Relevant bibliographies by topics / Tissuee inhibitors of metalloproteinase

Academic literature on the topic 'Tissuee inhibitors of metalloproteinase'

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Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Tissuee inhibitors of metalloproteinase"

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Hsia, Tain-Yen, Jeremy M. Ringewald, Robert E. Stroud, Nadia Roessler, Nidhi Kumar, Scott T. Reeves, and Francis G. Spinale. "Plasma profiling determinants of matrix homeostasis in paediatric dilated cardiomyopathy." Cardiology in the Young 21, no. 1 (October 27, 2010): 52–61. http://dx.doi.org/10.1017/s1047951110001381.

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AbstractObjectiveDilated cardiomyopathy is an important cause of cardiac failure in both children and adults, but is more progressive in children. In adult dilated cardiomyopathy, left ventricular remodelling is associated with changes in the plasma levels of matrix metalloproteinases and tissue inhibitor of metalloproteinases. Plasma matrix metalloproteinases and tissue inhibitors of metalloproteinase changes in paediatric dilated cardiomyopathy have not been examined. This study developed a low blood volume, high-sensitivity assay to test the hypothesis that unique and differential plasma matrix metalloproteinases and tissue inhibitors of metalloproteinase profile exist in patients with paediatric dilated cardiomyopathy.Methods/resultsA systemic blood sample (1 millilitre) was obtained from seven children aged 8 plus or minus 7 years with dilated cardiomyopathy and 26 age-matched normal volunteers. Using a high-throughput multiplex suspension immunoassay, plasma levels were quantified for collagenases (matrix metalloproteinase-8), gelatinases (matrix metalloproteinase-2 and -9), lysins (matrix metalloproteinase-3 and -7), and tissue inhibitor of metalloproteinases-1, -2, and -4. The matrix metalloproteinase to tissue inhibitors of metalloproteinases ratios were also calculated. The plasma matrix metalloproteinase-2, -7, -8, and -9 levels were increased by greater than twofold in patients with dilated cardiomyopathy than normal patients (with p less than 0.05). Patients with dilated cardiomyopathy also had significantly higher tissue inhibitors of metalloproteinases-1 and -4 (298% and 230%; with p less than 0.05).ConclusionsThese unique findings show that a specific plasma matrix metalloproteinase/tissue inhibitor of metalloproteinase profile occurs in paediatric dilated cardiomyopathy when compared to the cases of normal children. These distinct differences in the determinants of myocardial matrix structure and function may contribute to the natural history of dilated cardiomyopathy in children and may provide a novel biomarker platform in paediatric dilated cardiomyopathy.
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COWELL, Susan, Vera KNÄUPER, Margaret L. STEWART, Marie-Pia D'ORTHO, Heather STANTON, Rosalind M. HEMBRY, Carlos LÓPEZ-OTÍN, John J. REYNOLDS, and Gillian MURPHY. "Induction of matrix metalloproteinase activation cascades based on membrane-type 1 matrix metalloproteinase: associated activation of gelatinase A, gelatinase B and collagenase 3." Biochemical Journal 331, no. 2 (April 15, 1998): 453–58. http://dx.doi.org/10.1042/bj3310453.

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SW1353 chondrosarcoma cells cultured in the presence of interleukin-1, concanavalin A or PMA secreted procollagenase 3 (matrix metalloproteinase-13). The enzyme was detected in the culture medium by Western blotting using a specific polyclonal antibody raised against recombinant human procollagenase 3. Oncostatin M enhanced the interleukin-1-induced production of procollagenase 3, whereas interleukin-4 decreased procollagenase 3 synthesis. The enzyme was latent except when the cells had been treated with concanavalin A, when a processed form of 48 kDa, which corresponds to the active form, was found in the culture medium and collagenolytic activity was detected by degradation of 14C-labelled type I collagen. The concanavalin A-induced activation of procollagenase 3 coincided with the processing of progelatinase A (matrix metalloproteinase-2) by the cells, as measured by gelatin zymography. In addition, progelatinase B (matrix metalloproteinase-9) was activated when gelatinase A and collagenase 3 were in their active forms. Concanavalin A treatment of SW1353 cells increased the amount of membrane-type-1 matrix metalloproteinase protein in the cell membranes, suggesting that this membrane-bound enzyme participates in an activation cascade involving collagenase 3 and the gelatinases. This cascade was effectively inhibited by tissue inhibitors of metalloproteinases-2 and -3. Tissue inhibitor of metalloproteinases-1, which is a much weaker inhibitor of membrane-type 1 matrix metalloproteinase than tissue inhibitors of metalloproteinases-2 and -3 [Will, Atkinson, Butler, Smith and Murphy (1996) J. Biol. Chem. 271, 17119–17123], was a weaker inhibitor of the activation cascade.
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Adamson, R. E., and F. R. Hall. "Matrix metalloproteinases mediate the metastatic phenotype ofTheileria annulata-transformed cells." Parasitology 113, no. 5 (November 1996): 449–55. http://dx.doi.org/10.1017/s0031182000081518.

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SUMMARYTheileria annulatainfects and reversibly transforms bovine leucocytes. The parasite-transformed cells are immortalized, metastatic and express a number of metalloproteinases including matrix metalloproteinase 9 which they secrete. All the metalloproteinases observed on substrate gels are inhibited by tissue inhibitor of metalloproteinase 1 and 4 synthetic inhibitors BB94, GM6001, BRL29808AI and Ro31–4724. We have adapted anin vitroassay for metastatic behaviour that measures the ability of parasitized cells to cross reconstituted basement membrane, Matrigel™. Using this we demonstrated that macroschizont-infected cells are invasivein vitroand that their invasive properties can be almost eliminated by the same specific inhibitors of metalloproteinases as used in the substrate gels. This demonstrates that the metastatic behaviour of the infected cells is due in part to metalloproteinase activity and strongly suggests a role for the metalloproteinases we observed on gels. This is further supported by the fact that an attenuated vaccine line which shows much reduced metalloproteinase activity also exhibits a marked reduction in metastatic behaviour. We suggest that these metalloproteinases are virulence factors mediating some pathological features of the disease and their loss in the vaccine line could provide an explanation for attenuation.
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Lauer-Fields, Janelle L., Mare Cudic, Shuo Wei, Frank Mari, Gregg B. Fields, and Keith Brew. "Engineered Sarafotoxins as Tissue Inhibitor of Metalloproteinases-like Matrix Metalloproteinase Inhibitors." Journal of Biological Chemistry 282, no. 37 (July 10, 2007): 26948–55. http://dx.doi.org/10.1074/jbc.m611612200.

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Nagase, Hideaki, and Keith Brew. "Designing TIMP (tissue inhibitor of metalloproteinases) variants that are selective metalloproteinase inhibitors." Biochemical Society Symposia 70 (September 1, 2003): 201–12. http://dx.doi.org/10.1042/bss0700201.

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The tissue inhibitors of metalloproteinases (TIMPs) are endogenous inhibitors of the matrix metalloproteinases (MMPs), enzymes that play central roles in the degradation of extracellular matrix components. The balance between MMPs and TIMPs is important in the maintenance of tissues, and its disruption affects tissue homoeostasis. Four related TIMPs (TIMP-1 to TIMP-4) can each form a complex with MMPs in a 1:1 stoichiometry with high affinity, but their inhibitory activities towards different MMPs are not particularly selective. The three-dimensional structures of TIMP-MMP complexes reveal that TIMPs have an extended ridge structure that slots into the active site of MMPs. Mutation of three separate residues in the ridge, at positions 2, 4 and 68 in the amino acid sequence of the N-terminal inhibitory domain of TIMP-1 (N-TIMP-1), separately and in combination has produced N-TIMP-1 variants with higher binding affinity and specificity for individual MMPs. TIMP-3 is unique in that it inhibits not only MMPs, but also several ADAM (a disintegrin and metalloproteinase) and ADAMTS (ADAM with thrombospondin motifs) metalloproteinases. Inhibition of the latter groups of metalloproteinases, as exemplified with ADAMTS-4 (aggrecanase 1), requires additional structural elements in TIMP-3 that have not yet been identified. Knowledge of the structural basis of the inhibitory action of TIMPs will facilitate the design of selective TIMP variants for investigating the biological roles of specific MMPs and for developing therapeutic interventions for MMP-associated diseases.
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Curry, V. A., I. M. Clark, H. Bigg, and T. E. Cawston. "Large inhibitor of metalloproteinases (LIMP) contains tissue inhibitor of metalloproteinases (TIMP)-2 bound to 72,000-Mr progelatinase." Biochemical Journal 285, no. 1 (July 1, 1992): 143–47. http://dx.doi.org/10.1042/bj2850143.

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Connective-tissue cells in culture produce a family of metalloproteinases which, once activated, can degrade all the components of the extracellular matrix. These potent enzymes are all inhibited by the tissue inhibitor of metalloproteinases (TIMP), and it was thought that this inhibitor was solely responsible for the inhibition of these enzymes within connective tissue. However, other inhibitors have recently been described, including large inhibitor of metalloproteinases (LIMP) present in the culture medium of human foetal lung fibroblasts. Here we show that a large proportion of the inhibitory activity of LIMP consists of 72,000-M(r)-progelatinase bound to TIMP-2, a recently discovered low-M(r) metalloproteinase inhibitor closely related to TIMP. The physiological implications of the secretion of a complex of 72,000-M(r) progelatinase and TIMP-2 are discussed, and the separation of the complex in 6 M-urea is described.
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Kalinkina, T. V., N. V. Lareva, and M. V. Chistyakova. "Some indicators of left ventricular dysfunction in hypertensive patients, depending on the level of matrix metalloproteinases and tissue inhibitors of metalloproteinase-1." Kazan medical journal 102, no. 6 (December 13, 2021): 815–20. http://dx.doi.org/10.17816/kmj2021-815.

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Aim. To study the level of matrix metalloproteinases-1 and -2, and tissue inhibitor of metalloproteinases-1, the indicator of left ventricular myocardial deformation in patients with stage 12 hypertension. Methods. 114 patients (40 women and 74 men) with hypertension of 12 stages observed in the cardiology Department of the Road clinical hospital Chita II were examined. The median age was 428.3 years. Left ventriclular diastolic function was studied by using tissue Doppler imaging in apical four-chamber views. Serum matrix metalloproteinase-1, matrix metalloproteinase-2, and tissue inhibitor of metalloproteinases-1 levels were measured in all patients on automated immunoassay analyzers using ready-to-use ELISA kits. Results. An increase in serum levels of matrix metalloproteinases-1 and -2 in the group of patients with hypertension and diastolic dysfunction by 46 and 47%, respectively, was found against increased levels of serum tissue inhibitor of metalloproteinase-1 (р=0.049). In patients with diastole dysfunction, myocardial global longitudinal strain was decreased in was observed by 22.8% compared with patients without diastole dysfunction (p 0.05). The analysis revealed a moderate negative relationship between left ventricular global longitudinal strain and the serum levels of metalloproteinases-2 (r=0.64, p 0.05). Conclusion. In patients with hypertension and left ventricular diastolic dysfunction, a decrease in left ventricular global longitudinal strain is associated with the serum level of matrix metalloproteinase-2; a tissue inhibitor of metalloproteinases-1 is unrelated to left ventricular global myocardial strain.
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Inzitari, Domenico, Betti Giusti, Patrizia Nencini, Anna Maria Gori, Mascia Nesi, Vanessa Palumbo, Benedetta Piccardi, et al. "MMP9 Variation After Thrombolysis Is Associated With Hemorrhagic Transformation of Lesion and Death." Stroke 44, no. 10 (October 2013): 2901–3. http://dx.doi.org/10.1161/strokeaha.113.002274.

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Background and Purpose— Experimentally, matrix metalloproteinases (MMPs) play a detrimental role related to hemorrhagic transformation and severity of an ischemic brain lesion. Tissue-type plasminogen activator (tPA) enhances such effects. This study aimed to expand clinical evidence in this connection. Methods— We measured MMPs 1, 2, 3, 7, 8, 9, and tissue inhibitors of metalloproteinases 1, 2, 4 circulating level in blood taken before and 24 hours after tPA from 327 patients (mean age, 68.9±12.1 years; median National Institutes of Health Stroke Scale, 11) with acute ischemic stroke. Delta median values ([24 hours post tPA–pre tPA]/pre tPA) of each MMP or tissue inhibitors of metalloproteinase were analyzed across subgroups of patients undergoing symptomatic intracerebral hemorrhage, 3-month death, or 3-month modified Rankin Scale score 3 to 6. Results— Adjusting for major clinical determinants, only matrix metalloproteinase-9 variation proved independently associated with death (odds ratio [95% confidence interval], 1.58 [1.11–2.26]; P =0.045) or symptomatic intracerebral hemorrhage (odds ratio [95% confidence interval], 1.40 [1.02–1.92]; P =0.049). Both matrix metalloproteinase-9 and tissue inhibitors of metalloproteinase-4 changes were correlated with baseline, 24 hours, and 7 days National Institutes of Health Stroke Scale (Spearman P from <0.001 to 0.040). Conclusions— Our clinical evidence corroborates the detrimental role of matrix metalloproteinase-9 during ischemic stroke treated with thrombolysis, and prompts clinical trials testing agents antagonizing its effects.
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Thomas, Noel Vinay, and Se-Kwon Kim. "Metalloproteinase Inhibitors: Status and Scope from Marine Organisms." Biochemistry Research International 2010 (2010): 1–10. http://dx.doi.org/10.1155/2010/845975.

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Marine environment has been the source of diverse life forms that produce different biologically active compounds. Marine organisms are consistently contributing with unparalleled bioactive compounds that have profound applications in nutraceuticals, cosmeceuticals, and pharmaceuticals. In this process, screening of natural products from marine organisms that could potentially inhibit the expression of metalloproteinases has gained a huge popularity, which became a hot field of research in life sciences. Metalloproteinases, especially, matrix metalloproteinases (MMPs) are a class of structurally similar enzymes that contribute to the extracellular matrix degradation and play major role in normal and pathological tissue remodeling. Imbalance in the expression of MMPs leads to severe pathological condition that could initiate cardiac, cartilage, and cancer-related diseases. Three decades of endeavor for designing potent matrix metalloproteinase inhibitory substances (MMPIs) with many not making upto final clinical trials seek new resources for devising MMPIs. Umpteen number of medicinally valuable compounds being reported from marine organisms, which encourage current researchers to screen potent MMPIs from marine organisms. In this paper, we have made an attempt to report the metalloproteinase inhibiting substances from various marine organisms.
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Librach, C. L., Z. Werb, M. L. Fitzgerald, K. Chiu, N. M. Corwin, R. A. Esteves, D. Grobelny, R. Galardy, C. H. Damsky, and S. J. Fisher. "92-kD type IV collagenase mediates invasion of human cytotrophoblasts." Journal of Cell Biology 113, no. 2 (April 15, 1991): 437–49. http://dx.doi.org/10.1083/jcb.113.2.437.

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The specialized interaction between embryonic and maternal tissues is unique to mammalian development. This interaction begins with invasion of the uterus by the first differentiated embryonic cells, the trophoblasts, and culminates in formation of the placenta. The transient tumor-like behavior of cytotrophoblasts, which peaks early in pregnancy, is developmentally regulated. Likewise, in culture only early-gestation human cytotrophoblasts invade a basement membrane-like substrate. These invasive cells synthesize both metalloproteinases and urokinase-type plasminogen activator. Metalloproteinase inhibitors and a function-perturbing antibody specific for the 92-kD type IV collagen-degrading metalloproteinase completely inhibited cytotrophoblast invasion, whereas inhibitors of the plasminogen activator system had only a partial (20-40%) inhibitory effect. We conclude that the 92-kD type IV collagenase is critical for cytotrophoblast invasion.
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Dissertations / Theses on the topic "Tissuee inhibitors of metalloproteinase"

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Kranzhöfer, Alexander Friedrich. "Regulation of metalloproteinase expression in vascular pathology." Thesis, University of Bristol, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.251550.

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Kyllönen, H. (Heli). "Gelatinases, their tissue inhibitors and p53 in lymphomas." Doctoral thesis, University of Oulu, 2009. http://urn.fi/urn:isbn:9789514291319.

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Abstract Lymphomas are a heterogeneous group of malignancies, which usually have a good prognosis and high cure rates. Lymphomas are sensitive to chemotherapy and radiotherapy, and many patients can be cured even after a relapse, resulting in a need for effective follow-up. However, the cost-benefit ratio of radiological imaging in predicting the forthcoming relapses is poor. Consequently, there is a need for biological prognostic and predictive markers to distinguish patients at the highest risk of relapse at the time of diagnosis or during follow-up. Despite rapid progress in lymphoma treatments, some patients still die from lymphoma. Thus, more data on the basic biological features of lymphomas are also needed. Gelatinases (MMP-2 and MMP-9) and their tissue inhibitors (TIMP-1 and TIMP-2) have been found to play a role in the progression of solid tumours. TP53 is a tumour suppressor gene, the mutations and protein over-expression of which have been demonstrated to be associated with survival in most cancer types. There is also some evidence that these proteins could have prognostic significance in lymphomas as well. In the present study, the tissue expression, plasma concentrations and clinical value of gelatinases and their tissue inhibitors were evaluated in lymphomas. 249 primary tissue samples from patients with Hodgkin, follicular, or diffuse large B-cell lymphoma were analysed for expression of gelatinases and/or their inhibitors using immunohistochemistry. In follicular lymphoma, p53 protein expression was also investigated. The plasma samples of 126 lymphoma patients and a control group of 44 healthy volunteers were collected and studied by ELISA. TIMP-1 expression correlated with bulky tumour and nodular sclerosis subtype of Hodgkin lymphoma. In follicular lymphoma, p53 over-expression was an independent adverse prognostic factor for survival and a predictor of histological transformation. Plasma MMP-2-TIMP-2 complex appeared to be a potential follow-up marker predicting the risk of relapse in lymphoma patients. Plasma levels of the MMP-2-TIMP-2 complex, proMMP-2, TIMP-2 and proMMP-2/TIMP-2 ratio were at abnormal levels both in patients with newly diagnosed lymphoma and those in remission compared to healthy controls. The clinical significance of these markers needs further studies.
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Parkin, Ben. "The role of matrix metalloproteinase-2 and its inhibitors in keratoconus." Thesis, University of Bristol, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.343282.

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Williams, Darren Malfryn. "Investigation of the effects of hypoxia on matrix metalloproteinase and tissue inhibitors of matrix metalloproteinases expression in pancreatic cancer." Thesis, University of Birmingham, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.393836.

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Twitty, Anne. "The expression of tissue inhibitor of metalloproteinase during the early stages of bone graft healing." Thesis, Hong Kong : University of Hong Kong, 2000. http://sunzi.lib.hku.hk/hkuto/record.jsp?B21804023.

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Rauvala, M. (Marita). "Matrix metalloproteinases -2 and -9 and tissue inhibitors of metalloproteinases -1 and -2 in gynaecological cancers." Doctoral thesis, University of Oulu, 2006. http://urn.fi/urn:isbn:951428187X.

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Abstract The invasion of a tumour through tissue limiting basement membranes is the critical step in malignant growth. Gelatinases (MMP-2 and MMP-9) are endopeptidases capable of degrading extracellular and pericellular matrix proteins such as collagen IV, the major component of basement membranes. An over-expression of these gelatinases is generally found in malignant tumours and is linked to impaired prognosis in many cancer types. Tissue inhibitors of metalloproteinases (TIMPs), endogenous regulators of the MMP activity, have recently been introduced as multifunctional proteins, which have paradoxical roles in tumour growth. Little data exists on the clinical significance of the gelatinases and TIMPs in gynaecological cancers. In this study the clinical significance of the gelatinases was studied in endometrial and uterine cervical cancers by using immunohistochemical staining with specific antibodies. In epithelial ovarian cancer (EOC) these enzymes and their TIMPs were studied in the preoperative serum samples using ELISA assay. Additionally, sequential serum measurements were performed during chemotherapy to evaluate them as treatment response indicators. In endometrial cancer, MMP-9 positivity correlated to a poor histological differentiation and an advanced clinical stage. High MMP-2 expression correlated to a poor differentiation, and unfavourable survival in stage I cancers, with mortality rates of 5% and 19% in patients with MMP-2 negative versus intensively MMP-2 positive tumours, respectively. In cervical cancers high MMP-2 expression correlated to an increased mortality risk. High MMP-9 expression was connected to a good differentiation of a tumour. In EOC, a high circulating TIMP-1 value correlated to all the examined aggressive features of EOC, including poor survival. The serum measurements of TIMP-1 were uninformative about response evaluation during chemotherapy but paradoxically, an increase in gelatinases and TIMP-2 seemed to reflect a good response to treatment. In conclusion, the data from this study show that high MMP-2 expression in tumour tissue could be prognostic in endometrial and cervical cancer, and preoperative circulating TIMP-1 could serve as an additional prognostic marker in EOC. Studies with larger patient cohorts would be necessary to further explore the value of these enzymes in clinical practice in gynaecological cancers.
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McCrudden, Raymond. "Regulation of the synthesis of tissue inhibitors of metalloproteinase-1 and -2 by hepatic and pancreatic stellate cells." Thesis, University of Southampton, 2010. https://eprints.soton.ac.uk/372931/.

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Hepatic stellate cells (HSC) play a central role in fibrosis development by production of extracellular matrix and also by secretion of matrix metalloproteinases (MMPs) and Tissue inhibitors of metalloproteinases (TIMPs) including TIMP-2 and MMP-2. TIMP-2 has been shown to interact with Gelatinase A in conjunction with MT1-MMP (MMP-14). TIMP-2 has been traditionally considered to be constitutively expressed. There is some evidence that TIMP-2 expression is slightly enhanced in fibrotic disease and activation in tissue culture. Little is known in terms of TIMP-2 expression in the recently described pancreatic stellate cells (PSC). HSC were cultured on plastic having been isolated from rat and human liver resections. After culture on plastic northern analysis was performed for TIMP-2 mRNA expression. TIMP-2 promoter activity was examined in rat pancreatic stellate cells (PSC) and rat hepatic stellate cells. Early work led to subcloning the promoter into a different vector though subsequent promoter studies were unsuccessful. In vivo work in immunohistochemistry studies suggest there is increased TIMP-2 expression in evaluation of rat pancreas and liver in addition to human liver and pancreas specimens. By ribonuclease protection assay TIMP-2 was noted to be upregulated in human fibrotic liver compared to normal human liver tissue. In conclusion there is some evidence that TIMP-2 regulation may be altered in fibrotic liver states as well as in pancreatic inflammatory disease.
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Titz, Tiago de Oliveira. "Avaliação fenotípica e funcional dos eosinófilos da dermatite atópica do adulto." Universidade de São Paulo, 2015. http://www.teses.usp.br/teses/disponiveis/5/5133/tde-20052015-121525/.

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Introdução: A dermatite atópica (DA) é uma doença cutânea inflamatória de caráter crônico, recidivante, em que o prurido intenso e a xerose cutânea são frequentes. A etiopatogenia da DA é multifatorial, envolvendo fatores genéticos, ambientais e imunológicos. Eosinófilos são leucócitos polimorfonucleares multifuncionais que estão implicados na patogênese de diversos processos inflamatórios, incluindo a DA. Além da produção e secreção de diversas proteínas presentes nos grânulos citoplasmáticos, os eosinófilos também apresentam potencial para secretar metaloproteinases, enzimas proteolíticas que degradam vários componentes da matriz extracelular, e estão presentes em diversos processos fisiológicos e patológicos. Objetivo: Avaliar: 1) o perfil fenotípico dos eosinófilos na dermatite atópica do adulto, através da expressão das moléculas CCR3, CD23, CD38, CD69 e CD62L; 2) o perfil funcional, a partir da secreção de metaloproteinases, inibidores teciduais de metaloproteinases e RANTES por eosinófilos purificados. Métodos: Foram incluídos 41 adultos diagnosticados com DA, de acordo com os critérios de Hanifin & Rajka e 45 controles adultos sadios. A gravidade da doença foi mensurada através do escore de gravidade EASI (Eczema Area and Severity Index). Eosinófilos (LIN 1- CCR3+) do sangue periférico foram analisados para os marcadores CCR3, CD38, CD69, CD23 e CD62L através da citometria de fluxo (LSRFortessa, BD Biosciences) a análise foi realizada com o FlowJo 7.5.6 software. Eosinófilos purificados de indivíduos com DA e indivíduos controles foram estimulados com enterotoxina de Staphylococcus aureus B (SEB) e FSL-1 (agonista de receptores Toll-like 2 e 6), e os sobrenadantes foram coletados para dosagem de metaloproteinases (MMPs), inibidores teciduais de metaloproteinases 1 e 2 (TIMP-1 e TIMP-2) e RANTES por ELISA e por Cytometric bead array. Resultados: Indivíduos com DA apresentaram maior frequência de eosinófilos (LIN1- CCR3+), relacionada à gravidade da doença. Observou-se também, que a frequência de CD62L (L-selectina) e de CD23 (receptor de baixa afinidade para IgE) em eosinófilos (LIN1- CCR3+) diminui em pacientes com DA. Os receptores de ativação precoce (CD69) e tardio (CD38) não mostraram diferença estatística entre os grupos analisados. Os níveis séricos de MMPs e de TIMPs foram similares entre os controles e pacientes. Ao analisarmos a secreção de MMPs e de (TIMPs), a partir de eosinófilos purificados de pacientes com dermatite atópica, observamos diminuição dos níveis basais de TIMP-1 e TIMP-2 e de RANTES. Conclusões: Na DA do adulto, o perfil fenotípico e funcional dos eosinófilos mostrou: perfil de ativação da fase aguda, com expressão aumentada de CCR3; potencial de migração elevado, em decorrência da diminuição da expressão de CD62L; falhas no processo de ativação dos eosinófilos via CD23, bem como, no remodelamento tecidual mediado por TIMP-1 e TIMP-2 e na quimotaxia mediada por RANTES
Introduction: Atopic dermatitis (AD) is an inflammatory, chronic and recurrent skin disease characterized by intense pruritus and xerosis. AD has a complex etiopathogenesis, which involves the influence of genetics, environment, and immunological disorders, among others. Eosinophils are multifunctional polymorphonuclear leukocytes that contribute to the pathogenesis of several inflammatory processes, such as AD. In addition to the production and secretion of diverse proteins of the cytoplasmic granules, eosinophils have also the potential to secrete metalloproteinases (MMPs), proteolytic enzymes with a primary role for degrading several extracellular matrix components, present in distinct physiological and pathological processes. Objective: To evaluate:1) the phenotypic profile of eosinophils in adults with atopic dermatitis through the expression of CCR3, CD23, CD38, CD69 and CD62L molecules; 2) the functional profile through secretion of MMPs, tissue inhibitors of metalloproteinases 1 and 2 ( TIMP-1 and TIMP-2) and RANTES by purified eosinophils. Methods: This work enrolled 41 patients with AD, diagnosed according to Hanifin & Rajka\'s criteria) and 45 healthy controls. Severity of the disease was established utilizing EASI (Eczema Area and Severity Index). Eosinophils (Lineage cocktail 1- CCR3+) from peripheral blood were analyzed for CCR3, CD38, CD69, CD23 and CD62L by flow cytometry (LSRFortessa, BD Biosciences), and analysis was performed using the FlowJo 7.5.6 software. Purified eosinophils were stimulated with Staphylococcus aureus enterotoxin B (SEB) FSL-1 (Toll-like receptor 2/6 agonist), and supernatants were collected for MMPs, TIMPs and RANTES secretion, evaluated by ELISA and cytometric bead array (CBA). Results: Patients with AD have a higher frequency of eosinophils (LIN1- CCR3+), related to disease severity. Moreover, the frequency of CD62L (L-selectin) and CD23 (low-affinity receptor for IgE) in (LIN1- CCR3+) eosinophils was reduced in individuals with AD. CD69 and CD38 (early and late activation receptors) did not show significant difference in the studied groups. Serum levels of MMPs and of TIMP-1 and TIMP-2 were similar in healthy controls and AD patients. When analyzing secretion of MMPs and TIMPs by purified eosinophils from AD individuals, we detected a decrease in baseline levels of TIMP-1, TIMP-2, and reduced RANTES-mediated chemotaxis. Conclusions: Eosinophils in AD exhibit an activation profile of acute phase, with enhanced CCR3 expression, high potential for migration due to reduced expression of CD62, defective activation mechanisms via CD23, altered tissue remodeling process mediated by TIMP-1 and TIMP-2 and reduced RANTES-mediated chemotaxis
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Phillips, Blaine Wesley. "Transcriptional regulation of the tissue inhibitors of metalloproteinases." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape2/PQDD_0027/NQ49530.pdf.

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Groft, Lori Lynne. "Tissue inhibitors of metalloproteinases in human malignant gliomas." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape7/PQDD_0018/MQ48004.pdf.

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Books on the topic "Tissuee inhibitors of metalloproteinase"

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Gupta, Satya Prakash, ed. Matrix Metalloproteinase Inhibitors. Basel: Springer Basel, 2012. http://dx.doi.org/10.1007/978-3-0348-0364-9.

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Viani, Mary Anne. Expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases in the hematopoietic microenvironment. Ottawa: National Library of Canada, 2000.

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Clendeninn, Neil J., and Krzysztof Appelt. Matrix Metalloproteinase Inhibitors in Cancer Therapy. New Jersey: Humana Press, 2000. http://dx.doi.org/10.1385/159259011x.

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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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McElligott, Anthony M. The role of matrix metalloproteinases and their inhibitors, the tissue inhibitors of metalloproteinases, in renal cell carcinoma cell invasion and metastasis. [S.l: The Author], 1999.

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Inhibitors of Metalloproteinases Conference (1996 Banff, Alta.). Tissue inhibitors of metalloproteinases in development and disease: Proceedings of the Inhibitors of Metalloproteinases Conference, Banff, Alberta, Canada, September 25-29, 1996. Edited by Hawkes Susan P, Edwards Dylan R, and Khokha Rama. Australia: Harwood Academic, 2000.

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Gupta, Satya Prakash. Matrix metalloproteinase inhibitors: Specificity of binding and structure-activity relationships. Basel: Springer, 2012.

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J, Saklatvala, Nagase Hideaki, and Salvesen G, eds. Proteases and the regulation of biological processes. London: Portland Press, 2003.

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Reid, Helen M. Tissue inhibitors of matrix metalloproteinases are modulated differently by 12-0-Tetradeconoylphorbol-13-actate (TPA) and 1,1,1-Trichoro-2,2-Bis-(p-Chlorophenyl)-ethane (DDT). [S.l: The Author], 1997.

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Matrix Metalloproteinase Conference (1989 Sandestin Beach, Fla.). Matrix metalloproteinases and inhibitors: Proceedings of the Matrix Metalloproteinase Conference held at Sandestin Beach, FL, September 11-15, 1989. Edited by Birkedal-Hansen Henning. Stuttgart: G. Fischer Verlag, 1992.

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Book chapters on the topic "Tissuee inhibitors of metalloproteinase"

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Purcell, W. Thomas, and Manuel Hidalgo. "Matrix Metalloproteinase Inhibitors in Cancer Therapy." In Proteases in Tissue Remodelling of Lung and Heart, 75–118. Boston, MA: Springer US, 2003. http://dx.doi.org/10.1007/978-1-4419-9082-2_4.

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Nagase, H., K. Suzuki, Y. Itoh, C. C. Kan, M. R. Gehring, W. Huang, and K. Brew. "Involvement of Tissue Inhibitors of Metalloproteinases (TIMPS) During Matrix Metalloproteinase Activation." In Intracellular Protein Catabolism, 23–31. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4613-0335-0_3.

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Alameddine, Hala S. "The Matrix Metalloproteinase and Tissue Inhibitors of Metalloproteinase Balance in Physiological and Pathological Remodeling of Skeletal Muscles." In Proteases in Physiology and Pathology, 49–76. Singapore: Springer Singapore, 2017. http://dx.doi.org/10.1007/978-981-10-2513-6_3.

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Liu, Yiliang Ellie, and Y. Eric Shi. "Naked DNA-Mediated Gene Therapy: Clinical Application of Tissue Inhibitors of Matrix Metalloproteinase." In ACS Symposium Series, 1–13. Washington, DC: American Chemical Society, 2003. http://dx.doi.org/10.1021/bk-2003-0846.ch001.

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Toi, Masakazu, Shinsuke Ishigaki, and Takeshi Tominaga. "Metalloproteinases and tissue inhibitors of metalloproteinases." In Prognostic variables in node-negative and node-positive breast cancer, 203–14. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-5195-9_16.

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Guedez, Liliana, Enrique Zudaire, and William G. Stetler-Stevenson. "Tissue Inhibitors of Metalloproteinases." In Encyclopedia of Cancer, 1–3. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-642-27841-9_5825-2.

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Guedez, Liliana, Enrique Zudaire, and William G. Stetler-Stevenson. "Tissue Inhibitors of Metalloproteinases." In Encyclopedia of Cancer, 4555–57. Berlin, Heidelberg: Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-46875-3_5825.

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Guedez, Liliana, William G. Stetler-Stevenson, and Enrique Zudaire. "Tissue Inhibitors of Metalloproteinases." In Encyclopedia of Cancer, 3703–5. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16483-5_5825.

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Masciantonio, Marcello G., and Sean E. Gill. "Tissue Inhibitor of Metalloproteinase." In Encyclopedia of Signaling Molecules, 5457–65. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101950.

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Masciantonio, Marcello G., and Sean E. Gill. "Tissue Inhibitor of Metalloproteinase." In Encyclopedia of Signaling Molecules, 1–9. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4614-6438-9_101950-1.

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Conference papers on the topic "Tissuee inhibitors of metalloproteinase"

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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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DeClerck, Y. A., R. Bock, and W. E. Laug. "PRODUCTION OF A TISSUE INHIBITOR OF METALLOPROTEINASES BY BOVINE VASCULAR CELLS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644603.

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Tissue Inhibitor of Metalloproteinases (TIMP) plays an important role in collagen turnover in tissue due to its ability to irreversibly inhibit mammalian collagenases. We have investigated the production of such an inhibitor by various cells of bovine vessels including endothelial cells of arterial, venous and capillary origin and arterial smooth muscle cells. While large amounts of collagenase inhibitor (800 mU/106 cells/24 hr) were produced by vascular smooth muscle cells, smaller amounts were detected in* the medium conditioned by either arterial, capillary or venous endothelial cells (90, 1.7 and 1.1 mU/106 cells/24 hr respectively). An inhibitor with a Mr of 28,500 was purified from serum free medium conditioned by bovine smooth muscle cells using molecular sieve followed by heparin sepharose and carboxy-methylcellulose chromatography. It inhibited several vertebrate collagenases but was inactive against bacterial collagenase. This inhibitor was resistant to treatment with acid and heat but sensitive to trypsin and reduction alkylation. It formed with vertebrate collagenase an enzyme-inhibitor complex resistant to organomercurials or trypsin. This inhibitor, therefore, is similar to a collagenase inhibitor produced by human fibroblasts and a tissue inhibitor of metalloproteinases extracted from human amniotic fluid and rabbit bone.The production of TIMP by bovine vascular smooth muscle cells markedly increased during cell proliferation. In addition, when endothelial cells were grown on a preformed layer of smooth muscle cells, the production of TIMP was more than additive suggesting an enhancing effect of endothelial cells on vascular smooth muscle cells.These data suggest that the large amount of TIMP produced by vascular muscle cells may be responsible for the accumulation of collagen characteristically observed in conjunction with smooth muscle cells hyperplasia in atherosclerotic plaques.
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DiTullio, A. E., S. Park, P. A. Torzilli, and C. T. Chen. "Cyclic Compression of Chondrocytes Counteracts Pro-Inflammatory Tissue Remodeling Induced by Interleukin-1." In ASME 2008 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2008. http://dx.doi.org/10.1115/sbc2008-193027.

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Chondrocytes in tissue engineered constructs face challenging environments when first transplanted into a synovial joint, including high levels of compression/shear and pro-inflammatory cytokines. The joint level of interleukin 1 (IL-1) after trauma injury and in a repaired joint is acutely elevated. Matrix remodeling in tissue engineered constructs can be easily affected by the elevation and activation of aggrecanases (ADAMTS-4 and ADAMTS-5) and matrix metalloproteinases (MMPs) [2–4, 7–9, 11]. Several recent studies suggest that tensile loading and unconfined compression of chondrocytes has some anti-inflammatory effects against interleukin 1 (IL-1) by the downregulation of COX-2 and iNOS genes [1, 5, 6]. However, the role of loading in tissue repair at physiological levels is not clear. The objective of this study was to determine the effect of cyclic confined compression on the gene expression of MMPs and tissue inhibitors of metalloproteinases (TIMPs) in agarose-embedded chondrocytes in the presence of interleukin 1 (IL-1).
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Myh, Etriyel, Eryati Darwin, Eliza Nasrul, and Nur Rasyid. "The Role of Matrix Metalloproteinase-1 and Tissue Inhibitory Matrix Metalloproteinases-3 in the Case of Bladder Neck Contracture Post Transurethral Resection of Prostate." In Proceedings of the 1st EAI International Conference on Medical And Health Research, ICoMHER November 13-14th 2018, Padang, West Sumatera, Indonesia. EAI, 2019. http://dx.doi.org/10.4108/eai.13-11-2018.2283594.

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Barton, A., I. Richter, T. Ahrens, A. Alalwani, S. Lilge, K. Purschke, R. Merle, D. Barnewitz, and H. Gehlen. "Evaluation of matrix-metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) as biomarkers for sepsis and endotoxemia in equine colic." In 29. Jahrestagung der FG „Innere Medizin und klinische Labordiagnostik“ der DVG (InnLab) – Teil 2: Poster. Georg Thieme Verlag KG, 2021. http://dx.doi.org/10.1055/s-0041-1723882.

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Edwards, Alexander J. P., Murali Shyamsundar, Joseph S. Elborn, Cecilia M. O'Kane, and Danny F. McAuley. "Matrix Metalloproteinases And Their Tissue Inhibitors In In-Vitro Models Of Acute Lung Injury." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a2724.

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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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Muyal, Jai P., Claudia Wild, Alexander Plagens, Claus F. Vogelmeier, Heinz Fehrenbach, and Carola Seifart. "Effect Of Palifermin On MRNA Level Of Inflammatory Mediators, Matrix Metalloproteinases And Tissue Inhibitor Of Metalloproteinases In Rat Model Of Emphysema." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a4427.

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Wilop, Stefan, Edgar Jost, Claudia Schubert, James G. Herman, Tim H. Brümmendorf, and Oliver Galm. "Abstract 3142: Hypermethylation of the tissue inhibitor of metalloproteinases-2 gene in multiple myeloma." 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.am2012-3142.

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Uysal, Pelin, and Hafize Uzun. "Relationship between circulating serpina 3g, activity of matrix metalloproteinase-9 and tissue inhibitor of metalloproteinase-1, 2 with chronic obstructive pulmonary disease severity." In ERS International Congress 2018 abstracts. European Respiratory Society, 2018. http://dx.doi.org/10.1183/13993003.congress-2018.pa961.

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Reports on the topic "Tissuee inhibitors of metalloproteinase"

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Shi, Yuenian E. Novel Tissue Inhibitor of Metalloproteinase, TIMP-4, in Human Breast Cancer Growth and Metastasis. Fort Belvoir, VA: Defense Technical Information Center, October 2000. http://dx.doi.org/10.21236/ada393175.

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Shi, Yuenian. Novel Tissue Inhibitor of Metalloproteinase, TIMP-4, in Human Breast Cancer Growth and Metastasis. Fort Belvoir, VA: Defense Technical Information Center, October 1999. http://dx.doi.org/10.21236/ada383090.

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