Academic literature on the topic 'MMPs'

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Journal articles on the topic "MMPs"

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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, et al. "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 (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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Dr, Raj Kumar Gupta. "Comparison of Concentrations of MMP2 and MMP9 in Aqueous Humor of Patients Suffering with Acute Primary Angle Closure Short Title: MMPs and acute primary angle closure." International Journal of Innovative Science and Research Technology 7, no. 9 (2022): 1180–84. https://doi.org/10.5281/zenodo.7312298.

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Objective- Inflammation with neovascularization leads to elevated intraocular pressure( IOP) which is only modified risk factor for acute primary angle closure ( APAC) caused by decreased aqueous humor outflow from the anterior chamber. The present study has been planned to compare the levels of MMPs in aqueous humor of patients with APAC and aimed to analyse the molar ratio of MMPs with respect to the other MMPs. Methods- Aqueous humor samples were collected from 46 healthy control persons ( non-glaucomatous) and 52 APAC patients undergoing cataract surgery. Molar concentrations of all the MMPs were measured using multiplexed immunoassays Kit Methods. Statistical significance was assessed with Mann–Whitney U tests, and Spearman’s method was used to assess correlations with age and IOP. Results: Concentrations of MMP1 (p = 0.003), MMP2 (p = 0.0001), MMP3 (p = 0.002), MMP7 (p = 0.002), MMP8 (p = 0.001), MMP9 (p = 0.0001), MMP12(p = 0.002) and MMP13 (p = 0.002) were significantly increased in aqueous humor samples from APAC versus healthy control group. For the majority of MMP- molar ratios calculated and after comparing the APAC group to healthy controls, the molar ratios of MMP2 and MMP-9 with respect to other MMPs showed a significant increase in APAC samples. Conversely, the MMP2/MMP9 (p = 0.045) and MMP9/TIMP2 (p = 0.033) molar ratios were not significantly increased. Conclusions: An imbalance among concentrations of MMPs was found in glaucomatous aqueous humor samples, with a shift toward raised molar ratio of MMPs except MMP2/MMP9. This may result in the inhibition of MMP activity, leading to an altered ECM composition in the TM and thereby contributing to increased outflow resistance.
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Bartnykaitė, Agnė, Aistė Savukaitytė, Justina Bekampytė, et al. "The Role of Matrix Metalloproteinase Single-Nucleotide Polymorphisms in the Clinicopathological Properties of Breast Cancer." Biomedicines 10, no. 8 (2022): 1891. http://dx.doi.org/10.3390/biomedicines10081891.

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(1) Background. Breast cancer is the leading cancer type among women. Despite convenient diagnostics at early stages, there is a need for continuous monitoring to predict more aggressive or recurring breast cancer forms. The evidence suggests that the detection of genetic biomarkers could help in improving disease management and reduce mortality. Matrix metalloproteinases (MMPs) are a large family of enzymes that perform physiologically relevant functions and have the potential properties to be biomarkers for cancer assessment. We aimed to evaluate the contribution and association of single-nucleotide polymorphisms (SNPs) in MMP genes (MMP1, MMP2, MMP3, MMP7, MMP8, MMP9) with clinicopathological breast-cancer features. (2) Methods. In this study, 100 breast cancer patients were genotyped by polymerase chain reaction–restriction fragment length polymorphism methodology (PCR–RFLP). (3) Results. The presence of the MMP7 rs11568818 A allele was associated with lower chances for poorly differentiated breast cancer. The lower possibility for HER2-positive breast cancer was associated with the presence of the MMP9 rs3918242 C allele. (4) Conclusions. These results indicate that MMP7 rs11568818 and MMP9 rs3918242 are potential biomarkers for the anticipation of breast cancer aggressiveness.
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Казеко, Л. А., В. А. Захарова, and Ю. Д. Бенеш. "The Role of Matrix Metalloproteinases and Their Tissue Inhibitors in the Pathogenesis of Aggressive Periodontitis." Стоматология. Эстетика. Инновации, no. 4 (November 25, 2022): 329–36. http://dx.doi.org/10.34883/pi.2022.6.4.006.

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Нарушение баланса между уровнями MMPs и TIMPs является одним из звеньев патогенеза патологии периодонта. Данные о том, какие именно MMPs играют решающую роль в определении характера течения периодонтитов, весьма противоречивы. Цель. Установить роль параметров стромальной экспрессии MMPs и TIMPs в биопсийном материале десен пациентов в патогенезе быстропрогрессирующего периодонтита. Материалы и методы. Исследован биопсийный материал десен 26 пациентов с быстропрогрессирующим характером течения периодонтита, окрашенный с использованием моноклональных антител к MMP (-1, -2, -8, -9, -13, -14) и TIMP (-1, -2). Морфометрический и статистический анализ выполнен с использованием AperioImageScopev12.4.0.5043, Statistica10.0, р<0,01. Результаты. В группе пациентов с быстропрогрессирующим периодонтитом имеют место сопоставимые или более низкие параметры позитивности экспрессии MMP8 (5%), MMP9 (0,6%) и ММР13 (10%) по сравнению с таковыми ТIMP1 (12,5%) и TIMP2 (42%). Высокие же параметры позитивности экспрессии ММР1 (78,5%), ММР2 (56,5%) и ММР14 (77,0%), которые в 4–9 раз превышали таковые TIMP1 и до 6 раз TIMP2, отражают низкую эффективность ингибирующего действия на них вышеназванных TIMPs и, вероятно, вносят основной вклад в агрессивное течение периодонтита. Заключение. Сравнительный анализ уровней экспрессии MMPs и TIMPs показал, что в группе пациентов с быстропрогрессирующим течением периодонтита в ответ на рост параметров экспрессии MMPs значимо повышается экспрессия как TIMP1, так и TIMP2 с более эффективным ингибированием ими MMP8, MMP9 и ММР13. Сохранение же значимо более высоких параметров экспрессии ММР1, ММР2 и ММР14 по сравнению с таковыми TIMP1 и TIMP2 является отражением дисбаланса их экспрессии и, вероятно, может иметь решающее значение в патогенезе быстропрогрессирующей деструкции периодонтальных тканей и утраты альвеолярной кости. The imbalance between MMPs and TIMPs levels is one of the links in the pathogenesis of periodontal pathology. The data on which MMPs play a crucial role in determining the type of periodontitis course are quite controversial. Purpose. To determine the parameters of stromal expression of MMPs and TIMPs in the gingival biopsy material of patients with aggressive periodontitis. Material and methods. The gingival biopsy from 26 patients with aggressive periodontitis (AgP, n=26) was analyzed. Morphometric and statistical analysis of MMPs (-1, -2, -8, -9, -13, -14) and TIMP1 expression was performed using AperioImageScope v12.4.0.5043, Statistica 10.0, p<0.05. Results. In the AgP group, there are comparable or lower parameters of positive expression of MMP8 (5%), MMP9 (0.6%) and MMP13 (10%) compared with those of TIMP1 (12.5%) and TIMP2 (42%). The high parameters of the positive expression of MMP1 (78.5%), MMP2 (56.5%) and MMP14 (77.0%), which were 4–9 times higher than those of TIMP1 and up to 6 times TIMP2, reflect the low effectiveness of the inhibitory effect of the above-mentioned TIMPs on them and probably make the main contribution to the aggressive course of periodontitis. Conclusion. Comparative analysis of MMPs and TIMPs expression levels showed that in the AgP group, in response to an increase in MMPs expression parameters, the expression of both TIMP1 and TIMP2 significantly increased with more effective inhibition of MMP8, MMP9 and MMP13. The preservation of significantly higher expression parameters of MMP1, MMP2 and MMP14 compared to those of TIMP1 and TIMP2 is a reflection of the imbalance of their expression and, probably, may be crucial in the pathogenesis of progressive destruction of periodontal tissues and loss of alveolar bone.
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Sakowicz, Agata, Michalina Lisowska, Lidia Biesiada, et al. "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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Shurygina, Irina, Lyubov Rodionova, Natalia Ayushinova, Elena Chepurnykh, Irina Trukhan, and Michael Shurygin. "Effect of the p38 MAPK Inhibitor on the Expression of Metalloproteinases and Their Inhibitors during the Formation of Abdominal Adhesions." International Journal of Biomedicine 11, no. 4 (2021): 446–50. http://dx.doi.org/10.21103/article11(4)_oa9.

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Background: The aim of this study was to assess the effect of blockade of the p38 mitogen-activated protein kinase (MAPK) on the expression of genes encoding metalloproteinases (MMPs) during the formation of adhesions in the abdominal cavity. Methods and Results: The experiments were carried out on male Wistar rats (n=75). The studies were carried out in two groups: Group 1 (control, n=35) – modelling the adhesive process; Group 2 (experimental, n=35) – modelling the adhesive process with intraperitoneal administration of Seroguard®—a prolonged form of the p38 MAPK inhibitor. The expression of the MMP1a, MMP2, MMP7, MMP9, and TIMP genes was assessed using real-time PCR. In the control group, overexpression of the MMP1a and MMP7 genes began from 6 hours after modeling the adhesive process, MMP9 – from Day 1, MMP2 – from Day 7 and persisted until the end of observation. With local blockade of p38 MAPK, the level of overexpression of genes encoding MMPs in the early stages was higher than in the control group (MMP1a – by Day 1; MMP7 – by 6 hours and Day 1, MMP9 – by 12 hours). From Day 3 to Day 14, the MMP1a and MMP7 expression in the experimental group was significantly lower than in the control group. Conclusion: The performed study demonstrated the involvement of different types of MMPs—collagenases (MMP1a), gelatinases (MMP2 and 9), matrilysins (MMP7)—in the rearrangement of the extracellular matrix during the process of adhesion formation in the abdominal cavity.
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Decock, J., W. Hendrickx, M. Drijkoningen, et al. "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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Soboleva, Anna G., Vladimir V. Sobolev, Mari M. Karapetyan, et al. "Laser Therapy Changes the Expression of Matrix Metalloproteinases in Bleomycin-Induced Skin Fibrosis." Life 13, no. 3 (2023): 810. http://dx.doi.org/10.3390/life13030810.

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Matrix metalloproteinases (MMPs) are often considered biomarkers of skin fibrosis. At the early stages of the pathological process, an elevation of their enzymatic activity causes significant changes in the composition of the extracellular matrix. MMPs secreted by immune cells facilitate their migration to the site of damage. Then, the immune cells eliminate the affected cells and biomolecules. Moreover, bidirectional changes in the activity of proteolytic enzymes, including MMPs, accompany wound healing. This study aimed to assess changes in the expression of Mmp2, Mmp3, and Mmp9 after treating mice with laser therapy using the experimental model of bleomycin-induced skin fibrosis. Using immunohistochemistry, we characterized the histological features of scarred skin. We also analyzed changes in the expression of MMPs using real-time polymerase chain reaction before and after laser irradiation. We showed that treatment of the mice with a CO2 laser partially normalized the histological features of scarred skin. We also noticed a decrease in the expression of Mmp2, Mmp3 (both p < 0.05), and Mmp9 (p = 0.065) during scar healing. The obtained results suggest that normalization of skin homeostasis requires control of MMP activity via induction of genes.
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Huber, Vincent J., Hironaka Igarashi, Satoshi Ueki, et al. "Visualizing the Distribution of Matrix Metalloproteinases in Ischemic Brain Using In Vivo 19F-Magnetic Resonance Spectroscopic Imaging." Contrast Media & Molecular Imaging 2019 (January 6, 2019): 1–8. http://dx.doi.org/10.1155/2019/8908943.

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Matrix metalloproteinases (MMPs) damage the neurovascular unit, promote the blood-brain barrier (BBB) disruption following ischemic stroke, and play essential roles in hemorrhagic transformation (HT), which is one of the most severe side effects of thrombolytic therapy. However, no biomarkers have presently been identified that can be used to track changes in the distribution of MMPs in the brain. Here, we developed a new 19F-molecular ligand, TGF-019, for visualizing the distribution of MMPs in vivo using 19F-magnetic resonance spectroscopic imaging (19F-MRSI). We demonstrated TGF-019 has sufficient sensitivity for the specific MMPs suspected in evoking HT during ischemic stroke, i.e., MMP2, MMP9, and MMP3. We then utilized it to assess those MMPs at 22 to 24 hours after experimental focal cerebral ischemia on MMP2-null mice, as well as wild-type mice with and without the systemic administration of the recombinant tissue plasminogen activator (rt-PA). The 19F-MRSI of TGN-019-administered mice showed high signal intensity within ischemic lesions that correlated with total MMP2 and MMP9 activity, which was confirmed by zymographic analysis of ischemic tissues. Based on the results of this study, 19F-MRSI following TGN-019 administration can be used to assess potential therapeutic strategies for ischemic stroke.
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Dissertations / Theses on the topic "MMPs"

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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.<br>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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Ylipalosaari, M. (Merja). "Matrix metalloproteinases (MMPs) in oral carcinomas." Doctoral thesis, University of Oulu, 2005. http://urn.fi/urn:isbn:9514277309.

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Abstract Matrix metalloproteinases, MMPs, are a family of enzymes capable of modulating connective tissue components. The expression of several MMPs is increased in oral squamous cell carcinomas (OSCCs). They are assumed to have an important role in the development and progression of OSCCs. However, the exact role and mechanism of the regulation of MMPs in malignant transformation are still largely unknown. In this study, tumour-associated trypsin-2 (TAT-2) was detected in OSCC tissue sections, and its role in MMP-2 and -9 regulation in carcinoma cells was evaluated. The TAT-2 gene was transfected into two different OSCC cell lines and one immortalized oral epithelial cell line. In TAT-2-transfected cells, MMP-9 activation increased OSCC cell invasion in chicken chorionallantoic membrane assay. Increased intravasation was prevented by tumour-associated trypsin inhibitor or specific gelatinase-inhibiting CTT-peptide. TAT-2 also converted MMP-1, -8, -13 and -3 into smaller molecular weight forms in vitro. However, TAT-2-transfected OSCC cells showed no conversion. TAT-2 was demonstrated to degrade powerfully type I collagen into small fragments in vitro. The cell surface receptor αvβ6 integrin is strongly up-regulated in OSCCs. By using β6-transfected OSCC cells, it was demonstrated that αvβ6 integrin down-regulates MMP-13 expression. However, this integrin did not regulate other collagenases or TIMP-1. β6-transfected cells invaded more efficiently through the basement membrane matrix, but their migration through type I collagen remained unchanged. MMP-8 expression was detected for the first time in head and neck squamous cell carcinoma (HNSCC) cell lines and corresponding cultured dermal and tumour fibroblasts. The localization of MMP-8 in HNSCC was determined by immunohistochemical stainings and in situ hybridization. MMP-8 production levels in carcinoma cells were faint and sporadic in HNSCCs sections. Ninety-two primary mobile tongue SCCs were subjected to MMP-8 immunohistochemical staining, and the staining results were compared to survival rates. MMP-8 was associated with improved disease-free survival in females but not in males.
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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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Bourd-Boittin, Katia. "Rôle des métalloprotéinases matricielles (MMPs) dans l'odontologie." Paris 5, 2005. http://www.theses.fr/2005PA05M001.

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La dégradation protéolytique des constituants de la matrice extracellulaire par les métalloprotéinases matricielles (MMPs) joue un rôle majeur dans l'odontogénèse. Après avoir identifié la présence et le profil d'expression des gélatinases (MMP-2 et MMP-9), de la MMP-20 et des TIMP-1 et -2 dans l'incisive de rat, nous avons cherché à mieux comprendre comment les MMPs et plus particulièrement les gélatinases et la MMP-20 pouvaient agir dans les processus d'organisation et de minéralisation des matrices dentaires. L'inhibition de leur activité par un inhibiteur synthétique des MMPs à large spectre, le Marimastat, dans un modèle des germes embryonnaires de souris en culture, a pertubé les mécanismes de nucléation dans la matrice dentinaire et a provoqué des pertubations sévères de la mise en place et par conséquent de la minéralisation de l'émail. Ces importantes altérations observées au niveau structural sont associées à des modifications au niveau moléculaire. En présence de Marimastat, deux des protéines majoritaires du tissu dentaire, la sialoprotéine dentinaire (DSP) et plus particulièrement l'amélogénine s'accumulent de manière anormale dans la matrice extracellulaire. Ces pertubations se traduisent par une modification de leurs différentes formes moléculaires. Ceci démontre la nécessité de la dégradation progressive de ces constituants matriciels. Le clivage de l'amélogénine par la MMP-20 a déjà été rapporté. En revanche, la dégradation protéolytique de la DSP par des protéases n'a jamais été décrite auparavant, nous avons pu montrer que la DSP mais aussi l'amélogénine sont clivées de manière rapide et totale par la MMP-2 recombinante. Par contre la MMP-9 n'a pas d'effet sur ces deux protéines dans les mêmes conditions expérimentales. La large distribution de la MMP-2 au sein des tissus dentaires, ainsi que sa capacité à dégrader certains constituants spécifiques des matrices dentaires permettent de lui attribuer un rôle majeur en association avec la MMP-20 dans l'établissement et la minéralisation de la dentine et de l'émail<br>The proteolytic degradation of the ECM components by the matrix metalloproteinases (MMPs) is thought to play a crucial role in odontogenesis. The aim of this thesis was to analyse the expression of several MMPs, namely MMP-2, MMP-9 and MMP-20, as well as of their physiological inhibitors, the TIMP-1 and TIMP-2 during tooth development and study their role in the formation and maturation of dental matrices. The two gelatinases (MMP-2 and MMP-9), enamelysin (MMP-20) and TIMP-1 and -2 have shown a developmentally regulated expression and specific localization within the developing tootth. The role of these MMPs in the processing and mineralization of the dental matrix was further studied in an organotypic culture model of developing mouse tooth germ. The inhibition of the MMPs activity in this model by a broad spectrum synthetic inhibitor, Marimastat, altered dental matrix nucleation and caused severe disruptions of enamel organisation and mineralization. These macroscopic effects was associated with significant modifications at the molecular level. MMP inhibition deregulated the molecular processing of two major dental matrix proteins, amelogenin and dental sialoprotein (DSP), coinciding with their accumulation and the loss of their normal distribution. While the cleavage of amelogenin by MMP-20 has been extensively studied, that of DSP has not been previously described. Our experiments provide evidence that MMP-2 is able to efficiently degrade DSP as well as amelogenin, while under the same conditions, MMP-9 had no effect. Based on the intense expression and large distribution of MMP-2 and its importance in the processing of the dental matrix, we suggest a major role for this enzyme, in association with MMP-20, in the maturation and mineramization of dentin and enamel
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David, Arnaud. "Protéomique fonctionnelle des Métalloprotéases Matricielles (MMPs) dédiée à la détection des formes acitves de MMPs dans des protéomes complexes." Phd thesis, Museum national d'histoire naturelle - MNHN PARIS, 2007. http://tel.archives-ouvertes.fr/tel-00555061.

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Les Métalloprotéases matricielles (MMPs) constituent une famille des métalloprotéases à zinc capables conjointement de dégrader l'ensemble des protéines de la matrice extracellulaire. Aujourd'hui, vingt-trois MMPs humaines ont été identifiées et sont caractérisées par leur séquence en aminoacides et leur structure 3D fortement conservées. Ces enzymes sont exprimées de manière constitutive au cours des processus de remodelage tissulaire. Leur surexpression dans un certain nombre de pathologies étroitement liée au phénomène d'inflammation (arthrite, emphysème, cancer) fait des MMPs des cibles thérapeutiques de choix. Cependant, le remodelage entraînant des modifications des contacts cellulaires, les MMPs apparaissent aujourd'hui comme des protéines des voies de signalisation à part entière. Les récentes découvertes de substrats des MMPs ne faisant pas partie des constituants de la matrice extracellulaire renforcent cette vision. Dans le but d'identifier le rôle particulier et le taux d'expression protéique des MMPs dans un contexte pathologique, nous avons développé une technique de protéomique fonctionnelle dédiée à la détection des formes actives des MMPs dans des échantillons tumoraux. Cette technique repose sur le développement d'une nouvelle sonde de photoaffinité, basée sur la structure d'un puissant inhibiteur des MMPs de type phosphinique, permettant de cibler les MMPs sous forme active et de les isoler par marquage par photoaffinité. Le marquage par photoaffinité nous permet ainsi grâce à un élément radioactif incorporé à la sonde de radiomarquer les protéines ciblées. Cette sonde a montré in vitro sa capacité remarquable à modifier de manière covalente la hMMP-12 avec un rendement de 42 %, affichant une sensibilité extrême de détection (2.5 fmoles de hMMP-12). En présence de protéome complexe, la sensibilité de détection de la sonde pour la hMMP-12 est tout à fait comparable (5 fmoles) ; la hMMP-12 représente une fraction de 0.001 % de la quantité totale des protéines. Cette méthode nous a permis également d'identifier de manière indirecte les formes actives des gélatinases en comparant les extraits tumoraux traités par la sonde et les extraits tumoraux analysés en zymographie. Ces études indiquent que les niveaux d'expression des formes actives de MMPs sont très faibles (fmoles) ne permettant pas une caractérisation de celles-ci par spectrométrie de masse, ce qui constitue un véritable défi pouvant être abordé avec de nouvelles sondes incorporant une biotine. Cet exemple de protéines exprimées sous forme active en très faible abondance, implique une orientation des efforts à consentir vers le développement de nouvelles stratégies de capture.
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A, David Arnaud. "Protéomique fonctionnelle des métalloprotéases naturelles (MMPs) dédiée à la détection des formes actives de MMPs dans des protéomes complexes." Phd thesis, Museum national d'histoire naturelle - MNHN PARIS, 2007. http://tel.archives-ouvertes.fr/tel-00327187.

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Les Métalloprotéases matricielles (MMPs) constituent une famille des métalloprotéases à zinc capables conjointement de dégrader l'ensemble des protéines de la matrice extracellulaire. Aujourd'hui, vingt-trois MMPs humaines ont été identifiées et sont caractérisées par leur séquence en aminoacides et leur structure 3D fortement conservées. Ces enzymes sont exprimées de manière constitutive au cours des processus de remodelage tissulaire. Leur surexpression dans un certain nombre de pathologies étroitement liée au phénomène d'inflammation (arthrite, emphysème, cancer) fait des MMPs des cibles thérapeutiques de choix. Cependant, le remodelage entraînant des modifications des contacts cellulaires, les MMPs apparaissent aujourd'hui comme des protéines des voies de signalisation à part entière. Les récentes découvertes de substrats des MMPs ne faisant pas partie des constituants de la matrice extracellulaire renforcent cette vision. Dans le but d'identifier le rôle particulier et le taux d'expression protéique des MMPs dans un contexte pathologique, nous avons développé une technique de protéomique fonctionnelle dédiée à la détection des formes actives des MMPs dans des échantillons tumoraux. Cette technique repose sur le développement d'une nouvelle sonde de photoaffinité, basée sur la structure d'un puissant inhibiteur des MMPs de type phosphinique, permettant de cibler les MMPs sous forme active et de les isoler par marquage par photoaffinité. Le marquage par photoaffinité nous permet ainsi grâce à un élément radioactif incorporé à la sonde de radiomarquer les protéines ciblées. Cette sonde a montré in vitro sa capacité remarquable à modifier de manière covalente la hMMP-12 avec un rendement de 42 %, affichant une sensibilité extrême de détection (2.5 fmoles de hMMP-12). En présence de protéome complexe, la sensibilité de détection de la sonde pour la hMMP-12 est tout à fait comparable (5 fmoles) ; la hMMP-12 représente une fraction de 0.001 % de la quantité totale des protéines. Cette méthode nous a permis également d'identifier de manière indirecte les formes actives des gélatinases en comparant les extraits tumoraux traités par la sonde et les extraits tumoraux analysés en zymographie. Ces études indiquent que les niveaux d'expression des formes actives de MMPs sont très faibles (fmoles) ne permettant pas une caractérisation de celles-ci par spectrométrie de masse, ce qui constitue un véritable défi pouvant être abordé avec de nouvelles sondes incorporant une biotine. Cet exemple de protéines exprimées sous forme active en très faible abondance, implique une orientation des efforts à consentir vers le développement de nouvelles stratégies de capture.
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Candiani, Gabriele. "TNF-a et MMPs dans le remodelage cardiaque." Paris 11, 2006. http://www.theses.fr/2006PA11T016.

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Lund, Dane. "It's a Jungle Out There| Myoblasts, Matrix, and MMPs." Thesis, University of Missouri - Columbia, 2016. http://pqdtopen.proquest.com/#viewpdf?dispub=10182609.

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Le, Dour Gwennaël. "Synthèse de nouveaux inhibiteurs potentiels de métalloprotéinases matricielles (MMPs)." Reims, 2005. http://www.theses.fr/2005REIMP206.

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Les @métalloprotéinases matricielles (MMPs) sont des enzymes protéolytiques calcium et zinc dépendantes dont l'action principale est de dégrader les protéines et particulièrement celles de la matrice extracellulaire. Les MMPs jouent un rôle prépondérant dans divers processus physiologiques tels que le développement embryonnaire, la cicatrisation mais aussi pathologiques comme l'arthrite rhumatoïde et surtout le cancer. Du fait de l'intérêt grandissant pour l'inhibition des métalloprotéinases matricielles dans les thérapies anticancéreuses, le laboratoire s'est donné comme objectif de synthétiser de nouveaux inhibiteurs sélectifs. Nos recherches sont alors dirigées vers la synthèse d'analogues structuraux de l'Ilomastat®, inhibiteur puissant mais non sélectif. Trois familles de composés originaux sont développées tout en conservant leur activité et en tentant de leur conférer de meilleures sélectivité et biodisponibilité. Elles présentent des modifications structurales du squelette pseudopeptidique, pour une meilleure insertion dans les poches enzymatiques S'2, S'3, ainsi que sur le groupement fonctionnel chélatant l'ion zinc du site actif (" Zinc Binding Group "). La synthèse, l'évaluation et la sélectivité de ces différents inhibiteurs potentiels seront présentées<br>@Matrix metalloproteinase (MMPs) are proteolytic calcium and zinc dependent enzymes. Their principal action is to degrade proteins, mainly on the extracellular matrix. MMPs play a determining role in various physiological processes such as the embryonic development, wound healing and also in pathological ones like arthritis and especially cancer. Thus, in this ongoing interest for the inhibition of MMPs in the anti-cancer therapies, the goal of our laboratory is to synthesize new selective inhibitors. Our research is then directed towards the synthesis of structural analogues of Ilomastat®, a potent but a no selective inhibitor. Three families of original compounds are developed preserving their activity and offering a better selectivity and bioavailability. They present structural modifications of backbone pseudopeptide for a best insertion in the enzymatic pocket S'2, S'3 and new ZBG (zinc binding group) functions for higher affinity. The synthesis, the evaluation and the selectivity of these various potential inhibitors will be presented
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Behonick, Danielle J. "A study of MMPs during skeletal development and repair." Diss., Search in ProQuest Dissertations & Theses. UC Only, 2007. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&res_dat=xri:pqdiss&rft_dat=xri:pqdiss:3261265.

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Books on the topic "MMPs"

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IEEE Computer Society. Storage Systems Standards Committee., Institute of Electrical and Electronics Engineers., IEEE Standards Board, and IEEE Standards Association, eds. IEEE standard for Media Management System (MMS) Media Management Protocol (MMP). Institute of Electrical and Electronics Engineers, 2000.

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Hathaway, Starke R. MMPI-2. University of Minnesota Press, 1989.

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

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

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

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

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Ralph, Daniel. MMS. John Wiley & Sons, Ltd., 2004.

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

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Battelle Memorial Institute. Columbus Laboratories, ed. MMPDS-04: Metallic materials properties development and standardization (MMPDS). Federal Aviation Administration, 2008.

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William J. Hughes Technical Center (U.S.), United States. Department of Defense, and United States. National Aeronautics and Space Administration, eds. Metallic materials properties development and standardization (MMPDS): MMPDS-06. Federal Aviation Administration, 2011.

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Book chapters on the topic "MMPs"

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

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Okada, Yasunori. "Immunohistochemistry of MMPs and TIMPs." In Methods in Molecular Biology. Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60327-299-5_12.

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Fisher, Jed F., and Shahriar Mobashery. "Mechanism-Based Profiling of MMPs." In Methods in Molecular Biology. Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60327-299-5_27.

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Shimokawa, Ken-ichi, and Hideaki Nagase. "Purification of MMPs and TIMPs." In Methods in Molecular Biology. Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60327-299-5_8.

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Jia, Di, Roopali Roy, and Marsha A. Moses. "MMPs in Biology and Medicine." In Matrix Metalloproteinase Biology. John Wiley & Sons, Inc, 2015. http://dx.doi.org/10.1002/9781118772287.ch10.

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Grünwald, Barbara, Pascal Schlage, Achim Krüger, and Ulrich auf dem Keller. "MMPs: From Genomics to Degradomics." In Matrix Metalloproteinase Biology. John Wiley & Sons, Inc, 2015. http://dx.doi.org/10.1002/9781118772287.ch9.

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Banerjee, Suvankar, Sandip Kumar Baidya, Nilanjan Adhikari, and Tarun Jha. "Other MMPs and Their Inhibitors." In Modeling Inhibitors of Matrix Metalloproteinases. CRC Press, 2023. http://dx.doi.org/10.1201/9781003303282-11.

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Banerjee, Suvankar, Sandip Kumar Baidya, Nilanjan Adhikari, and Tarun Jha. "Modeling Inhibitors of Other MMPs." In Modeling Inhibitors of Matrix Metalloproteinases. CRC Press, 2023. http://dx.doi.org/10.1201/9781003303282-18.

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Lahat, Nitza, Sarah Shapiro, Michael Inspector, Reuben Reich, Rosa Gershtein, and Ariel Miller. "Matrix-Metalloproteinases (MMPS) in Astroglial Cells." In Advances in Behavioral Biology. Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-5337-3_21.

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Conference papers on the topic "MMPs"

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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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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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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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Wei, Bing, Yujiao He, Junyu You, Shuqin Wen, and Jinyu Tang. "Interpretable Machine Learning for Prediction of Minimum Miscibility Pressure in CO2-Oil System Considering Nano-Confinement Effect." In International Petroleum Technology Conference. IPTC, 2024. http://dx.doi.org/10.2523/iptc-23899-ms.

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Abstract The determination of the minimum miscibility pressure (MMP) in CO2-oil systems is critical for modeling CO2-EOR processes experimentally and numerically. Nevertheless, in nano-confined space, the existing experimental and empirical formula methods present limitations regarding the utilization conditions and prediction accuracy respectively. Thus, in this study, a novel approach combining ML model with Shapley Additive Explanations (SHAP) algorithm is introduced, which aims to provide more precise and physically correct estimates of the MMPs considering the influence of nano-confinement. A database containing MMPs in CO2 injection process under different conditions is firstly established based on 348 samples collected from experimental results and open publications. The input parameters determining MMPs include reservoir temperature, pore size, and oil composition. In this framework, XGBoost and MLP are used to mimic the input-output relations of the database. Then, SHAP is employed to comprehensively interpret the impact of the inputting factors on the MMPs by calculating the SHAP values. The present study revealed that both the proposed XGBoost and MLP models exhibited R2 score exceeding 80% and demonstrated good predictive accuracy, as evidenced by small MAE, MSE, and MAPE values. Moreover, a comparative analysis of the SHAP interpretation results of the two models revealed that the explanatory patterns of the MLP model were more consistent with established physical laws, thereby rendering it more suitable for constructing an MMP prediction model based on the dataset employed in this investigation. It is noteworthy that although the SHAP interpretation of the XGBoost model did not entirely conform to actual physical laws, the influence of pore size on MMP followed the same pattern as elucidated by the MLP model. Specifically, within the nano-confined spaces, MMP decreased as the pore size decreased, and the pore size played a crucial role in predicting MMP (ranking first in the XGBoost model and second in the MLP model). The outcomes demonstrate that the developed interpretable machine learning framework, which incorporates the effects of nano-confinement, can accurately predicts MMP under diverse conditions while maintaining the consistency of physical laws. Consequently, this framework offers valuable insights for the implementation and optimization of CO2-enhanced oil recovery processes.
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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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Jenkin, Alan B., Glenn E. Peterson, Katie Steward, et al. "Case Study of Meteoroid Fluence on a Mars Sample Return Mission." In 2022 16th Hypervelocity Impact Symposium. American Society of Mechanical Engineers, 2022. http://dx.doi.org/10.1115/hvis2022-24.

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Abstract This paper presents results from an analysis to assess the fluence of meteoroids on the Mars Sample Return Campaign Micrometeoroid Protection System (MMPS) and probability of damage to the Earth Entry System Thermal Protection System (TPS). Results are presented for the mission Outbound trajectory from Earth to Mars. The MEM3 meteoroid environment model was used for the assessment. Results are presented showing the reduction in fluence on cube faces and on the MMPS that can be achieved by selection of an anti-velocity orientation of the MMPS. A methodology is presented that determines the cumulative fluence on the MMPS using the MEM3 meteoroid fluxes and the spacecraft attitude profile over the trajectory. Resulting distributions of fluence over impact velocity, angle, and mass are presented. The fluence results are used to establish velocity-angle scenarios for hydrocode simulation and to assess net damage fluence to the TPS. Example tables containing Smooth Particle Hydrodynamics Code (SPHC) simulation scenarios as well as hypothetical hydrocode simulation scenarios for illustration purposes are presented. The tables present the resulting net damaging fluence to the TPS for each scenario and the total across the scenarios. Additionally, examples of CTH hydrocode simulation are included, demonstrating their use for determining critical impactor across the impactor parameter space, and damage of impactors that penetrate the MMPS.
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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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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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9

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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Xue, Ruyue, Li Yang, Zhenyu Tang, Jin Zhang, Yequan Wang, and K. L. Paul Sung. "MMPs and TIMPs Expression and the Anterior Cruciate Ligament Repair." In 2009 3rd International Conference on Bioinformatics and Biomedical Engineering (iCBBE). IEEE, 2009. http://dx.doi.org/10.1109/icbbe.2009.5163062.

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Reports on the topic "MMPs"

1

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

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2

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

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3

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

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4

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

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

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MARNERIS, I. SIMULATION RESULTS OF RUNNING THE AGS MMPS, BY STORING ENERGY IN CAPACITOR BANKS. Office of Scientific and Technical Information (OSTI), 2006. http://dx.doi.org/10.2172/896443.

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7

He, Pengfei, Wenhui Li, and Lian Yang. The association between MMP2, MMP3, and MMP9 promoter polymorphisms and head and neck cancer risk. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, 2024. http://dx.doi.org/10.37766/inplasy2024.1.0018.

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8

Thiolloy, Sophie. Understanding the Mechanism through which Matrix Metalloproteinases (Mmps) Contribute to Breast Cancer-Associated Osteolytic Lesions. Defense Technical Information Center, 2008. http://dx.doi.org/10.21236/ada485198.

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Thiolloy, Sophie. Understanding the Mechanisms Through Which Matrix Metalloproteinases (MMPs) Contribute to Breast Cancer-Associated Osteolytic Lesions. Defense Technical Information Center, 2009. http://dx.doi.org/10.21236/ada506755.

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Thiolly, Sophie. Understanding the Mechanism through which Matrix Metalloproteinases (MMPs) Contribute to Breast Cancer-Associated Osteolytic Lesions. Defense Technical Information Center, 2007. http://dx.doi.org/10.21236/ada469268.

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