TY - JOUR. T1 - Tissue inhibitor of metalloproteinases-3 promoter methylation is an independent prognostic factor for bladder cancer. AU - Hoque, Mohammad Obaidul. AU - Begum, Shahnaz. AU - Brait, Mariana. AU - Jeronimo, Carmen. AU - Zahurak, Marianna. AU - Ostrow, Kimberly Laskie. AU - Rosenbaum, Eli. AU - Trock, Bruce. AU - Westra, William H.. AU - Schoenberg, Mark. AU - Goodman, Steven N.. AU - Sidransky, David. PY - 2008/2. Y1 - 2008/2. N2 - Purpose: TIMP-3 (tissue inhibitor of metalloproteinases-3) is 1 of 4 members of a family of proteins that were originally classified according to their ability to inhibit matrix metalloproteinases. We analyzed TIMP-3 methylation in 175 urine sediment DNA samples from patients with bladder cancer with well characterized clinicopathological parameters, including patient outcome. Materials and Methods: We examined urine sediment DNA for aberrant methylation of 9 genes, including TIMP-3, by quantitative fluorogenic real-time polymerase chain reaction. ...
To the Editor:. It was with great interest that I read the article by Tuomainen et al1 recently published in this journal on the association of matrix metalloproteinase (MMP)-8 and tissue inhibitor of MMP-1 (TIMP-1) with cardiovascular diseases. The authors measured both analytes in serum and concluded from their results that serum MMP-8 and the ratio of MMP-8 to TIMP-1 were useful biomarkers with prognostic and diagnostic significances in men with cardiovascular disease, especially in those with prevalent or subclinical arteriosclerosis.1 Although I am not experienced in this clinical field, I believe it might be meaningful to make the readership of this journal aware of an important issue that was obviously not considered by Tuomainen et al in their study design. It refers to the influence of blood sample processing as essential precondition for the correct determination of circulating MMPs and TIMPs in peripheral blood. The effect of the type of blood sample, either collected as serum with or ...
A member of the family of TISSUE INHIBITOR OF METALLOPROTEINASES. It is a 21-kDa nonglycosylated protein found in tissue fluid and is secreted as a complex with progelatinase A by human fibroblast and uncomplexed from alveolar macrophages. An overexpression of TIMP-2 has been shown to inhibit invasive and metastatic activity of tumor cells and decrease tumor growth in vivo.
Research Topics, Genomes and Genes, Research Grants, Scientific Experts, Publications, Species about tissue inhibitor of metalloproteinase 2
TY - JOUR. T1 - Cellular distribution of tissue inhibitor of metalloproteimases-1 and-2 transcripts in human hepatocellalar carunoma(共著). AU - Ashida, Kouzou. PY - 1995. Y1 - 1995. M3 - Article. VL - 22. SP - 192. EP - 192. JO - HEPATOLOGY. JF - HEPATOLOGY. IS - 4. ER - ...
Catalog No :RS01Ab0134Organism- HumanClonality :MonoclonalHost :MouseConcentration :500ug/mlApplication :WB, ICC, IHC-P, IHC-F, ELISA Immunoglobulin Type: IgGPurification: Affinity ChromatographyConjugate: No Conjugate IMMUNOGEN INFORMATIONImmunogen: Recombinant TIMP1 (Thr25~Ala207) expressed in E.coli.ANTIBODY SPECIFI
Balanced expression of proteases and their inhibitors is one prerequisite of tissue homeostasis. Metastatic spread of tumor cells through the organism depends on proteolytic activity and is the death determinant for cancer patients. Paradoxically, increased expression of tissue inhibitor of metalloproteinases-1 (TIMP-1), a natural inhibitor of several endometalloproteinases, including matrix metalloproteinases and a disintegrin and metalloproteinase-10 (ADAM-10), in cancer patients is negatively correlated with their survival, although TIMP-1 itself inhibits invasion of some tumor cells. Here, we show that elevated stromal expression of TIMP-1 promotes liver metastasis in two independent tumor models by inducing the hepatocyte growth factor (HGF) signaling pathway and expression of several metastasis-associated genes, including HGF and HGF-activating proteases, in the liver. We also found in an in vitro assay that suppression of ADAM-10 is in principle able to prevent shedding of cMet, which may be one
The protocol describes a novel, rapid, and no-wash one-step immunoassay for highly sensitive and direct detection of the complexes between matrix metalloproteinases (MMPs) and their tissue inhibitor of metalloproteinases (TIMPs) based on AlphaLISA® technology. We describe two procedures: (i) one approach is used to analyze MMP-9-TIMP-1 interactions using recombinant human MMP-9 with its corresponding recombinant human TIMP-1 inhibitor and (ii) the second approach is used to analyze native or endogenous MMP-9-TIMP-1 protein interactions in samples of human plasma. Evaluating native MMP-9-TIMP-1 complexes using this approach avoids the use of indirect calculations of the MMP-9/TIMP-1 ratio for which independent MMP-9 and TIMP-1 quantifications by two conventional ELISAs are needed. The MMP-9-TIMP-1 AlphaLISA® assay is quick, highly simplified, and cost-effective and can be completed in less than 3 h. Moreover, the assay has great potential for use in basic and preclinical research as it allows direct
Badr, A. M., Interleukin-6 induces secretion of tissue inhibitors of metalloproteinases by breast carcinoma cells, Pakistan Journal of Pharmaceutical Sciences, vol. 29, issue 6, pp. 1969-1975, 2016 ...
MMP-2, MMP-9 and their inhibitors TIMP-2 and TIMP-1 production by human monocytes in vitro in the presence of different forms of hydroxyapatite particles.. . Biblioteca virtual para leer y descargar libros, documentos, trabajos y tesis universitarias en PDF. Material universiario, documentación y tareas realizadas por universitarios en nuestra biblioteca. Para descargar gratis y para leer online.
Murine tissue inhibitor of metalloproteinases-1 (mTIMP-1) was expressed in baculovirus-infected insect cells (Sf9). The protein secreted into the culture medium was purified to homogeneity by means of heparin-Sepharose CL-6B and FPLC. The purified protein showed metalloproteinase-inhibitory activity in two independent assays: reverse zymography and inhibition of collagenase activity. Digestion of the recombinant TIMP-1 with peptide-N-glycanaseF revealed that both N-glycosylation sites are used. I-125-mTIMP-1 intraveneously injected into a male Sprague Dawley rat disappeared within 2 min from the circulation. 5 min after injection more than 50% of the I-125-mTIMP-1 were found in the liver and 20% in the kidneys. At later times, trichloroacetic-acid-soluble material accumulated in the intestinal tract ...
Purpose: While antiretroviral therapy (ART) has improved the quality of life and survival of HIV-1-infected patients, HIV-1-associated neurocognitive disorders (HAND) remain a major problem in over 30% of cases. All forms of HAND are associated with CNS inflammation. Astrocytes, the principal type of glial cells, are involved in signaling, homeostasis, and repair during CNS pathology. Some astrocytes become non-productively infected by HIV-1. The balance between matrix metalloproteinases (MMP) and their inhibitors must be tightly regulated during CNS inflammation. In the brain, tissue inhibitor of MMPs (TIMP)-1 protects human neurons from HIV-1-induced apoptosis and is mainly produced by astrocytes. Further, astrocyte TIMP-1 is differentially regulated during acute and chronic IL-1β-activation. However, the direct or indirect effects of astrocyte HIV-1 protein expression on TIMP-1 regulation are not well studied. Here, we investigated downstream effects of HIV-1 Tat and gp120 expression in astrocytes
A tissue inhibitor of metalloproteinases (TIMP)-1 was isolated from human polymorphonuclear leukocytes (PMNL) in a complex with latent 95-kDa gelatinase (matrixmetalloproteinase, MMP-9). It was separated from the enzyme by gel fitration in the presence of SDS. Using a competitive ELISA procedure, we determined that 10% of the isolated gelatinase was complexed with TIMP-1. The presence of the inhibitor in isolated PMNL could also be demonstrated by indirect immunofluorescence using a specific antibody against TIMP-1. Cellular mRNA was isolated from PMNL, which were highly purified by separation via formylMet-Leu-Pro-stimulated chemotactic migration in a Boyden chamber. Using reverse-transcription PCR and Northern blotting, TIMP-1 mRNA was shown to be present in PMNL, suggesting that these cells are also capable of synthesizing TIMP-1 ...
Cellular pathways for induction of programmed cell death (PCD) have been identified, but little is known about specific extracellular matrix processes that may affect apoptosis along those pathways. In this study, a series of Burkitts lymphoma (BL) cell lines were assayed for their expression of tissue inhibitor of metalloproteinases (TIMP)-1. Results indicate that TIMP-1-positive BL lines show resistance to cold-shock-induced apoptosis. Furthermore, recombinant TIMP-1, but not TIMP-2 or a synthetic metalloproteinase inhibitor (BB-94), confers resistance to apoptosis induced by both CD95-dependent and -independent (cold shock, serum deprivation, and gamma-radiation) pathways in TIMP-1-negative BL lines. TIMP-1 suppression of PCD is not due to metalloproteinase inhibition, as reduction and alkylation of the TIMP-1 did not abolish this activity. Retroviral induction of TIMP-1 not only resulted in cell survival but also in continued DNA synthesis for up to 5 d in the absence of serum, while ...
The simplest interpretation of our in vitro studies is that increased expression of the MMP-9 proenzyme leads to the formation of active enzyme, which, in turn, degrades type IV collagen, leading to amnion cell apoptosis. Alternative interpretations include the possibility that the increased proMMP-9 sequestered endogenous tissue inhibitors of me-talloproteinases, leading to increased activities of […] ...
Based on automated MP annotations supported by experiments on knockout mouse models. Click on icons to go to all Timp3 data for that phenotype. ...
IntroductionThe tissue inhibitors of metalloproteinases (TIMPs) are naturally occurring proteins that specifically inhibit matrix metalloproteinases…
Results By 1 year 103 patients had died and 173 patients had died or been readmitted with HF. MMP-3 was significantly greater in males (p , 0.001), those with hypertension (p , 0.01) and with a past history of chronic HF (p = 0.01) and chronic kidney disease (CKD) (p , 0.001). MMP-3 was significantly correlated with age (p , 0.001) while being inversely correlated with eGFR (p , 0.001) and heart rate (p , 0.008). MMP-3 was significantly greater in patients with a LVEF , 40% compared with those with EF , 40% (p = 0.017). MMP-3 levels were significantly greater in the 108 patients who died compared to those who did not [median = 29.7 [19. to 41.1] vs. 18.9 [11.8 to 30.7] pg/ml, p , 0.001) as well as in those with the combined endpoint compared to those without (26.1 [16.7 to 36.4] vs. 17.9 [11.4 to 31.3] pg/ml, p , 0.001). In Kaplan-Meier analysis, patients with above median MMP-3 levels were significantly more likely to experience the endpoint (p , 0.001) compared to those who did not.. Discharge ...
Effect of interleukin (IL)-17A and IL-17E on the production of matrix metalloproteinase (MMP)-3, MMP-12, and tissue inhibitor of metalloproteinase (TIMP)-1 by i
The active forms of all of the matrix metalloproteinases (MMPs) are inhibited by a family of specific inhibitors, the tissue inhibitors of metalloproteinases (TIMPs). Inhibition represents a major level of control of MMP activity. A detailed knowledge of the mechanisms controlling TIMP gene expression is therefore important. We have isolated a genomic clone of the human TIMP-1 gene. A 3 kbp XbaI fragment has been sequenced; this fragment contains 1718 bp 5′ flanking sequences, exon 1, a 929 bp intron 1 and part of exon 2. Computer analysis reveals 10 consensus sequences for Sp1, six for activating protein 1 (AP-1), six for polyoma enhancer A3 (PEA3), 12 for AP-2 and five CCAAT boxes. The region hybridizing with a murine TIMP-1 promoter fragment has been subcloned and analysed further. RNase protection identifies six transcription start points, making exon 1 up to 48 bp in length. Transient transfection of promoter-chloramphenicol O-acetyltransferase reporter constructs into primary human ...
Chemically and conformationally authentic active domain of human tissue inhibitor of metalloproteinases-2 refolded from bacterial inclusion ...
In the present study, we identified, for the first time, the adiponectin-inducible antiinflammatory molecule, IL-10. Adiponectin rapidly upregulated IL-10 and subsequently increased TIMP-1 levels in HMMs. This effect of adiponectin is specific to HMMs among vascular component cells. It is generally accepted that MMPs and TIMPs play a crucial role in arteriosclerosis and plaque disruptions.1 The balance between MMPs and TIMPs determines the actual metalloproteinase activities and controls the extracellular matrix degradation. We focused on MMP-9 and TIMP-1 because they have been dominantly secreted from HMMs. In this study, adiponectin selectively increased the expression of TIMP-1 in both mRNA and protein levels, whereas the mRNA, protein levels, and activities of MMP-9 were not changed in HMMs.. We have reported that adiponectin suppressed stimulated vascular cellular response in vitro, and overexpression of adiponectin with recombinant adenovirus suppressed the development of atherosclerosis ...
Aneurysms are characterized by dilation, i.e. expansion and thinning of all the arterial wall layers, which is accompanied by remodeling of the connective tissue. Genes involved in the regulation of tissue remodeling are therefore candidate genes. We analyzed TIMP1 and TIMP2 coding sequences in 12 i …
Name of the Test: Matrix Metalloproteinase- 2 (MMP-2) Alias names: Gelatinase-A Clinical Research applications: Matrix metalloproteinases
MMPs and TIMPs grouped according to the MFI (low MFI: Goutallier score 0-1 (n = 10); high MFI: Goutallier score 2-4 (n = 20)). qRT-PCR was performed to anal
APOC4 Antibody 16530-1-AP has been identified with IF, WB, ELISA. 16530-1-AP detected 17 kDa band in human plasma tissue with 1:200-1:1000 dilution...
Our secondary aims are: (1) To explore whether plasma MMP-9 levels can be used as a marker for MMP-9 inhibition in the vascular malformation lesional ...
PURPOSE: To test if recombinant tissue inhibitor of metalloproteinases (TIMP-1) was effective in reducing corneal ulceration after alkali injury to the rabbit cornea. The effect of TIMP-1 was compared with that of a proven synthetic metalloproteinase inhibitor. METHODS: After a defined alkali injury to the rabbit cornea, a topical treatment regimen was followed for 24 days; one group was treated with vehicle only, a second group with recombinant TIMP-1, and a third group with the synthetic metalloproteinase inhibitor. Corneas were scored for ulceration during the 24-day period and the scores for the three groups were compared. RESULTS: The incidence and progression of ulceration and perforation, in the alkali-burned corneas receiving treatment with recombinant TIMP-1 or the synthetic inhibitor, were significantly less than in corneas receiving vehicle treatment alone. CONCLUSION: Recombinant TIMP-1 is as effective as a proven synthetic inhibitor in ameliorating corneal ulceration and perforation ...
Tissue inhibitor of metalloproteinase-3 (TIMP-3) is a dual inhibitor of the matrix metalloproteinases (MMPs) and some adamalysins, two families of extracellular and cell surface metalloproteinases that function in extracellular matrix turnover and the shedding of cell surface proteins. The mechanism of inhibition of MMPs by TIMPs has been well characterized, and since the catalytic domains of MMPs and adamalysins are homologous, it was assumed that the interaction of TIMP-3 with adamalysins is closely similar. Here we report that the inhibition of the extracellular region of ADAM-17 (tumor necrosis factor alpha-converting enzyme (TACE)) by the inhibitory domain of TIMP-3 (N-TIMP-3) shows positive cooperativity. Also, mutations in the core of the MMP interaction surface of N-TIMP-3 dramatically reduce the binding affinity for MMPs but have little effect on the inhibitory activity for TACE. These results suggest that the mechanism of inhibition of ADAM-17 by TIMP-3 may be distinct from that for MMPs. The
Aim: To compare serum level of matrix metalloproteinase 3 (MMP3) and tissue inhibitor metallo-proteinase 1 (TIMP1) in vascular dementia patients and healthy control subjects. Methods: A case control study was carried out in Ain Shams University hospital, Cairo, Egypt. 32 cases with vascular dementia were collected and classified into 2 subgroups; vascular dementia of multiinfarct type (VDMI) 14 patients, and vascular dementia of subcortical type (VDSC) 18 subjects. 23 cases with normal cognitive functions were collected as control group. Cases were subjected to comprehensive geriatric assessment, neurological examination, neuropsychological testing and brain CT scan. Blood sample was collected to analyze serum level of matrix metalloproteinase 3 (MMP3) and tissue inhibitor metalloproteinase 1 (TIMP1). Results: Mean serum level of TIMP1 (20.85 × 103 picogram/ml) was significantly lower than mean serum level of TIMP1 in control group (27.69 × 103 picogram/ml) (p = 0.018). The same finding was also
Tumor necrosis factor-alpha is released from cells by a proteolytic cleavage. Previous work suggested that a specific, non-matrix metalloproteinase carries out this cleavage, but matrix metalloproteinases have also been implicated. In this paper, we report that none of the matrix metalloproteinases tested cleaved peptide substrates as specifically as the non-matrix metalloproteinase. A matrix metalloproteinase did process tumor necrosis factor-alpha extracted from COS cells, but neither tissue inhibitor of metalloproteinases-1 nor -2 blocked tumor necrosis factor-alpha processing by human monocytes. Moreover, tissue inhibitor of metalloproteinases-1 had at most a partial effect on the in vivo release of the cytokine in mice. We conclude that a non-matrix metalloproteinase is the major physiological tumor necrosis factor-alpha convertase.
Tissue inhibitors of metalloproteinases (TIMPs) inhibit matrix metalloproteinases (MMPs) by forming a 1:1 stoichiometric complex, but the inhibition mechanism of these inhibitors is not known. Here we have investigated the reactive site of TIMP-1 by its proteinase susceptibility before and after forming a complex with MMP-3 (stromelysin 1). When TIMP-1 was allowed to react with human neutrophil elastase, its inhibitory activity was destroyed. This resulted from cleavage of the Val69-Cys70 bond. However, cleavage of this bond by neutrophil elastase was prevented when TIMP-1 formed a complex with the catalytic domain of MMP-3, and full TIMP-1 activity was restored after dissociation of the complex at pH 3.0 in the presence of EDTA. These results indicate that the region around Val69 closely associates with an active MMP. The three-dimensional structure of the N-terminal domain of TIMP-2 elucidated by NMR studies [Williamson, Martorell, Carr, Murphy, Docherty, Freedman and Feeney (1994) ...
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1. Dickstein K, Cohen-Solal A, Filippatos G, McMurray JJ, Ponikowski P, Poole-Wilson PA. et al. ESC Guidelines for the diagnosis and treatment of acute and chronic heart failure 2008: the Task Force for the Diagnosis and Treatment of Acute and Chronic Heart Failure 2008 of the European Society of Cardiology. Developed in collaboration with the Heart Failure Association of the ESC (HFA) and endorsed by the European Society of Intensive Care Medicine (ESICM). Eur Heart J. 2008;29:2388-442 2. Graham HK, Horn M, Trafford AW. Extracellular matrix profiles in the progression to heart failure. European Young Physiologists Symposium Keynote Lecture-Bratislava 2007. Acta Physiol (Oxf). 2008;194:3-21 3. Yamazaki T, Lee JD, Shimizu H, Uzui H, Ueda T. Circulating matrix metalloproteinase-2 is elevated in patients with congestive heart failure. Eur J Heart Fail. 2004;6:41-5 4. George J, Patal S, Wexler D, Roth A, Sheps D, Keren G. Circulating matrix metalloproteinase-2 but not matrix metalloproteinase-3, ...
PubMed journal article Overexpression of matrix metalloproteinase-9 (MMP-9) rescues insulin-mediated impairment in the 5XFAD model of Alzheimers diseas were found in PRIME PubMed. Download Prime PubMed App to iPhone or iPad.
TIMP1, 0.1 mg. Tissue Inhibitors of Metalloproteinases (TIMPs) inhibit the proteolytic invasiveness of tumor cells and normal placental trophoblast cells.
TIMP1, 0.1 mg. Tissue Inhibitors of Metalloproteinases (TIMPs) inhibit the proteolytic invasiveness of tumor cells and normal placental trophoblast cells.
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Thermo Scientific™ Sino Biological™ TIMP1 Recombinant Human Protein 5 x 5ug; 21kDa Thermo Scientific™ Sino Biological™ TIMP1...
AlphaLISA no-wash assay kit for detection and quantitation of mouse Matrix Metalloproteinase-9 (MMP9) in serum, buffered solution or cell culture medium.
Elena Vladareanu da voce tuturor vocilor care soptesc pe la colturi, dar nu vorbesc despre propria conditie, da o voce, in mod radical, frustrarii, furiei si fricilor unor artisti care nu mai au timp sa se ocupe de arta lor, fiind confiscati de stiinta supravietuirii, captivi in ecuatia bani/munca/timp liber. O voce plasata in afara metaforei si a iluziei.
Prediction on the Inhibition Ratio of Pyrrolidine Derivatives on Matrix Metalloproteinase Based on Gene Expression Programming. . Biblioteca virtual para leer y descargar libros, documentos, trabajos y tesis universitarias en PDF. Material universiario, documentación y tareas realizadas por universitarios en nuestra biblioteca. Para descargar gratis y para leer online.
Title: Matrix Metalloproteinase-9 and Airway Remodeling in Asthma. VOLUME: 4 ISSUE: 2. Author(s):Hiroyuki Ohbayashi and Kaoru Shimokata. Affiliation:Department of Internal Medicine, Tohno-Kousei Hospital, 76-1, Toki-cho, Mizunami City, Gifu Pref. 509-6101, Japan.. Keywords:matrix metalloproteinase, asthma, the extracellular matrix, tissue inhibitor of metalloproteinase. Abstract: Airway remodeling is a major change responsible for irreversible asthmatic airflow restriction. The Th-2 cytokines-dominant eosinophilic inflammatory mechanism cannot fully explain the progressive subepithelial fibrosis and structural changes in the extracellular matrix (ECM). Matrix metalloproteinases (MMPs) are the key enzymes responsible for ECM degradation. MMPs are normally produced and secreted under the tight regulation of, at least, 3 different levels: the gene transcriptional level, the activation of the latent form of enzyme, and the inactivation by specific endogenous inhibitors. In asthmatic condition, as ...
Tissue inhibitors of metalloproteinases (TIMPs) are a family of closely related proteins that inhibit matrix metalloproteinases (MMPs). In the central nervous system (CNS), TIMPs 2, 3, and 4 are constitutively expressed at high levels, whereas TIMP1 can be induced by various stimuli. Here, we studied the effects of constitutive expression of TIMP1 in the CNS in transgenic mice. Transgene expression started prenatally and persisted throughout lifetime at high levels. Since MMP activity has been implicated in CNS development, in proper function of the adult CNS, and in inflammatory disorders, we investigated Timp1-induced CNS alterations. Despite sufficient MMP inhibition, high expressor transgenic mice had a normal phenotype. The absence of compensatory up-regulation of MMP genes in the CNS of Timp1 transgenic mice indicates that development, learning, and memory functions do not require the entire MMP arsenal. To elucidate the effects of strong Timp1 expression in CNS inflammation, we induced ...
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History The upregulation of matrix metalloproteinase-1 (MMP-1) continues to be proven correlated with lymph node metastasis of nasopharyngeal carcinoma (NPC) as the activation of protease-activated receptor-1 (PAR-1) mediates proliferation and invasion of NPC cells. in 190 (71.43%) and 182 (68.42%) from the 266 NPC sufferers. Furthermore the mixed MMP-1 and PAR-1 appearance was significantly connected with advanced T-stage (= 0.01) advanced clinical stage (= 0.002) positive recurrence (= 0.01) and metastatic position (= 0.01) of NPC. Furthermore the overall success in NPC sufferers MAP3K8 with MMP-1 and PAR-1 dual overexpression was considerably shorter than in people that have dual low appearance (< 0.001). Furthermore the multivariate analyses indicated the fact that mixed MMP-1 and PAR-1 overexpression was an unbiased prognostic aspect for overall success (= 0.001) in NPC sufferers however the upregulation of MMP-1 and PAR-1 alone is at each case no independent prognostic aspect because of ...
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. The encoded preproprotein is proteolytically processed to generate the mature enzyme. This enzyme may degrade collagen type IV, fibronectin, fibrinogen, and beta-casein, and activate matrix metalloproteinase-9 by cleavage. The protein differs from most MMP family members in that it lacks a conserved C-terminal protein domain. The encoded protein may promote cell invasion in multiple human cancers. [provided by RefSeq, May 2016 ...
Experimental evidence suggests that matrix metalloproteinase-13 (MMP-13) protein may promote breast tumor progression. Bin Zhang, Xuchen Cao, Yanxue Liu, W
Vilen, S.T., Salo, T., Sorsa, T. and Nyberg, P. (2013) Fluctuating Roles of Matrix Metalloproteinase-9 in Oral Squamous Cell Carcinoma. The Scientific World Journal, 2013, Article ID 920595.
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