Relevant bibliographies by topics / Matrix Metalloproteinase 2 (MMP2)

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Academic literature on the topic 'Matrix Metalloproteinase 2 (MMP2)'

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Published: 6 September 2023

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Journal articles on the topic "Matrix Metalloproteinase 2 (MMP2)"

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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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Bartnykaitė, Agnė, Aistė Savukaitytė, Justina Bekampytė, Rasa Ugenskienė, Danguolė Laukaitienė, Erika Korobeinikova, Jurgita Gudaitienė, and Elona Juozaitytė. "The Role of Matrix Metalloproteinase Single-Nucleotide Polymorphisms in the Clinicopathological Properties of Breast Cancer." Biomedicines 10, no. 8 (August 4, 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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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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Coven, İlker, Ozge Ozer, Ozlem Ozen, Feride İffet Şahin, and Nur Altinors. "Presence of matrix metalloproteinase–2 and tissue inhibitor matrix metalloproteinase–2 gene polymorphisms and immunohistochemical expressions in intracranial meningiomas." Journal of Neurosurgery 121, no. 6 (December 2014): 1478–82. http://dx.doi.org/10.3171/2014.8.jns13515.

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Object Meningiomas are benign extraaxial tumors with a slow progression. Some of them, in spite of being benign in nature, may show an aggressive progression pattern. To investigate the behavioral characteristics of meningiomas, researchers have studied matrix metalloproteinases (MMPs), their tissue inhibitors (TIMPs), interstitial collagens, proteins, vascular endothelial growth factors (VEGF), and tumor necrosis factors. Methods In this study, the authors investigated MMP2 and TIMP2 gene polymorphisms in formalin-fixed paraffin-embedded tissue samples obtained from meningioma patients who had previously undergone surgery at the authors' institution. In addition, brain invasion, Ki-67 index, and MMP-2 and TIMP-2 expressions were investigated using immunohistochemical methods. MMP2 (735C>T, 1575G>A, 1306C>T) and TIMP2 (418G>C, 303C>T) gene polymorphisms were investigated from paraffin-embedded tissue sections using the polymerase chain reaction–restriction fragment length polymorphism method. Results There were statistically significant differences between genotype (p = 0.001) and allele frequencies (p = 0.001 and OR 7.4 [95% CI 1.5–36.2]) in patient and control groups for MMP2 1306C>T polymorphism. The authors did not find a statistically significant difference for other polymorphisms. GA genotype was found to be more frequent when brain invasion was suspected for MMP2 1575G>A polymorphism (p = 0.006). There was not a statistically significant difference for other MMP2 or TIMP2 gene polymorphisms. Conclusions The authors' results support the importance of MMPs and their tissue inhibitors in meningioma pathogenesis. In future studies, these gene polymorphisms, especially MMP2 1306C>T and 1575G>A, should be investigated for meningioma or brain invasion susceptibility in larger study groups.
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WIPFF, JULIEN, PHILIPPE DIEUDE, JEROME AVOUAC, KIET TIEV, ERIC HACHULLA, JEAN-LUC CRACOWSKI, ELIZABETH DIOT, et al. "Association of Metalloproteinase Gene Polymorphisms with Systemic Sclerosis in the European Caucasian Population." Journal of Rheumatology 37, no. 3 (January 28, 2010): 599–602. http://dx.doi.org/10.3899/jrheum.090973.

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Objective.Systemic sclerosis (SSc) is classified among the complex genetic disorders and is characterized by massive extracellular matrix deposits. These may be due to overactivation of transforming growth factor ß that may be in part a result of abnormal remodeling of extracellular matrix and microfibrils. Metalloproteinases (MMP) are a family of proteolytic enzymes, and MMP 2, 9, and 14 contribute to the degradation of microfibrils. Our aim was to determine whether polymorphisms of the MMP2, MMP9, and MMP14 genes confer susceptibility to SSc in a large population.Methods.A case–control study was performed in 659 SSc patients and 511 healthy matched controls from a European Caucasian population. Six Tag single-nucleotide polymorphisms (SNP) of the MMP2 gene and 2 SNP of MMP9 and MMP14 genes were genotyped.Results.All SNP were in Hardy-Weinberg equilibrium in the control population. There was no association between the MMP2, MMP9, and MMP14 variants we investigated and SSc for allelic and genotype frequencies. No association was observed for the different subphenotypes of SSc patients.Conclusion.Our results in a large cohort of European Caucasian SSc patients do not support that MMP2, MMP9, and MMP14 genes are involved in the genetic background of SSc.
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Detry, Benoit, Charlotte Erpicum, Jenny Paupert, Silvia Blacher, Catherine Maillard, Françoise Bruyère, Hélène Pendeville, et al. "Matrix metalloproteinase-2 governs lymphatic vessel formation as an interstitial collagenase." Blood 119, no. 21 (May 24, 2012): 5048–56. http://dx.doi.org/10.1182/blood-2011-12-400267.

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Abstract Lymphatic dysfunctions are associated with several human diseases, including lymphedema and metastatic spread of cancer. Although it is well recognized that lymphatic capillaries attach directly to interstitial matrix mainly composed of fibrillar type I collagen, the interactions occurring between lymphatics and their surrounding matrix have been overlooked. In this study, we demonstrate how matrix metalloproteinase (MMP)–2 drives lymphatic morphogenesis through Mmp2-gene ablation in mice, mmp2 knockdown in zebrafish and in 3D-culture systems, and through MMP2 inhibition. In all models used in vivo (3 murine models and thoracic duct development in zebrafish) and in vitro (lymphatic ring and spheroid assays), MMP2 blockage or down-regulation leads to reduced lymphangiogenesis or altered vessel branching. Our data show that lymphatic endothelial cell (LEC) migration through collagen fibers is affected by physical matrix constraints (matrix composition, density, and cross-linking). Transmission electron microscopy and confocal reflection microscopy using DQ-collagen highlight the contribution of MMP2 to mesenchymal-like migration of LECs associated with collagen fiber remodeling. Our findings provide new mechanistic insight into how LECs negotiate an interstitial type I collagen barrier and reveal an unexpected MMP2-driven collagenolytic pathway for lymphatic vessel formation and morphogenesis.
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Ren, Xiaoyu, Graham D. Lamb, and Robyn M. Murphy. "Distribution and activation of matrix metalloproteinase-2 in skeletal muscle fibers." American Journal of Physiology-Cell Physiology 317, no. 3 (September 1, 2019): C613—C625. http://dx.doi.org/10.1152/ajpcell.00113.2019.

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A substantial intracellular localization of matrix metalloproteinase 2 (MMP2) has been reported in cardiomyocytes, where it plays a role in the degradation of the contractile apparatus following ischemia-reperfusion injury. Whether MMP2 may have a similar function in skeletal muscle is unknown. This study determined that the absolute amount of MMP2 is similar in rat skeletal and cardiac muscle and human muscle (~10–18 nmol/kg muscle wet wt) but is ~50- to 100-fold less than the amount of calpain-1. We compared mechanically skinned muscle fibers, where the extracellular matrix (ECM) is completely removed, with intact fiber segments and found that ~30% of total MMP2 was associated with the ECM, whereas ~70% was inside the muscle fibers. Concordant with whole muscle fractionation, further separation of skinned fiber segments into cytosolic, membranous, and cytoskeletal and nuclear compartments indicated that ~57% of the intracellular MMP2 was freely diffusible, ~6% was associated with the membrane, and ~37% was bound within the fiber. Under native zymography conditions, only 10% of MMP2 became active upon prolonged (17 h) exposure to 20 μM Ca2+, a concentration that would fully activate calpain-1 in seconds to minutes; full activation of MMP2 would require ~1 mM Ca2+. Given the prevalence of intracellular MMP2 in skeletal muscle, it is necessary to investigate its function using physiological conditions, including isolation of any potential functional relevance of MMP2 from that of the abundant protease calpain-1.
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Sultan, Baqur A., and Raad Ajam Sayhel Al.Jorany. "Evaluation of Matrix Metalloproteinase-2 (MMP2) in Aborted Women Infected with Toxoplasma gondii." Kufa Journal for Nursing Sciences 6, no. 2 (August 29, 2016): 122–29. http://dx.doi.org/10.36321/kjns.vi20162.2704.

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Background: Toxoplasmosis is one of the most common zoonotic pathogens worldwide; Life cycle of this parasite was affected by synthesis of specific enzyme like Matrix metalloproteinase-2 (MMP2). Objectives: The major objectives of this study detection of prevalence expression of Matrix metalloproteinase-2 (MMP2) among ninety-six aborted women were tested; seventy-six of them was with recurrent abortions due to Toxoplasmosis and twenty without Toxoplasmosis as control group in Najaf governorate. Methodology: Descriptive case-control ,purposive (probability) sample among ninety six aborted women were tested, attending in Central Health Laboratory, Al-Zahra Maternity & pediatric Teaching Hospital , The data collected from January 2014 to January 2015. The concentration level of Matrix metalloproteinase-2 (MMP2) in aborted women was measured by ELISA technique according to many parameters such as age, occupation, residence and number of abortions. Results: The result indicated that the concentration of MMP2was elevated in women with one or two abortions. The high concentration of MMP2 in infected aborted women with age group (20-24), (25-29).there was significant differences in study groups according to occupation and there were differences in MMP2concentration levels according to residency. It was demonstrated that the high concentration of MMP2 was appear in rural infected aborted women and low in urban women with Toxoplasmosis, Results were analyzed by using statistical methods (Levene test, ANOVA test, t test). Conclusion: Matrix metalloproteinase-2(MMP2) play a significant role in immunity against infection with Toxoplasma gondii. Recommendation: Further studies are recommended to know the concentration of MMP2 among pregnant women to be one of an important laboratory tests in the induction of immune response against this type of infection.
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Kan, Taichi, Hiromi Ueda, Taishi Takahara, Yoshimasa Tsuchiya, Mayuko Kishimoto, Yasue Uchida, Tetsuya Ogawa, Wataru Ohashi, Toyonori Tsuzuki, and Yasushi Fujimoto. "Association of Matrix Metalloproteinase-2 mRNA Expression with Subtypes of Pediatric Cholesteatoma." BioMed Research International 2021 (March 10, 2021): 1–8. http://dx.doi.org/10.1155/2021/6644897.

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Objective. Cholesteatoma is a clinically heterogeneous disease, with some patients showing spontaneous regression, while others experiencing an aggressive, lethal disease. Cholesteatoma in children can be divided into two types: congenital and acquired. Identifying good prognostic markers is needed to help select patients who will require immediate surgical intervention. Matrix metalloproteinase-2 (MMP2) was previously reported to play an important role in cholesteatoma progression, by promoting bone destruction and keratinocyte infiltration. Herein, we analyzed MMP2 mRNA expression level in cholesteatoma using RNA-in situ hybridization in formalin-fixed, paraffin-embedded (FFPE) tissue samples. Methods. Sixty patients with cholesteatoma under 15 years old, who underwent their primary surgery at Aichi Medical University’s Otolaryngology Department, were analyzed for MMP2 expression level, using RNA-in situ hybridization. Results. There were no significant differences in MMP2 mRNA expression level between congenital cholesteatoma and acquired cholesteatomas. In congenital cholesteatoma, higher MMP2 signals were observed in the open type than in the closed type ( p < 0.001 ). In acquired cholesteatoma, higher MMP2 signals were observed in the pars tensa than in the pars flaccida ( p < 0.001 ). MMP2 mRNA expression level was almost exclusively found in the fibroblasts or in the inflammatory cells in the stroma, but not in the epithelium. Conclusion. Our study reveals that MMP2 mRNA expression level is strongly associated with the subtypes of cholesteatoma. The findings suggest that the level of expression of MMP2 mRNA may be related to the pathogenesis and aggressive features of cholesteatoma.
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Zhang, Jianmei, Mi-Yeon Kim, and Jae Youl Cho. "Euodia pasteuriana Methanol Extract Exerts Anti-Inflammatory Effects by Targeting TAK1 in the AP-1 Signaling Pathway." Molecules 25, no. 23 (December 7, 2020): 5760. http://dx.doi.org/10.3390/molecules25235760.

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Euodia pasteuriana A. Chev. ex Guillaumin, also known as Melicope accedens (Blume) T.G. Hartley, is a herbal medicinal plant native to Vietnam. Although Euodia pasteuriana is used as a traditional medicine to treat a variety of inflammatory diseases, the pharmacological mechanisms related to this plant are unclear. This study aimed to investigate the anti-inflammatory effects of a methanol extract of Euodia pasteuriana leaves (Ep-ME) on the production of inflammatory mediators, the mRNA expression of proinflammatory genes, and inflammatory signaling activities in macrophage cell lines. The results showed that Ep-ME strongly suppressed the release of nitric oxide (NO) in RAW264.7 cells induced with lipopolysaccharide (LPS), pam3CysSerLys4 (Pam3CSK), and polyinosinic-polycytidylic acid (poly I:C) without cytotoxicity. A reverse transcription-polymerase chain reaction further confirmed that Ep-ME suppressed the expression of interleukin 6 (IL-6), matrix metalloproteinase-1 (MMP1), matrix metalloproteinase-2 (MMP2), matrix metalloproteinase-3 (MMP3), tumor necrosis factor-α (TNF-α), and matrix metalloproteinase-9 (MMP9) at the transcriptional level and reduced the luciferase activities of activator protein 1 (AP-1) reporter promoters. In addition, immunoblotting analyses of the whole lysate and nuclear fraction, as well as overexpression assays demonstrated that Ep-ME decreased the translocation of c-Jun and suppressed the activation of transforming growth factor beta-activated kinase 1 (TAK1) in the AP-1 signaling pathways. These results imply that Ep-ME could be developed as an anti-inflammatory agent that targets TAK1 in the AP-1 signaling pathway.
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Dissertations / Theses on the topic "Matrix Metalloproteinase 2 (MMP2)"

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Teh, Elaine. "Matrix metalloproteinase-2 (MMP2) and myocardial dysfunction associated with urgent cardiac surgery." Thesis, King's College London (University of London), 2013. https://kclpure.kcl.ac.uk/portal/en/theses/matrix-metalloproteinase2-mmp2-and-myocardial-dysfunction-associated-with-urgent-cardiac-surgery(de82119f-7ae0-4131-a743-03a8d168b62a).html.

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Background: Current management of patients presenting with acute coronary syndrome (ACS) includes aggressive and expeditious revascularisation, including surgical revascularisation. However, early surgery following ACS is associated with high mortality, as subsequent global ischaemia induced during surgery is imposed on infarcted myocardium. Emerging evidence suggests that matrix metalloproteinases (MMPs), especially MMP2, may have an important role in the acute myocardial dysfunction seen after global ischaemia-reperfusion injury, by targeting intracellular functional and structural proteins. Aims: To investigate whether MMP2 has a causative role in heart dysfunction when previously infarcted hearts were subjected to further global ischaemia-reperfusion, as occurs in cardiac surgery, with and without cardioplegic protection. Methods and Results: MI was surgically induced in male Wistar rats, (250-350 g body weight) by in vivo ligation of the left anterior descending artery. The animals were recovered for 7 days prior to excision of hearts and isolated Langendorff perfusion, followed by induction of further global ischaemia and reperfusion. The recovery of mechanical function (left ventricular developed pressure: LVDP) of the heart was assessed during reperfusion. MMP2 activity was also measured during the early reperfusion phase in the heart tissues. Infarcted hearts had less capacity to recover function after an additional period of global ischaemia, which was associated with higher MMP2 activity in the infarcted hearts compared to normal hearts. Inhibition of MMP2 improved recovery of function. When an MMP inhibitor was used as an adjunct to St Thomas’ Hospital cardioplegia, there was a trend towards improved recovery if the inhibitor was present before, during and after ischaemia. Conclusion: MMP2 has a role in causing cardiac dysfunction when infarcted hearts were subjected to further global ischaemia-reperfusion. Inhibition of MMP2 resulted in improved recovery of the function of the hearts during reperfusion. With cardioplegia, MMP2 inhibition before, during and after ischaemia was crucial to improve cardioprotection during early reperfusion.
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Kuittinen, O. (Outi). "Matrix metalloproteinase-2 (MMP-2) and -9 (MMP-9) in hematological malignancies." Doctoral thesis, University of Oulu, 2003. http://urn.fi/urn:isbn:951426942X.

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Abstract Gelatinases (MMP-2 and MMP-9) play a key role during invasion and metastazising of malignant cells and they have been shown to be associated to invasive phenotype and poor prognosis in several solid tumours. However little is known about their role in hematological malignancies. In the present work, gelatinase expression and its clinicopathological correlations were studied with immunohistochemical staining in 10 cases representing normal bone marrow aspirate smears, 123 cases representing diagnostic bone marrow samples of patients with different leukaemias (35 AML, 7 CLL, 6 CML, 75 ALL), 67 diagnostic paraffin-embedded lymph node biopsies from patients with Hodgkin's lymphoma and 57 biopsies from patients with non-Hodgkin's lymphomas. The lymphoma samples were also stained with factor VIII antibody to evaluate the extent of new vessel formation and the non-Hodgkin's lymphoma cases also with tissue inhibitor of metalloproteinases -1 (TIMP-1) antibody. CLL did not express either of the MMP enzymes, while CML in the chronic phase expressed strongly both of the enzymes. In ALL, gelatinase expression was weak and detectable in pediatric cases in only 12.7% and in the adults in 65% of the cases. In adult ALL, MMP-2 expression correlated strongly with an extramedullary and invasive pattern of disease presentation. In AML MMP-2 positivity had markedly favorable prognostic and predictive power. In lymphoma studies, no correlations could be detected between gelatinase expression and the clinical parameters of invasion. MMP-9 positivity was related to the presence of B symptoms, which difference was statistically significant in Hodgkin's lymphoma. In Hodgkin's lymphoma, strong MMP-9 expression also implicated decreased neovascularization. In both lymphoma types, strong MMP-9 expression correlated with unfavorable prognosis, which difference was statistically significant in non-Hodgkin's lymphomas and remained as a tendency in Hodgkin's lymphoma. MMP-2 had statistically significant association with a favorable prognosis in Hodgkin's lymphoma. Combination of the results of both stainings further increased prognostic power. All together these findings implicate that gelatinases could be used as prognostic tools in AML and lymphomas albeit this needs to be verified in larger materials.
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Coughlan, Andrew Richard. "Matrix metalloproteinase (MMP) 2 and 9 in canine arthritis." Thesis, University of Liverpool, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.243201.

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Guo, Chung. "Divergent regulation of MMP-2 secretion and activation in adult rat cardiac fibroblasts." Thesis, De Montfort University, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.247642.

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Bergman, Robert Loring. "Matrix Metalloproteinases 2 and 9 in Normal Canine Cerebrospinal Fluid." Thesis, Virginia Tech, 2001. http://hdl.handle.net/10919/33750.

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Cerebrospinal fluid (CSF) analysis is a standard part of a diagnostic evaluation. Commonly evaluated components include the cell count, protein concentration, glucose, and cytology. CSF analysis can be diagnostic in some diseases such as fungal infections and CNS lymphoma. Often, CSF analysis is not specific, but more information can be obtained. Matrix Metalloproteinases (MMPs) are enzymes that have been found in human CSF. They are calcium and zinc dependent endoproteinases with overlapping substrates. They hydrolyze at least one component of tissue extracellular matrix (ECM), such as collagen or elastin. They are important in normal physiologic processes such as angiogenesis, reproduction and wound healing. One class of MMPs, the gelatinases, degrade gelatins and type IV collagen include MMP 2 and MMP 9. MMPs are important in many pathological processes that involve unregulated matrix destruction such as arthritis, neoplasia and CNS diseases. MMP2 is known to be constituitively produced in CSF while MMP 9 is present only in certain pathologic conditions such as multiple sclerosis, neoplasia and inflammatory diseases. We hypothesize that MMP2 is present in normal canine CSF while MMP 9 is absent. Cerebrospinal fluid samples were taken from 23 normal dogs that were being used for other research purposes. Each CSF sample was evaluated immediately for red blood cells (RBCs), white blood cells (WBCs), protein, and glucose, and then stored at -70°C. Cytological examination was also performed. CSF samples were considered normal if the protein was less than 25 mg/dl, WBCs were less than 6 µl, and RBCs were less than 25 µl. Each dog was euthanized and the brains processed for routine histopathology. MMP analysis was done using gelatin zymography and an enzyme linked immunosorbent assay (ELISA). Bands of enzyme activity were visible following staining due to enzyme degradation of the gelatin. A commercially available polyclonal sandwich ELISA was used to identify the pro form of MMP2. The mean WBC count for the CSF samples was 0.96 WBC/ml with a range of 0-3 WBC/ml. The mean protein was 12 mg/dl, with a range of 8-17 mg/dl. The mean RBC count was 3.65 RBC/ml with a range of 0-21 RBC/ml. All normal samples of CSF contained a band of clearing that corresponded to the human commercial standard of proMMP2. No other major bands of clearing were noted on normal samples. The commercial human standards also contained ProMMP2. Other bands were present, but were faint and variable. Using a polyclonal antibody based sandwich ELISA, with samples run in triplicate, the mean pro MMP 2 levels were determined to be 5.61 ng/ml with a range of 3.36 - 10.83 ng/ml. We conclude that normal CSF values are narrower than what has been previously reported for protein concentration and WBC count. Also, the pro form of MMP 2 is present in normal canine CSF based on results of gelatin zymography and ELISA.
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Renaud, Virginie. "Étude de la voie de présentation de l'antigène MMP-2 par les cellules tumorales." Nantes, 2009. http://www.theses.fr/2009NANT2099.

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Un nouvel antigène de tumeur, MMP-2, a été caractérisé dans notre laboratoire. Il est reconnu par un clone T CD8+ dans le contexte HLA-A*0201. De façon surprenante, les lignées de mélanome présentent cet antigène par la voie de présentation croisée (Godefroy et al. , 2005). Le sujet de cette thèse porte sur les mécanismes impliqués dans l’absence de présentation de la MMP-2 par la voie endogène. La MMP-2 est constitué de 8 ponts disulfures et nous avons voulu évaluer l’impact de ces ponts sur cette présentation. En remplaçant une cystéine par une alanine dans l’ADNc codant pour la MMP-2 puis en transfectant ces ADNc mutés dans des cellules tumorales, nous avons montré que l'élimination d’un pont disulfure dans la MMP-2 permet sa présentation par la voie endogène. Par cinétique de chasse, nous avons aussi démontré que la MMP-2 mutée est plus rapidement dégradée que la MMP-2 sauvage. La conformation de la MMP-2 semble jouer un rôle important dans son absence de présentation par la voie endogène classique. Ensuite, nous avons essayé de déterminer la voie cellulaire impliquée dans la présentation croisée de la MMP-2. En utilisant des drogues, nous avons mis en évidence que la présentation croisée de la MMP-2 nécessite la machinerie de rétrotranslocation, le protéasome et TAP, tous impliqués dans la voie de présentation endogène. Pour déterminer les compartiments impliqués dans cette présentation croisée, nous avons testé les « Organelles lights » (Invitrogen) dans le but de cibler des structures intracellulaires in vivo
From a patient still melanoma free after TIL injection, we characterized a new tumor antigen, MMP-2, recognized by a CD8 T cell clone in HLA-A*0201 context. Surprisingly melanoma cell lines present this tumor antigen by the cross presentation pathway (Godefroy & al. , 2005). In the first part, we wondered if disulfide bonds present in MMP-2 were not responsible for its absence of presentation by the endogenous pathway. By mutagenesis, we replaced a cystein by an alanine in the cDNA coding for MMP-2, in order to induce a disulfide bond deletion and then we transfected these cDNA mutants in COS-7 and human tumor cell lines. We showed that MMP-2 deletion of one disulfide bond induce its presentation by the endogenous pathway. By pulse chase experiments we also demonstrated that MMP-2 mutated form is more rapidly degraded than the wild form. MMP-2 folding and consequently conformation seems to play an important role in the absence of its presentation by the classical pathway. In the second part, we try to determine intracellular pathway implicated in MMP-2 cross-presentation in melanoma cells. Indeed, after secretion, MMP-2 is internalized by melanoma cells in an v3 dependent manner and by an unknown pathway. MMP-2 is finally processed by the proteasome and loaded on MHC class I molecule (Godefroy & al. , 2005). By using drugs, we determined that MMP-2 cross-presentation involves the retrotranslocation machinery, the proteasome and TAP, all implicated in the endogenous pathway. To determine compartments necessary to MMP-2 cross-presentation we tested Organelles lights (Invitrogen). These reagents provide a method for targeted specific subcellular structures within living cells
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Kuntze, Luciana Bärg. "Efeito inibitório do captopril sobre a Metaloproteinase-2 da Matriz Extracelular (MMP-2) in vitro." Universidade de São Paulo, 2012. http://www.teses.usp.br/teses/disponiveis/17/17133/tde-27072016-160209/.

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A MMP-2 é uma protease que está envolvida em muitos eventos fisiológicos e patológicos e que compartilha similaridades estruturais com a enzima conversora de angiotensina (ECA), de modo que os inibidores da ECA passaram a ser estudados com relação ao efeito inibitório também sobre a MMP-2. No entanto, este potencial inibitório não foi ainda testado na MMP-2 altamente purificada. Este estudo teve como objetivo investigar o potencial inibitório do captopril sobre a atividade da MMP- 2. Primeiramente, supôs-se que a dissolução do captopril poderia induzir a mudanças no pH de soluções tampão. Em segundo lugar, avaliou-se o efeito direto do captopril sobre a MMP-2 presente no plasma humano e a MMP-2 recombinante humana (rhMMP-2) produzida e purificada de E. coli. As análises de atividade in vitro incluíram zimogramas com gelatina e ensaios fluorimétricos com DQ gelatin. A solubilização do captopril reduziu significativamente o pH da solução tampão 50 mM (p<0,01) mas não alterou o pH da solução tampão 200 mM (p>0,05). Resultados de zimografia do plasma e da rhMMP-2 mostraram inibição da atividade gelatinolítica com significância estatística somente em concentrações iguais ou maiores que 4 e 1 mM de captopril, respectivamente (p<0,05). A presença de captopril nos ensaios de fluorimetria resultaram na inibição significante da atividade de rhMMP-2 somente em concentrações iguais ou maiores que 2 mM (p<0,01), enquanto a rhMMP-2 ativada com APMA apresentou inibição significativa diante de 0,5 mM de captopril (p<0,01). As concentrações de captopril efetivas em inibir a MMP-2 in vitro foram muito superiores àquelas referentes à concentração plasmática máxima encontrada no plasma humano após a administração de uma dose de 50 mg de captopril. Em conjunto nossos resultados sugerem que o captopril não parece promover inibição significativa da MMP-2 nas concentrações relatadas in vivo. Além disso, o pH das soluções tamponantes é um aspecto que requer mais atenção durante ensaios de inibição de protease in vitro.
MMP-2 is involved in many physiological and pathological processes. This protease shares structural similarities with the angiotensin-converting enzyme (ACE), and ACE inhibitors have been described to inhibit MMP-2. However, this inhibitory potential has not been tested using a highly purified MM-2 so far. This study aimed at investigating the inhibitory potential of captopril on MMP-2 activity. First it was tested whether the dissolution of captopril would induce changes in the pH of the solutions. Secondly, the direct inhibitory effect of captopril on plasma MMP-2 and on a recombinant human MMP-2 (rhMMP-2) produced and purified from E. coli was tested. The in vitro activity assays included gelatin zymography and a fluorimetric assay with DQ gelatin. Captopril solubilization significantly decreased the pH of the 50 mM Tris buffer solution (p<0.01) but did not decreased the pH of the 200 mM Tris Buffer solution (p>0.05). Zymography results of plasma and rhMMP-2 showed that inhibition of the activity only reached statistical significance >= 4 and 1 mM of captopril, respectively (p<0,05). The presence of captopril in the fluorimetric assay resulted in a significant inhibition of the rhMMP-2 activity only at concentrations >= 2 mM (p<0.01), whereas APMA-activated rhMMP-2 was inhibited by 0.5 mM of captopril (p<0.01). The captopril concentrations found to inhibit MMP-2 are several times of magnitude higher than the maximum plasma concentration after a dose of 50 mg of captopril. In conclusion, captopril does not seem to cause significant inhibition of MMP-2 in the concentrations found in vivo, and more attention has to be given to the pH of the solutions when testing protease inhibition in vitro.
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Vasala, K. (Kaija). "Matrix metalloproteinase MMP-2 and MMP-9 and their inhibitors TIMP-1 and TIMP-2 in bladder carcinoma." Doctoral thesis, University of Oulu, 2008. http://urn.fi/urn:isbn:9789514288746.

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Abstract Bladder cancer when superficial has a good prognosis but it has a high recurrence risk and about 10–15% of the superficial carcinomas will progress into muscle invasive or metastatic type. The most powerful factor for predicting the behavior of bladder carcinoma is the stage of the tumor. Invasion to the lamina propria increases the risk of recurrence and progress to muscle-invasive tumor. Also grade of the tumor and tumor multiplicity associates with high risk for recurrence. New markers are still needed to find those patients who need more and better treatments to avoid the recurrence and progress. The need for new non-invasive markers to diminish the need for frequent cystoscopy in follow-up is also obvious. Gelatinases MMP-2 and MMP-9 are known to associate to tumor invasion and progression. Also their tissue inhibitors TIMP-1 and TIMP-2 take part in these diversified processes and metastasis formation. In the present work the expression and clinical value of gelatinases MMP-2 and MMP-9 and their tissue inhibitors TIMP-1 and TIMP-2 were evaluated in bladder carcinoma. Primary tissue samples of 121 patients were analyzed for expression of MMP-2 and/or MMP-9 using immunohistochemistry. The serum samples of 87 patients who were treated in the Oncology Department of Oulu University Hospital were collected and studied with ELISA. The control group consisted of 44 healthy volunteers. Overexperssion of MMP-2 protein correlated significantly to disease-specific survival and showed an independent prognostic value as a biomarker. High MMP-9 expression instead correlated to favorable overall survival of bladder cancer patients. Circulating proMMP-2, TIMP-2 and MMP-2:TIMP-2 complex levels were lower in cancer patients than in healthy volunteers in control group. High levels of all these three markers correlated with better prognosis in bladder cancer patients.
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Kim, Yu Shin. "Correlation Between MMP-2 and -9 Levels and Local Stresses in Arteries Using a Heterogeneous Mechanical Model." Diss., Georgia Institute of Technology, 2007. http://hdl.handle.net/1853/16134.

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The mechanical environment influences vascular smooth muscle cell (VSMC) functions related to the vascular remodeling. However, the relationships are not appropriately addressed by most mechanical models of arteries assuming homogeneity. Accounting for the effects of heterogeneity is expected to be important to our understanding of VSMC functions. We hypothesized that local stresses computed using a heterogeneous mechanical model of arteries positively correlate to the levels of matrix metalloproteinase (MMP)-2 and -9 in situ. We developed a mathematical model of an arterial wall accounting for nonlinearity, residual strain, anisotropy, and structural heterogeneity. The distributions of elastin and collagen fibers, quantified using their optical properties, showed significant structural heterogeneity. Anisotropy was represented by the direction of collagen fibers, which was measured by the helical angle of VSMC nuclei. The recruiting points of collagen fibers were computed assuming a uniform strain of collagen fibers under physiological loading conditions; an assumption motivated by the morphology. This was supported by observed uniform length and orientation of VSMC nuclei under physiological loading. The distributions of circumferential stresses computed using both heterogeneous and corresponding homogeneous models were correlated to the distributions of expression and activation of MMP-2 and -9 in porcine common carotid arteries, which were incubated in an ex vivo perfusion organ culture system under either normotensive or hypertensive conditions for 48 hours. While strains computed using incompressibility were identical in both models, the heterogeneous model, unlike the homogeneous model, predicted higher circumferential stresses in the outer layer. The tissue levels of MMP-2 and -9 were positively correlated to circumferential stresses computed using the heterogeneous model, which implies that areas of high stress are expected to be sites of localized remodeling and agrees with results from cell culture studies. The results support the role of mechanical stress in vascular remodeling and suggest the importance of structural heterogeneity in studying mechanobiological responses.
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Farooqi, Owais Ali. "Effect of methamphetamine on gingival fibroblast production of matrix metalloproteinase (MMP)-2 and -9 and tissue inhibitor of metalloproteinase (TIMP)-1 and -2 in vitro." View the abstract Download the full-text PDF version, 2009. http://etd.utmem.edu/ABSTRACTS/2009-023-Farooqi-index.htm.

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Thesis (M.S.)--University of Tennessee Health Science Center, 2009.
Title from title page screen (viewed on August 5, 2009). Research advisor: David A. Tipton, D.D.S., Ph.D. Document formatted into pages (vi, 39 p. : ill.). Vita. Abstract. Includes bibliographical references (p. 27-38).
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Books on the topic "Matrix Metalloproteinase 2 (MMP2)"

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Yeung, Oliver. Differential regulation of matrix metalloproteinase-2 (MMP-2) by phorbol myrisate acetate, and by DL-[alpha]-difluoromethylornithine, in cell lines of varying tumorigenic and metastatic potential. Ottawa: National Library of Canada, 1999.

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Baragwanath, Philip. Matrix metalloproteinase-2 and -9 in human wound healing. Birmingham: University of Birmingham, 2000.

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Book chapters on the topic "Matrix Metalloproteinase 2 (MMP2)"

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Salajegheh, Ali. "Matrix Metalloproteinase 2 (MMP2)." In Angiogenesis in Health, Disease and Malignancy, 203–8. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-28140-7_31.

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Hinterseher, I., D. Krex, D. Ockert, E. Kuhlisch, H. K. Schackert, and H. D. Saeger. "Analyse des Matrix Metalloproteinase-2 Genes (MMP-2) als ätiologischer Faktor spontaner Aortenaneurysmen." In Zurück in die Zukunft, 460–61. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-642-55611-1_280.

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Hinterseher, Irene, D. Krex, D. Ockert, E. Kuhlisch, H. K. Schackert, and H. D. Saeger. "Genomische Analyse des Matrix Metalloproteinase-2 Gens (MMP-2) als potentieller ätiologischer Faktor spontaner Aortenaneurysmen." In Deutsche Gesellschaft für Chirurgie, 549–50. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-642-19024-7_151.

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Sienel, W., R. Seen-Hibler, W. Wöckel, O. Thetter, W. Mutschler, and B. Passlick. "Die Überexpression von Matrix Metalloproteinase 2 (MMP-2) ist mit einer Frühdisseminierung bei operablem Adenokarzinom der Lunge assoziiert." In Deutsche Gesellschaft für Chirurgie, 93–95. Berlin, Heidelberg: Springer Berlin Heidelberg, 2001. http://dx.doi.org/10.1007/978-3-642-56698-1_24.

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Lopes Barreto, Deirisa, and Raymond T. Krediet. "Matrix Metalloproteinase-2 (MMP-2) and Plasminogen Activator Inhibitor-1 (PAI-1) in Peritoneal Dialysis: Biological Implications and Clinical Utility." In Biomarkers in Kidney Disease, 911–30. Dordrecht: Springer Netherlands, 2016. http://dx.doi.org/10.1007/978-94-007-7699-9_25.

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Lopes Barreto, Deirisa, and Raymond T. Krediet. "Matrix Metalloproteinase-2 (MMP-2) and Plasminogen Activator Inhibitor-1 (PAI-1) in Peritoneal Dialysis: Biological Implications and Clinical Utility." In Biomarkers in Kidney Disease, 1–20. Dordrecht: Springer Netherlands, 2015. http://dx.doi.org/10.1007/978-94-007-7743-9_25-1.

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Chan, Brandon Y. H., Andrej Roczkowsky, Ramses Ilarraza, and Richard Schulz. "Matrix Metalloproteinase-2." In Encyclopedia of Signaling Molecules, 2996–3005. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101708.

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Chan, Brandon Y. H., Andrej Roczkowsky, Ramses Ilarraza, and Richard Schulz. "Matrix Metalloproteinase-2." In Encyclopedia of Signaling Molecules, 1–10. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_101708-1.

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Tyagi, Suresh C., Larry Meyer, Richard A. Schmaltz, Hanumanth K. Reddy, and Donald J. Voelker. "Proteinases and Restenosis: Matrix Metalloproteinase and their Inhibitor and Activator." In Cardiovascular Disease 2, 19–30. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1959-1_3.

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Kalev-Altman, Rotem, Efrat Monsonego-Ornan, and Dalit Sela-Donenfeld. "The Role of Matrix Metalloproteinase-2 and Metalloproteinase-9 in Embryonic Neural Crest Cells and Their Derivatives." In Proteases in Physiology and Pathology, 27–48. Singapore: Springer Singapore, 2017. http://dx.doi.org/10.1007/978-981-10-2513-6_2.

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Conference papers on the topic "Matrix Metalloproteinase 2 (MMP2)"

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Dutta, Anindita, Jing Li, Huimin Lu, Jacqueline Akech, Jitesh Pratap, Tao Wang, Thomas J. FitzGerald, et al. "Abstract C40: αvβ6 integrin promotes a TGFβ1-mediated cancer cell autonomous osteolytic program through upregulation of matrix metalloproteinase 2 (MMP2)." In Abstracts: AACR Special Conference on Tumor Invasion and Metastasis - January 20-23, 2013; San Diego, CA. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.tim2013-c40.

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Revilla Lopez, E. M., M. Boada, V. Ruiz De Miguel, S. Gomez Ollés, and B. Saez. "Exploring the role of matrix metalloproteinase 2 (MMP-2) as a biomarker in lymphangioleiomyomatosis." In ERS International Congress 2022 abstracts. European Respiratory Society, 2022. http://dx.doi.org/10.1183/13993003.congress-2022.144.

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Pitchford, Simon C., Stefania Momi, Clive P. Page, and Paolo Gresele. "The Role Of Platelet Matrix-Metalloproteinase 2 (MMP2) On Platelet And Leukocyte Migration Through Lung Tissue In A Murine Model Of Allergic Inflammation." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a2784.

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Stott-Miller, Marni, John Houck, Pawadee Lohavanichbutr, Stephen M. Schwartz, Melissa P. Upton, and Chu Chen. "Abstract 3819: Matrix metalloproteinase-1 (MMP1) is an important marker of oral squamous cell carcinoma." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-3819.

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Mudiyanselage, Chandana S. K. Herath, Neil Mitra, Dasuni Niyagama Gamage, Hiromichi Miyagaki, Abhinit Shah, Xiaohong Yan, Vesna Cekic, and Richard L. Whelan. "Abstract 1145: Assessing the diagnostic value of the combination of Matrix Metalloproteinase 2 (MMP2) and Progranulin (PGRN) preoperative plasma levels for colorectal cancer (CRC)." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-1145.

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Seccareccia, Erica, Shun Li, and Pnina Brodt. "Abstract 5255: The role of IGF1 signaling in site specific tumor metastasis: Regulating matrix metalloproteinase (MMP) expression." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-5255.

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Song, Nan, Hyuna Sung, Sujee Jeon, Yunhee Lee, Ji-Yeob Choi, Sue K. Park, Kyoung-Mu Lee, et al. "Abstract 4494: Preoperative serum levels of matrix metalloproteinase-2 (MMP-2) and survival of breast cancer among Korean women." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-4494.

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Ng, Ho Yin, Brian G. Oliver, Janette K. Burgess, Vera P. Krymskaya, Judith L. Black, and Lyn M. Moir. "Inhibition Of Matrix Metalloproteinase-2 (MMP-2) Decreases Migration Of TSC2-Null Mouse Embryonic Fibroblasts – Relevance To Pulmonary Lymphangioleiomyomatosis (LAM)." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a3662.

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Ito, Yusuke, Hitoshi Ishiguro, Naohito Kobayashi, Hisashi Hasumi, Masatoshi Watanabe, Masahiro Yao, and Hiroji Uemura. "Abstract 435: Adipocyte-derived monocyte chemotactic protein-1 (MCP-1) promotes prostate cancer progression through matrix metalloproteinase (MMP-2) mediated extracellular matrix degradation." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-435.

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Wang, Ying, John A. Johnson, Abigail Fulp, Michael A. Sutton, and Susan M. Lessner. "Adhesive Strength of Atherosclerotic Plaques Depends on Collagen Content." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80433.

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Atherosclerotic plaque rupture is a major cause of myocardial infarction, coronary thrombosis and stroke. In a previous study, we proposed a new plaque rupture mechanism, plaque separation at the shoulder, and developed a novel quantitative mechanical test to measure the adhesive strength between the atherosclerotic plaque and the underlying vascular wall in mouse models using the local energy release rate, G, as a quantifiable metric for direct comparison of plaque separation strengths (1). We have now investigated structure-function relationships between the local energy release rate and local plaque composition. We hypothesize that adhesive strength varies with plaque composition in mice of different genotypes, and that it correlates with collagen deposition and macrophage content in lesions. Mice which are genetically deficient in matrix metalloproteinase 12 (MMP12), have previously been shown to demonstrate altered lesion composition (2). Therefore, we used apoE knockout (KO) and apoE MMP-12 double knockout (DKO) mice for our experiments and expected to see a difference in local energy release rates between strains.
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Reports on the topic "Matrix Metalloproteinase 2 (MMP2)"

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Hernandez-Barrantes, Sonia, and Rafael Fridman. Extracellular Matrix Regulations of Membrane Type 1-Matrix Metalloproteinase (MT1-MMP) and Matrix Metalloproteinase-2 (MMP-2) in Human Breast Fibroblasts. Fort Belvoir, VA: Defense Technical Information Center, August 2002. http://dx.doi.org/10.21236/ada413613.

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Hernandez-Barrantes, Sonia, and Rafael Fridman. Extracellular Matrix Regulations of Membrane Type 1-Matrix Metalloproteinasis (MT1-MMP) and Matrix Metalloproteinase-2 (MMP-2) in Human Breast Fibroblasts. Fort Belvoir, VA: Defense Technical Information Center, August 2000. http://dx.doi.org/10.21236/ada395355.

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Harnandez-Barrantes, Sonia, and Rafael Fridman. Extracellular Matrix Regulations of Membrane Type 1 - Matrix Metalloproteinasis (MT1-MMP) and Matrix Metalloproteinase-2 (MMP-2) in Human Breast Fibroblasts. Fort Belvoir, VA: Defense Technical Information Center, August 2001. http://dx.doi.org/10.21236/ada396694.

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Samah, Nazirah, Azizah Ugusman, Adila A. Hamid, Nadiah Sulaiman, and Amilia Aminuddin. Role of matrix metalloproteinase-2 among coronary artery disease (CAD) patients: A systematic review. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, April 2023. http://dx.doi.org/10.37766/inplasy2023.4.0058.

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