ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.
An actinomycete from which the antibiotics STREPTOMYCIN, grisein, and CANDICIDIN are obtained.
A metallic element of atomic number 30 and atomic weight 65.38. It is a necessary trace element in the diet, forming an essential part of many enzymes, and playing an important role in protein synthesis and in cell division. Zinc deficiency is associated with ANEMIA, short stature, HYPOGONADISM, impaired WOUND HEALING, and geophagia. It is known by the symbol Zn.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA.
Enzyme that is a major constituent of kidney brush-border membranes and is also present to a lesser degree in the brain and other tissues. It preferentially catalyzes cleavage at the amino group of hydrophobic residues of the B-chain of insulin as well as opioid peptides and other biologically active peptides. The enzyme is inhibited primarily by EDTA, phosphoramidon, and thiorphan and is reactivated by zinc. Neprilysin is identical to common acute lymphoblastic leukemia antigen (CALLA Antigen), an important marker in the diagnosis of human acute lymphocytic leukemia. There is no relationship with CALLA PLANT.
A genus of gram-positive, endospore-forming, thermophilic bacteria in the family BACILLACEAE.
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
Compounds containing the -SH radical.
A potent natriuretic and vasodilatory peptide or mixture of different-sized low molecular weight PEPTIDES derived from a common precursor and secreted mainly by the HEART ATRIUM. All these peptides share a sequence of about 20 AMINO ACIDS.
A class of drugs whose main indications are the treatment of hypertension and heart failure. They exert their hemodynamic effect mainly by inhibiting the renin-angiotensin system. They also modulate sympathetic nervous system activity and increase prostaglandin synthesis. They cause mainly vasodilation and mild natriuresis without affecting heart rate and contractility.
PRESSURE of the BLOOD on the ARTERIES and other BLOOD VESSELS.
The number of times the HEART VENTRICLES contract per unit of time, usually per minute.
Processes and properties of the CARDIOVASCULAR SYSTEM as a whole or of any of its parts.
The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.
Messages between computer users via COMPUTER COMMUNICATION NETWORKS. This feature duplicates most of the features of paper mail, such as forwarding, multiple copies, and attachments of images and other file types, but with a speed advantage. The term also refers to an individual message sent in this way.
Minute projections of cell membranes which greatly increase the surface area of the cell.
A subclass of EXOPEPTIDASES that act on the free N terminus end of a polypeptide liberating a single amino acid residue. EC 3.4.11.
Zinc-binding metalloproteases that are members of the type II integral membrane metalloproteases. They are expressed by GRANULOCYTES; MONOCYTES; and their precursors as well as by various non-hematopoietic cells. They release an N-terminal amino acid from a peptide, amide or arylamide.
Short-term debt obligations and assets occurring in the regular course of operational transactions.
Antibodies produced by a single clone of cells.
The property of antibodies which enables them to react with some ANTIGENIC DETERMINANTS and not with others. Specificity is dependent on chemical composition, physical forces, and molecular structure at the binding site.
Organic or inorganic compounds that contain the -N3 group.
Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).
Sites on an antigen that interact with specific antibodies.
An enzyme the catalyzes the degradation of insulin, glucagon and other polypeptides. It is inhibited by bacitracin, chelating agents EDTA and 1,10-phenanthroline, and by thiol-blocking reagents such as N-ethylmaleimide, but not phosphoramidon. (Eur J Biochem 1994;223:1-5) EC 3.4.24.56.
Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).
The most common clinical variant of MULTIPLE SCLEROSIS, characterized by recurrent acute exacerbations of neurologic dysfunction followed by partial or complete recovery. Common clinical manifestations include loss of visual (see OPTIC NEURITIS), motor, sensory, or bladder function. Acute episodes of demyelination may occur at any site in the central nervous system, and commonly involve the optic nerves, spinal cord, brain stem, and cerebellum. (Adams et al., Principles of Neurology, 6th ed, pp903-914)
An autoimmune disorder mainly affecting young adults and characterized by destruction of myelin in the central nervous system. Pathologic findings include multiple sharply demarcated areas of demyelination throughout the white matter of the central nervous system. Clinical manifestations include visual loss, extra-ocular movement disorders, paresthesias, loss of sensation, weakness, dysarthria, spasticity, ataxia, and bladder dysfunction. The usual pattern is one of recurrent attacks followed by partial recovery (see MULTIPLE SCLEROSIS, RELAPSING-REMITTING), but acute fulminating and chronic progressive forms (see MULTIPLE SCLEROSIS, CHRONIC PROGRESSIVE) also occur. (Adams et al., Principles of Neurology, 6th ed, p903)
A form of multiple sclerosis characterized by a progressive deterioration in neurologic function which is in contrast to the more typical relapsing remitting form. If the clinical course is free of distinct remissions, it is referred to as primary progressive multiple sclerosis. When the progressive decline is punctuated by acute exacerbations, it is referred to as progressive relapsing multiple sclerosis. The term secondary progressive multiple sclerosis is used when relapsing remitting multiple sclerosis evolves into the chronic progressive form. (From Ann Neurol 1994;36 Suppl:S73-S79; Adams et al., Principles of Neurology, 6th ed, pp903-914)
One of the type I interferons produced by fibroblasts in response to stimulation by live or inactivated virus or by double-stranded RNA. It is a cytokine with antiviral, antiproliferative, and immunomodulating activity.
The determination of the pattern of genes expressed at the level of GENETIC TRANSCRIPTION, under specific circumstances or in a specific cell.
Hybridization of a nucleic acid sample to a very large set of OLIGONUCLEOTIDE PROBES, which have been attached individually in columns and rows to a solid support, to determine a BASE SEQUENCE, or to detect variations in a gene sequence, GENE EXPRESSION, or for GENE MAPPING.
The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.
Viruses whose host is Staphylococcus.
Potentially pathogenic bacteria found in nasal membranes, skin, hair follicles, and perineum of warm-blooded animals. They may cause a wide range of infections and intoxications.
The phenomenon by which a temperate phage incorporates itself into the DNA of a bacterial host, establishing a kind of symbiotic relation between PROPHAGE and bacterium which results in the perpetuation of the prophage in all the descendants of the bacterium. Upon induction (VIRUS ACTIVATION) by various agents, such as ultraviolet radiation, the phage is released, which then becomes virulent and lyses the bacterium.
Viruses whose hosts are bacterial cells.
Rupture of bacterial cells due to mechanical force, chemical action, or the lytic growth of BACTERIOPHAGES.
An autolytic enzyme bound to the surface of bacterial cell walls. It catalyzes the hydrolysis of the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell wall glycopeptides, particularly peptidoglycan. EC 3.5.1.28.
An immunoassay utilizing an antibody labeled with an enzyme marker such as horseradish peroxidase. While either the enzyme or the antibody is bound to an immunosorbent substrate, they both retain their biologic activity; the change in enzyme activity as a result of the enzyme-antibody-antigen reaction is proportional to the concentration of the antigen and can be measured spectrophotometrically or with the naked eye. Many variations of the method have been developed.
Diabetes mellitus induced by PREGNANCY but resolved at the end of pregnancy. It does not include previously diagnosed diabetics who become pregnant (PREGNANCY IN DIABETICS). Gestational diabetes usually develops in late pregnancy when insulin antagonistic hormones peaks leading to INSULIN RESISTANCE; GLUCOSE INTOLERANCE; and HYPERGLYCEMIA.
A test to determine the ability of an individual to maintain HOMEOSTASIS of BLOOD GLUCOSE. It includes measuring blood glucose levels in a fasting state, and at prescribed intervals before and after oral glucose intake (75 or 100 g) or intravenous infusion (0.5 g/kg).
Tumors or cancer of the LUNG.
The status during which female mammals carry their developing young (EMBRYOS or FETUSES) in utero before birth, beginning from FERTILIZATION to BIRTH.
A chronic PELVIC PAIN characterized by pain deep in the buttock that may radiate to posterior aspects of the leg. It is caused by the piriformis muscle compressing or irritating the SCIATIC NERVE due to trauma, hypertrophy, inflammation or anatomic variations.
Either of two fleshy protuberances at the lower posterior section of the trunk or HIP in humans and primate on which a person or animal sits, consisting of gluteal MUSCLES and fat.
Facilities for collecting and organizing information. They may be specialized by subject field, type of source material, persons served, location, or type of services.
The immovable joint formed by the lateral surfaces of the SACRUM and ILIUM.
A condition characterized by pain radiating from the back into the buttock and posterior/lateral aspects of the leg. Sciatica may be a manifestation of SCIATIC NEUROPATHY; RADICULOPATHY (involving the SPINAL NERVE ROOTS; L4, L5, S1, or S2, often associated with INTERVERTEBRAL DISK DISPLACEMENT); or lesions of the CAUDA EQUINA.
A nerve which originates in the lumbar and sacral spinal cord (L4 to S3) and supplies motor and sensory innervation to the lower extremity. The sciatic nerve, which is the main continuation of the sacral plexus, is the largest nerve in the body. It has two major branches, the TIBIAL NERVE and the PERONEAL NERVE.
Sharp instruments used for puncturing or suturing.

Comparative molecular genetic profiles of anaplastic astrocytomas/glioblastomas multiforme and their subsequent recurrences. (1/4803)

Malignant glial tumors (anaplastic astrocytomas and glioblastomas multiforme) arise mostly either from the progression of low grade precursor lesions or rapidly in a de novo fashion and contain distinct genetic alterations. There is, however, a third subset of malignant gliomas in which genetic lesions remain to be identified. Following surgical resection, all gliomas appear to have an inherent tendency to recur. Comparative molecular analysis of ten primary malignant gliomas (three anaplastic astrocytomas and seven glioblastomas multiforme) with their recurrences identified two distinct subgroups of recurrent tumors. In one group, primary tumors harbored genetic aberrations frequently associated with linear progression or de novo formation pathways of glial tumorigenesis and maintained their genetic profiles upon recurrence. In the other subset with no detectable known genetic mutations at first presentation, the recurrent tumors sustained specific abnormalities associated with pathways of linear progression or de novo formation. These included loss of genes on chromosomes 17 and 10, mutations in the p53 gene, homozygous deletion of the DMBTA1 and p16 and/ or p15 genes and amplification and/or overexpression of CDK4 and alpha form of the PDGF receptor. Recurrent tumors from both groups also displayed an abnormal expression profile of the metalloproteinase, gel A, and its inhibitor, TIMP-2, consistent with their highly invasive behavior. Delineation of the molecular differences between malignant glioblastomas and their subsequent recurrences may have important implications for the development of rational clinical approaches for this neoplasm that remains refractory to existing therapeutic modalities.  (+info)

Expression and tissue localization of membrane-type 1, 2, and 3 matrix metalloproteinases in human astrocytic tumors. (2/4803)

Three different membrane-type matrix metalloproteinases (MT1-, MT2-, and MT3-MMPs) are known to activate in vitro the zymogen of MMP-2 (pro-MMP-2, progelatinase A), which is one of the key MMPs in invasion and metastasis of various cancers. In the present study, we have examined production and activation of pro-MMP-2, expression of MT1-, MT2-, and MT3-MMPs and their correlation with pro-MMP-2 activation, and localization of MMP-2, MT1-MMP, and MT2-MMP in human astrocytic tumors. The sandwich enzyme immunoassay demonstrates that the production levels of pro-MMP-2 in the anaplastic astrocytomas and glioblastomas are significantly higher than that in the low-grade astrocytomas (P<0.05 and P<0.01, respectively), metastatic brain tumors (P<0.05), or normal brains (P<0.01). Gelatin zymography indicates that the pro-MMP-2 activation ratio is significantly higher in the glioblastomas than in other astrocytic tumors (P<0.01), metastatic brain tumors (P<0.01), and normal brains (P<0.01). The quantitative reverse transcription polymerase chain reaction analyses demonstrate that MT1-MMP and MT2-MMP are expressed predominantly in glioblastoma tissues (17/17 and 12/17 cases, respectively), and their expression levels increase significantly as tumor grade increases. MT3-MMP is detectable in both astrocytic tumor and normal brain tissues, but the mean expression level is approximately 50-fold lower compared with that of MT1-MMP and MT2-MMP in the glioblastomas. The activation ratio of pro-MMP-2 correlates directly with the expression levels of MT1-MMP and MT2-MMP but not MT3-MMP. In situ hybridization indicates that neoplastic astrocytes express MT1-MMP and MT2-MMP in the glioblastoma tissues (5/5 cases and 5/5 cases, respectively). Immunohistochemically, MT1-MMP and MT2-MMP are localized to the neoplastic astrocytes in glioblastoma samples (17/17 cases and 12/17 cases, respectively), which are also positive for MMP-2. In situ zymography shows gelatinolytic activity in the glioblastoma tissues but not in the normal brain tissues. These results suggest that both MT1-MMP and MT2-MMP play a key role in the activation of pro-MMP-2 in the human malignant astrocytic tumors and that the gelatinolytic activity is involved in the astrocytic tumor invasion.  (+info)

Enhanced tumor growth and invasiveness in vivo by a carboxyl-terminal fragment of alpha1-proteinase inhibitor generated by matrix metalloproteinases: a possible modulatory role in natural killer cytotoxicity. (3/4803)

Matrix metalloproteinases (MMPs) are believed to contribute to the complex process of cancer progression. They also exhibit an alpha1-proteinase inhibitor (alphaPI)-degrading activity generating a carboxyl-terminal fragment of approximately 5 kd (alphaPI-C). This study reports that overexpression of alphaPI-C in S2-020, a cloned subline derived from the human pancreas adenocarcinoma cell line SUIT-2, potentiates the growth capability of the cells in nude mice. After stable transfection of a vector containing a chimeric cDNA encoding a signal peptide sequence of tissue inhibitor of metalloproteinase-1 followed by cDNA for alphaPI-C into S2-020 cells, three clones that stably secrete alphaPI-C were obtained. The ectopic expression of alphaPI-C did not alter in vitro cellular growth. However, subcutaneous injection of the alphaPI-C-secreting clones resulted in tumors that were 1.5 to 3-fold larger than those of control clones with an increased tendency to invasiveness and lymph node metastasis. These effects could be a result of modulation of natural killer (NK) cell-mediated control of tumor growth in nude mice, as the growth advantage of alphaPI-C-secreting clones was not observed in NK-depleted mice, and alphaPI-C-secreting clones showed decreased NK sensitivity in vitro. In addition, production of alphaPI and generation of the cleaved form of alphaPI by MMP were observed in various human tumor cell lines and in a highly metastatic subline of SUIT-2 in vitro. These results provide experimental evidence that the alphaPI-degrading activity of MMPs may play a role in tumor progression not only via the inactivation of alphaPI but also via the generation of alphaPI-C.  (+info)

Collagenase-3 (MMP-13) is expressed by tumor cells in invasive vulvar squamous cell carcinomas. (4/4803)

Collagenase-3 (MMP-13) is a human matrix metalloproteinase specifically expressed by invading tumor cells in squamous cell carcinomas (SCCs) of the head and neck. Here, we have further elucidated the role of MMP-13 in tumor invasion by examining its expression in invasive malignant tumors of the female genital tract. Using in situ hybridization, expression of MMP-13 mRNA was detected in 9 of 12 vulvar SCCs, primarily in tumor cells, but not in intact vulvar epithelium, in cervical SCCs (n = 12), or in endometrial (n = 11) or ovarian adenocarcinomas (n = 8). MMP-13 expression was especially abundant in vulvar carcinomas showing metastasis to lymph nodes and was associated with expression of membrane type 1 MMP by tumor cells and gelatinase-A (MMP-2) by stromal cells, as detected by immunohistochemistry. MMP-13 mRNAs were detected in 9 of 11 cell lines established from vulvar carcinomas and in 4 of 6 cell lines from cervical carcinomas, whereas endometrial (n = 10) and ovarian (n = 9) carcinoma cell lines were negative for MMP-13 mRNA. No correlation was detected between MMP-13 expression and p53 gene mutations in vulvar SCC cell lines. However, MMP-13 expression was detected in 5 of 6 vulvar and cervical SCC cell lines harboring HPV 16 or 68 DNA. These results show that MMP-13 is specifically expressed by malignantly transformed squamous epithelial cells, including vulvar SCC cells, and appears to serve as a marker for their invasive capacity.  (+info)

The cytoplasmic carboxy-terminal amino acid determines the subcellular localization of proTGF-(alpha) and membrane type matrix metalloprotease (MT1-MMP). (5/4803)

Transforming growth factor alpha (TGF-(alpha)) is synthesized as a precursor transmembrane molecule (proTGF-(alpha)) whose ectodomain is shed from the cell surface generating mature, soluble, growth factor. In agreement with recent reports, here we show that the structural determinant that targets proTGF-(alpha) to the cell surface maps to the very C-terminal cytoplasmic amino acid, valine. The primary localization of proTGF-(alpha) C-terminal mutants is a perinuclear area that colocalizes with ER markers. Since the ectodomain shedding machinery that acts on proTGF-(alpha) is known to be located at the cell surface, deficient transport provides an explanation for the previously reported lack of PKC activated ectodomain shedding of proTGF-(alpha) C-terminal mutants. The transport of wild-type proTGF-(alpha) to the cell surface was found to be mediated by a mechanism that includes a specific component saturable by wild-type proTGF-(alpha) but not by cell surface transmembrane proteins whose trafficking is independent of their cytoplasmic tail such as betaglycan. C-terminal valines are likely to be a general determinant of the subcellular location of cell surface transmembrane proteins since the maturation and trafficking of MT1-MMP C-terminal mutants are severely impaired. Our data suggest the existence of a targeting mechanism that acts on cell surface transmembrane molecules as diverse as proTGF-(alpha) and MT1-MMP and that the interaction with such a mechanism depends on the identity of the C-terminal amino acid of the targeted molecules.  (+info)

A novel clan of zinc metallopeptidases with possible intramembrane cleavage properties. (6/4803)

Computer-based database searching and protein multiple sequence alignment has identified a novel clan of zinc metallopeptidases, which, by phylogenetic analysis, has been shown to contain six subfamilies. The family is characterized by four common transmembrane segments and three conserved sequence motifs. The combination of topology analysis and motif identification has detected three potential Zn2+ coordinating residues. Only two of the sequences of this novel zinc metallopeptidase clan possess any functional annotation, one of which is able to cleave its substrate within a cytosol/transmembrane segment junction. A number of observations suggest that the remaining members of this novel clan may also cleave their substrates within transmembrane segments.  (+info)

Expression of stromelysin-3 in atherosclerotic lesions: regulation via CD40-CD40 ligand signaling in vitro and in vivo. (7/4803)

Stromelysin-3 is an unusual matrix metalloproteinase, being released in the active rather than zymogen form and having a distinct substrate specificity, targeting serine proteinase inhibitors (serpins), which regulate cellular functions involved in atherosclerosis. We report here that human atherosclerotic plaques (n = 7) express stromelysin-3 in situ, whereas fatty streaks (n = 5) and normal arterial specimens (n = 5) contain little or no stromelysin-3. Stromelysin-3 mRNA and protein colocalized with endothelial cells, smooth muscle cells, and macrophages within the lesion. In vitro, usual inducers of matrix metalloproteinases such as interleukin-1, interferon-gamma, or tumor necrosis factor alpha did not augment stromelysin-3 in vascular wall cells. However, T cell-derived as well as recombinant CD40 ligand (CD40L, CD154), an inflammatory mediator recently localized in atheroma, induced de novo synthesis of stromelysin-3. In addition, stromelysin-3 mRNA and protein colocalized with CD40L and CD40 within atheroma. In accordance with the in situ and in vitro data obtained with human material, interruption of the CD40-CD40L signaling pathway in low density lipoprotein receptor-deficient hyperlipidemic mice substantially decreased expression of the enzyme within atherosclerotic plaques. These observations establish the expression of the unusual matrix metalloproteinase stromelysin-3 in human atherosclerotic lesions and implicate CD40-CD40L signaling in its regulation, thus providing a possible new pathway that triggers complications within atherosclerotic lesions.  (+info)

Dynorphin A processing enzyme: tissue distribution, isolation, and characterization. (8/4803)

Limited proteolysis of the dynorphin precursor (prodynorphin) at dibasic and monobasic processing sites results in the generation of bioactive dynorphins. In the brain and neurointermediate lobe of the pituitary, prodynorphin is processed to produce alpha and beta neo endorphins, dynorphins (Dyn) A-17 and Dyn A-8, Dyn B-13, and leucine-enkephalin. The formation of Dyn A-8 from Dyn A-17 requires a monobasic cleavage between Ile and Arg. We have identified an enzymatic activity capable of processing at this monobasic site in the rat brain and neurointermediate lobe of the bovine pituitary; this enzyme is designated "dynorphin A-17 processing enzyme." In the rat brain and neurointermediate lobe, a majority of the Dyn A processing enzyme activity is membrane-associated and can be released by treatment with 1% Triton X-100. This enzyme has been purified to apparent homogeneity from the membrane extract of the neurointermediate lobe using preparative iso-electrofocussing in a granulated gel pH 3.5 to 10, FPLC using anion exchange chromatography, and non-denaturing electrophoresis. The Dyn A processing enzyme exhibits a pI of about 5.8 and a molecular mass of about 65 kDa under reducing conditions. The Dyn A processing enzyme is a metalloprotease and has a neutral pH optimum. It exhibits substantial sensitivity to metal chelating agents and thiol agents suggesting that this enzyme is a thiol-sensitive metalloprotease. Specific inhibitors of other metallopeptidases such as enkephalinase [EC 3.4.24.11], the enkephalin generating neutral endopeptidase [EC 3.4.24.15], or NRD convertase do not inhibit the Dyn A processing enzyme activity. In contrast, specific inhibitors of angiotensin converting enzyme inhibit the activity. The purified enzyme is able to process a number of neuropeptides at both monobasic and dibasic sites. These characteristics are consistent with a role for the Dyn A processing enzyme in the processing of Dyn A-17 and other neuropeptides in the brain.  (+info)

Zinc metallopeptidases that contain the His-Glu-Xaa-Xaa-His (HEXXH) motif generally have a third ligand of the metal ion that may be either a Glu residue (in clan MA) or a His residue (in clan MB) (Rawlings and Barrett (1995) Methods Enzymol. 248, 183-228). Thimet oligopeptidase has not yet been assigned to either clan, and both Glu and His residues have been proposed as the third ligand. We mutated candidate ligand residues in the recombinant enzyme and identified Glu, His and Asp residues that are important for catalytic activity and/or stability of the protein. However, neither of the Glu and His residues close to the HEXXH motif that have previously been suggested to be ligands is required for the binding of zinc. We conclude that thimet oligopeptidase is not a member of clan MA or clan MB and it is likely that the enzyme possesses a catalytic site and protein fold different from those identified in any metallopeptidase to date. The definitive identification of the third zinc ligand may well require
Compare a disintegrin-like and metallopeptidase (reprolysin type) with thrombospondin type 1 motif, 15 ELISA Kits from leading suppliers on Biocompare. View specifications, prices, citations, reviews, and more.
Pneumococci display large zinc metalloproteinases on the surface, including the IgA protease, which cleaves human IgA1 in the hinge region, the ZmpC proteinase, which cleaves human matrix metalloproteinase 9 (MMP-9), and two other proteinases, ZmpB and ZmpD, whose substrates have not yet been identified. Surface metalloproteinases are antigenic and have been linked to virulence. The genes encoding these proteinases reside in three distinct loci: two loci specific for zmpB and zmpC, and a third, the iga locus, containing iga and zmpD. Data obtained by this and other groups have shown that pneumococcal metalloproteinase genes are transcribed and yield mature and enzymatically active proteins. Since the presence of the four proteinase genes is variable in the pneumococcal strains whose genomes have been sequenced, the presence of these genes in a collection of 218 pneumococcal isolates, mostly from invasive disease, was investigated. The data showed that zmpB and iga were present in all the isolates
FUNCTION: This gene encodes a member of the matrix metalloproteinase family of extracellular matrix-degrading enzymes that are involved in tissue remodeling, wound repair, progression of atherosclerosis and tumor invasion. Mice harboring certain mutations in this gene exhibit congenital heart defects. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Feb 2016 ...
Shop Mitochondrial metalloendopeptidase ELISA Kit, Recombinant Protein and Mitochondrial metalloendopeptidase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
Shop Beta-lytic metalloendopeptidase ELISA Kit, Recombinant Protein and Beta-lytic metalloendopeptidase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
Neurolysin antibody LS-C169730 is an unconjugated rabbit polyclonal antibody to Neurolysin (NLN) (aa88-137) from human. It is reactive with human, bat, bovine and other species. Validated for WB.
This gene encodes a member of the matrix metalloproteinase family. Proteins in this family are involved in the breakdown of extracellular matrix for both normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, and disease processes, such as asthma and tumor metastasis. The encoded protein may play an important role in embryogenesis, particularly in neuronal cells, as well as in lymphocyte development and survival. [provided by RefSeq, May 2013 ...
Background:. A continuing challenge in breast cancer surgery is the difficulty with intraoperative lymph node status determination and achieving negative surgical margins. Current techniques such as frozen section, touch prep and intraoperative radiographic imaging are time consuming and vary in accuracy from institution to institution. Our study is a first-in-human study of a novel ratiometric activatable cell penetrating fluorescent peptide dye conjugate that labels breast cancer tumor tissue in vivo.. Methods:. AVB-620 is a substrate for and activated by proteases in the matrix metalloproteinase family. It has two fluorophores moieties linked by a cleavable peptide. Upon cleavage, there is an increase in fluorescence intensity and a change in the predominant wavelength of fluorescence emission. AVB-620 was given preoperatively via intravenous infusion to stage 0-III breast cancer patients. Patients were monitored for safety and AVB-620 pharmacokinetic parameters determined. After 12-20 hours, ...
Description: Description of target: The protein encoded by this gene is a kininase that uses zinc as a cofactor. The encoded oligopeptidase cleaves cytosolic peptides, making them unavailable for display on antigen-presenting cells. This protein also cleaves neuropeptides under 20 aa in length and can degrade beta-amyloid precursor protein to amyloidogenic peptides.;Species reactivity: Human;Application: ELISA;Assay info: Assay Methodology: Quantitative Sandwich ELISA;Sensitivity: 0.13 ng/ ...
Pz-peptidase was purified from chicken liver as a protein of Mr 80,000 and pI 5.2. The purified enzyme hydrolysed phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-D-Arg, 2,4-dinitrophenyl-Pro-Leu-Gly-Pro-Trp-D-Lys. 7-methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-D-(2,4-dinitropheny l)Lys, benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate, Ac-Ala4 (at the Ala-1-Ala-2 bond) and bradykinin (at the Phe-5-Ser-6 bond). No hydrolysis of proteins was detected. Loss of activity in the presence of EDTA or 1,10-phenanthroline was time-dependent. Metal ions found to restore activity after treatment with EDTA were Zn2+, Mn2+, Ca2+, Co2+ and Cd2+, in decreasing order of effectiveness. Ni2+, Fe2+ and higher concentrations of Zn2+ were inhibitory. Inhibition by N-[1-(RS)-carboxy-3-phenylpropyl]-Ala-Ala-Tyr-p-aminobenzoate and related compounds showed Ki values (down to 5 nM) somewhat lower than those for the rat enzyme. Pz-peptidase was activated by low concentrations of 2-mercaptoethanol and dithiothreitol, but inhibited by ...
(2,4-dinitrophenyl)-seryl-threonyl-alanyl-threonyl-lysyl-leucyl-seryl-tryptophan: substrate for lysine-specific metalloendopeptidases
The KOMP Repository is located at the University of California Davis and Childrens Hospital Oakland Research Institute. Question? Comments? For Mice, Cells, and germplasm please contact us at [email protected], US 1-888-KOMP-MICE or International +1-530-752-KOMP, or for vectors [email protected] or +1-510-450-7917 ...
Kessler J.H., Khan S., Seifert U., Le Gall S., Chow K.M., Paschen A., Bres-Vloemans S.A., de Ru A., van Montfoort N., Franken K.L.M.C., Benckhuijsen W.E., Brooks J.M., van Hall T., Ray K., Mulder A., Doxiadis I.I.N., van Swieten P.F., Overkleeft H.S., Prat A., Tomkinson B., Neefjes J., Kloetzel P.M., Rodgers D.W., Hersh L.B., Drijfhout J.W., van Veelen P.A., Ossendorp F. & Melief C.J.M. (2011), Antigen processing by nardilysin and thimet oligopeptidase generates cytotoxic T cell epitopes, Nature Immunology 12(1 ...
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Complete information for NRDC gene (Protein Coding), Nardilysin Convertase, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Cell-permeable. A broad spectrum matrix metalloprotease (MMP) inhibitor with Ki values of 0.4 nM, 0.5 nM, 27 nM, 3.7 nM, 0.1 nM, 0.2 nM, 3.6 nM, 13.4 nM, 0.36 nM for MMPs
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
Endothelin-converting enzyme (ECE-1) is a type II integral membrane protein which plays a key role in the biosynthetic pathway of the vasoconstricting endothelins. Three ECE-1 isoforms, differing by their N-terminal cytoplasmic tails, are generated from a single gene. When expressed in CHO cells, they display comparable enzymatic activity but whereas ECE-1a is strongly expressed at the cell surface, ECE-1b is exclusively intracellular and ECE-1c presents an intermediate distribution. In the present study these different localizations were further described at the ultrastructural level, by electron microscope immunocytochemistry. To characterize the motifs responsible for the intracellular localization of ECE-1b we constructed chimeric proteins and point mutants. Two di-leucine-based motifs, contained in the N-terminal part of ECE-1b, were thus identified. One of these motifs (LV), displayed by both ECE-1b and ECE-1c, accounts for the reduced surface expression of ECE-1c as compared to ECE-1a. ...
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 - Roles of the signal peptide and mature domains in the secretion and maturation of the neutral metalloprotease from Streptomyces cacaoi. AU - Chang, Su Chih. AU - Su, Mei Han. AU - Wu Lee, Yan-Hwa. PY - 1997/1/1. Y1 - 1997/1/1. N2 - The neutral metalloprotease (Npr) of Streptomyces cacaoi is synthesized as a prepro-Npr precursor form consisting of a secretory signal peptide, a propeptide and the mature metalloprotease. The maturation of Npr occurs extracellularly via an autoproteolytic processing of the secreted pro-Npr. The integrity of the propeptide is essential for the formation of mature active Npr but not for its secretion. In this study we investigated whether the secretion and maturation of Npr require the integrity of its signal peptide region and mature protease domain. Five signal peptide mutants were generated, including the substitution mutations at the positively charged region (mutant 1R6LE), the central hydrophobic region (mutants GI19EL and G19N), the boundary of ...
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 ...
Matrix metalloproteinase expression is under strict regulation in physiological conditions. Disruption of the regulatory mechanisms can lead to tissue destruction and is associated with tumour invasion and metastasis. Using the one-hybrid assay technique with a cis-element in the promoter region of the stromelysin (matrix metalloproteinase-3) gene, a cDNA encoding a transcription factor termed ZBP-89 was obtained. The interaction between ZBP-89 and the stromelysin promoter element was confirmed by electrophoretic mobility shift assays with a recombinant ZBP-89. Reporter gene expression under the control of the stromelysin promoter in transiently transfected cells was significantly increased when the cells were cotransfected with a ZBP-89 expression construct. These results indicate that ZBP-89 interacts with the stromelysin promoter and upregulates its activity. As ZBP-89 expression is known to be increased in gastric carcinoma cells, induction of stromelysin expression may be a significant factor in
Fingerprint Dive into the research topics of The endothelin-converting enzyme-1/endothelin-1 pathway plays a critical role in inflammation-associated premature delivery in a mouse model. Together they form a unique fingerprint. ...
Pitrilysin is a bacterial protease that is similar to the mammalian insulin-degrading enzyme, which is hypothesized to protect against the onset of Alzheimers disease, and the yeast enzymes Axl1p and Ste23p, which are responsible for production of the a-factor mating pheromone in Saccharomyces cerevisiae. The lack of a phenotype associated with pitrilysin deficiency has hindered studies of this enzyme. Herein, we report that pitrilysin can be heterologously expressed in yeast such that it functionally substitutes for the shared roles of Axl1p and Ste23p in pheromone production, resulting in a readily observable phenotype. We have exploited this phenotype to conduct structure-function analyses of pitrilysin and report that residues within four sequence motifs that are highly conserved among M16A enzymes are essential for its activity. These motifs include the extended metalloprotease motif, a second motif that has been hypothesized to be important for the function of M16A enzymes, and two others not
Ectopic expression of the Mycobacterium tuberculosis PE- family gene Rv1818c, triggers apoptosis in the mammalian Jurkat T cells, which is blocked by anti-apoptotic protein Bcl-2. Although complete overlap is not observed, a considerable proportion of cellular pools of ectopically expressed Rv1818c localizes to mitochondria. However, recombinant Rv1818c does not trigger release of cytochrome c from isolated mitochondria even though Rv1818c protein induced apoptosis of Jurkat T cells. Apoptosis induced by Rv1818c is blocked by the broad-spectrum caspase inhibitory peptide zVAD-FMK. Unexpectedly, Rv1818c-induced apoptosis is not blocked in a Jurkat sub-clone deficient for caspase-8 (JI 9.2) or in cells where caspase-9 function is inhibited or expression of caspase-9 reduced by siRNA, arguing against a central role for these caspases in Rv1818c-induced apoptotic signaling. Depleting cellular pools of the mitochondrial protein Smac/DIABLO substantially reduces apoptosis consistent with mitochondrial ...
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
The closely related type III secretion system zinc metalloprotease effector proteins GtgA, GogA, and PipA are translocated into host cells during infection. They then cleave nuclear factor κ-light-chain-enhancer of activated B cells (NF-κB) transcription factor subunits, dampening activation of the NF-κB signaling pathway and thereby suppressing host immune responses. We demonstrate here that GtgA, GogA, and PipA cleave a subset of NF-κB subunits, including p65, RelB, and cRel but not NF-κB1 and NF-κB2, whereas the functionally similar type III secretion system effector NleC of enteropathogenic and enterohemorrhagic cleaved all five NF-κB subunits. Mutational analysis of NF-κB subunits revealed that a single nonconserved residue in NF-κB1 and NF-κB2 that corresponds to the P1 residue Arg-41 in p65 prevents cleavage of these subunits by GtgA, GogA, and PipA, explaining the observed substrate specificity of these enzymes. Crystal structures of GtgA in its apo-form and in complex with ...
A phosphoramidon-sensitive metalloendopeptidase in peptidase family M13 (neprilysin family). An integral membrane protein predominantly of endothelial cells, which genera
Strikingly, inactivation or loss of the m-AAA protease does not result in the accumulation of long OPA1 isoforms, as predicted by experiments in yeast (Duvezin-Caubet et al., 2007), but decreases their stability. The accelerated cleavage of OPA1 in the absence of the m-AAA protease is mediated by OMA1, a new member of a conserved and widespread family of membrane-bound M48 metallopeptidases. We have previously identified yeast Oma1 in the mitochondrial inner membrane as a peptidase that can substitute for the function of the m-AAA protease during degradation of a misfolded membrane protein (Käser et al., 2003). Similarly, synthetic growth defects have been observed when mutations in the bacterial AAA protease FtsH were combined with mutations in HtpX, which is a distant homologue of OMA1, indicating overlapping proteolytic activities (Shimohata et al., 2002). In agreement with these findings, we demonstrate in this study that mammalian OMA1, similar to the m-AAA protease, can cleave OPA1. The ...
This gene encodes a member of the matrix metalloproteinase family of endopeptidases that are involved in remodeling extracellular matrix during, for example, embryonic development and tumor progression. The encoded protein undergoes post-translational proteolytic processing by furin endopeptidase to form an active enzyme. Subcutaneous introduction of cells expressing the encoded protein into nude mice results in increased tumor incidence. Mice lacking the encoded protein exhibit a decreased incidence of chemically-induced tumors. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Apr 2015 ...
Clone REA650 recognizes the human ADAM15 antigen, a transmembrane protein, which contains disintegrin and metalloprotease domains. ADAM15 belongs to the membrane linked metalloproteinase family (ADAM), which has gelatinolytic and collagenolytic activities. It has several functions, for example, it is involved in wound healing process and in glomerular cell migration. Furthermore ADAM15 suppresses beta-1 integrins-mediated cell adhesion and migration of smooth muscle cells.Expression of ADAM-15 is found in airway smooth muscle, glomerular mesangial cells, colon, small testine, and chondrocytes. It is highly expressed in atherosclerotic lesions.Additional information: Clone REA650 displays negligible binding to Fc receptors. | Canada
Multiple myeloma (MM) can be an indolent B-cell disease that develops in the bone tissue marrow and it is connected with osteolytic lesions in 1174043-16-3 the advanced phases [1]. site thats turned on in Tyr1356 and Tyr1349. The phosphorylation of the region leads to the induction of MET signaling through the activation of many downstream …Read More. ...
CD10 (Membrane Metalloendopeptidase) Antibody - Without BSA and Azide, Mouse Monoclonal Antibody [Clone CB-CALLA ] validated in IF, FC (AH11845-100), Abgent
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Adam protein (A Disintegrin and Metalloproteinase Protein) is a family of peptidase proteins[1]. ADAMs are also known as the Adamalysin family. ADAMs are classified as Sheddases because they cut off or shed extracellular portions of transmembrane proteins. For example, ADAM 10 can cut off part of the HER2 receptor, activating it[2] and ADAM 17 can cut off part of the EGFR once it has bound its ligand, freeing the ligand to go and stimulate another cell[3]. Therapeutic ADAM inhibitors can potentiate anti-cancer therapy[citation needed]. It is categorized under EC 3.4.24.46. Types include: ...
A team of developmental biologists at the University of Massachusetts Amherst led by Dominique Alfandari, with others at MIT, report in a new paper that they have for the first time described how two transcription factors that are absolutely essential for human development are regulated by a cell surface metalloprotease known as ADAM13.
The present invention relates to Compounds having the structure of Formula I: wherein n is an integer from 1 to 5; R.sub.1 is optionally substituted alkyl, alkenyl, alkynyl, cycloalkyl, aryl, heterocyclyl, heteroaryl, aralkyl, alkoxy, aryloxy, alkenyloxy or alkynyloxy; R.sub.2 is alkenyl, allcynyl, aryl, heterocyclyl, heteroaryl, cycloalkyl, NR.sub.4R.sub.5, --NHC(.dbd.Y)R.sub.4, --NHC(.dbd.Y)NR.sub.5R.sub..chi., --NHC(.dbd.O)OR.sub.4, --NHSO.sub.2R.sub.4, C(.dbd.Y)NR.sub.4R.sub.5, C(.dbd.O)OR.sub.6 [wherein Y is oxygen or sulphur], OR.sub.5, --O(C.dbd.O)NR.sub.4R.sub.5, O-acyl, S(O).sub.mR.sub.4, --SO.sub.2N(R.sub.4).sub.2, cyano, amidino or guanidino [wherein R.sub.4 is alkyl, alkenyl, alkynyl, cycloalkyl, aryl, heterocyclyl, heteroaryl, aralkyl, heteroarylalkyl, heterocyclylalkyl or cycloalkylalkyl and m is an integer 0-2; R.sub.5 is hydrogen or R.sub.4; R.sub.x is R.sub.4 or --SO.sub.2N(R.sub.4).sub.2 and R.sub.6 is hydrogen, alkyl, cycloalkyl,
Purified Recombinant Human ADAM33 293 Cell Lysate from Creative Biomart. Recombinant Human ADAM33 293 Cell Lysate can be used for research.
The protein encoded by this gene is a zinc metalloprotease that displays some activity against angiotensin-3. The encoded protein is inhibited by the aminopeptidase inhibitor amastatin, as well as by the general inhibitors o-phenanthroline and batimastat. Defects in this gene may be associated with lung tumorigenesis. [provided by RefSeq, Oct 2016 ...
Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7 and MMP-9.
1B8Y: X-ray structure of human stromelysin catalytic domain complexed with nonpeptide inhibitors: implications for inhibitor selectivity.
Matrix metalloproteinases are a group of zinc-containing calcium-dependent endopeptidases that play a crucial role in the pathogenesis of disorders
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class=publication>Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href=http://www.nrbook.com/b/bookcpdf.php>Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
Reaktivität: Fledermaus, Huhn, Schimpanse and more. 328 verschiedene TIMP2 Antikörper vergleichen. Alle direkt auf antikörper-online bestellbar!
Protease capable of digesting collagen fibrils. Contains high levels of collagenase and caseinase activity. Produced using animal component-free materials.
GW 3333 inhibits the matrix metalloproteases (MMPs) tumour necrosis factor-α-converting enzyme (TACE), collagenase 1 (MMP-1), gelatinase A (MMP-2), stromelysin
6NYY: Unique Structural Features of the Mitochondrial AAA+ Protease AFG3L2 Reveal the Molecular Basis for Activity in Health and Disease.
Ece1 - Ece1 (untagged) - Mouse endothelin converting enzyme 1 (Ece1), (10ug) available for purchase from OriGene - Your Gene Company.
... metalloendopeptidases (3.4.24). Well known metalloendopeptidases include ADAM proteins and matrix metalloproteinases, and M16 ...
Murphy, G; Willenbrock, F (1995). Tissue inhibitors of matrix metalloendopeptidases. Methods Enzymol. Methods in Enzymology. ...
J. S. Bond & R. J. Benyon (1995). "The astacin family of metalloendopeptidases". Protein Science. 4 (7): 1247-1261. doi:10.1002 ...
Norman MU, Lew RA, Smith AI, Hickey MJ (June 2003). "Metalloendopeptidases EC 3.4.24.15/16 regulate bradykinin activity in the ... Neurolysin, with 704 amino acid residues, is a zinc metalloendopeptidase with a conserved HEXXH motif. It has an overall ... Shrimpton CN, Smith AI, Lew RA (October 2002). "Soluble metalloendopeptidases and neuroendocrine signaling". Endocrine Reviews ... "Identification of membrane-bound variant of metalloendopeptidase neurolysin (EC 3.4.24.16) as the non-angiotensin type 1 (non- ...
The astacin family of metalloendopeptidases (EC 3.4.24.21) encompasses a range of proteins found in hydra to humans, in mature ... Bond JS, Beynon RJ (July 1995). "The astacin family of metalloendopeptidases". Protein Science. 4 (7): 1247-61. doi:10.1002/pro ... Proteins containing the astacin domain include: Astacin-like metallo-endopeptidase (ASTL) Bone morphogenetic protein 1 (BMP1) ... Astacins are a family of multidomain metalloendopeptidases which are either secreted or membrane-anchored. These ...
Jiang W, Le B (2000). "Structure and expression of the human MEP1A gene encoding the alpha subunit of metalloendopeptidase ... 1991). "The astacin family of metalloendopeptidases". J. Biol. Chem. 266 (32): 21381-5. PMID 1939172. Kärgel HJ, Dettmer R, ... for the alpha and beta subunits of the metalloendopeptidase meprin map to human chromosomes 6p and 18q, respectively". Genomics ...
Blumberg S, Tauber Z (October 1983). "Inhibition of metalloendopeptidases by 2-mercaptoacetyl-dipeptides". European Journal of ...
Rawlings, N.D.; Barrett, A.J. (1991). "Homologues of insulinase, a new superfamily of metalloendopeptidases". Biochem. J. 275 ( ...
"Entrez Gene: Membrane metallo-endopeptidase". Galy, Anne; Travis, Marilyn; Cen, Dazhi; Chen, Benjamin (Oct 1995). "Human T, B, ... Neprilysin (/ˌnɛprɪˈlaɪsɪn/), also known as membrane metallo-endopeptidase (MME), neutral endopeptidase (NEP), cluster of ...
Orlowski M, Michaud C, Chu TG (1983). "A soluble metalloendopeptidase from rat brain. Purification of the enzyme and ... involvement of a thermolysin-like metalloendopeptidase (enkephalinase), angiotensin-converting enzyme, and other unidentified ...
TOP2 (also known as thimet metalloendopeptidase 2) is located in the cytosol and has the AT5G10540 gene. The distinctive genes ... Orlowski M, Michaud C, Chu TG (September 1983). "A soluble metalloendopeptidase from rat brain. Purification of the enzyme and ... Tisljar U (February 1993). "Thimet oligopeptidase--a review of a thiol dependent metallo-endopeptidase also known as Pz- ... TOP1 (also known as OOP, organellar oligopeptidase, TOPorg, and thimet metalloendopeptidase 1) is located in the mitochondria ...
Turner AJ, Isaac RE, Coates D (March 2001). "The neprilysin (NEP) family of zinc metalloendopeptidases: Genomics and function ...
Membrane metallo-endopeptidase-like 1 is a protein that in humans is encoded by the MMEL1 gene. The protein encoded by this ... "Entrez Gene: Membrane metallo-endopeptidase-like 1". Whyteside AR, Turner AJ (July 2008). "Human neprilysin-2 (NEP2) and NEP ... gene is a member of the neutral endopeptidase (NEP) or membrane metallo-endopeptidase (MME) family. Family members play ...
Ferro ES, Tullai JW, Glucksman MJ, Roberts JL (1999). "Secretion of metalloendopeptidase 24.15 (EC 3.4.24.15)". DNA Cell Biol. ... 1999). "The association of metalloendopeptidase EC 3.4.24.15 at the extracellular surface of the AtT-20 cell plasma membrane". ... "Cloning and functional expression of a metalloendopeptidase from human brain with the ability to cleave a beta-APP substrate ...
Becker AB, Roth RA (May 1992). "An unusual active site identified in a family of zinc metalloendopeptidases". Proceedings of ... Anastasi A, Knight CG, Barrett AJ (March 1993). "Characterization of the bacterial metalloendopeptidase pitrilysin by use of a ...
Astacin-like metallo-endopeptidase (M12 family) is a protein that in humans is encoded by the ASTL gene. GRCh38: Ensembl ... "Entrez Gene: Astacin-like metallo-endopeptidase (M12 family)". Human ASTL genome location and ASTL gene details page in the ...
Its structure is similar to that of the M23 family of metalloendopeptidases. Unlike this family of peptidases, however, LECT2 ... Reveals a Mechanistic Basis of Functional Evolution in a Mammalian Protein with an M23 Metalloendopeptidase Fold". The Journal ... has not been found to possess enzymatic activity and does not appear to share any functions with M23 metalloendopeptidases. ...
This membrane-bound metalloendopeptidase is present in mouse intestines. Kounnas MZ, Wolz RL, Gorbea CM, Bond JS (September ...
... (EC 3.4.24.51, Ophiophagus metalloendopeptidase) is an enzyme. This enzyme catalyses the following chemical reaction ...
Membrane metallo-endopeptidase". v t e. ...
Nonaka, T; Y Hashimoto; K Takio (1998). "Kinetic characterization of lysine-specific metalloendopeptidases from Grifola ... "Straightforward ladder sequencing of peptides using a Lys-N metalloendopeptidase". Nat Methods. 5 (5): 405-407. doi:10.1038/ ...
... is a metalloendopeptidase found in the mushroom Grifola frondosa that cleaves proteins on the amino side of lysine ... "Straightforward ladder sequencing of peptides using a Lys-N metalloendopeptidase". Nature Methods. 5 (5): 405-7. doi:10.1038/ ... "Kinetic characterization of lysine-specific metalloendopeptidases from Grifola frondosa and Pleurotus ostreatus fruiting bodies ...
... (EC 3.4.24.54, Trimeresurus metalloendopeptidase A, mucrotoxin A) is an enzyme. This enzyme catalyses the following ...
"The purification and properties of a fibrinolytic neutral metalloendopeptidase from Streptococcus faecalis". Arch. Biochem. ... "Purification and substrate specificity of a strongly hydrophobic extracellular metalloendopeptidase ("gelatinase") from ...
... (EC 3.4.24.50, Bothrops metalloendopeptidase J, J protease) is an enzyme. This enzyme catalyses the following ...
1995). "Molecular cloning and sequence analysis of flavastacin: an O-glycosylated prokaryotic zinc metalloendopeptidase". Arch ... Xaa-Glu This zinc metalloendopeptidase belong to the peptidase family M12. It has recently been described as cleaving ...
OMA1: Metalloendopeptidase OMA1, mitochondrial. *OVGP1: Oviductal glycoprotein 1. *PARK7 (1p36): Parkinson disease (autosomal ...
... are a family of single-pass transmembrane and secreted metalloendopeptidases. All ADAMs are characterized by a particular ...
Genetic Engineering and Biotechnology Research Institute describes research in metalloendopeptidases". Science Letter - via ...
Atrolisin A (bahasa Inggris: atrolysin A, Crotalus atrox metalloendopeptidase a; hemorrhagic toxin a; Crotalus atrox α- ...
A metalloendopeptidase is an enzyme that functions as a metalloproteinase endopeptidase. Metalloendopeptidase at the US ...
IgA-specific+metalloendopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Biology portal. ... IgA-specific metalloendopeptidase (EC 3.4.24.13, immunoglobulin A1 proteinase, IgA protease, IgA1-specific proteinase, IgA1 ...
metalloendopeptidase-like protein. Locus tag. Synpcc7942_0138. Gene type. protein coding. RefSeq status. PROVISIONAL. Organism ... Synpcc7942_0138 metalloendopeptidase-like protein [ Synechococcus elongatus PCC 7942 ] Gene ID: 3773478, discontinued on 5-Feb- ...
... inhibiting the catalytic activities of snake venom metalloendopeptidases through the establishment of high-affinity, non- ... The research on natural snake venom metalloendopeptidase inhibitors (SVMPIs) began in the 18th century with the pioneering work ... Natural Inhibitors of Snake Venom Metalloendopeptidases: History and Current Challenges. Viviane A. Bastos 1,2. ... The research on natural snake venom metalloendopeptidase inhibitors (SVMPIs) began in the 18th century with the pioneering work ...
AsaP1 inactive mutant E294Q, an extracellular toxic zinc metalloendopeptidase. *DOI: 10.2210/pdb2X3C/pdb ... Structural Evidence of Intramolecular Propeptide Inhibition of the Aspzincin Metalloendopeptidase Asap1.. Bogdanovic, X., Palm ...
Bond JS, and Beynon RJ (1995) The astacin family of metalloendopeptidases. Protein Sci 4: 1247-1261PubMedCrossRefGoogle Scholar ... Jiang W, and Bond JS (1992) Families of metalloendopeptidases and their relationships. FEBS Lett 312: 110-114PubMedCrossRef ... Bond JS, and Beynon RJ (1986) Meprin: A membrane-bound metalloendo-peptidase. Curr Top Cell Regul 28: 263-290PubMedGoogle ... Bond JS, Beynon RJ, Reckelhoff JF, and David CS (1984) Mep-1 gene controlling a kidney metalloendopeptidase is linked to the ...
Menin and Daxx coregulate expression of membrane metallo-endopeptidase, Mme (CD10). Next, we sought to determine whether menin ... Membrane metalloendopeptidase (CD10/CALLA): distribution, physiologic and pathophysiologic functions and its inhibitors. Lijec ... Menin and Daxx Interact to Suppress Neuroendocrine Tumors through Epigenetic Control of the Membrane Metallo-Endopeptidase. ... Menin and Daxx Interact to Suppress Neuroendocrine Tumors through Epigenetic Control of the Membrane Metallo-Endopeptidase ...
Straightforward and de Novo Peptide Sequencing by MALDI-MS/MS Using a Lys-N Metalloendopeptidase. Paul J. Boersema, Nadia ... Metalloendopeptidase Lys-N was obtained from Seikagaku Corp. (Tokyo, Japan). Iodoacetamide, TFA, and α-cyano-4-hydroxycinnamic ... Rao, K. C. S., Palamalai, V., Dunlevy, J. R., and Miyagi, M. (2005 ) Peptidyl-Lys metalloendopeptidase-catalyzed 18O labeling ... In this work, we explore the potential of the metalloendopeptidase Lys-N for MALDI-MS/MS proteomics applications. Initially we ...
Chicken liver Pz-peptidase, a thiol-dependent metallo-endopeptidase. A J Barrett, M A Brown ... Chicken liver Pz-peptidase, a thiol-dependent metallo-endopeptidase Message Subject (Your Name) has forwarded a page to you ... Moreover, the properties of chicken Pz-peptidase agree with those described for mammalian soluble metallo-endopeptidase and ... We conclude that chicken Pz-peptidase is a metallo-endopeptidase with thiol-dependence. ...
Although the activated metalloendopeptidase is further degraded by trypsin, plasma kallikrein and thermolysin during a ... In vivo it is probable that the precursor of this metalloendopeptidase is activated either by direct limited proteolysis by ... Y Okada, E D Harris, H Nagase; The precursor of a metalloendopeptidase from human rheumatoid synovial fibroblasts. Purification ... 261, 14245-14255]. To study the mechanisms of activation the precursor of this metalloendopeptidase has now been purified. The ...
SCH 39370, a neutral metalloendopeptidase inhibitor, potentiates biological responses to atrial natriuretic factor and lowers ... SCH 39370, a neutral metalloendopeptidase inhibitor, potentiates biological responses to atrial natriuretic factor and lowers ... SCH 39370, a neutral metalloendopeptidase inhibitor, potentiates biological responses to atrial natriuretic factor and lowers ... SCH 39370, a neutral metalloendopeptidase inhibitor, potentiates biological responses to atrial natriuretic factor and lowers ...
A biosynthetic study of meprin: a mouse renal microvillar membrane metallo-endopeptidase. RICHARD J. HEADS, ROBERT J. BEYNON ... A biosynthetic study of meprin: a mouse renal microvillar membrane metallo-endopeptidase ... A biosynthetic study of meprin: a mouse renal microvillar membrane metallo-endopeptidase ... A biosynthetic study of meprin: a mouse renal microvillar membrane metallo-endopeptidase ...
CD10 (Membrane Metalloendopeptidase) Antibody - Without BSA and Azide, Mouse Monoclonal Antibody [Clone CB-CALLA ] validated in ... CD10 (Membrane Metalloendopeptidase) Antibody - Without BSA and Azide is for research use only and not for use in diagnostic or ... home , Products , Primary Antibodies , Stem Cells , CD10 (Membrane Metalloendopeptidase) Antibody - Without BSA and Azide ... CD10 (Membrane Metalloendopeptidase) Antibody - Without BSA and Azide. Mouse Monoclonal Antibody [Clone CB-CALLA ]. ...
Recombinant Protein and Mitochondrial metalloendopeptidase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and ... Mitochondrial metalloendopeptidase OMA1. Mitochondrial metalloendopeptidase OMA1 ELISA Kit. Mitochondrial metalloendopeptidase ... Mitochondrial metalloendopeptidase OMA1 Antibody. Protease that is part of the quality control system in the inner membrane of ... Below are the list of possible Mitochondrial metalloendopeptidase products. If you cannot find the target and/or product is not ...
Recombinant Protein and Beta-lytic metalloendopeptidase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and ... Beta-lytic metalloendopeptidase. Beta-lytic metalloendopeptidase ELISA Kit. Beta-lytic metalloendopeptidase Recombinant. Beta- ... lytic metalloendopeptidase Antibody. Also known as Beta-lytic metalloendopeptidase (Beta-lytic protease).. ... Below are the list of possible Beta-lytic metalloendopeptidase products. If you cannot find the target and/or product is not ...
"Metalloendopeptidases" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... This graph shows the total number of publications written about "Metalloendopeptidases" by people in this website by year, and ... Below are the most recent publications written about "Metalloendopeptidases" by people in Profiles. ... whether "Metalloendopeptidases" was a major or minor topic of these publications. To see the data from this visualization as ...
Oocyte-specific oolemmal receptor involved in sperm and egg adhesion and fertilization. Plays a role in the polyspermy inhibition. Probably acts as a protease for the post-fertilization cleavage of ZP2. Cleaves the sperm-binding ZP2 at the surface of the zona pellucida after fertilization and cortical granule exocytosis, rendering the zona pellucida unable to support further sperm binding (By similarity ...
title = "Secretion of metalloendopeptidase 24.15 (EC 3.4.24.15)",. abstract = "The metalloendopeptidase EP24.15 (EC3.4.24.15) ... Secretion of metalloendopeptidase 24.15 (EC 3.4.24.15). / Ferro, Emer S.; Tullai, John W.; Glucksman, Marc J.; Roberts, James L ... Ferro, E. S., Tullai, J. W., Glucksman, M. J., & Roberts, J. L. (1999). Secretion of metalloendopeptidase 24.15 (EC 3.4.24.15) ... Ferro, ES, Tullai, JW, Glucksman, MJ & Roberts, JL 1999, Secretion of metalloendopeptidase 24.15 (EC 3.4.24.15), DNA and Cell ...
Metalloendopeptidases / genetics * Middle Aged * Multiple Sclerosis, Relapsing-Remitting / genetics* * Multiple Sclerosis, ...
Metalloendopeptidases / biosynthesis * Metalloendopeptidases / genetics* * Protein Biosynthesis * Proteins / genetics* * ...
Metalloendopeptidases. Grant support. *CA75115-01/CA/NCI NIH HHS/United States. LinkOut - more resources. Full Text Sources. * ...
anti Membrane Metallo Endopeptidase MME. anti Membrane Metallo Endopeptidase MME :. Porcine Membrane metallo endopeptidase, MME ... Astacin Like Metallo Endopeptidase (ASTL) Antibody (HRP) from Abbexa 20-abx308044 , [100 ug: < span>411.00 EUR] [1 mg: < span> ... Astacin Like Metallo Endopeptidase (ASTL) Antibody (FITC) from Abbexa 20-abx308045 , [100 ug: < span>411.00 EUR] [1 mg: < span> ... Human Astacin Like Metallo Endopeptidase (ASTL) ELISA Kit from DLdevelop DL-ASTL-Hu-192 , 1 kit of 192 tests: < span>1152.00 ...
Subclass 3.4 (Peptidases) ,, Sub-subclass 3.4.24 (Metalloendopeptidases) ,, Peptidase 3.4.24.69. Enzymology. BRENDA database. ...
3.Structural and functional characterization of M23 family metalloendopeptidases that lyse bacterial cell wall peptidoglycans. ... 3. Structural and functional characterization of M23 family metalloendopeptidases that lyse bacterial cell wall peptidoglycans ...
Metalloendopeptidases. *Muscle Contraction. *Muscular Atrophy. *Muscular Diseases/Impairments. *Myofascial Pain Syndromes. * ...
metalloendopeptidase homolog PEX. *PEX. *PHEX_HUMAN. *phosphate regulating endopeptidase homolog, X-linked ...
Molecular Cloning and Primary Structure of Rat Testes Metalloendopeptidase EC 3.4.24.15. In: Biochemistry. 1990 ; Vol. 29, No. ... The complete amino acid sequence of rat testes metalloendopeptidase (EC 3.4.24.15) was deduced from the nucleotide sequence of ... Molecular Cloning and Primary Structure of Rat Testes Metalloendopeptidase EC 3.4.24.15. / Pierotti, Adrian; Glucksman, Marc J ... abstract = "The complete amino acid sequence of rat testes metalloendopeptidase (EC 3.4.24.15) was deduced from the nucleotide ...
GO:0004222 metalloendopeptidase activity Cellular Component. No terms assigned in this category. ...
Biological markers in pneumoconioses : plasma metalloendopeptidase and matrix metalloendopeptidase Jean-Marc Porcher 1 R. El ... plasma metalloendopeptidase and matrix metalloendopeptidase. 7. International Symposium on Inhaled Particles, Sep 1991, ...
Peptidyl-Lys metalloendopeptidase. Pleurotus ostreatus (Oyster mushroom) (White-rot fungus) ... Peptidyl-Lys metalloendopeptidase UniProtKBInterProInteractive Modelling. 168 aa; Sequence (Fasta) It is possible new templates ...
  • SCH 39370, a neutral metalloendopeptidase inhibitor, potentiates biological responses to atrial natriuretic factor and lowers blood pressure in desoxycorticosterone acetate-sodium hypertensive rats. (aspetjournals.org)
  • SCH 39370 (N-[N-[1-(S)-carboxyl-3-phenylpropyl]-(S)-phenyl-alanyl]-(S)-isoserin e) is a potent and specific inhibitor of neutral metalloendopeptidase (NEP) from rabbit kidney (IC50 = 11.2 +/- 1.9 nM) and is devoid of angiotensin-converting enzyme inhibitory activity at 1 microM. (aspetjournals.org)
  • and metalloendopeptidase inhibitor activity. (jax.org)
  • The metalloendopeptidase EP24.15 (EC3.4.24.15) is a neuropeptide- metabolizing enzyme present in neural and endocrine tissues, presumably functioning extracellularly. (uthscsa.edu)
  • The complete amino acid sequence of rat testes metalloendopeptidase (EC 3.4.24.15) was deduced from the nucleotide sequence of a cDNA clone isolated by screening a rat testes library with a polyclonal antibody raised against a homogeneous preparation of the rat testes enzyme. (uthscsa.edu)
  • Along this migratory pathway, GnRH is cleaved by the zinc metalloendopeptidase EC 3.4.24.15 (abbreviated EP24.15), to generate GnRH-(1-5) ( 9 - 11 ). (frontiersin.org)
  • Recently we explored a new method for mass spectrometry-based sequencing of peptides using a little explored metalloendopeptidase with Lys-N cleavage specificity ( 24 ). (mcponline.org)
  • No amino acid sequence homology, beyond this active site, was found with thermolysin, a bacterial zinc metalloendopeptidase, nor with several mammalian zinc metallopeptidases. (uthscsa.edu)
  • Also known as Beta-lytic metalloendopeptidase (Beta-lytic protease). (mybiosource.com)
  • Below are the list of possible Mitochondrial metalloendopeptidase products. (mybiosource.com)
  • Astl or ovastacin (astacin-like metalloendopeptidase (M12 family)) encodes an oocyte-specific metalloendoprotease involved in cleavage of the zona pellucida protein ZP2. (jax.org)
  • Gene Ontology (GO) annotations related to this gene include metalloendopeptidase activity . (genecards.org)
  • Predicted to have metalloendopeptidase activity. (mcw.edu)
  • The precursor of a metalloendopeptidase from human rheumatoid synovial fibroblasts. (portlandpress.com)
  • In vivo it is probable that the precursor of this metalloendopeptidase is activated either by direct limited proteolysis by tissue or plasma endopeptidases, or, alternatively, by factors that cause certain conformational changes in the zymogen molecule. (portlandpress.com)
  • Two active forms (Mr 45,000 and 28,000) of a metalloendopeptidase that digest proteoglycans and other extracellular matrix components of connective tissues have previously been purified from rheumatoid synovial cells and characterized [Okada, Nagase & Harris (1986) J. Biol. (portlandpress.com)
  • A metalloendopeptidase is an enzyme that functions as a metalloproteinase endopeptidase. (wikipedia.org)
  • E.G. ErdÖs, W.W. Schulz, J.T. Gafford, and R. Defendini, Neutral metalloendopeptidase in human male genital tract: comparison to angiotensin I-converting enzyme, Lab. (springer.com)
  • Although the activated metalloendopeptidase is further degraded by trypsin, plasma kallikrein and thermolysin during a prolonged incubation, it is relatively stable against plasmin and chymotrypsin. (portlandpress.com)
  • Crystal structures of alpha-mercaptoacyldipeptides in the thermolysin active site: structural parameters for a Zn monodentation or bidentation in metalloendopeptidases. (expasy.org)
  • Human NEP can be classified as a thermolysin-type metalloendopeptidase (2,10,11). (springer.com)
  • Metalloendopeptidases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (rush.edu)
  • Well known metalloendopeptidases include ADAM proteins and matrix metalloproteinases . (wikidoc.org)
  • A.R. Johnson, J. Ashton, W.W. Schulz, and E.G. ErdÖs, Neutral metalloendopeptidase in human lung tissue and cultured cells, Am. Rev. Respir. (springer.com)
  • Female mice homozygous for the null Astl or ovastacin (astacin-like metalloendopeptidase (M12 family)) allele exhibit moderately reduced fecundity. (jax.org)
  • This graph shows the total number of publications written about "Metalloendopeptidases" by people in this website by year, and whether "Metalloendopeptidases" was a major or minor topic of these publications. (rush.edu)
  • The research on natural snake venom metalloendopeptidase inhibitors (SVMPIs) began in the 18th century with the pioneering work of Fontana on the resistance that vipers exhibited to their own venom. (mdpi.com)
  • This cell surface metalloendopeptidase inactivates a number of signaling molecules and serves as a major regulator in the nervous, immune and other systems. (fishersci.com)
  • In this work, we explore the potential of the metalloendopeptidase Lys-N for MALDI-MS/MS proteomics applications. (mcponline.org)