Relevant bibliographies by topics / Matrix metalloproteinase 1 (MMP1)

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Academic literature on the topic 'Matrix metalloproteinase 1 (MMP1)'

Author: Grafiati
Published: 4 June 2021
Last updated: 8 February 2022

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Journal articles on the topic "Matrix metalloproteinase 1 (MMP1)"

1

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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Skov, Vibe, Mads Thomassen, Lasse Kjær, Caroline Riley, Thomas Stauffer Larsen, Ole Weis Bjerrum, Torben A. Kruse, and Hans Carl Hasselbalch. "Extracellular Matrix-Related Genes Are Deregulated in Peripheral Blood from Patients with Myelofibrosis and Related Neoplasms." Blood 132, Supplement 1 (November 29, 2018): 5491. http://dx.doi.org/10.1182/blood-2018-99-117122.

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Abstract Introduction: The Philadelphia-negative chronic myeloproliferative neoplasms (MPNs) which include essential thrombocythemia (ET), polycythemia vera (PV) and primary myelofibrosis (PMF) are characterized by varying degrees of bone marrow fibrosis and endothelial proliferation. We and others have previously reported that these stromal alterations are reflected by increased serum levels of matrix derived metabolites, striated collagens type I/III and basement membrane components. The existence of a prefibrotic seromarker profile in MPNs is further evidenced by reports on increased serum levels of matrix metalloproteinase-3 (MMP-3) and decreased tissue inhibitor of metalloproteinase- I (TIMP-I). Using whole blood gene expression profiling, we aimed to provide a comprehensive gene signature of extracellular matrix-related proteins in MPNs with particular focus on genes associated with the regulation of major stromal proteins and MMPs. Methods: Gene expression profiling was performed on whole blood from 21 control subjects, 19 patients with ET, 41 patients with PV, and 9 patients with PMF. RNA was converted to biotin labeled amplified RNA (aRNA) using the MessageAmpTM III RNA amplification kit, and fragmented aRNA was hybridized to Affymetrix HG-U133 Plus 2.0 microarray chips recognizing 54,675 probe sets (38,500 genes). The R statistical software was applied to perform data preprocessing and statistical analysis of microarray data. Results: We identified 20,439, 25,307, and 17,417 probe sets that were differentially expressed between controls and patients with ET, PV, and PMF, respectively (FDR£0.05). These genes included 116 genes encoding extracellular matrix and adhesion molecules (ECM) important for cell-cell and cell-matrix interactions. These genes are represented on the Qiagen Human ECM panel, and in addition, all remaining collagen genes have been included. In patients with ET, COL1A1, COL1A2, COL3A1, COL4A2, COL4A5, LAMA2, LAMB1, MMP1, MMP7, MMP11, MMP12, MMP14, AND TIMP3 were among the 42 upregulated ECM genes (FDR<0.05). In patients with PV, 53 ECM genes were upregulated including COL1A1, COL1A2, COL3A1, COL4A2, LAMA2, LAMB1, MMP1, MMP7, MMP8, MMP9, MMP11, MMP12, MMP14, and TIMP3 (FDR<0.05). In PMF, COL1A2, COL3A1, COL4A2, COL4A5, LAMA2, MMP1, MMP8, MMP9, MMP14, and TIMP3 were among the 26 upregulated genes (FDR<0.05) (Table 1). 17, 14, and 13 ECM genes were significantly downregulated in ET, PV, and PMF, respectively (FDR<0.05) (data not shown). ITGA7, ITGB3, and MMP1 were significantly upregulated from ET over PV to PMF, whereas ITGAL, SPG7, and TGFBI were significantly downregulated from ET over PV to PMF. ADAMTS8, ADAMTS13, COL10A1, COL14A1, COL1A2, COL29A1, COL3A1, COL4A2, COL6A1, ITGA7, ITGB3, ITGB5, LAMA2, MMP1, MMP14, NCAM1, THBS2, and TIMP3 were significantly upregulated in both ET, PV, and PMF (FDR<0.05). COL4A3BP, COL6A2, ITGA4, ITGA5, ITGAL, ITGB1, PECAM1, SPG7, and TGFBI were significantly downregulated in both ET, PV, and PMF (FDR<0.05). In table 2a-b are shown the 10 most significantly up- and downregulated genes. Discussion and conclusions: Bone marrow fibrosis and endothelial proliferation in MPNs are elicited due to the release of fibrogenic and angiogenic growth factors primarily from hyperproliferating megakaryocytes. The connective tissue components of the bone marrow in MPNs include type III collagen, which is deposited in the early disease stages (ET/PV) as "reticulin fibrosis" being accompanied and substituted by mature Van Giesson positive collagen (type I collagen) in the advanced myelofibrosis stage. Increased endothelial cell proliferation is followed by the development of continuous sheets of basement membrane material beneath endothelial cells as assessed by increased deposition of type IV collagen and laminin. Using whole blood gene expression profiling, we provide evidence that abnormal extracellular matrix metabolism is reflected in the gene signature of peripheral blood cells from patients with MPNs. Further studies are needed to determine whether these changes represent local bone marrow fibrogenesis and/or systemic disease manifestations. Disclosures Hasselbalch: Novartis: Research Funding.
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Mogulevtseva, J. A., A. V. Mezentsev, and S. A. Bruskin. "RNAI-MEDIATED SILENCING OF MATRIX METALLOPROTEINASE 1 IN EPIDERMAL KERATINOCYTES INFLUENCES THE BIOLOGICAL EFFECTS OF INTERLEUKIN 17A." Vavilov Journal of Genetics and Breeding 22, no. 4 (July 3, 2018): 425–32. http://dx.doi.org/10.18699/vj18.378.

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Matrix metalloproteinases (MMPs) are important for the pathogenesis of psoriasis and other autoimmune disorders. In the extracellular matrix, accumulation of proinflammatory cytokines, such as interleukin 17A (IL-17A), leads to induction of several MMPs, including MMP1. MMPs change the composition and other properties of the extracellular matrix. These changes facilitate tissue remodeling and promote the development of psoriatic plaques. The aim of this study was to explore how MMP1 silencing might influence the biological effects of IL-17A on migration and proliferation of human epidermal keratinocytes and the expression of genes involved in their division and differentiation. The experiments were performed with MMP1-deficient and control epidermal keratinocytes, HaCaT-MMP1 and HaCaT-KTR, respectively. Cell proliferation and migration were assessed by comparative analysis of the growth curves and scratch assay, respectively. To quantify cell migration, representative areas of cell cultures were photographed at the indicated time points and compared to each other. Changes in gene expression were analyzed by real-time PCR. The obtained results demonstrated that MMP1 silencing in the cells treated with IL-17A resulted in downregulation of MMP9 and -12, FOSL1, CCNA2, IVL, KRT14 and -17 as well as upregulation of MMP2, CCND1 and LOR. Moreover, MMP1 silencing led to a decrease in cell proliferation and an impairment of cell migration. Thus, MMP1-deficiency in epidermal keratinocytes can be beneficial for psoriasis patients that experience an accumulation of IL-17 in lesional skin. Knocking MMP1 down could influence migration and proliferation of epidermal keratinocytes in vivo, as well as help to control the expression of MMP1, -2, -9 и -12, CCNA2, CCND1, KRT14 and -17 that are crucial for the pathogenesis of psoriasis.
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Chen, Chao, Congcong Li, Weichun Liu, Feng Guo, Xi Kou, Si Sun, Taiyang Ye, Shanji Li, and Aimin Zhao. "Estrogen-induced FOS-like 1 regulates matrix metalloproteinase expression and the motility of human endometrial and decidual stromal cells." Journal of Biological Chemistry 295, no. 8 (January 14, 2020): 2248–58. http://dx.doi.org/10.1074/jbc.ra119.010701.

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The regulation mechanisms involved in matrix metalloproteinase (MMP) expression and the motility of human endometrial and decidual stromal cells (ESCs and DSCs, respectively) during decidualization remain unclear. DSCs show significant increased cell motility and expression of FOS-like 1 (FOSL1) and MMP1, MMP2, and MMP9 compared with ESCs, whereas lack of decidualization inducers leads to a rapid decrease in FOSL1 and MMP1 and MMP9 expression in DSCs in vitro. Therefore, we hypothesized that a link exists between decidualization inducers and FOSL1 in up-regulation of motility during decidualization. Based on the response of ESCs/DSCs to different decidualization systems in vitro, we found that progesterone (P4) alone had no significant effect and that 17β-estradiol (E2) significantly increased cell motility and FOSL1 and MMP1 and MMP9 expression at the mRNA and protein levels, whereas 8-bromo-cAMP significantly decreased cell motility and FOSL1 and MMP9 expression in the presence of P4. In addition, we showed that E2 triggered phosphorylation of estrogen receptor 1 (ESR1), which could directly bind to the promoter of FOSL1 in ESCs/DSCs. Additionally, we also revealed silencing of ESR1 expression by siRNA abrogated E2-induced FOSL1 expression at the transcript and protein levels. Moreover, silencing of FOSL1 expression by siRNA was able to block E2-induced MMP1 and MMP9 expression and cell motility in ESCs/DSCs. Taken together, our data suggest that, in addition to its enhancement of secretory function, the change in MMP expression and cell motility is another component of the decidualization of ESCs/DSCs, including estrogen-dependent MMP1 and MMP9 expression mediated by E2–ESR1–FOSL1 signaling.
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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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Zaidi, Sana Jafar, Nabeela Riaz, Asifa Iqbal, and Ayyaz Ali Khan. "Salivary Matrix Metalloproteinase (MMP)-1 as Non-Invasive Tool for The Diagnosis of Oral Squamous Cell Carcinoma (OSCC)." Journal of the Pakistan Dental Association 30, no. 1 (February 14, 2021): 18–23. http://dx.doi.org/10.25301/jpda.301.18.

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OBJECTIVE: To determine the diagnostic accuracy of salivary MMP1 as non-invasive diagnostic biomarker of OSCC through conventional sandwich ELISA technique. Analytical cross-sectional study. METHODOLOGY: Individuals with clinical suspicion for OSCC (IWCS-OSCC) were included in the study after fulfilling selection criteria. Saliva samples were collected from IWCS-OSCC. To confirm OSCC, the patients were referred for biopsy. After definitive diagnosis on biopsy, patients were labeled OSCC positive or OSCC negative. The colorimetric sandwich-ELISA test was performed on saliva samples to measure the level of MMP1. Data was entered in "Statistical Package for the Social Sciences (SPSS) -16" and levels of MMP1 were correlated with the biopsy status of patient (OSCC positive or OSCC negative). RESULTS: Our sample included twice as many males as females (2.1:1) and a wide age range of 22-77years with median age of 50yrs. Of all the IWCS-OSCC 85% were OSCC +ve and 15% were OSCC-ve. Diagnostic accuracy was measured as; Area under curve (AUC) = 0.623, Sensitivity (Sn) = 50%, Specificity (Sp)= 83.3%, Positive predictive value (PPV)= 94.4%, Negative predictive value (NPV)= 22.7% CONCLUSION: MMP1 as detected by conventional sandwich-ELISA technique is not proven as an accurate diagnostic biomarker of OSCC. KEY WORDS: OSCC; MMP1; IWCS-OSCC; Sandwich-ELISA HOW TO CITE: Zaidi SJ, Riaz N, Iqbal A, Khan AA. Salivary matrix metalloproteinase (MMP)-1 as non-invasive tool for the diagnosis of oral squamous cell carcinoma (OSCC). J Pak Dent Assoc 2021;30(1):18-23.
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Korytina, G. F., L. Z. Akhmadishina, D. G. Yanbaeva, Sh Z. Zagidullin, and T. V. Viktorova. "Association of polymorphic variants of matrix metalloproteinase and antiprotease genes with development and severity of chronic obstructive pulmonary disease." PULMONOLOGIYA, no. 1 (February 28, 2008): 33–38. http://dx.doi.org/10.18093/0869-0189-2008-0-1-33-38.

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To evaluate a role of polymorphic variants of metalloproteinase and protease genes for hereditary susceptibility to COPD and its severity, we analyzed polymorphic loci of MMP1, MMP9, MMP12, PI, and AACT genes in COPD patients (n = 318) and healthy persons (n = 319) living at the Bashkortostan Republic. Results showed that frequency of genotypes and alleles of G(-1607)GG gene MMP1, С(-1562)T gene MMP9, A(-82)G gene MMP12, and Ala 15 Thr gene ААСТ did not differ in COPD patients and healthy subjects. The Zand S-mutations of the PI gene were also similar in both the groups. The heterozygous GA genotype of G1237A locus in the 3'-non-translated region of PI gene was associated with COPD occurrence (OR = 2.09; 95 % CI: 1.15–3.81). To determine polymorphic variants associated with severity of clinical course and age of the disease manifestation, a comparative analysis of rates of genotypes and alleles was performed in patients with different COPD stages and of different age. The stage IV COPD patients significantly more often carried rare T allele in С(-1562)T locus of the MMP9 gene (15.89 % vs 8.38 %; χ2 = 7.804; df = 1; p = 0.005; OR = 2.06; 95 % CI: 1.22–3.49). Individuals with rare TT genotype of MMP9 gene were found only among the stage IV COPD patients (3.97 % vs 0 %; χ2 = 4.78; p = 0.029; pcor = 0.058). Moreover, analysis of this locus in patients with early manifestation of COPD (younger the 55 yrs) revealed significantly more frequent rate of T allele in patients with stage IV COPD compared to patients of the same age but less severe COPD (χ2 = 5.26; df = 1; p = 0.022).
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Morais Junior, Gilberto Santos, Nathalia Oliveira Rodrigues, Adriane Dallanora Henriques, Audrey Cecília Tonet-Furioso, Ciro José Brito, Lucy Oliveira Gomes, Clayton Franco Moraes, and Otávio Toledo Nóbrega. "Matrix Metalloproteinase-1 Gene Polymorphism Associated with Ultrasound-Assessed Carotid Thickness among Older Adults." Journal of Aging Research 2018 (June 21, 2018): 1–6. http://dx.doi.org/10.1155/2018/1475890.

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Background and Aim. Due to the high incidence of vascular diseases, it is necessary to identify new circulating or structural markers for predicting risk for chronic diseases. Some studies suggest that MMP1 gene polymorphisms are associated with the enzyme expression levels in situ (e.g., in atherosclerotic plaques). Objectives. Thus, the study of this polymorphism may help understanding the pathophysiology of coronary disease. Methods. We performed cross-sectional clinical and laboratory evaluations (including measurement of intima-media thickness of carotid arteries) and genotyping of the MMP1 SNP rs495366 (A/G) in 366 elderly people. Results. No significant differences between genotypes were noted for biochemical, metabolic, inflammatory, or clinical variables except for a significant difference in intima-media thickness for the left carotid artery and a trend toward significance for the right counterpart. Conclusion. Carriers of the allele associated with lower MMP1 expression (allele A) presented greater carotid thickness. We suggest that the phenomenon can be explained by impaired remodeling of the arterial wall (poor degradation of collagen fibers in this scenario), yielding carotid wall thickening and a greater intrinsic risk for cerebrovascular events.
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Said, Anan H., Shien Hu, Ameer Abutaleb, Tonya Watkins, Kunrong Cheng, Ahmed Chahdi, Panjamurthy Kuppusamy, Neeraj Saxena, Guofeng Xie, and Jean-Pierre Raufman. "Interacting post-muscarinic receptor signaling pathways potentiate matrix metalloproteinase-1 expression and invasion of human colon cancer cells." Biochemical Journal 474, no. 5 (February 20, 2017): 647–65. http://dx.doi.org/10.1042/bcj20160704.

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M3 muscarinic receptor (M3R) expression is increased in colon cancer; M3R activation stimulates colon cancer cell invasion via cross-talk with epidermal growth factor receptors (EGFR), post-EGFR activation of mitogen-activated protein kinase (MAPK) extracellular signal-related kinase 1/2 (ERK1/2), and induction of matrix metalloproteinase-1 (MMP1) expression. MMP1 expression is strongly associated with tumor metastasis and adverse outcomes. Here, we asked whether other MAPKs regulate M3R agonist-induced MMP1 expression. In addition to activating ERK1/2, we found that treating colon cancer cells with acetylcholine (ACh) stimulated robust time- and dose-dependent phosphorylation of p38 MAPK. Unlike ERK1/2 activation, ACh-induced p38 phosphorylation was EGFR-independent and blocked by inhibiting protein kinase C-α (PKC-α). Inhibiting activation of PKC-α, EGFR, ERK1/2, or p38-α/β alone attenuated, but did not abolish ACh-induced MMP1 expression, a finding that predicted potentiating interactions between these pathways. Indeed, ACh-induced MMP1 expression was abolished by incubating cells with either an EGFR or MEK/ERK1/2 inhibitor combined with a p38-α/β inhibitor. Activating PKC-α and EGFR directly with the combination of phorbol 12-myristate 13-acetate (PMA) and EGF potentiated MMP1 gene and protein expression, and cell invasion. PMA- and ACh-induced MMP1 expression were strongly diminished by inhibiting Src and abolished by concurrently inhibiting both p38-α/β and Src, indicating that Src mediates the cross-talk between PKC-α and EGFR signaling. Using siRNA knockdown, we identified p38-α as the relevant p38 isoform. Collectively, these studies uncover novel functional interactions between post-muscarinic receptor signaling pathways that augment MMP1 expression and drive colon cancer cell invasion; targeting these potentiating interactions has therapeutic potential.
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Sauter, Wiebke, Albert Rosenberger, Lars Beckmann, Silke Kropp, Kirstin Mittelstrass, Maria Timofeeva, Gabi Wölke, et al. "Matrix Metalloproteinase 1 (MMP1) Is Associated with Early-Onset Lung Cancer." Cancer Epidemiology Biomarkers & Prevention 17, no. 5 (May 2008): 1127–35. http://dx.doi.org/10.1158/1055-9965.epi-07-2840.

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Dissertations / Theses on the topic "Matrix metalloproteinase 1 (MMP1)"

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Kumar, Deepak. "Mechanism of induction of matrix metalloproteinase-1 (MMP-1) during osteoarthritis /." Free to MU Campus, others may purchase, 2004. http://wwwlib.umi.com/cr/mo/fullcit?p3144432.

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Sroka, Isis Calsoyas. "Regulation Of Membrane-Type 1 Matrix Metalloproteinase In Prostate Cancer." Diss., The University of Arizona, 2007. http://hdl.handle.net/10150/194830.

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Membrane type-1 matrix metalloproteinase (MT1-MMP) is a metalloproteinase which becomes upregulated in prostate cancer and has been implicated in processes of prostate cancer metastasis. Here, we show that MT1-MMP is minimally expressed in nonmalignant primary prostate cells, moderately expressed in DU-145 cells, and highly expressed in invasive PC-3 and PC-3N cells. Using MT1-MMP promoter reporters and mobility shift assays, we show that Sp1 regulates MT1-MMP expression in DU-145, PC-3, and PC-3N cells and in PC3-N cells using chromatin immunoprecipitation analysis and silencing RNA. Investigation of signaling pathways in these cells showed that DU-145 cells express constitutively phosphorylated extracellular stress-regulated kinase (ERK), whereas PC-3 and PC-3N cells express constitutively phosphorylated AKT/PKB and c-Jun NH2 terminal kinase (JNK). We show that MT1-MMP and Sp1 levels are decreased in PC-3 and PC-3N cells when PI-3K and JNK are inhibited, and that MT1-MMP levels are decreased in DU-145 cells when MEK is inhibited. Transient transfection of PC-3 and PC-3N cells with a dominant-negative JNK or p85, and DU-145 cells with a dominant negative ERK, reduced MT1-MMP promoter activity. We also identified the insulin-like growth factor (IGF-1R) as an upstream regulatory component of MT1-MMP in PC-3N and LNCaP cells, which express high and low levels of the enzyme, respectively. Treatment of PC-3N cells with an IGF-1R specific inhibitor decreased MT1-MMP promoter activity, RNA and protein levels. Additionally, treatment of LNCaP cells with a synthetic androgen to increase IGF-1R levels and subsequent treatment with IGF-I increased MT1-MMP promoter activity, RNA and protein levels. Analysis of MT1-MMP and IGF-1R expression in human prostate cancer tissues demonstrated that MT1-MMP expression was high in the apical cytoplasmic regions of PIN and prostate cancer and less intense in the basalateral cytoplasmic membrane regions of benign glands. IGF-1R was expressed in normal glands and highly expressed in prostate cancer. In conclusion, we have identified several novel mechanisms regulating MT1-MMP expression in prostate cancer cell lines as well as differential localization of the enzyme in human prostate cancer tissues. These results provide insight into the complex mechanisms of prostate cancer metastasis and may be useful for developing future diagnostic procedures or therapies.
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Anand, Monika. "FUNCTION AND REGULATION OF MATRIX METALLOPROTEINASE-1 IN GLIOBLASTOMA MULTIFORME." VCU Scholars Compass, 2010. http://scholarscompass.vcu.edu/etd/2214.

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Glioblastoma Multiforme (GBM) is an aggressive and fatal cancer of the brain. It is characterized with augmented morbidity and elusion to therapies due in part to the incessant infiltration and spread of tumor cells in normal brain. We investigated the function of Matrix metalloproteinase-1, an important enzyme noted to be responsible for invasion in other cancers, in GBM and its regulation by epidermal growth factor receptor (EGFR) signaling. Previous studies from our laboratory demonstrated elevated levels of MMP-1 in GBM. Further studies indicated the involvement of MMP-1 in GBM invasion. The GBM cell lines T98G, U251MG and U87MG were used for this study. In T98G cell lines, inhibition of MMP-1 by siRNA significantly suppressed basal in vitro invasion without impacting cell viability. The over-expression of MMP-1 was accomplished in U251MG and U87MG using the mammalian expression vector, pIRES, encoding full length MMP-1 cDNA. The MMP-1 over-expressing U251MG and U87MG cells exhibited significantly enhanced invasion in vitro with no modification in the cell proliferation rates. A majority of GBM patients present defective EGFR signaling due to over-expression, amplification or mutation in the receptor. MMP-1 is known to be up-regulated by various stimulatory agents including growth factors. We examined the regulation of MMP-1 by EGFR activation and observed the induction of MMP-1 after EGF treatment. Inhibition of the receptor by pharmaceutic inhibitor treatment and genetic approaches led to reduction in MMP-1 levels. We also observed that this regulation is primarily mediated by the downstream MAPK pathway. Inhibition of MAPK and not PI3K pathway resulted in diminished MMP-1 protein levels even in the presence of EGF. These studies demonstrate the importance of the EGFR-MAPK signaling pathway in the induction of MMP-1 in glioma cell lines. In addition, MMP-1 plays a role in glioma cell invasion in vitro. These results along with the reports of MMP-1 over-expression in GBM warrant future studies examining the function of MMP-1 in vivo.
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Mullet, Emily. "Functional Consequences of Matrix Metalloproteinase-1 Over-Expression in Human Gliomas." VCU Scholars Compass, 2006. http://hdl.handle.net/10156/1437.

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Nguyen, Khanh Vu Thuy. "The Effects of Scaling and Root Planing on the Systemic Levels of Matrix Metalloproteinase-9 (MMP-9) and Tissue Inhibitor of Matrix Metalloproteinase-1 (TIMP-1)." VCU Scholars Compass, 2007. http://scholarscompass.vcu.edu/etd_retro/160.

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Balance between matrix metalloproteinases (MMPs) and tissue inhibitors of matrix metalloproteinases (TIMPs) is required for normal wound healing. Chronic inflammation, such as that seen in cardiovascular and periodontal diseases, may upset this balance. The aim of this study was to determine whether initial periodontal therapy would have an effect systemically on the levels of MMP-9 and TIMP-1. Twenty-one patients with generalized chronic periodontitis were enrolled in the study. Clinical examinations were conducted and parameters measured. Scaling and root planing was performed and blood analysis done to determine the plasma concentrations of MMP-9 and serum concentrations of TIMP-1. Initial periodontal therapy resulted in improvements in gingival inflammation and plaque levels. No effect on the plasma concentrations of MMP-9 and serum concentrations of TIMP-1 could be found following therapy.
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Arnold, Laurence. "Biophysical characterisation of collagen binding by the hemopexin domain of matrix metalloproteinase-1 (MMP-1)." Thesis, University of Portsmouth, 2010. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.516871.

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Li, He. "A study of fibroblast-mediated contraction in ocular scarring : gene expression profiling and the role of small GTPases in Matrix Metalloproteinase 1 (MMP1) regulation." Thesis, University College London (University of London), 2017. http://discovery.ucl.ac.uk/10024949/.

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Understanding the molecular mechanisms involved in fibroblast-mediated tissue contraction is essential for developing future therapeutics for anti-scaring and fibrosis treatment not only for eyes, but also for a wide range of fibrotic diseases. The small Rho GTPase Rac1 is a master regulator of actin dynamics, which plays an essential role in protrusive activity, tissue repair and wound healing. A genome wide microarray study was performed with/without the transient treatment of human conjunctival fibroblasts with Rac1 inhibitor NSC23766 in a collagen gel contraction model to unveil the signalling events underlying contractile activity and the contribution of Rac1 activation. Through a comprehensive analysis that combined a pilot parallel study of scarring in an in vivo model in rabbit following glaucoma filtration surgery, and previously obtained microarray data of human ocular fibrotic diseases (including trachoma and thyroid-associated orbitopathy), it was identified that the contraction process consisted of two phases: an early phase that exhibited a classic serum/wound response profile with upregulation of genes related to inflammation, matrix remodelling, and transcription activation; and a late stage when the hyperactive signal receded and the gene profile progressed to promote fibrosis. The transient treatment with NSC23766 altered gene expression, and the early inhibition of Rac1 blocked the fibroblasts from entering the contractile phenotype as a whole. Interestingly, NSC23766 did not supress the mRNA expression of Matrix Metalloproteinase (MMP) 1, 3 and 10 during contraction, but reduced their enzymatic activity. The link between the activation of the Rho GTPase and MMP expression was subsequently investigated using MMP1 as an example. The results showed Rac1, Cdc42 and RhoA differently regulated MMP1 expression and secretion in fibroblasts during contraction, suggesting that the rate-limiting step for modulating MMP is the release in the extracellular medium rather than expression levels, drawing some interesting new prospects for therapies.
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Sritharan, Kajanatharshni. "The role of membrane type-1 matrix metalloproteinase (MT1-MMP) in carotid plaque instability." Thesis, Imperial College London, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.517390.

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Wang, Fang St George Clinical school UNSW. "Oxidative stress induced C-Jun N-terminal Kinase (JNK) activation in tendon cells upregulates MMP1 mRNA and protein expression." Awarded by:University of New South Wales. St George Clinical school, 2006. http://handle.unsw.edu.au/1959.4/28815.

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To explore the potential mechanisms of tendon degeneration, we investigated the role of c-Jun N-terminal Kinase (JNK) activation and the regulation of matrix metalloproteinase 1 (MMP1) in tendon matrix degradation under oxidative stress. JNK and MMP1 activity in samples from normal and ruptured human supraspinatus tendons were evaluated by immunohistochemistry. Real-time quantitative PCR was utilized to evaluate MMP1 mRNA expression and western blotting for MMP1 and JNK protein detection. JNK activation and increased MMP1 activity were found in the torn human supraspinatus tendon tissue, as well as in human tendon cells under in vitro oxidative stress. Inhibition of JNK prevented MMP1 over-expression in oxidative stressed human tendon cells. Results from the current study indicated that stress activated JNK plays an important role in tendon matrix degradation, possibly through upregulating of MMP1.
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Harada, Tomika. "Membrane-type matrix metalloproteinase-1(MT1-MMP) gene is overexpressed in highly invasive hepatocellular carcinomas." Kyoto University, 1999. http://hdl.handle.net/2433/181703.

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Books on the topic "Matrix metalloproteinase 1 (MMP1)"

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Clark, Ian M., ed. Matrix Metalloproteinase Protocols. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60327-299-5.

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Clendeninn, Neil J., and Krzysztof Appelt, eds. Matrix Metalloproteinase Inhibitors in Cancer Therapy. Totowa, NJ: Humana Press, 2001. http://dx.doi.org/10.1007/978-1-59259-011-7.

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Matrix Metalloproteinase. MDPI, 2020. http://dx.doi.org/10.3390/books978-3-03936-649-1.

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Lee, Hyejin (Rosa). Critical role of membrane-type 1 matrix metalloproteinase in collagen phagocytosis by fibroblasts. 2007.

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Book chapters on the topic "Matrix metalloproteinase 1 (MMP1)"

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Grams, Frank, Hans Brandstetter, Richard A. Engh, Dagmar Glitz, Hans-Willi Krell, Valeria Livi, Ernesto Menta, et al. "Research on MMP Inhibitors with Unusual Scaffolds." In Matrix Metalloproteinase Inhibitors in Cancer Therapy, 223–43. Totowa, NJ: Humana Press, 2001. http://dx.doi.org/10.1007/978-1-59259-011-7_9.

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Zhou, Jiehao, Stephen A. Stohlman, Norman W. Marten, and David R. Hinton. "Regulation of Matrix Metalloproteinase (MMP) and Tissue Inhibitor of Matrix Metalloproteinase (TIMP) Genes During JHMV Infection of the Central Nervous System." In Advances in Experimental Medicine and Biology, 329–34. Boston, MA: Springer US, 2001. http://dx.doi.org/10.1007/978-1-4615-1325-4_49.

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Walia, Vijay, and Yardena Samuels. "Analysis of Enzymatic Activity of Matrix Metalloproteinase (MMP) by Collagen Zymography in Melanoma." In Methods in Molecular Biology, 97–106. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-7595-2_10.

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Lalu, Manoj M., Cindy Q. Gao, and Richard Schulz. "Matrix metalloproteinase inhibitors attenuate endotoxemia induced cardiac dysfunction: A potential role for MMP-9." In Biochemistry of Hypertrophy and Heart Failure, 61–66. Boston, MA: Springer US, 2003. http://dx.doi.org/10.1007/978-1-4419-9238-3_9.

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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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Lahat, Nitza, Sarah Shapiro, Michael Inspector, Reuben Reich, Rosa Gershtein, and Ariel Miller. "Matrix-Metalloproteinases (MMPS) in Astroglial Cells." In Advances in Behavioral Biology, 149–57. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-5337-3_21.

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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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Brown, Peter D., and Mark Whittaker. "Matrix Metalloproteinase Inhibitors." In Antiangiogenic Agents in Cancer Therapy, 205–23. Totowa, NJ: Humana Press, 1999. http://dx.doi.org/10.1007/978-1-59259-453-5_13.

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Stetler-Stevenson, William G. "Matrix Metalloproteinase Inhibitors." In Cancer Therapeutics, 241–61. Totowa, NJ: Humana Press, 1997. http://dx.doi.org/10.1007/978-1-59259-717-8_12.

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Conference papers on the topic "Matrix metalloproteinase 1 (MMP1)"

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Morishita, Asahiro, Chien-Hung Gow, and Jeanine D'Armiento. "The Role Of Macrophages-Specific Matrix Metalloproteinase-1 (MMP1) In Cigarette Smoke Induced Lung Metastasis." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a2634.

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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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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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Hassan, Neveen, Aliae Mohamed-Hussein, Ebtssam Mohamed, Omnia Mohamed, Hanan Mohamed, and Manal Tammam. "Matrix metalloproteinase- 9 (MMP-9) and tissue inhibitor of metalloproteinase-1(TIMP-1) as non-invasive biomarkers of remodelling in asthma." In Annual Congress 2015. European Respiratory Society, 2015. http://dx.doi.org/10.1183/13993003.congress-2015.oa1467.

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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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Biswas, Swethajit, Kenneth Rankin, Anna Long, Sohail Nisar, Craig Gerrand, Petra Dildey, and John Lunec. "Abstract 5580: Membrane-Type 1 Matrix Metalloproteinase (MT1-MMP): A predictive biomarker of chemotherapy response in osteosarcoma." 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.am2012-5580.

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Stallings-Mann, M., M. Raeeszadeh-Sarmazdeh, E. Miller, E. Radisky, and D. Radisky. "Adenoviral Delivery of Matrix Metalloproteinase 3 (MMP3)-Directed Tissue Inhibitor of Metalloproteinase 1 (TIMP1) Variants Ameliorates Fibrosis Established by Transforming Growth Factor Beta (TGFB) or Bleomycin in Mice." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a7868.

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Pardo, Annie, Iliana Herrera, Elena Anso, Jose Cisneros, Remedios Ramirez, Moises Selman, and Navdeep S. Chandel. "Matrix Metalloproteinase (MMP-1) Induces Alveolar Epithelial Cell Migration And Proliferation, Protects From Apoptosis And Represses Mitochondrial Oxygen Consumption." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a5564.

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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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Anand, Monika, Zendra E. Zehner, and Helen L. Fillmore. "Abstract 261: Epidermal growth factor receptor (EGFR)-mediated upregulation of matrix metalloproteinase-1(MMP-1) in glioblastoma cell lines involves multiple signaling pathways." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-261.

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Reports on the topic "Matrix metalloproteinase 1 (MMP1)"

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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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Cao, Jian, and Stanley Zucker. Examination of the Role of Membrane Type-1 Matrix Metalloproteinase (MTI-MMP) in Breast Cancer Metastasis. Fort Belvoir, VA: Defense Technical Information Center, August 2001. http://dx.doi.org/10.21236/ada398200.

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Cao, Jian, and Stanley Zucker. Examination of the Role of Membrane Type-1 Matrix Metalloproteinase (MTI-MMP) in Breast Cancer Metastasis. Fort Belvoir, VA: Defense Technical Information Center, August 1999. http://dx.doi.org/10.21236/ada384239.

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Cao, Jian. Examination of the Unique Role of Membrane Type 1-Matrix Metalloproteinase (MT1-MMP) in Prostate Cancer Invasion and Metastasis. Fort Belvoir, VA: Defense Technical Information Center, January 2003. http://dx.doi.org/10.21236/ada413311.

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Sehgal, Inder. TGF(Beta)1 Regulation of Matrix Metalloproteinase-9 in Human Prostate Cancer Metastasis. Fort Belvoir, VA: Defense Technical Information Center, June 2003. http://dx.doi.org/10.21236/ada421319.

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Cao, Jian, and Stanley Zucker. Examination of the Role of Membrane Type-1 Matrix Metalloproteinase in Breast Cancer Metastasis. Fort Belvoir, VA: Defense Technical Information Center, August 2000. http://dx.doi.org/10.21236/ada393382.

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Brinckerhoff, Constance E. Genetic Analysis of a Single Nucleotide Polymorphism in the Matrix Metalloproteinase 1 Promoter in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, July 2002. http://dx.doi.org/10.21236/ada407580.

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Brinckerhoff, Constqance B. Genetic Analysis of a Single Nucleotide Polymorphism in the Matrix Metalloproteinase 1 Promoter in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, July 2003. http://dx.doi.org/10.21236/ada419338.

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