MMPI-A casebook. Odessa, Fla: Psychological Assessment Resources, 1994.

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P, Anderson Wayne, ed. MMPI & MMPI-2: Interpretation manual for counselors and clinicians. 4th ed. Bristol, Pa: Accelerated Development, 1995.

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1933-, Butcher James Neal, and Seelen Joyce, eds. The MMPI, MMPI-2 & MMPI-A in court: A practical guide for expert witnesses and attorneys. 2nd ed. Washington, DC: American Psychological Association, 2000.

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1933-, Butcher James Neal, and Seelen Joyce, eds. The MMPI, MMPI-2 & MMPI-A in court: A practical guide for expert witnesses and attorneys. Washington, DC: American Psychological Association, 1993.

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Lewak, Richard W. Therapist guide to MMPI & MMPI-2: Providing feedback and treatment. Muncie, Ind: Accelerated Development Inc., 1990.

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Book chapters on the topic "MMPZ"

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Leeth, Chris. "MMPI." In Encyclopedia of Child Behavior and Development, 958. Boston, MA: Springer US, 2011. http://dx.doi.org/10.1007/978-0-387-79061-9_1808.

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Fingleton, Barbara. "MMPs." In Cancer Therapeutic Targets, 591–601. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4419-0717-2_21.

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Fingleton, Barbara. "MMPs." In Cancer Therapeutic Targets, 1–11. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4614-6613-0_21-3.

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Oette, Mark, Marvin J. Stone, Hendrik P. N. Scholl, Peter Charbel Issa, Monika Fleckenstein, Steffen Schmitz-Valckenberg, Frank G. Holz, et al. "MMP." In Encyclopedia of Molecular Mechanisms of Disease, 1337. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-29676-8_8142.

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Temple, Richard. "Validity Scales (MMPI)." In Encyclopedia of Clinical Neuropsychology, 3549–50. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-57111-9_2015.

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Temple, Richard. "Validity Scales (MMPI)." In Encyclopedia of Clinical Neuropsychology, 2581–82. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-0-387-79948-3_2015.

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Temple, Richard. "Validity Scales (MMPI)." In Encyclopedia of Clinical Neuropsychology, 1–2. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-56782-2_2015-2.

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Sellbom, Martin, and Tayla T. C. Lee. "Assessment of Anxiety Symptoms Using the MMPI-2, MMPI-2-RF, and MMPI-A." In Handbook of Assessing Variants and Complications in Anxiety Disorders, 139–62. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-6452-5_10.

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Swain, Niharika, Jigna Pathak, Shilpa Patel, and Rashmi Maruti Hosalkar. "MMP-9." In Encyclopedia of Signaling Molecules, 3162–67. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_102000.

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Swain, Niharika, Jigna Pathak, Shilpa Patel, and Rashmi Maruti Hosalkar. "MMP-9." In Encyclopedia of Signaling Molecules, 1–6. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4614-6438-9_102000-1.

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Conference papers on the topic "MMPZ"

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Hurley, Jennifer R., Abdul Q. Sheikh, Meredith Beckenhaupt, Cameron Ingram, Andrew Mutchler, and Daria A. Narmoneva. "Self-Assembling Peptide Nanofibers for MMP Delivery and Cardiac Regeneration in Diabetes." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53761.

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Diabetes is a serious problem in the United States, afflicting 7.8% of the population with annual medical costs estimated at $116B in 2007 (1). Diabetic cardiomyopathy (DCM) is a cardiovascular complication of diabetes resulting in pathological alterations to the myocardium including circulatory defects, impaired heart muscle contraction, and progressive fibrosis. Cardiac fibrosis is associated with an imbalance between the deposition of the extracellular matrix (ECM) proteins by cardiac fibroblasts and the ECM proteolytic degradation via matrix metalloproteinases (MMPs). Recent studies have demonstrated that in the diabetic heart, expression and activity of MMP-2 are reduced, resulting in increased collagen accumulation and cardiac dysfunction (2). These observations suggest that a MMP-related mechanism may contribute to cardiac fibrosis, and that it may be attenuated through stimulation of native MMP-2 expression or delivery of exogenous MMP-2. Therefore, reduced MMP-2 activity in DCM may represent a novel target for therapeutic treatment (3). To achieve this, a special proteolytically-stable delivery scaffold would be needed, because native ECM is rapidly degraded by MMPs. The goal of this study is to determine if self-assembling peptide nanofibers can be used for long-term (several weeks) MMP delivery and enhancement of cardiac remodeling. This study tests the hypothesis that increased MMP-2 concentration (native or exogenous) in the nanofiber environment will promote matrix remodeling in diabetic cardiac fibroblasts in vitro.
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Sakamoto, Naoya, Toshiro Ohashi, and Masaaki Sato. "High Shear Stress Induces Production of Matrix Metalloproteinase in Endothelial Cells." In ASME 2008 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2008. http://dx.doi.org/10.1115/sbc2008-192695.

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One of the major physiological functions of vascular endothelial cells (ECs) includes remodeling of vessel walls. ECs secrete matrix metalloproteinases (MMPs) to degrade extracellular matrix (ECM), such as elastin and collagen. At least 23 different MMPs have been identified and have the capacity to degrade components of ECM. For example, MMP-9, known as a gelatinase, can degrade elastic fibers. The balance between MMPs and their specific inhibitors, tissue inhibitor of metalloproteinases (TIMPs), tightly governs vascular remodeling and is belived to play a central role in the pathogenesis of arterial aneurysms [1].
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Javid, Khalid, Hadil Abu Khalifeh, Hadi Belhaj, and Mohammed Haroun. "Improving MMP by Co-Injection of Miscible CO2 With Abu Dhabi Crude Oil." In ASME 2013 32nd International Conference on Ocean, Offshore and Arctic Engineering. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/omae2013-10258.

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Miscible CO2 injection is a method to increase oil production. Combinations of Carbon dioxide with other gases as miscible solvents are emphasized in this paper to improve CO2 miscible injection process. Emphasis is on identifying CO2 solvent mixtures with reduced MMP to achieve miscibility at reasonable injection pressures in Abu Dhabi fields. Two targeted crude oils (Oil 1 and Oil 2) from Abu Dhabi carbonate reservoirs are utilized. The minimum miscibility pressure (MMP) of targeted oils with mixtures of N2, CH4, C2H6, and HC rich gas of varying composition with CO2 injection gas are evaluated through simulation. Cell to Cell and Semi-analytical (key tie lines) methods are applied using CMG simulator. Results show that miscibility is predicted to occur with multiple contact miscibility (MCM): vaporization and/or condensation mechanisms. The increase of C2H6 concentration in the CO2 injected gas reduced MMPs for targeted Oil 1 by 100 psi/10 mol%. However, N2, CH4 and HC rich gas increments in CO2 injected gas increased the MMPs for targeted Oil 1. MMP was observed to be 2300 psi for pure ethane with Oil 1. In addition, MMPs for targeted oils with N2/ C2H6 and N2/ CH4 injected gas mixtures are assessed. This study can open possibilities for future enriching of CO2 and N2 miscible injection to improve miscibility and recovery of oil.
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Shaverdashvili, Khvaramze, Poki Wong, Jun Ma, Keman Zhang, Iman Osman, and Barbara Bedogni. "Abstract B07: Targeting an MT1-MMP/MMP2 axis in melanoma by a novel MT1-MMP/MMP2 inhibitor." In Abstracts: AACR Special Conference on Advances in Melanoma: From Biology to Therapy; September 20-23, 2014; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.mel2014-b07.

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Milisavljevic, Jelena, Sesh Commuri, Janet K. Allen, and Farrokh Mistree. "A Concurrent Design Exploration Method for Realizing Networked Manufacturing Systems." In ASME 2017 International Design Engineering Technical Conferences and Computers and Information in Engineering Conference. American Society of Mechanical Engineers, 2017. http://dx.doi.org/10.1115/detc2017-67557.

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Multistage manufacturing processes (MMPs) are networked manufacturing systems consisting of multiple operational stations that have characteristics of mechanical and control systems. Common challenges in the design of MMPs are the selection of sensors and tools as this not only affects the dimensional quality of the finished product, but also influences the computational complexity in representing and analyzing the problem. Imprecise or incomplete information results in uncertainty in the models used to represent the MMP and limit the use of traditional design approaches. In this paper, an exploration method for the concurrent design (CDEM) of MMPs under uncertainty is presented wherein the attributes of tools and sensors are treated as design variables, thereby allowing flexibility in a design process. The proposed method is illustrated using an example of automotive panel stamping process. Our focus in this paper is on the method rather than the results per se.
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Ding, Yu, Jianjun Shi, and Dariusz Ceglarek. "Diagnosability Analysis of Multi-Station Manufacturing Processes." In ASME 2002 International Mechanical Engineering Congress and Exposition. ASMEDC, 2002. http://dx.doi.org/10.1115/imece2002-32343.

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Variation propagation in a multi-station manufacturing process (MMP) is described by the theory of “Stream of Variation.” Given that the measurements are obtained via certain sensor distribution scheme, the problem of whether the stream of variation of an MMP is diagnosable is of great interest to both academia and industry. We present a comprehensive study of the diagnosability of MMPs in this paper. It is based on the state space model and is parallel to the concept of observability in control theory. Analogous to the observability matrix and index, the diagnosability matrix and index are first defined and then derived for MMP systems. The result of diagnosability study is applied to the evaluation of sensor distribution strategy. It can also be used as the basis to develop an optimal sensor distribution algorithm. An example of a three-station assembly process with multi-fixture layouts is presented to illustrate the methodology.
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Ni, Qingwen, and Shuo Chen. "Assessing the Effect of Matrix Metalloproteinase-9 on the Growth of Mice Teeth." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53708.

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Dentin and bone are formed when odontoblasts and osteoblasts synthesize and secrete collagen type I-rich extracellular matrix that mineralizes in a highly controlled manner. A wide spectrum of mouse and human disorders affecting tooth and bone biomineralization shows that dentin and bone formation are under strict genetic control. Although the controlling mechanisms of dentinogenesis and osteogenesis require further study, a large body of evidence points to the importance of the matrix metalloproteinases (MMPs) participate in a wide variety of extracellular matrix degradation. Detailed knowledge of MMPs may be important for understanding the pathogenesis of tooth development. Some researchers have pointed MMP-9 is an extracelluar proteinase that is highly expressed in osteoclasts and has been postulated to play an important role in their resorptive activity. Although MMP-9 has been reported to play a role in bone resorption, the association of this enzyme during deciduous tooth resorption has not yet been clarified. Based on accumulating evidence, we hypothesized that MMP-9 should play a role in teeth attrition. In this study, we have applied NMR relaxation technique to assess age-related MMP-9 KO tooth quality in vitro by quantifying changes in dentin and pulp simultaneously. The major hypothesis in this paper was that whether noninvasive NMR relaxation time measurements could be used to characterize MMP-9 KO changes in dentin and pulp, and to predict tooth quality. Specifically, we tested that age-related MMP-9 KO tooth changes result in an alteration of the NMR spin-spin (T2) relaxation time signal due to the structural changes in the tooth matrix. This signal can be further processed to produce a T2 relaxation distribution spectrum related to dentin and pulp, and their derived parameters can be used as descriptors of age-related MMP-9 KO tooth changes. In this study, the proton liquid-like NMR spin-spin (T2) relaxation decay signal was obtained from the Carr-Purcell-Meiboom-Gill (CPMG) NMR spin echo train method [1,2], then the relaxation decay signal was converted to T2 relaxation distribution spectra describing the size domain of dentin and pulp. Therefore, we can calibrate the intensities in NMR inversion T2 relaxation distribution spectra corresponding to the amount of dentin and pulp related to the structural changes. Here, we propose an NMR calibration method “NMR standard estimation” — the ratio of the amount of pulp to the amount of dentin obtained from NMR T2 distribution spectra that can be used to measure the age-related MMP-9 KO structural changes in teeth [3]. We are cognizant of the biological and physiological variability manifest in teeth size variations, but feel that this kind of NMR standard estimation — the ratio of amount of dentin to amount of pulp from the NMR T2 inversion spectrum can be used to determine age-related MMP-9 KO structural changes in teeth and eliminate any variations in size of teeth.
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Wyatt, Karla E. K., Jonathan W. Bourne, and Peter A. Torzilli. "Deformation-Dependent Enzyme Cleavage of Collagen." In ASME 2007 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2007. http://dx.doi.org/10.1115/sbc2007-176502.

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Collagen degradation is a mechanism for normal musculoskeletal development and extracellular matrix (ECM) maintenance, and in response to trauma, disease and inflammation. Matrix metalloproteinases (MMP-1, 8, and 13, the collagenases) are the primary enzymes that act to degrade collagen. These MMPs gain access to the collagen triple helix by binding to the enzyme’s attachment domain along the α-chains, followed by separation (unwinding) of the α-chains to expose the 3/4–1/4 cleavage site, and then cleavage of the α-chain by the enzyme’s catalytic domain [3, 5].
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"26th Annual Midwest Microbial Pathogenesis Conference (MMPC)." In 26th Annual Midwest Microbial Pathogenesis Conference (MMPC). Frontiers Media SA, 2020. http://dx.doi.org/10.3389/978-2-88963-591-7.

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Jin, Weizhong, and Jiaoli Wang. "Adipocyte-derived exosomes promote lung cancer metastasis byincreasing MMP9 activity via transferring MMP3 to lung cancer cells." In ERS International Congress 2017 abstracts. European Respiratory Society, 2017. http://dx.doi.org/10.1183/1393003.congress-2017.pa3300.

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Reports on the topic "MMPZ"

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Seits, Margaret. Identifying pedophiles with the MMPI. Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.5734.

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Gregg, Michael C., and Jack B. Miller. Modular Microstructure Profiler (MMP). Fort Belvoir, VA: Defense Technical Information Center, September 2007. http://dx.doi.org/10.21236/ada605602.

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Funk, Russell. MMPI and the juvenile sex offender Russell Funk. Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.5694.

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Fresquez, Nancy. MMP Overview Briefing for Savannah River. Office of Scientific and Technical Information (OSTI), November 2020. http://dx.doi.org/10.2172/1711358.

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Lynch, Conor C. How MMPs Impact Bone Responses to Metastatic Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, February 2010. http://dx.doi.org/10.21236/ada529376.

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Benson, J., and M. Meth. ANALYZING POWER SPECTRUM CALCULATIONS MADE ON THE BOOSTER MMPS. Office of Scientific and Technical Information (OSTI), November 1991. http://dx.doi.org/10.2172/1150601.

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Marneris I. and A. G. Ruggiero. Running the AGS MMPS at 5 HZ, 24 GEV. Office of Scientific and Technical Information (OSTI), March 2000. http://dx.doi.org/10.2172/1061608.

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Lynch, Conor C. How MMPs Impact Bone Responses to Metastatic Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, February 2008. http://dx.doi.org/10.21236/ada482544.

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Lynch, Conor C. How MMPs Impact Bone Responses to Metastatic Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, April 2011. http://dx.doi.org/10.21236/ada544473.

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Gregg, Michael C., and Jack B. Miller. Construction of a Modular Microstructure Profiler (MMP). Fort Belvoir, VA: Defense Technical Information Center, May 2009. http://dx.doi.org/10.21236/ada499710.

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