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Prions are the cause of neurodegenerative disease in humans and other mammals. The structural conversion of the prion protein (PrP) from a normal cellular protein (PrPC) to a protease-resistant isoform (PrPSc) is thought to relate to Cu2+ binding to histidine residues. In this study, we focused on the membrane-type matrix metalloproteinases (MT-MMPs) such as MT1-MMP and MT3-MMP, which are expressed in the brain as PrPC-degrading proteases. We synthesized 21 prion fragment peptides. Each purified peptide was individually incubated with recombinant MT1-MMP or MT3-MMP in the presence or absence of Cu2+ and the cleavage sites determined by LC-ESI-MS analysis. Recombinant MMP-7 and human serum (HS) were also tested as control. hPrP61-90, from the octapeptide-repeat region, was cleaved by HS but not by the MMPs tested here. On the other hand, hPrP92-168 from the central region was cleaved by MT1-MMP and MT3-MMP at various sites. These cleavages were inhibited by treatment with Cu2+. The C-terminal peptides
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The membrane-type matrix metalloproteinases (MT-MMPs) are a subclass of the matrix metalloproteinase (MMP) family which uniquely possess a C-terminal transmembrane domain and are initiators of an activation cascade for progelatinase A (MMP-2). Recent studies have shown that they can also efficiently directly degrade a number of matrix macromolecules. We now show that cells expressing MT1-MMP on their cell surfaces cause subjacent proteolysis of a gelatin film and that this proteolysis is inhibited by TIMP-2 but not by TIMP-1. These data indicate that expression of MT1-MMP on the cell surface may lead to both progelatinase A activation and extracellular matrix degradation.
In spite of ample experimental and clinical evidence implicating various MMPs in tumor progression, the synthetic MMP inhibitors developed in the late 1980s and early 1990s were disappointingly ineffective in human studies. Several reasons can explain the failure of these inhibitors in clinical trials (6, 7, 19, 20). These drugs inhibited most, if not all, MMPs. This lack of specificity had two important consequences. It is now known that some MMPs, such as MMP-8 and MMP-12, have a protective effect from cancer (36-38); therefore, their inhibition favors tumor progression. In addition, MMPs mediate the physiologic turnover of the ECM in the whole organism; inhibiting this process produced adverse effects such as fibrosis, musculoskeletal pain and joint inflammation (musculoskeletal syndrome), observed with essentially all the MMP inhibitors tested (21). These effects were reversible, but led to lowered and possibly suboptimal doses in subsequent trials (20, 21). Importantly, in all the clinical ...
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TY - JOUR. T1 - Role of membrane-type matrix metalloproteinase 1 (MT-1-MMP), MMP-2, and its inhibitor in nephrogenesis. AU - Kanwar, Yashpal S.. AU - Ota, Kosuke. AU - Yang, Qiwei. AU - Wada, Jun. AU - Kashihara, Naoki. AU - Tian, Yufeng. AU - Wallner, Elisabeth I.. PY - 1999/12. Y1 - 1999/12. N2 - Extracellular matrix (ECM) proteins, their integrin receptors, and matrix metalloproteinases (MMPs), the ECM- degrading enzymes, are believed to be involved in various biological processes, including embryogenesis. In the present study, we investigated the role of membrane type MMP, MT-1-MMP, an activator pro-MMP-2, in metanephric development. Also, its relationship with MMP-2 and its inhibitor, TIMP-2, was studied. Since mRNAs of MT-1-MMP and MMP-2 are respectively expressed in the ureteric bud epithelia and mesenchyme, they are ideally suited for juxtacrine/paracrine interactions during renal development. Northern blot analyses revealed a single ~4.5-kb mRNA transcript of MT-1-MMP, and its ...
Among the five membrane-type matrix metalloproteinases (MT-MMPs), MT1-, MT2-, MT3-, and MT5-MMPs have about a 20-amino acid cytoplasmic tail following the transmembrane domain. In contrast, a putative transmembrane domain of MT4-MMP locates at the very C-terminal end, and the expected cytoplasmic tail is very short or nonexistent. Such sequences often act as a glycosylphosphatidylinositol (GPI) anchoring signal rather than as a transmembrane domain. We thus examined the possibility that MT4-MMP is a GPI-anchored proteinase. Our results showed that [(3)H]ethanolamine, which can be incorporated into the GPI unit, specifically labeled the MT4-MMP C-terminal end in a sequence-dependent manner. In addition, phosphatidylinositol-specific phospholipase C treatment released the MT4-MMP from the surface of transfected cells. These results indicate that MT4-MMP is the first GPI-anchored proteinase in the MMP family. During cultivation of the transfected cells, MT4-MMP appeared to be shed from the cell surface by
Matrix metalloproteinases (MMPs) are a group of structurally related proteolytic enzymes containing a zinc ion in the active site. They are secreted from cells or bound to the plasma membrane and hydrolyze extracellular matrix (ECM) and cell surface-bound molecules. They therefore play key roles in morphogenesis, wound healing, tissue repair and remodeling in diseases such as cancer and arthritis. Although the cell anchored membrane-type MMPs (MT-MMPs) function pericellularly, the secreted MMPs have been considered to act within the ECM, away from the cells from which they are synthesized. However, recent studies have shown that secreted MMPs bind to specific cell surface receptors, membrane-anchored proteins or cell-associated ECM molecules and function pericellularly at focussed locations. This minireview describes examples of cell surface and pericellular partners of MMPs, as well as how they alter enzyme function and cellular behaviour.
Principal Investigator:ITOH Yoshifumi, Project Period (FY):1998 - 1999, Research Category:Grant-in-Aid for Scientific Research (C), Section:一般, Research Field:Functional biochemistry
BioreclamationIVT provides various types of matrices from human and animal species. The human samples are collected from consented donors at IRB approved facilities located in the United States. The animal samples are collected at facilities located in the United States. Both collections follow BioreclamationIVT Standard Operating Procedures. This allows us to customize every order according to your exact specifications, while maintaining the highest level of product quality. The list of matrices that is provided is not all inclusive. Our large network of sites provides us with limitless options when procuring other fluid type matrices. Amniotic Fluid Feces Sputum Aqueous Humor Gastric Fluid Synovial Fluid (lavage) Bile Hair Tears Bone Marrow Nasal Swabs Throat Swabs Breast Milk Nasal Swabs Urine Bronchial Lavage Saliva Vaginal Fluid Cerebrospinal Fluid Semen Vitreous Humor
Matrix Metalloproteinase-2 (MMP-2) is secreted as a zymogen, the activation of which has been associated with metastatic progression in human breast cancer (HBC). Concanavalin A (Con A) has been found to induce activation of MMP-2 in invasive HBC cell lines. Con A effects on the expression of mRNA for membrane-type matrix metalloproteinase (MT-MMP), a newly described cell surface-associated MMP, showed a close temporal correlation with induction of MMP-2 activation. It is surprising that MT-MMP mRNA is constitutively present in the uninduced MDA-MB-231 cell, despite a lack of MMP-2 activation. We have used actinomycin D to demonstrate a partial requirement for de novo gene expression in the induction of MMP-2 activation by Con A in MDA-MB-231 HBC cells. Furthermore, this transcriptional response to Con A appeared to require the continued presence of Con A for its manifestation. The nontranscriptional component of the Con A induction manifests rapidly, is quite substantial, and persists strongly ...
TY - JOUR. T1 - Cell surface binding and activation of gelatinase A induced by expression of membrane-type-1-matrix metalloproteinase (MT1-MMP). AU - Sato, Hiroshi. AU - Takino, Takahisa. AU - Kinoshita, Takeshi. AU - Imai, Kazushi. AU - Okada, Yasunori. AU - Stetler Stevenson, William G.. AU - Seiki, Motoharu. PY - 1996/5/6. Y1 - 1996/5/6. N2 - Gelatinase A is secreted as a proenzyme (progelatinase A) which is activated and bound on the surface of tumor and normal cells. We have reported that the expression of a membrane-type-1-matrix metalloproteinase (MT1-MMP) induces activation of progelatinase A. Here we demonstrate that the expression of MT1-MMP in COS-1 cells induces cell-surface binding of progelatinase A which is consequently processed to an intermediate form. Processing from the intermediate to the fully active form is dependent on the gelatinase A concentration. These results suggest that the cell-surface binding concentrates the gelatinase A intermediate form locally to allow ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Anyone else experiencing anything similar? I have been running low doses of mt2 on and off over the last 7 years. Within the last 5 months I have expe
The processing mechanism and gelatinolytic activity of the membrane-type matrix metalloproteinase 1 (MT-MMP-1) were examined by expressing in COS-1 cells a deletion mutant of MT-MMP-1 lacking the trans-membrane domain (delta MT1) and its site-directed mutant with a furin-resistant sequence in the propeptide domain (mutant delta MT1). delta MT1, but not mutant delta MT1, was processed to an active form and exhibited gelatinolytic activity as seen using gelatin zymography. delta MT1 isolated in a complex form with tissue inhibitor of metalloproteinases 2 (TIMP-2) from the stable transfectants demonstrated the NH2-terminal sequence of Ala113-IIe-Gln-Leu, indicating cleavage at one amino acid down-stream from the furin recognition sequence. The delta MT1/TIMP-2 complex formed a ternary complex with proMMP-2 through the COOH termini of TIMP-2 and proMMP-2. A human breast carcinoma cell line (MDA-MB-231 cells) also secreted MT-MMP-1 into culture media, which was purified in a complex form with TIMP-2 and
MMP9小鼠单克隆抗体[56-2A4](ab58803)可与大鼠, 兔, 豚鼠, 人样本反应并经WB, IHC, ICC/IF实验严格验证,被14篇文献引用并得到5个独立的用户反馈。
TY - JOUR. T1 - Cloning of murine membrane-type-1-matrix metalloproteinase (MT-1-MMP) and its metanephric developmental regulation with respect to MMP-2 and its inhibitor. AU - Ota, Kosuke. AU - Stetler-Stevenson, William G.. AU - Yang, Qiwei. AU - Kumar, Anil. AU - Wada, Jun. AU - Kashihara, Naoki. AU - Wallner, Elisabeth I.. AU - Kanwar, Yashpal S.. PY - 1998. Y1 - 1998. N2 - Background. Extracellular matrix macromolecules regulate morphogenesis of embryonic organs, and are developmentally regulated. Their expression and turnover is regulated by matrix metalloproteinases (MMPs). Recently, an epithelial cell membrane associated metalloproteinase (MT-1-MMP) has been identified that acts as an activator of a secreted MMP-2, and is produced by mesenchymal fibroblasts. The activity of MMP-2 is inhibited by a soluble tissue inhibitor of MMP-2, TIMP-2. The role of MT-1-MMP in renal development is unknown. Methods. MT-1-MMP was cloned from embryonic mouse kidney cDNA library, and its ...
Proteolysis is essential during branching morphogenesis but the functions of MT-MMPs and their proteolytic products are not clearly understood. into how MT2-MMP-dependent release of bioactive NC1 domains from collagen IV P505-15 is critical for integrating collagen IV synthesis and proteolysis with epithelial proliferation during branching morphogenesis. 8 and 2-fold whereas and did not change (Physique […]. ...