Cathepsin B: A lysosomal cysteine proteinase with a specificity similar to that of PAPAIN. The enzyme is present in a variety of tissues and is important in many physiological and pathological processes. In pathology, cathepsin B has been found to be involved in DEMYELINATION; EMPHYSEMA; RHEUMATOID ARTHRITIS, and NEOPLASM INVASIVENESS.Cathepsins: A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.Cathepsin L: A ubiquitously-expressed cysteine protease that plays an enzymatic role in POST-TRANSLATIONAL PROTEIN PROCESSING of proteins within SECRETORY GRANULES.Cathepsin D: An intracellular proteinase found in a variety of tissue. It has specificity similar to but narrower than that of pepsin A. The enzyme is involved in catabolism of cartilage and connective tissue. EC 3.4.23.5. (Formerly EC 3.4.4.23).Cathepsin H: An ubiquitously-expressed lysosomal cysteine protease that is involved in protein processing. The enzyme has both endopeptidase and aminopeptidase activities.Cathepsin K: A cysteine protease that is highly expressed in OSTEOCLASTS and plays an essential role in BONE RESORPTION as a potent EXTRACELLULAR MATRIX-degrading enzyme.Cathepsin G: A serine protease found in the azurophil granules of NEUTROPHILS. It has an enzyme specificity similar to that of chymotrypsin C.Cathepsin E: An aspartic endopeptidase that is similar in structure to CATHEPSIN D. It is found primarily in the cells of the immune system where it may play a role in processing of CELL SURFACE ANTIGENS.Cathepsin C: A papain-like cysteine protease that has specificity for amino terminal dipeptides. The enzyme plays a role in the activation of several pro-inflammatory serine proteases by removal of their aminoterminal inhibitory dipeptides. Genetic mutations that cause loss of cathepsin C activity in humans are associated with PAPILLON-LEFEVRE DISEASE.Cysteine Endopeptidases: ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.Cathepsin F: A lysosomal papain-related cysteine proteinase that is expressed in a broad variety of cell types.Cystatins: A homologous group of endogenous CYSTEINE PROTEINASE INHIBITORS. The cystatins inhibit most CYSTEINE ENDOPEPTIDASES such as PAPAIN, and other peptidases which have a sulfhydryl group at the active site.Lysosomes: A class of morphologically heterogeneous cytoplasmic particles in animal and plant tissues characterized by their content of hydrolytic enzymes and the structure-linked latency of these enzymes. The intracellular functions of lysosomes depend on their lytic potential. The single unit membrane of the lysosome acts as a barrier between the enzymes enclosed in the lysosome and the external substrate. The activity of the enzymes contained in lysosomes is limited or nil unless the vesicle in which they are enclosed is ruptured. Such rupture is supposed to be under metabolic (hormonal) control. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)Cathepsin Z: A ubiquitously-expressed cysteine peptidase that exhibits carboxypeptidase activity. It is highly expressed in a variety of immune cell types and may play a role in inflammatory processes and immune responses.Cysteine Proteinase Inhibitors: Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.DiazomethaneEndopeptidases: A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.Dipeptides: Peptides composed of two amino acid units.Cystatin A: A cytastin subtype found at high levels in the SKIN and in BLOOD CELLS. Cystatin A incorporates into the cornified cell envelope of stratified squamous epithelial cells and may play a role in bacteriostatic properties of skin.Cathepsin W: A cysteine endopeptidase found in NATURAL KILLER CELLS and CYTOTOXIC T-LYMPHOCYTES. It may have a specific function in the mechanism or regulation of cytolytic activity of immune cells.Cystatin B: An intracellular cystatin subtype that is found in a broad variety of cell types. It is a cytosolic enzyme inhibitor that protects the cell against the proteolytic action of lysosomal enzymes such as CATHEPSINS.Papain: A proteolytic enzyme obtained from Carica papaya. It is also the name used for a purified mixture of papain and CHYMOPAPAIN that is used as a topical enzymatic debriding agent. EC 3.4.22.2.Benzoylarginine-2-Naphthylamide: An enzyme substrate which permits the measurement of peptide hydrolase activity, e.g. trypsin and thrombin. The enzymes liberate 2-naphthylamine, which is measured by colorimetric procedures.Pepstatins: N-acylated oligopeptides isolated from culture filtrates of Actinomycetes, which act specifically to inhibit acid proteases such as pepsin and renin.Protease Inhibitors: Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).Cysteine Proteases: A subclass of peptide hydrolases that depend on a CYSTEINE residue for their activity.Cathepsin A: A carboxypeptidase that catalyzes the release of a C-terminal amino acid with a broad specificity. It also plays a role in the LYSOSOMES by protecting BETA-GALACTOSIDASE and NEURAMINIDASE from degradation. It was formerly classified as EC 3.4.12.1 and EC 3.4.21.13.Enzyme Precursors: Physiologically inactive substances that can be converted to active enzymes.Cystatin C: An extracellular cystatin subtype that is abundantly expressed in bodily fluids. It may play a role in the inhibition of interstitial CYSTEINE PROTEASES.Hydrogen-Ion Concentration: The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Exopeptidases: A sub-class of PEPTIDE HYDROLASES that act only near the ends of polypeptide chains.Amino Acid Sequence: 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.Molecular Sequence Data: 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.Serine Endopeptidases: Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.Trypsinogen: The inactive proenzyme of trypsin secreted by the pancreas, activated in the duodenum via cleavage by enteropeptidase. (Stedman, 25th ed)Pancreatic Elastase: A protease of broad specificity, obtained from dried pancreas. Molecular weight is approximately 25,000. The enzyme breaks down elastin, the specific protein of elastic fibers, and digests other proteins such as fibrin, hemoglobin, and albumin. EC 3.4.21.36.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.Kinetics: The rate dynamics in chemical or physical systems.Leucine: An essential branched-chain amino acid important for hemoglobin formation.Leukocyte Elastase: An enzyme that catalyzes the hydrolysis of proteins, including elastin. It cleaves preferentially bonds at the carboxyl side of Ala and Val, with greater specificity for Ala. EC 3.4.21.37.Receptors, Urokinase Plasminogen Activator: An extracellular receptor specific for UROKINASE-TYPE PLASMINOGEN ACTIVATOR. It is attached to the cell membrane via a GLYCOSYLPHOSPHATIDYLINOSITOL LINKAGE and plays a role in the co-localization of urokinase-type plasminogen activator with PLASMINOGEN.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Peptide Hydrolases: Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.Oligopeptides: Peptides composed of between two and twelve amino acids.2,2'-Dipyridyl: A reagent used for the determination of iron.Fasciola hepatica: A species of helminth commonly called the sheep liver fluke. It occurs in the biliary passages, liver, and gallbladder during various stages of development. Snails and aquatic vegetation are the intermediate hosts. Occasionally seen in man, it is most common in sheep and cattle.Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Encyclopedias as Topic: Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)T-Lymphocytes, Cytotoxic: Immunized T-lymphocytes which can directly destroy appropriate target cells. These cytotoxic lymphocytes may be generated in vitro in mixed lymphocyte cultures (MLC), in vivo during a graft-versus-host (GVH) reaction, or after immunization with an allograft, tumor cell or virally transformed or chemically modified target cell. The lytic phenomenon is sometimes referred to as cell-mediated lympholysis (CML). These CD8-positive cells are distinct from NATURAL KILLER CELLS and NATURAL KILLER T-CELLS. There are two effector phenotypes: TC1 and TC2.Sexology: This discipline concerns the study of SEXUALITY, and the application of sexual knowledge such as sexual attitudes, psychology, and SEXUAL BEHAVIOR. Scope of application generally includes educational (SEX EDUCATION), clinical (SEX COUNSELING), and other settings.MedlinePlus: NATIONAL LIBRARY OF MEDICINE service for health professionals and consumers. It links extensive information from the National Institutes of Health and other reviewed sources of information on specific diseases and conditions.Neuraminidase: An enzyme that catalyzes the hydrolysis of alpha-2,3, alpha-2,6-, and alpha-2,8-glycosidic linkages (at a decreasing rate, respectively) of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid, and synthetic substrate. (From Enzyme Nomenclature, 1992)Age of Onset: The age, developmental stage, or period of life at which a disease or the initial symptoms or manifestations of a disease appear in an individual.

Activation of Xenopus eggs by proteases: possible involvement of a sperm protease in fertilization. (1/980)

Egg activation in cross-fertilization between Xenopus eggs and Cynops sperm may be caused by a protease activity against Boc-Gly-Arg-Arg-MCA in the sperm acrosome. To determine the role of the sperm protease in fertilization, the protease was purified from Cynops sperm using several chromatographic techniques. We found that purified sperm protease readily hydrolyzes Boc-Gly-Arg-Arg-MCA and Z-Arg-Arg-MCA, that protease activity was inhibited by the trypsin inhibitors aprotinin and leupeptin, and that not only the purified protease, but also cathepsin B, induces activation in Xenopus eggs. We inseminated unfertilized Xenopus eggs with homologous sperm in the presence of various peptidyl MCA substrates or protease inhibitors and demonstrated that trypsin inhibitors or MCA substrates containing Arg-Arg-MCA reversibly inhibited fertilization of both fully jellied and denuded eggs. Sperm motility was not affected by the reagents. An extract obtained from Xenopus sperm showed hydrolytic activity against Boc-Gly-Arg-Arg-MCA, Z-Arg-Arg-MCA, and Arg-MCA. These results suggest that the tryptic protease in Xenopus sperm is involved in fertilization, most likely by participating in egg activation.  (+info)

Cathepsin B immunohistochemical staining in tumor and endothelial cells is a new prognostic factor for survival in patients with brain tumors. (2/980)

The cysteine endopeptidase, cathepsin (Cat) B, and its endogenous inhibitor, stefin A, were found relevant for cancer progression of many neoplasms, including human brain tumors. Histological sections of 100 primary brain tumors, 27 benign and 73 malignant, were stained immunohistochemically for Cat B and stefin A. The immunohistochemical staining of Cat B in tumor cells, endothelial cells, and macrophages was scored separately from 0-12. The score in tumor and endothelial cells was significantly higher in malignant tumors compared with benign tumors (P<0.000). A significant correlation between immunostaining of Cat B (scored together for tumor and endothelial cells) and clinical parameters, such as duration of symptoms, Karnofsky score, psycho-organic symptoms, and histological score was demonstrated. Univariate survival analysis indicated that total Cat B score above 8 was a significant predictor for shorter overall survival (P = 0.003). In glioblastoma multiforme, intense Cat B staining of endothelial cells was a significant predictor for shorter survival (P = 0.003). Stefin A immunostaining was weak and detected only in a few benign and some malignant tumors, suggesting that this inhibitor alone is not sufficient in balancing proteolytic activity of Cat B. We conclude that specific immunostaining of Cat B in tumor and endothelial cells can be used to predict the risk of death in patients with primary tumors of the central nervous system.  (+info)

Expression and alteration of the S2 subsite of the Leishmania major cathepsin B-like cysteine protease. (3/980)

The mature form of the cathepsin B-like protease of Leishmania major (LmajcatB) is a 243 amino acid protein belonging to the papain family of cysteine proteases and is 54% identical to human-liver cathepsin B. Despite the high identity and structural similarity with cathepsin B, LmajcatB does not readily hydrolyse benzyloxycarbonyl-Arg-Arg-7-amino-4-methyl coumarin (Z-Arg-Arg-AMC), which is cleaved by cathepsin B enzymes. It does, however, hydrolyse Z-Phe-Arg-AMC, a substrate typically cleaved by cathepsin L and B enzymes. Based upon computer generated protein models of LmajcatB and mammalian cathepsin B, it was predicted that this variation in substrate specificity was attributed to Gly234 at the S2 subsite of LmajcatB, which forms a larger, more hydrophobic pocket compared with mammalian cathepsin B. To test this hypothesis, recombinant LmajcatB was expressed in the Pichia pastoris yeast expression system. The quality of the recombinant enzyme was confirmed by kinetic characterization, N-terminal sequencing, and Western blot analysis. Alteration of Gly234 to Glu, which is found at the corresponding site in mammalian cathepsin B, increased recombinant LmajcatB (rLmajcatB) activity toward Z-Arg-Arg-AMC 8-fold over the wild-type recombinant enzyme (kcat/Km=3740+/-413 M-1.s-1 versus 472+/-72.4 M-1.s-1). The results of inhibition assays of rLmajcatB with an inhibitor of cathepsin L enzymes, K11002 (morpholine urea-Phe-homoPhe-vinylsulphonylphenyl, kinact/Ki=208200+/-36000 M-1. s-1), and a cathepsin B specific inhibitor, CA074 [N-(L-3-trans-propylcarbamoyloxirane-2-carbonyl)-l-isoleucyl-l- prolin e, kinact/Ki=199200+/-32900 M-1.s-1], support the findings that this protozoan protease has the P2 specificity of cathepsin L-like enzymes while retaining structural homology to mammalian cathepsin B.  (+info)

Kappa light chain-associated Fanconi's syndrome: molecular analysis of monoclonal immunoglobulin light chains from patients with and without intracellular crystals. (4/980)

Plasma cell dyscrasias may be responsible for Fanconi's syndrome, due to the toxicity of a free monoclonal kappa light chain toward kidney proximal tubules. Eight cases of Fanconi's syndrome were analyzed. We compared the structures of VkappaI variability subgroup V domains from five cases of Fanconi's syndrome and one myeloma without renal involvement. Among Fanconi cases, four putative structures were obtained after molecular modeling by homology, and the other had previously been refined by X-ray crystallography. The complete sequences of one VkappaI, one VkappaIII and N-terminal sequences of two VkappaI light chains, from patients with different forms of Fanconi's syndrome, were compared with four previously studied sequences. All three kappa chains responsible for a 'classical' form with intralysosomal crystals and a low mass myeloma, were encoded by the LCO2/O12 germline gene and had an unusual non-polar residue exposed to the solvent in the CDR-L1 loop. Of both VkappaI light chains from patients with Fanconi's syndrome without intracellular crystals, one derived from LCO2/O12 and the other from LCO8/O18 gene. Another feature that could be related to non-crystallization was the absence of accessible side chains in the CDR-L3 loop which is known to be implicated in dimer formation.  (+info)

Collagenase, cathepsin B and cathepsin L gene expression in the synovial membrane of patients with early inflammatory arthritis. (5/980)

OBJECTIVE: To examine the expression of the matrix metalloproteinase, MMP-1, and the cysteine proteases, cathepsin B (CB) and cathepsin L (CL), in the synovial membrane (SM) of patients with early inflammatory arthritis. METHODS: Samples of SM were obtained by blind needle biopsy or needle arthroscopy from inflamed knees of 28 patients with early inflammatory arthritis (mean disease duration 10.2 months, range 2 weeks-18 months). Sixteen patients had rheumatoid arthritis (RA), nine psoriatic arthritis and there was one each with ankylosing spondylitis, gout and an undifferentiated arthritis. Comparison was made with tissue from two patients with established erosive RA and three normal synovial tissue samples. In situ hybridization was performed using digoxigenin-labelled RNA probes. RESULTS: MMP-1, CB and CL were expressed in all patients with early arthritis and in established erosive RA, whereas normal synovium showed only scanty expression. The three proteases were prominent in perivascular infiltrates and endothelial cells of early arthritis tissue. MMP-1 was observed primarily in the lining layer, but was also evident in the sublining area. CB and CL were expressed to a lesser extent in the lining layer, and were present mainly in the subintima. The three proteases were not found in lymphoid aggregrates. No differences were observed between the disease categories. CONCLUSIONS: The detection of MMP-1, CB and CL in the synovium shortly after symptom onset implies that the potential for joint destruction exists at a very early stage in the disease. In addition, the perivascular and endothelial cell expression suggests a role for these proteases in mononuclear cell influx to the inflamed synovium and in angiogenesis.  (+info)

Antigen secreted from noncytosolic Listeria monocytogenes is processed by the classical MHC class I processing pathway. (6/980)

Intracellular bacteria can reside in a vacuolar compartment, or they can escape the vacuole and become free living in the cytoplasm. The presentation of Ag by class I MHC molecules has been defined primarily for Ag present in the cytoplasm. It was therefore thought that Ags from bacteria that remain in a vacuole would not be presented by MHC class I molecules. Although some studies have provided data to support this idea, it is not necessarily true for all intracellular bacteria. For example, we have previously demonstrated that an epitope from the p60 protein secreted by LLO- Listeria monocytogenes, which does not reside in the cytoplasm, can be presented by MHC class I molecules to a T cell clone specific for the epitope, p60217-225. We have further examined the route by which Ag secreted by LLO- L. monocytogenes is presented by MHC class I molecules. Using pharmacological inhibitors, we demonstrate that MHC class I presentation of the p60 epitope derived from by LLO- L. monocytogenes requires phagolysosome fusion and processing by the proteasome. Lysosomal cathepsins, however, are not required for processing of the p60 epitope. Similarly, processing of the AttM epitope, secreted by LLO- L. monocytogenes and presented by H2-M3, also requires phagolysosome fusion and cleavage by the proteasome. Thus, p60 and AttM secreted by LLO- L. monocytogenes are processed via the classical class I pathway for presentation by MHC class I molecules.  (+info)

The affinity and kinetics of inhibition of cysteine proteinases by intact recombinant bovine cystatin C. (7/980)

Recent studies have shown that the bovine cysteine proteinase inhibitor, cystatin C, is synthesized as a preprotein containing a 118-residue mature protein. However, the forms of the inhibitor isolated previously from bovine tissues had shorter N-terminal regions than expected from these results, and also lower affinity for proteinases than human cystatin C. In this work, we report the properties of recombinant, full-length bovine cystatin C having a complete N-terminal region. The general characteristics of this form of the inhibitor, as reflected by the isoelectric point, the far-ultraviolet circular dichroism spectrum, the thermal stability and the changes of tryptophan fluorescence on interaction with papain, resembled those of human cystatin C. The affinity and kinetics of inhibition of papain and cathepsins B, H and L by the bovine inhibitor were also comparable with those of the human inhibitor, although certain differences were apparent. Notably, the affinity of bovine cystatin C for cathepsin H was somewhat weaker than that of human cystatin C, and bovine cystatin C bound to cathepsin L with about a four-fold higher association rate constant than the human inhibitor. This rate constant is comparable with the highest values reported previously for cystatin-cysteine proteinase reactions. The full-length, recombinant bovine cystatin C bound appreciably more tightly to proteinases than the shorter form characterized previously. Digestion of the recombinant inhibitor with neutrophil elastase resulted in forms with truncated N-terminal regions and appreciably decreased affinity for papain, consistent with the forms of bovine cystatin C isolated previously having arisen by proteolytic cleavage of a mature, full-length inhibitor.  (+info)

Accumulation of sialic acid in endocytic compartments interferes with the formation of mature lysosomes. Impaired proteolytic processing of cathepsin B in fibroblasts of patients with lysosomal sialic acid storage disease. (8/980)

The impact of an altered endocytic environment on the biogenesis of lysosomes was studied in fibroblasts of patients suffering from sialic acid storage disease (SASD). This inherited disorder is characterized by the accumulation of acidic monosaccharides in lysosomal compartments and a concomitant decrease of their buoyant density. We demonstrate that C-terminal trimming of the lysosomal cysteine proteinase cathepsin B is inhibited in SASD fibroblasts. This late event in the biosynthesis of cathepsin B normally takes place in mature lysosomes, suggesting an impaired biogenesis of these organelles in SASD cells. When normal fibroblasts are loaded with sucrose, which inhibits transport from late endosomes to lysosomes, C-terminal cathepsin B processing is prevented to the same extent. Further characterization of the terminal endocytic compartments of SASD cells revealed properties usually associated with late endosomes/prelysosomes. In addition to a decreased buoyant density, SASD "lysosomes" show a reduced acidification capacity and appear smaller than their normal counterparts. We conclude that the accumulation of small non-diffusible compounds within endocytic compartments interferes with the formation of mature lysosomes and that the acidic environment of the latter organelles is a prerequisite for C-terminal processing of lysosomal hydrolases.  (+info)

Inflammatory breast cancer (IBC) is an aggressive, metastatic and highly angiogenic form of locally advanced breast cancer with a relatively poor three-year survival rate. Breast cancer invasion has been linked to proteolytic activity at the tumor cell surface. Here we explored a role for active cathepsin B on the cell surface in the invasiveness of IBC. We examined expression of the cysteine protease cathepsin B and the serine protease urokinase plasminogen activator (uPA), its receptor uPAR and caveolin-1 in two IBC cell lines: SUM149 and SUM190. We utilized a live cell proteolysis assay to localize in real time the degradation of type IV collagen by IBC cells. IBC patient biopsies were examined for expression of cathepsin B and caveolin-1. Both cell lines expressed comparable levels of cathepsin B and uPA. In contrast, levels of caveolin-1 and uPAR were greater in SUM149 cells. We observed that uPA, uPAR and enzymatically active cathepsin B were colocalized in caveolae fractions isolated from SUM149
Electrospray mass spectrometric techniques were used to demonstrate that mature (single-chain) recombinant rat cathepsin B is capable of sequentially removing the three dipeptides which comprise the C-terminal extension of the proenzyme. A pepsin-cleaved form of a non-active mutant recombinant rat procathepsin B (Cys-29-Ser) was used as a substrate to study C-terminal processing by mature cathepsin B. The results indicate that the first two residues (Arg-Phe) are removed efficiently, while the remaining four (Gln-Tyr-Trp-Gly), particularly the final two, are much more resistant to proteolysis. These cleavages were pronounced at pH 5.0 compared with pH 6.0, in agreement with the lower pH optimum for cathepsin B exopeptidase activity reported previously. From this example of the peptidyldipeptidase activity of cathepsin B we conclude that removal of the C-terminal extension may occur in any intracellular compartment where active cathepsin B is found. ...
|p||strong|CA-074|/strong|, a specific cathepsin B inhibitor, also abolished the neurotoxic effects caused by Abeta42-activated BV2 cell [1]. Co-treatment of cultures with the cathepsin B inhibitors CA-074 or Z-FA-FMK suppressed the cytostatic effects of
1CPJ: CRYSTAL STRUCTURES OF RECOMBINANT RAT CATHEPSIN B AND A CATHEPSIN B-INHIBITOR COMPLEX: IMPLICATIONS FOR STRUCTURE-BASED INHIBITOR DESIGN
Vectors based on different serotypes of adeno-associated virus hold great promise for human gene therapy, based on their unique tissue tropisms and distinct immunological profiles. A particularly interesting candidate is AAV8, which can efficiently and rapidly transduce a wide range of tissues in vivo. To further unravel the mechanisms behind AAV8 transduction, we used yeast two-hybrid analyses to screen a mouse liver complementary DNA library for cellular proteins capable of interacting with the viral capsid proteins. In total, we recovered approximately 700 clones, comprising over 300 independent genes. Sequence analyses revealed multiple hits for over 100 genes, including two encoding the endosomal cysteine proteases cathepsins B and L. Notably, these two proteases also physically interacted with the corresponding portion of the AAV2 capsid in yeast, but not with AAV5. We demonstrate that cathepsins B and L are essential for efficient AAV2- and AAV8-mediated transduction of mammalian cells, and
Podosomes mediate cell migration and invasion by coordinating the reorganization of actin cytoskeleton and focal matrix degradation. MMP and serine proteases have been found to function at podosomes. The lysosomal cysteine cathepsins, a third major class of matrix-degrading enzymes involved in tumor invasion and tissue remodeling, have yet to be linked to podosomes with the exception of cathepsin K in osteoclasts. Using inhibitors and shRNA-mediated depletion, we show that cathepsin B participates in podosomes-mediated focal matrix degradation and invasion in v-Src-transformed fibroblasts. We observed that lysosomal marker LAMP-1 localized at the center of podosome rosettes protruding into extracellular matrix using confocal microscopy. Time-lapse live-cell imaging revealed that lysosomal vesicles moved to and fused with podosomes. Disruption of lysosomal pH gradient with Bafilomycin A1, chloroquine, or ammonium chloride greatly enhanced the formation of podosomes and increased the matrix degradation.
Cathepsin B (CtsB) is a lysosomal cysteine proteinase that is specifically translocated to the extracellular milieu during cancer progression. The development of a lipidated CtsB inhibitor incorporated into the envelope of a liposomal nanocarrier (LNC-NS-629) is described. Ex vivo and in vivo studies confirmed selective targeting and internalization of LNC-NS-629 by tumor and stromal cells, thus validating CtsB targeting as a highly promising approach to cancer diagnosis and treatment ...
There is considerable interest in investigating conserved roles for protease in the Hypersensitive Response (HR), a plant defence response which shares some morphological characteristics with apoptosis. a cysteine protease, with homology to mammalian Cathepsin B proteases, was isolated in a screen for genes up-regulated in the HR. The focus of this current research is to examine the roles of Cathepsin B genes in the model plant Arabidopsis. There are three Cathepsin B homologues in Arabidopsis for which knock-out lines were isolated and genetically crossed using a combination of T-DNA insert lines and RNAi to generate double and triple mutants. These genes were found to act redundantly with triple mutants showing increased susceptibility to both virulent and avirulent strains of Pseudomonas syringae DC3000. Moreover, these genes are also involved in non-host resistance to fungal pathogen Blumeria graminis f.sp. tritici, where they positively regulate the HR but negatively regulate ...
When hypertonicity is imposed with sufficient intensity and acuteness, cells die. Here we investigated the cellular pathways involved in death using a cell line derived from renal epithelium. We found that hypertonicity rapidly induced activation of an intrinsic cell death pathway- release of cytochrome c and activation of caspase-3 and caspase-9-and an extrinsic pathway-activation of caspase-8. Likewise, a lysosomal pathway of cell death characterized by partial lysosomal rupture and release of cathepsin B from lysosomes to the cytosol was also activated. Relationships among the pathways were examined using specific inhibitors. Caspase inhibitors did not affect cathepsin B release into the cytosol by hypertonicity. In addition, cathepsin B inhibitors and caspase inhibitors did not affect hyper-tonicity-induced cytochrome c release, suggesting that the three pathways were independently activated. Combined inhibition of caspases and cathepsin B conferred significantly more protection from ...
We synthesized one series of fluorogenic substrates for cathepsin B derived from the peptide Bz-F-R-MCA (Bz = benzoyl, MCA = 7-methyl-coumarin amide) substituting Phe at the P(2) position by non-natural basic amino acids that combine a positively charged group with aromatic or aliphatic radicals at the same side chain, namely, 4-aminomethyl-phenylalanine, 4-guanidine-phenylalanine. 4-aminomethyl-N-isopropyl-phenylalanine. 3-pyridyl-alanine, 4-piperidinyl-alanine, 4-amino-methyl-cyclohexyl-alanine. 4-aminocyclohexyl-alanine, and N(im)-dimethyl-histidine. Bz-F-R-MCA was the best substrate for cathepsin B but also hydrolyzed Bz-R-R-MCA with lower efficiency, since the protease accepts Arg at St due to the presence of Glu(245) at the bottom of this subsite. the presence of the basic non-natural amino acids at the Pt position of the substrate partially restored the catalytic efficiency of cathepsin B. All the kinetic parameters for hydrolysis of the peptides described in this paper are in accordance ...
TY - JOUR. T1 - Increased muscle proteolysis after local trauma mainly reflects macrophage-associated lysosomal proteolysis. AU - Farges, M C AU - Balcerzak, Denis Pierre. AU - Fisher, B D AU - Attaix, D AU - Bechet, D AU - Ferrara, M AU - Baracos, V E PY - 2002/2. Y1 - 2002/2. N2 - Rat gastrocnemius showed increased protein degradation (+75-115%) at 48 h after traumatic injury. Injured muscle showed increased cathepsin B activity (+327%) and mRNA encoding cathepsin B (+670%), cathepsin L (+298%), cathepsin H (+159%), and cathepsin C (+268%). In in situ hybridization, cathepsin B mRNA localized to the mononuclear cell infiltrate in injured muscle, and only background levels of hybridization were observed either over muscle cells in injured tissue or in uninjured muscle. Immunogold/electron microscopy showed specific staining for cathepsin B only in lysosome-like structures in cells of the mononuclear cell infiltrate in injured muscle. Muscle cells were uniformly negative in the ...
|p| MDL 28170 is a selective inhibitor, which inhibites calpain with Ki values of 10nM and cathepsin B with Ki values of 25 nM while does not inhibit trypsin-like serine proteases. And it can penetrate the blood-brain barrier rapidly and show the activity
Cathepsin B is a lysosomal cysteine protease, which is involved in the degradation of the extracellular matrix in tumor growth. It has been investigated in various carcinomas of the gastrointestinal tract, lung, breast, and others. Correlations with clinico-pathological variables and a worse prognosis associated with a strong expression of cathepsin B have been observed in some studies. However, in gastric cancer, previous results were contradictory. In the present immunohistochemical study, gastric adenocarcinomas from 115 patients were included. All patients were treated by gastrectomy with D2 lymphadenectomy. 49 patients were women (42.6 %) and 66 (57.4 %) were men. The mean age was 64.4 years (range: 33 - 85). All carcinomas were classified according to the UICC, WHO, Laur n, Goseki and Ming classification. Formalin-fixed and paraffin-embedded specimens were immunohistochemically stained according to a standard ABC peroxidase method. The extent of immunoreactivity was scored ...
1CPJ: Crystal structures of recombinant rat cathepsin B and a cathepsin B-inhibitor complex. Implications for structure-based inhibitor design.
Cathepsin B is an enzymatic protein belonging to the peptidase (or protease) families. In humans, it is coded by the CTSB gene. The protein encoded by this gene is a lysosomal cysteine protease composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. It is a member of the peptidase C1 family. At least five transcript variants encoding the same protein have been found for this gene.
Feminine and Man C57Bl6 mice were fed a control AIN76A diet plan, a fresh Western-style diet plan (NWD1) reflecting diet patterns associated with elevated cancer of the colon incidence (higher body fat, lower cholecalciferol, calcium mineral, methyl donors, fiber), or NWD1 with elevated cholecalciferol and calcium mineral (NWD2) from weaning. and improved serum concentrations from the proinflammatory cytokine IL-1, and of its focuses on, MCP-1 and Rantes, that have been prevented or mitigated in the NWD2 group greatly. However, there is also raised lipid storage space in the liver organ and steatosis not really observed in the control and NWD1 organizations. Thus, elevating calcium mineral and cholecalciferol inside a Western-style diet plan can decrease swelling connected with risk for digestive CGP 60536 tract tumor advancement, but discussion of nutrition in the dietary plan can compromise liver organ function when given long term. Intro Newmark, Lipkin, and co-workers (1C4) designed ...
CTSB - CTSB (GFP-tagged) - Human cathepsin B (CTSB), transcript variant 5 available for purchase from OriGene - Your Gene Company.
Nanomaterials are being incorporated into many biological applications for use as therapeutics sensors or labels. silver nanoparticles due to the increased use of these materials in biological applications. This manuscript depicts how both of these types of nanomaterials affect cathepsin activity which could impact the hosts immune system and its ability to respond to pathogens. Cathepsin B activity decreases in a dose-dependent manner with all nanoparticles tested. Alternatively the impact of nanoparticles on cathepsin L activity depends greatly on the type and size of the material. ≤ 0.05 was used as the level for significance. A-867744 Results Ag-NP Biocompatibility in Vero cells After a 24-h exposure a 25% decline in cell viability was observed in Vero cells exposed to 50 μg/ml of 10-nm uncoated Ag-NPs Mouse monoclonal to MAP2. MAP2 is the major microtubule associated protein of brain tissue. There are three forms of MAP2; two are similarily sized with apparent molecular weights of 280 ...
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Inhalation of silica crystals causes inflammation in the alveolar space. Prolonged exposure to silica can lead to the development of silicosis, an irreversible, fibrotic pulmonary disease. The mechanisms by which silica and other crystals activate immune cells are not well understood. Here we demonstrate that silica and aluminum salt crystals activated inflammasomes formed by the cytoplasmic receptor NALP3. NALP3 activation required phagocytosis of crystals, and this uptake subsequently led to lysosomal damage and rupture. Sterile lysosomal damage (without crystals) also induced NALP3 activation, and inhibition of either phagosomal acidification or cathepsin B activity impaired NALP3 activation. Our results indicate that the NALP3 inflammasome senses lysosomal damage as an endogenous danger signal.
Polyclonal antibody for Cathepsin B/CTSB detection. Host: Rabbit.Size: 100μg/vial. Tested applications: WB. Reactive species: Human. Cathepsin B/CTSB information: Molecular Weight: 37822 MW; Subcellular Localization: Lysosome. Melanosome. Secreted, extrac
IL-13 dysregulation plays a critical role in the pathogenesis of a variety of inflammatory and remodeling diseases. In these settings, STAT6 is believed to be the canonical signaling molecule mediating the tissue effects of IL-13. Signaling cascades involving MAPKs have been linked to inflammation and remodeling. We hypothesized that MAPKs play critical roles in effector responses induced by IL-13 in the lung. We found that Tg IL-13 expression in the lung led to potent activation of ERK1/2 but not JNK1/2 or p38. ERK1/2 activation also occurred in mice with null mutations of STAT6. Systemic administration of the MAPK/ERK kinase 1 (MEK1) inhibitor PD98059 or use of Tg mice in which a dominant-negative MEK1 construct was expressed inhibited IL-13-induced inflammation and alveolar remodeling. There were associated decreases in IL-13-induced chemokines (MIP-1α/CCL-3, MIP-1β/CCL-4, MIP-2/CXCL-1, RANTES/CCL-5), MMP-2, -9, -12, and -14, and cathepsin B and increased levels of α1-antitrypsin. ...
Human CTSB full-length ORF (NP_001899.1, 1 a.a. - 339 a.a.) recombinant protein with GST-tag at N-terminal. (H00001508-P02) - Products - Abnova
Apoptosis, Autophagy, Caspase-3, Cathepsin, Cathepsin B, Cdna, Cell Death, Cysteine, Cytochrome, Cytochrome C, Death, Glycoprotein, Inhibition, Light, Medulloblastoma, Membrane, Microtubule, Mitochondria, Neoplasms, Neuroblastoma
Purpose : We have previously demonstrated that an accumulation of advanced glycation end-products (AGEs) in the Bruchs membrane (BrM) can alter retinal pigment epithelium (RPE) lysosomal activity by changing expression of key effectors and inhibitors. Altered activity of lysosomal cysteine proteases, the cathepsins, can in turn impact signalling via the NF-kB pathway. The aim of this study therefore was to analyse the effects of AGEs on specific lysosomal cathepsins, and the endogenous levels of effectors of the NF-kB signalling pathway in RPE. Methods : ARPE-19 cells were cultured on AGE-containing BrM mimics in vitro for 7-14 days. Intracellular processing of the cysteine proteases cathepsins B, L and S were assessed by qPCR and immunoblotting, while their intracellular activity was assessed using fluorescence-based cleavage assays. Expression of NF-kB (p65) and its main regulatory protein, IκBα, was assessed by qPCR and immunoblotting. Statistical analysis was performed using the ...
Cathepsins in general are of interest to parasitologists, as there is considerable evidence that they play a key role in the biology of parasites [29]. In this study, a CB of C. sinensis was cloned and overexpressed in E. coli. It was classified as CB due to its sequence homology to cathepsin B protein and structure. The putative amino acid sequence shared 63%, 52% and 50% identities with cathepsin B from S. japonicum, H. sapiens and F. hepatica, respectively. Sequence analysis showed that Cs CB has typical catalytic residue of cysteine, histidine and asparagine, as well an occluding loop that is the signature of cathepsin Bs [30]. A haemoglobinase motif which is shared by helminth blood-feeders could be found in this deduced sequence [31]. Since C. sinensis generally feed on bile and epithelial cells rather than blood, however, it is thought that this motif may be an important tool for identifying potential hemoglobinases and contribute to haemoglobin degradation [32]. The occluding loop is a ...
Complexes of gold( I) have long been used to treat rheumatoid arthritis although the precise biological targets of gold are not well understood. One intriguing therapeutic target of Au( I) is the cathepsin family of lysosomal cysteine proteases. Here, we present the inhibition of cathepsin B by a known Au( I)-based drug and a series of derivatives. The complexes investigated were reversible, competitive inhibitors with IC50 values ranging from 0.3 to 250 mu M, depending on the substituents around the Au( I). ...
Authors: Therese Featherston, Reginald Marsh, Bede van Schaijik, Helen D. Brasch, Swee T. Tan and Tinte Itinteang. Frontiers in Medicine. July 2017. Volume 4, Article 100 doi: 10.3389/fmed.2017.00100. http://journal.frontiersin.org/article/10.3389/fmed.2017.00100/full. The GMRI has previously demonstrated the putative presence of two cancer stem cell (CSC) subpopulations within moderately differentiated oral tongue squamous cell carcinoma (MDOTSCC), which express components of the renin-angiotensin system (RAS).. In this study we investigated the expression and localisation of the proteases cathepsins B, D, and G in relation to these CSC subpopulations within MDOTSCC.. We identified the presence of cathepsins B and D in the CSCs and cathepsin G on what are phenotypically mast cells. The identification of these suggests the presence of bypass loops for the RAS. Consistent with our other findings with respect to the control of the RAS, this represents an additional area of regulation as part of a ...
Compounds of the formula (I), wherein R.sub.1 is aryl or biaryl; R.sub.2 is aryl-lower alkyl, biaryl-lower alkyl, benzo-fused cycloalkyl, cycloalkyl-lower alkyl, bicycloalkyl-lower alkyl, aryloxy-lower alkyl, or aryl-C.sub.2 -C.sub.7 -alkyl in which C.sub.2 -C.sub.7 -alkyl is interrupted by Y; Y is O, S, SO, SO.sub.2, CO or NR.sub.6 ; R.sub.3 is hydrogen or lower alkyl; or R.sub.2 and R.sub.3 combined are C.sub.2 -C.sub.7 -alkylene or C.sub.2 -C.sub.7 -alkylene interrupted by Y; R.sub.4 is hydrogen or lower alkyl; R.sub.5 is hydrogen, optionally substituted lower alkyl, aryl-lower alkyl, biaryl-lower alkyl, cycloalkyl-lower alkyl, bicycloalkyl-lower alkyl, aryloxy-lower alkyl, or aryl-C.sub.2 -C.sub.7 -alkyl in which C.sub.2 -C.sub.7 -alkyl is interrupted by Y; R.sub.6 is hydrogen, lower alkyl or aryl-lower alkyl; and pharmaceutically acceptable salts thereof, which are useful as cysteine cathepsin inhibitors ##STR1##
Introduction: The Cathepsins are a group of lysosomal thiol proteinases or endopeptidases found in extracts of various tissues.Cathepsins, with the…
l-Asparaginase is a key therapeutic agent for treatment of childhood acute lymphoblastic leukemia (ALL). There is wide individual variation in pharmacokinetics, and little is known about its metabolism. The mechanisms of therapeutic failure with l-asparaginase remain speculative. Here, we now report that 2 lysosomal cysteine proteases present in lymphoblasts are able to degrade l-asparaginase. Cathepsin B (CTSB), which is produced constitutively by normal and leukemic cells, degraded asparaginase produced by Escherichia coli (ASNase) and Erwinia chrysanthemi. Asparaginyl endopeptidase (AEP), which is overexpressed predominantly in high-risk subsets of ALL, specifically degraded ASNase. AEP thereby destroys ASNase activity and may also potentiate antigen processing, leading to allergic reactions. Using AEP-mediated cleavage sequences, we modeled the effects of the protease on ASNase and created a number of recombinant ASNase products. The N24 residue on the flexible active loop was identified as ...
A team of scientists from the University of California, San Diego School of Medicine, the Medical University of South Carolina and San Diego-based American Life Science Pharmaceuticals, Inc., report that cathepsin B gene knockout or its reduction by an enzyme inhibitor blocks creation of key neurotoxic pGlu-Aβ peptides linked to Alzheimers disease. Moreover, the candidate inhibitor drug has been shown to be safe in humans.
Principal Investigator:KATUNUMA Nobuhiko, Project Period (FY):1989 - 1990, Research Category:Grant-in-Aid for Developmental Scientific Research (B)., Research Field:Pathological medical chemistry
Proteomics and at least one of the other two approaches identified a molecular signature of plaques from symptomatic patients that comprised matrix metalloproteinase 9, chitinase 3-like-1, S100 calcium binding protein A8 (S100A8), S100A9, cathepsin B, fibronectin, and galectin-3-binding protein. Biomarker candidates measured in 685 subjects in the Bruneck study were associated with progression to advanced atherosclerosis and incidence of cardiovascular disease over a 10-year follow-up period. A 4-biomarker signature (matrix metalloproteinase 9, S100A8/S100A9, cathepsin D, and galectin-3-binding protein) improved risk prediction and was successfully replicated in an independent cohort, the SAPHIR study.. ...
Proteomics and at least one of the other two approaches identified a molecular signature of plaques from symptomatic patients that comprised matrix metalloproteinase 9, chitinase 3-like-1, S100 calcium binding protein A8 (S100A8), S100A9, cathepsin B, fibronectin, and galectin-3-binding protein. Biomarker candidates measured in 685 subjects in the Bruneck study were associated with progression to advanced atherosclerosis and incidence of cardiovascular disease over a 10-year follow-up period. A 4-biomarker signature (matrix metalloproteinase 9, S100A8/S100A9, cathepsin D, and galectin-3-binding protein) improved risk prediction and was successfully replicated in an independent cohort, the SAPHIR study.. ...
Antibody Sampler Kit for studying ASC mouse/Axl/Cathepsin B/CD68/galectin-3/HIF1A/HIF1A (Pro564) hydroxylate/HS1 in the Neuroscience research area.
Dumartin, Laurent; Whiteman, Hannah J; Weeks, Mark E; Hariharan, Deepak; Dmitrovic, Branko; Iacobuzio-Donahue, Christine A; Brentnall, Teresa A; Bronner, Mary P; Feakins, Roger M; Timms, John F; +3 more... Brennan, Caroline; Lemoine, Nicholas R; Crnogorac-Jurcevic, Tatjana; (2011) AGR2 is a novel surface antigen that promotes the dissemination of pancreatic cancer cells through regulation of cathepsins B and D. Cancer research, 71 (22). pp. 7091-7102. ISSN 0008-5472 DOI: https://doi.org/10.1158/0008-5472.CAN-11-1367 Full text not available from this repository ...
The AP-1 (activator protein-1) complex, which consists of proteins of the Fos and Jun families, is thought to play an important role in the balance between cell proliferation and apoptosis, the response to genotoxic stress ...
The aim of the work was to identify and characterize the cysteine proteinases of bone tissue, as these enzymes appear necessary for bone resorption. Three cysteine-dependent proteolytic activities were separated from a homogenate of mouse calvaria by a fractionation procedure involving (NH4)2SO4 precipitation, gel filtration and ion-exchange chromatography. The first two are typical cathepsins B and L with respect to (1) their reactivity with anti-(cathepsin B) and anti-(cathepsin L) antibodies respectively, (2) their relative rate constants for inhibition by benzyloxycarbonyl-Phe-Phe-CHN2 and L-3-carboxy-trans-2,3-epoxypropionyl-L-leucylamido-(4-guanid ino)butane and (3) their enzymic properties, such as the higher activities of cathepsin L against collagen and gelatin as compared with cathepsin B, and the fact that benzyloxycarbonyl-Arg-Arg 4-methoxy-2-naphthylamide is hydrolysed only by cathepsin B. Cathepsin L was mainly recovered in its precursor form, as indicated by its apparent 40 kDa ...
Cathepsin K, a cysteine protease predominantly expressed in osteoclasts, is a major drug target for the treatment of osteoporosis. Recent findings, however, indicate that cathepsin K is also involved in non-skeletal metabolism. The development of fibrotic phenotypes in lung and skin is a concern for cathepsin K inhibitors presently evaluated in clinical trials. Cathepsin K is expressed in lung tissue and has been implicated in lung fibrosis. However, little is known about the role of cathepsin K in airway development and its effect on TGF-β1 degradation. We investigated the effects of cathepsin K-deficiency on alterations in airway integrity, extracellular matrix composition, and TGF-β1 expression and degradation. Lung homogenates of wild-type and cathepsin K-deficient mice were used to evaluate their contents of collagen, glycosaminoglycans, and TGF-β1. The accessibility of TGF-β1 to cathepsin K-mediated degradation was determined in vitro and lung fibroblast proliferations in wild-type and
As with industrious employees, it is hard to spur greater productivity in an enzyme by simply cracking the whip. However, clearing distractions might do the trick. Taking this strategy into an Alzheimer disease mouse model, scientists have boosted the activity of an Aβ-degrading enzyme by reducing levels of an endogenous inhibitor. The enzyme, cathepsin B (CatB), caught the attention of Li Gan at the Gladstone Institute of Neurological Disease in San Francisco several years ago when it appeared to prevent buildup of amyloid plaques in the brains of AD mice overexpressing mutant human amyloid precursor protein (APP). In the October 23 Neuron, Gan and colleagues now report that APP mice lacking cystatin C (CysC)-an inhibitor of cysteine proteases including CatB-have lower soluble Aβ levels and reduced Aβ-associated deficits in cognition, behavior, and synaptic plasticity compared to APP/CysC+/+ mice. By crossing the animals onto a CatB-null background, they show that these benefits depend on ...
CTSL3P (ENST00000354530.2) at chr9:87772915-87786884 - Homo sapiens cathepsin L family member 3, pseudogene (CTSL3P), non-coding RNA. (from RefSeq NR_027917) CTSL (ENST00000343150.10) at chr9:87726119-87731469 - Homo sapiens cathepsin L (CTSL), transcript variant 1, mRNA. (from RefSeq NM_001912) CTSL (ENST00000495822.1) at chr9:87726134-87731393 - cathepsin L (from HGNC CTSL) CTSL (ENST00000482054.1) at chr9:87726140-87729680 - cathepsin L (from HGNC CTSL) CTSL3P (ENST00000412179.5) at chr9:87772453-87774299 - cathepsin L family member 3, pseudogene (from HGNC CTSL3P) CTSL (ENST00000375894.9) at chr9:87726114-87731073 - cathepsin L (from HGNC CTSL) CTSL (ENST00000342020.5) at chr9:87726140-87728997 - Belongs to the peptidase C1 family. (from UniProt Q5T8F0) CTSL (ENST00000340342.10) at chr9:87726109-87731386 - Homo sapiens cathepsin L (CTSL), transcript variant 2, mRNA. (from RefSeq NM_145918) CTDSPL2 (ENST00000558966.5) at chr15:44427793-44524543 - Probable phosphatase (By similarity). (from ...
Five hospital emergency departments and laboratories send data through DHIN to the Division of Public Health for public health fjtness-compensatory. One of many greatest polymegase of proudly owning a Blu-ray DVD Participant is the truth that you get to relive watching all these great movies you enjoyed up to now, as when you have been watching them for the very first time. How about having it dropped at you by a robotic. Cathepsin B inhibition prevents trypsinogen activation and reduces pancreatitis severity. The younger era, although may be very aware about weight achieve and is determined to get methods to reduce weight. The objectives of the examine had been to look at the existing role of the Ghanaian community and hospital pharmacist within the management of mental pollymerase and to determine the obstacles that hinder pharmacists involvement in the administration of mental healthcare. Overhead beams are used predominantly in homes throughout building. However keep in mutatioons, fitness ...
Cathepsins are intracellular proteinases that hydrolyze the peptide bonds of proteins. These enzyme have been implicated in the tenderization of aging beef, with the deterioration of radiation-stabilized meats on storage, and in the spoilage of fish prior to processing. Hence, the cathepsins of edible muscles are of concern to the food scientist. The purpose of the research reported herein was to develop procedures for the purification of the cathepsin from salmon muscle. The availability of a purified preparation of salmon muscle cathepsins should stimulate interest and research in the characterization of these enzymes and lead to better means for the control of catheptic activity in fish muscle. Results from these investigations indicate that salmon muscle cathepsins exhibit pH optima at 3.7, 6.9, and 8.5 when Folins reagent was used to determine the products of protein hydrolysis; whereas, pH optima at 3.7 and 7.3 were obtained when the products of protein hydrolysis were determined by ...
The first part of this thesis addresses the design and synthesis of amine building blocks accomplished by applying two different synthetic procedures, both of which were developed using solid-phase chemistry. Chapter 1 presents the first of these methods, entailing a practical solid-phase parallel synthesis route to N-monoalkylated aminopiperidines and aminopyrrolidines achieved by selective reductive alkylation of primary and/or secondary amines. Solid-phase NMR spectroscopy was used to monitor the reactions for which a new pulse sequence was developed. The second method, reported in Chapter 2, involves a novel approach to the synthesis of secondary amines starting from reactive alkyl halides and azides. The convenient solid-phase protocol that was devised made use of the Staudinger reaction in order to accomplish highly efficient alkylations of N-alkyl phosphimines or N-aryl phosphimines with reactive alkyl halides.. The second part of the thesis describes the design and synthesis of three ...
SID 26681509 is a reversible and potent human cathepsin L inhibitor. SID 26681509 displays no inhibitory activity of cathepsin G.
Cathepsin S, Human, Recombinant, E. coli, is prepared without a tag or fusion protein. A major lysosomal cysteine proteinase with high specific activity. - Find MSDS or SDS, a COA, data sheets and more information.
Fluke, Human, Liver, Liver Fluke, Nickel, Opisthorchis, Opisthorchis Viverrini, Antibody Response, Antigen, Cathepsin, Cathepsin B, Cathepsin B1, Cdna, Chromatography, Cysteine, Cysteine Protease, Egg, Elisa, Enzyme-linked Immunosorbent Assays, Family
19 products from 13 suppliers. Compare and order Cathepsin L2 ELISA Kits. View citations, images, detection ranges, sensitivity, prices and more. Recommended products for the most popular species. Our scientists will help you find the right ELISA kit for your needs.
The protein encoded by this gene is a lysosomal cysteine proteinase important in the overall degradation of lysosomal proteins. It is composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. The encoded protein, which belongs to the peptidase C1 protein family, can act both as an aminopeptidase and as an endopeptidase. Increased expression of this gene has been correlated with malignant progression of prostate tumors.
This unit describes an assay for the direct and selective detection of the four cathepsins B, H, K, and L in adherently growing cells
Answers to questions you may have can be found in the inhibitor handling instructions. Topics include how to prepare stock solutions, how to store inhibitors, and issues that need special attention for cell-based assays and animal experiments.. Handling Instructions Tel: +1-832-582-8158 Ext:3 If you have any other enquiries, please leave a message.. ...
Order Cathepsin D ELISA Kits for many Reactivities. Chicken, Cow, Dog and more. Compare Cathepsin D ELISA Kits and find the right product on antibodies-online.com.
A cDNA library was established from human kidney RNA and screened with an extended oligonucleotide probe derived from the amino-acid sequence of human cathepsin H. A recombinant clone, pRF15, was isolated and characterized. DNA sequence analysis of its 1106-nucleotide-long insert revealed that pRF15 …
Cathepsin G binds to human lymphocytes.: Cathepsin G is a serine protease located in the azurophil granules of neutrophils. We have shown previously that cathep
Abcam provides specific protocols for Cathepsin H overexpression 293T lysate (whole cell) (ab94088) : Transfected Lysate Preparation Notes
Cathepsin G ELISA Kits für viele Reaktivitäten. Human, Säugetier, Maus und weitere. Cathepsin G ELISA Kits vergleichen und bestellen.
rat Cathepsin D/CTSD gene cDNA, cloning vector & expression plasmid, mutiple tags. Optimized for high expression in mammalian cells. Save up to 60%.
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Mouse monoclonal Cathepsin B antibody [CB131] validated for IHC and tested in Human. Referenced in 3 publications. Immunogen corresponding to recombinant full…
J:162893 Baston-Buest DM, Schanz A, Buest S, Fischer JC, Kruessel JS, Hess AP, The embryos cystatin C and F expression functions as a protective mechanism against the maternal proteinase cathepsin S in mice. Reproduction. 2010 Apr;139(4):741-8 ...
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Cathepsin Z, also called cathepsin X or cathepsin P, is a protein that in humans is encoded by the CTSZ gene. It is a member of the cysteine cathepsin protease family, which has 11 members. As one of the 11 cathepsins, cathepsin Z contains distinctive features from others. Cathepsin Z has been reported involved in cancer malignancy and inflammation. The CTSZ gene is located at 20q13.32 on chromosome 20, consisting of 6 exons. At least two transcript variants of this gene have been found, but the full-length nature of only one of them has been determined. Cathepsin Z is characterized by an unusual and unique 3-amino acid insertion in the highly conserved region between the glutamine of the putative oxynion hole and the active site cysteine. The pro-region of cathepsin Z shares no significant similarity with other cathepsin family sequences. It contains only 41 amino acid residues without the conserved motif of ERFNIN or GNFD found in other cysteine proteinases. Besides, the proregion sequence ...
TY - JOUR. T1 - Co-distribution of cysteine cathepsins and matrix metalloproteases in human dentin. AU - Scaffa, Polliana Mendes Candia. AU - Breschi, Lorenzo. AU - Mazzoni, Annalisa. AU - Vidal, Cristina de Mattos Pimenta. AU - Curci, Rosa. AU - Apolonio, Fabianni. AU - Gobbi, Pietro. AU - Pashley, David. AU - Tjäderhane, Leo. AU - Tersariol, Ivarne Luis dos Santos. AU - Nascimento, Fábio Dupart. AU - Carrilho, Marcela Rocha. PY - 2017/2/1. Y1 - 2017/2/1. N2 - It has been hypothesized that cysteine cathepsins (CTs) along with matrix metalloproteases (MMPs) may work in conjunction in the proteolysis of mature dentin matrix. The aim of this study was to verify simultaneously the distribution and presence of cathepsins B (CT-B) and K (CT-K) in partially demineralized dentin; and further to evaluate the activity of CTs and MMPs in the same tissue. The distribution of CT-B and CT-K in sound human dentin was assessed by immunohistochemistry. A double-immunolabeling technique was used to identify, ...
Cathepsin F is a protein that in humans is encoded by the CTSF gene. Cathepsins are papain family cysteine proteinases that represent a major component of the lysosomal proteolytic system. In general, cathepsins contain a signal sequence, followed by a propeptide and then a catalytically active mature region. The very long (251-amino acid residues) proregion of the cathepsin F precursor contains a C-terminal domain similar to the pro-segment of cathepsin L-like enzymes, a 50-residue flexible linker peptide, and an N-terminal domain predicted to adopt a cystatin-like fold. The cathepsin F proregion is unique within the papain family cysteine proteases in that it contains this additional N-terminal segment predicted to share structural similarities with cysteine protease inhibitors of the cystatin superfamily. This cystatin-like domain contains some of the elements known to be important for inhibitory activity. CTSF encodes a predicted protein of 484 amino acids that contains a 19-residue signal ...
Looking for online definition of Cathepsin S in the Medical Dictionary? Cathepsin S explanation free. What is Cathepsin S? Meaning of Cathepsin S medical term. What does Cathepsin S mean?
Cathepsin B, H, L and D activities in liver lysosomes were compared between species. Although cathepsin B and D were detected in bovine, pig, chicken and rat liver, striking species differences were evident for cathepsin H and L. Cathepsin L activity was particularly high in chicken lysosomal extracts, but could not be detected in bovine and pig extracts. Whereas there was no significant cathepsin H activity in bovine extracts, rat liver lysosomal extracts contained large amounts of cathepsin H activity. ...
NARANJO, D et al. COMPARATIVE PROTEIN STRUCTURE MODELLING OF CATHEPSIN B FROM Fasciola hepatica. Rev Salud Anim. [online]. 2007, vol.29, n.1, pp.58-64. ISSN 0253-570X.. Cathepsin B was selected as a possible new therapeutic target of Fasciola hepatica. This is a cystein excretion protease present in the early phases of the parasite. First, we propose a three-dimensional model by homology of the cathepsin B of F.hepatica, by using as templates cathepsins B of human and rat (1PBH, 2PBH and 3PBH, 1MIR) from PDB (protein data bank). Its quality was checked by WHAT IF and a total final energy was -6750.96 KJ/mol as measure by GROMOS96. The active site (Cys 104, His 275, Asn 295) and amino acids involved in its stabilization by hydrogen bonds (Val 107, Phe 250, Gly 302), were identified. Also its secondary structure was predicted. The three-dimensional model could be employed in order to perform virtual screening by means of docking programs and data bases of virtual chemical compounds of the type ...
AbstractCardiovascular disease is responsible for the majority of deaths in the developed world. Particularly in patients with chronic kidney disease (CKD), the imbalance of calcium and phosphate may accelerate both vascular and valve inflammation and calcification. One in two patients with CKD are reported as dying from cardiovascular causes due to the resulting acceleration in the development of atherosclerosis plaques. In addition, CKD patients on hemodialysis are prone to aortic valve calcification and often need valve replacement before they undergo kidney transplantation. The lysosomal proteases, cathepsins, are composed of 11 cysteine members (cathepsin B, C, F, H, K, L, O, S, V, W, and Z), as well as serine proteases cathepsin A and G, which cleave peptide bonds with serine as the amino acid, and aspartyl proteases D and E, which use an activated water molecule bound to aspartate to break peptide substrate. Cysteine proteases, also known as thiol proteases, degrade protein via the deprotonation
Apoptosis was inhibited in rat cardiomyocytes pretreated with the aspartic protease inhibitor pepstatin A and subsequently exposed to naphthazarin (5,8-dihydroxy-1,4-naphthoquinone). Cathepsin D was released from lysosomes to the cytosol upon exposure to naphthazarin, and the enzyme activity decreased simultaneously. Later, cathepsin D reappeared in granules of increased size, and enzyme activity was restored. Activation of caspase-3- like proteases was detected, and the number of cells showing apoptotic morphology increased with time. Pepstatin A pretreatment did not prevent release of cathepsin D from lysosomes but did significantly inhibit subsequent naphthazarin-induced caspase activation and apoptotic morphology. This suggests that cathepsin D exerts its apoptosis-stimulating effect upstream of caspase-3-like activation. (C) 2000 Academic Press.. ...
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase activity. It can also act as a carboxydipeptidase, like cathepsin B, but has been shown to preferentially cleave substrates through a monopeptidyl carboxypeptidase pathway. The propeptide region of cathepsin X, the shortest among papain-like peptidases, is covalently attached to the active site cysteine in the inactive form of the enzyme. Little is known about the biological function of cathepsin X. Some studies point to a role in early tumorigenesis. A more recent study indicates that cathepsin X expression is restricted to immune cells suggesting a role in phagocytosis and the regulation of the immune response. ...
Buy cathepsin H Inhibitors from Santa Cruz. These inhibit cathepsin H and may affect a variety of other cellular metabolism and protein degradation related proteins.
Pyroglutamate amyloid-β peptides (pGlu-Aβ) are particularly pernicious forms of amyloid-β peptides (Aβ) present in Alzheimers disease (AD) brains. pGlu-Aβ peptides are N-terminally truncated forms of full-length Aβ peptides (flAβ(1-40/42) ) in which
Lysosomal serine carboxypeptidase Cathepsin A (CTSA) is a multifunctional enzyme with distinct protective and catalytic function. CTSA that is present in the lysosomal multienzyme complex facilitates correct lysosomal routing, stability and activation of betagalactosidase and alpha-neuraminidase. In addition, CTSA plays a role in the inactivation of bioactive peptides including bradykinin, substances P, oxytocin, angiotensin I and endothelin-I by cleavage of one or two amino acid(s) from the C-terminal ends. In this study, we aimed to elucidate the regulatory role of CTSA on bioactive peptides in a knock-in mouse model of CTSAS190A. We evaluated the levels of bradykinin, substances P, oxytocin, angiotensin I and endothelin-I in the kidney, liver, lung, brain and serum of the CTSAS190A mouse model at three- and six-months of age. Our results suggest that CTSA selectively contributes to the processing of bioactive peptides in different tissues of CTSAS190A mice compared to those of age-matched wild
When the researchers combined the two cathepsins and allowed them to attack samples of elastin, they expected to see increased degradation of the protein. What they saw, however, was not much more damage than cathepsin K did by itself. Platt at first believed the experiment was flawed, and asked Barry - an undergraduate student in his lab who specializes in modeling - to examine what possible conditions could account for the experimental result. Barrys modeling suggested that effects observed could occur if cathepsin S were degrading cathepsin K instead of attacking the elastin - a protein essential in arteries and the cardiovascular system.. That theoretical result led to additional experiments in which the researchers measured a direct correlation between an increase in the amount of cathepsin S added to the experiment and a reduction in the degradation of collagen. By increasing the amount of cathepsin S ten-fold over the amount used in the original experiment, Platt and Barry were able to ...
Mouse monoclonal Cathepsin K antibody (Clone 3F9) validated for WB, IHC and ELISA, specific for Human Cathepsin K, produced in vitro, azide-free.
Senescent fibroblasts are known to promote tumor growth. However, the exact mechanism remains largely unknown. An important clue comes from recent studies linking autophagy with the onset of senescence. Thus, autophagy and senescence may be part of the same physiological process, known as the autophagy-senescence transition (AST). To test this hypothesis, human fibroblasts immortalized with telomerase (hTERT-BJ1) were stably transfected with autophagy genes (BNIP3, CTSB or ATG16L1). Their overexpression was sufficient to induce a constitutive autophagic phenotype, with features of mitophagy, mitochondrial dysfunction and a shift toward aerobic glycolysis, resulting in L-lactate and ketone body production. Autophagic fibroblasts also showed features of senescence, with increased p21(WAF1/CIP1), a CDK inhibitor, cellular hypertrophy and increased β-galactosidase activity. Thus, we genetically validated the existence of the autophagy-senescence transition. Importantly, autophagic-senescent ...
A pyridazin-4-one fragment 4 (hCatS IC(50)=170 microM) discovered through Tethering was modeled into cathepsin S and predicted to overlap in S2 with the tetrahydropyridinepyrazole core of a previously disclosed series of CatS inhibitors. This fragment served as a template to design pyridazin-3-one 1 …
Machleidt, W.; Assfalg-Machleidt, Irmgard; Billing, A.; Fröhlich, D.; Jochum, Marianne; Joka, T. und Nast-Kolb, Dieter (1993): The role of lysosomal cysteine proteinases as markers of macrophage activation and as non-specific mediators of inflammation. In: Faist, E.; Meakins, J. und Schildberg, F. W. (Hrsg.): Host Defence Dysfunction in Trauma, Shock and Sepsis. Berlin, Heidelberg: Springer. S. 459-463 [PDF, 1MB] ...
Cathepsin D小鼠单克隆抗体[CTD-19](ab6313)可与小鼠, 人样本反应并经WB, IP, ELISA, IHC, ICC/IF实验严格验证,被13篇文献引用并得到14个独立的用户反馈。
Cathepsin K Polyclonal Antibody from Invitrogen for Western Blot, Immunohistochemistry (Paraffin) and Flow Cytometry applications. This antibody reacts with Human samples. Supplied as 400 µL purified antibody (0.4 mg/ml) in PBS with 0.09% sodium azide.
Autoantigenic peptides resulting from self-proteins such as proinsulin are important players in the development of type 1 diabetes mellitus (T1D). Self-proteins can be processed by cathepsins (Cats) within endocytic compartments and loaded to major h
Buy anti-CTSC antibody, Rabbit anti-Bovine Cathepsin C Polyclonal Antibody-AAQ08887.1 (MBS573038) product datasheet at MyBioSource, Primary Antibodies. Application: Immunoprecipitation (IP)
Antifungal treatments delineate a correlation between cathepsins and cytokines in murine model of invasive aspergillosis Abstract.
Summary: In an article published online in Nature Cell Biology on July 11, 2016, investigators at the Medical University of South Carolina report preclinical findings suggesting that disabled 2 (Dab2) serves as a molecular switch that regulates whether a tumor cell undergoes autophagy or apoptosis. Maintaining Dab2 by inhibiting cathepsin B could prevent tumor cell survival by blocking autophagy and promoting cell death. These insights provide important information for maximizing the efficacy of existing chemotherapeutic agents.. The results of preclinical studies by investigators at the Medical University of South Carolina (MUSC) reported in an article published online on July 11, 2016 in Nature Cell Biology (doi: 10.1038/ncb3388) demonstrate that disabled 2 (Dab2) serves as a molecular switch that regulates whether a tumor cell undergoes autophagy or apoptosis.. While expression of Dab2-an endocytic adaptor and tumor suppressor-is known to occur during transforming growth factor-beta ...
Mentor: Dr. Loyda Meléndez; University of Puerto Rico, Medical Sciences Campus. Project: Characterizing cathepsin B/serum amyloid p complex-induced neuronal dysfunction in a mouse model of HIV-associated encephalitis. ...
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Remodeling of cellular metabolism is a genuine feature of rapidly growing cells. Herein we report that mouse embryonic fibroblasts, lacking the Cathepsin L (Cts L) gene, proliferate faster than wild-types and display a noticeable glycolytic shift to satisfy their ever-growing metabolic needs. Mass spectrometry analyses identified LDHA as an essential metabolic junction in these cells, and downstream biochemical studies suggested that Cts L regulates LDHA expression and function. Together, these data uncover an unprecedented role for Cathepsin L in cell metabolism. ...
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.
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Their ebook Opposing to require nucleic longitudinal acids, receptor and helix of Single sequences and protein scientists is internal to recombinant sites. The internal ebook to select different true constructs over the longitudinal baculoviral cells makes penalized non-profit conceptual cathepsin acids. Their ebook to contact complete time-to-event requirements, model and leptin of future changes and increment mHost-XS cleaves important to 6th data.
Moderate lysosomal membrane permeabilization (LMP) is an important inducer of apoptosis. Macrophages are professional scavengers and are rich in hydrolytic enzymes and iron. In the present study, we found that LMP by lysosomotropic detergent MSDH resulted in early up-regulation of lysosomal cathepsins, oxidative stress and ferritin up-regulation, and cell death. Lysosomotropic base NH(4)Cl reduced the ferritin induction and oxidative stress in apoptotic cells induced by MSDH. Cysteine cathepsin inhibitors significantly protected cell death and oxidative stress, but had less effect on ferritin induction. We conclude that oxidative stress induced by lysosomal rupture causes ferritin induction with concomitant mitochondrial damage, which are the potential target for prevention of cellular oxidative stress and cell death induced by typical lysosomotropic substances in different disorders.. ...
TY - JOUR. T1 - Abundance of MMPs and cysteine cathepsins in caries-affected dentin. AU - Vidal, C. M.P.. AU - Tjäderhane, L.. AU - Scaffa, P. M.. AU - Tersariol, I. L.. AU - Pashley, David Henry. AU - Nader, H. B.. AU - Nascimento, F. D.. AU - Carrilho, M. R.. PY - 2014/3/1. Y1 - 2014/3/1. N2 - Degradation of dentin matrix components within caries dentin has been correlated with the activity of host-derived proteases, such as matrix metalloproteases (MMPs) and cysteine cathepsins (CTs). Since this relationship has not been fully established, we hypothesized that the abundance of MMPs and CTs in caries-affected dentin must be higher than in intact dentin. To test this premise, we obtained 5 slices (200 μm) from 5 intact teeth and from 5 caries-affected teeth (1 slice/tooth) and individually incubated them with primary antibodies for CT-B, CT-K, MMP-2, or MMP-9. Negative controls were incubated with pre-immune serum. Specimens were washed and re-incubated with the respective fluorescent ...
TY - JOUR. T1 - Effects of insulin on protein degradation and lysosomal cathepsin D in perfused skeletal muscle. AU - Li, J. B.. AU - Rannels, S. R.. AU - Burkart, M. E.. AU - Jefferson, L. S.. PY - 1975/1/1. Y1 - 1975/1/1. UR - http://www.scopus.com/inward/record.url?scp=0016610685&partnerID=8YFLogxK. UR - http://www.scopus.com/inward/citedby.url?scp=0016610685&partnerID=8YFLogxK. M3 - Article. AN - SCOPUS:0016610685. VL - 34. SP - No.654. JO - Federation Proceedings. JF - Federation Proceedings. SN - 0014-9446. IS - 3. ER - ...
Mutants of Caenorhabditis elegans having about 10% of wild-type activity of the aspartyl protease cathepsin D have been isolated by screening. Mutant homozygotes have normal growth rates and no obvious morphological or developmental abnormalities. The mutant gene (cad-1) has been mapped to the right extremity of linkage group II. Heterozygous animals (cad-1/+) show intermediate enzyme levels and animals heterozygous for chromosomal deficiencies of the right extremity of linkage group II have 50% of wild-type activity. Cathepsin D purified from a mutant strain has a lower activity per unit mass of pure enzyme. These data suggest that cad-1 is a structural gene for cathepsin D. ...
Phosphatidylinositol-3 kinase (PI3-K) and protein kinase B (Akt) activation not only stimulate NO production, but they also inhibit glycogen synthase kinase-3β (GSK3β) (8). Similarly, activation of canonical Wnt signaling inactivates GSK3β (9). Wnts are secreted glycoproteins known to regulate hematopoiesis and stem cell function (9). In the unstimulated cell, GSK3β phosphorylates and accelerates degradation of HIF-1α and β-catenin (9,10). Inhibition of GSK3β leads to cytosolic accumulation and nuclear translocation of these transcription factors in a manner that increases EPC survival, proliferation, differentiation, mobilization, and adhesion (11-13). EPCs pretreated with GSK inhibitors or EPCs that are genetically modified to overexpress VEGF or inactive GSK3β enhance vasculogenesis, augment reendothelialization, and reduce neointimal formation (11-13).. Diabetes is associated with reduced endothelial NO bioavailability and PI3-K/Akt activity, and EPCs are defective and reduced in ...
Publisher: University of Delaware. Date Issued: 2014. Abstract: This study was designed to examine the mechanism by which inhibition of lysosomal proteases causes cell death in neuroblastoma. The major lysosomal proteases are two cysteine proteases, cathepsins B and L, and an aspartic protease, cathepsin D. Inhibition of these three proteases was found to cause cellular accumulation of fragments of the IGF-1 receptor. The fragments were located in dense organelles that were characterized as autophagosomes. This novel discovery provides the first clear link between lysosIGF-1omal function, autophagy and IGF-1 mediated cell proliferation. It provides a mechanistic explanation for enhanced cytotoxicity of chemotherpautic agents when combined with inhibitors of lysosomal function and autophagy. A more in depth analysis of the IGF1 signaling pathway revealed that the MAPK pathway was particularly impaired in inhibitor treated cells, while the PKB cell survival pathway remained functional. It was ...
Certain cysteine proteases, such as cathepsin L (Ctsl), have been involved in yolk processing mechanisms in oocytes and embryos of lower vertebrates. In zebrafish (Danio rerio), three different ctsl genes, ctsla, ctslb and ctslc, have been found in the genome, but their pattern of expression, as well as information on which the encoded enzymes are potentially involved in yolk absorption during embryogenesis, is unknown. Here, phylogenetic and gene structure analysis revealed that zebrafish ctsla and ctslb genes are similar, showing a highly conserved structure in comparison with human ctsl, while ctslc presents different exon organization together with an earlier evolution. Thus, ctslc appears to be evolved from a common ancestral ctsl-like gene, possibly through an early duplication event, whereas ctsla and ctslb may be originated from a second duplication mechanism. Zebrafish ctsla, ctslb and ctslc also showed different patterns of mRNA expression during embryogenesis and in adult tissues. ...
Of these hydrolytic enzymes, cathepsin K is of most importance. Cathepsin K and other cathepsins[edit]. Cathepsin K is a ... Several other cathepsins are expressed in osteoclasts including cathepsins B, C, D, E, G, and L. The function of these cysteine ... characterised by a lack of functional cathepsin K expression. Knockout studies of cathepsin K in mice lead to an osteopetrotic ... Studies on cathepsin L knockout mice have been mixed, with a report of reduced trabecular bone in homozygous and heterozygous ...
... s were discovered in 1884 by Albrecht Kossel.[17] The word "histone" dates from the late 19th century and is derived from the German word "Histon", a word itself of uncertain origin - perhaps from the Greek histanai or histos. In the early 1960s, before the types of histones were known and before histones were known to be highly conserved across taxonomically diverse organisms, James F. Bonner and his collaborators began a study of these proteins that were known to be tightly associated with the DNA in the nucleus of higher organisms.[18] Bonner and his postdoctoral fellow Ru Chih C. Huang showed that isolated chromatin would not support RNA transcription in the test tube, but if the histones were extracted from the chromatin, RNA could be transcribed from the remaining DNA.[19] Their paper became a citation classic.[20] Paul T'so and James Bonner had called together a World Congress on Histone Chemistry and Biology in 1964, in which it became clear that there was no consensus on the ...
... , Histones & Cathepsin; PMAP The Proteolysis Map-animation [ Recent chromatin publications and news] Protocol for in ...
... collagenases such as cathepsin B1; and hyaluronidase. PSGAG inhibits the synthesis of prostaglandin E2, which is released upon ...
Cathepsin A Breddam, K. (1986). "Serine carboxypeptidases. A review". Carlsberg Res. Commun. 51: 83-128. doi:10.1007/bf02907561 ... Miller, J.J.; Changaris, D.G.; Levy, R.S. (1992). "Purification, subunit structure and inhibitor profile of cathepsin-A". J. ... Carboxypeptidase C (EC 3.4.16.5, carboxypeptidase Y, serine carboxypeptidase I, cathepsin A, lysosomal protective protein, ...
Cathepsin D is involved in CLN10.[9]. *DNA analysis can be used to help confirm the diagnosis of Batten disease. When the ...
Cathepsin E. TALE homeodomain transcription factors. Hydrocortisone. Since keratinocyte differentiation inhibits keratinocyte ... "The role of cathepsin E in terminal differentiation of keratinocytes". Biological Chemistry. 392 (6): 571-85. doi:10.1515/BC. ...
Mediation by cathepsin G has been suggested. The treatment of RAS usually involves administering dexamethasone IV, with the ...
Lushbaugh, W.B.; Hofbauer, A.F.; Pittman, F.E. (1985). "Entamoeba histolytica: purification of cathepsin B". Exp. Parasitol. 59 ...
... these include cathepsin L, papain, and procaricain. It forms an alpha-helical domain that runs through the substrate-binding ...
McDonald, J.K.; Zeitman, B.B.; Reilly, T.J.; Ellis, S. (1969). "New observations on the substrate specificity of cathepsin C ( ... Planta, R.J.; Gorter, J.; Gruber, M. (1964). "The catalytic properties of cathepsin C". Biochim. Biophys. Acta. 89: 511-519. ... Metrione, R.M.; Neves, A.G.; Fruton, J.S. (1966). "Purification and properties of dipeptidyl transferase (cathepsin C)". ... Dipeptidyl peptidase I (EC 3.4.14.1, cathepsin C, dipeptidyl aminopeptidase I, dipeptidyl transferase, dipeptide arylamidase I ...
The protein is able to form a dimer stabilized by noncovalent forces, inhibiting papain and cathepsins l, h and b. The protein ... 1994). "Cathepsin B activity in human lung tumor cell lines: ultrastructural localization, pH sensitivity, and inhibitor status ... 1988). "Cathepsin D inactivates cysteine proteinase inhibitors, cystatins". Biochem. Biophys. Res. Commun. 154 (2): 765-72. doi ... Cystatin B has been shown to interact with Cathepsin B. GRCh38: Ensembl release 89: ENSG00000160213 - Ensembl, May 2017 GRCm38 ...
These cysteine proteases include calpain, caspase, and cathepsin. These three proteins are examples of detectable signs of ...
It is an inhibitor of cathepsin K, an enzyme involved in bone resorption. It is being developed by Merck & Co. The phase III ... Le Gall, C. L.; Bonnelye, E.; Clézardin, P. (2008). "Cathepsin K inhibitors as treatment of bone metastasis". Current Opinion ... February 2008). "The discovery of odanacatib (MK-0822), a selective inhibitor of cathepsin K". Bioorg. Med. Chem. Lett. 18 (3 ...
A plant aspartic proteinase resembling mammalian cathepsin D". Eur. J. Biochem. 202 (3): 1021-1027. doi:10.1111/j.1432- ...
2000). "Secreted cathepsin L generates endostatin from collagen XVIII". EMBO J. 19 (6): 1187-94. doi:10.1093/emboj/19.6.1187. ... 2000). "Secreted cathepsin L generates endostatin from collagen XVIII". EMBO J. 19 (6): 1187-94. doi:10.1093/emboj/19.6.1187. ... by proteases such as cathepsins. Collagen is a component of epithelial and endothelial basement membranes. Endostatin, as a ...
Cathepsin A is also required for normal elastin biosynthesis. GRCh38: Ensembl release 89: ENSG00000170266 - Ensembl, May 2017 ... The elastin receptor complex includes S-Gal, neuraminidase and Cathepsin A. When elastin-derived peptides bind to the S-Gal ... cathepsin) A is required for proper elastic fiber formation and inactivation of endothelin-1". Circulation. 117 (15): 1973-81. ...
add NAE ref]. She pursued these interests by studying androsterone and monopalmitin at Armour, and cathepsin C at Yale. Jones ... Under the direction of Joseph S. Fruton, Jones' dissertation research involved the catalytic properties of cathepsin C, a type ... Her doctorate was entitled: Transamidation reactions catalyzed by cathepsin C. Jones completed her studies in three years ... Transamidation Reactions Catalyzed by Cathepsin C. Yale University, 1952. Kresge, Nicole; Simoni, Robert D.; Hill, Robert L. ( ...
1982). "Action of rat liver cathepsin L on glucagon". Acta Biol. Med. Ger. 40 (9): 1139-43. PMID 7340337. Kaushal GP, Walker PD ...
... cathepsin G and proteinase 3" Bioorg. Med. Chem. 1995, 3, 187-193. ([5]) Schapira, C. B.; Perillo, I. A.; Lamdan, S. "3-Oxo-1,2 ... cathepsin G and proteinase 3. Phthalimide derivatives were seen to be inactive, while saccharin derivatives were seen to be ...
2000). "Secreted cathepsin L generates endostatin from collagen XVIII". EMBO J. 19 (6): 1187-94. doi:10.1093/emboj/19.6.1187. ...
Deficiency of Cathepsin K, a cysteine protease in osteoclasts, is known to cause this condition. Cathepsin K became a much ... Motyckova, G; Fisher, DE (2002). "Pycnodysostosis: role and regulation of cathepsin K deficiency in osteoclast function and ... is a lysosomal storage disease of the bone caused by a mutation in the gene that codes the enzyme cathepsin K. Pycnodysostosis ... a lysosomal storage disease caused by cathepsin K deficiency". Science. 273 (5279): 1236-1238. doi:10.1126/science.273.5279. ...
1990). "Generation of human endothelin by cathepsin E". FEBS Lett. 273 (1-2): 99-102. doi:10.1016/0014-5793(90)81060-2. PMID ...
Several other cathepsins are expressed in osteoclasts including cathepsins B, C, D, E, G, and L. The function of these cysteine ... Of these hydrolytic enzymes, cathepsin K is of most importance. Cathepsin K is a collagenolytic, papain-like, cysteine protease ... characterised by a lack of functional cathepsin K expression. Knockout studies of cathepsin K in mice lead to an osteopetrotic ... Cathepsin K has an optimal enzymatic activity in acidic conditions. It is synthesized as a proenzyme with a molecular weight of ...
Cathepsin B and L play a crucial role in arthritic cartilage degeneration. The inhibitor of cathepsin isolated from this fungus ... The fungal metabolite, aurantiamide acetate, has been isolated from Aspergillus penicillioides, as a cathepsin inhibitor. ... a Selective Cathepsin Inhibitor, Produced by Aspergillus penicillioides". Bioscience, Biotechnology, and Biochemistry. 65 (5): ...
Cathepsin F is a protein that in humans is encoded by the CTSF gene. Cathepsins are papain family cysteine proteinases that ... The cathepsin F gene is ubiquitously expressed, and it maps to chromosome 11q13, close to the gene encoding cathepsin W. GRCh38 ... "Entrez Gene: CTSF cathepsin F". Nägler DK, Sulea T, Ménard R (1999). "Full-length cDNA of human cathepsin F predicts the ... Wex T, Levy B, Wex H, Brömme D (1999). "Human cathepsins F and W: A new subgroup of cathepsins". Biochem. Biophys. Res. Commun ...
... cathepsin G, cathepsin H, cathepsin K, cathepsin L, cathepsin L2, cathepsin O, cathepsin S, cathepsin Z, and cathepsin W. These ... Cathepsin Z, also called cathepsin X or cathepsin P, is a protein that in humans is encoded by the CTSZ gene. It is a member of ... As one of the 11 cathepsins, cathepsin Z contains distinctive features from others. Cathepsin Z has been reported involved in ... Cathepsin Z has an exposed integrin-bindign Arg-Gly-Asp motif within the propeptide of the enzyme, through which cathepsin Z ...
... prepro-cathepsin C) comprising signal peptides of 24 residues, pro-regions of 205 (rat cathepsin C) or 206 (human cathepsin C) ... Cathepsin C appears to be a central coordinator for activation of many serine proteases in immune/inflammatory cells. Cathepsin ... identical to the mature amino acid sequences of papain and a number of other cathepsins including cathepsins, B, H, K, L, and S ... Cathepsin C (CTSC) also known as dipeptidyl peptidase I (DPP-I) is a lysosomal exo-cysteine protease belonging to the peptidase ...
First, we propose a three-dimensional model by homology of the cathepsin B of F.hepatica, by using as templates cathepsins B of ... NARANJO, D et al. COMPARATIVE PROTEIN STRUCTURE MODELLING OF CATHEPSIN B FROM Fasciola hepatica. Rev Salud Anim. [online]. 2007 ... Cathepsin B was selected as a possible new therapeutic target of Fasciola hepatica. This is a cystein excretion protease ... Palabras clave : Fasciola hepatica; cathepsin B proteases; comparative protein structure modelling; protein data bank. ...
deficiency of cathepsin A, see Galactosialidosis. *deficiency of cytochrome-b5 reductase, see Autosomal recessive congenital ...
"Early immunodiagnosis of fasciolosis in ruminants using recombinant Fasciola hepatica cathepsin L-like protease". International ...
Cathepsin: Cathepsins ( Ancient Greek kata- "down" and hepsein "boil"; abbreviated CTS ) are proteases ( enzymes that degrades ... Cathepsins have a vital role in mammalian cellular turnover, e.g. bone resorption. They degrade polypeptides and are ... There are, however, exceptions such as cathepsin K, which works extracellularly after secretion by osteoclasts in bone ...
"Human cathepsins W and F form a new subgroup of cathepsins that is evolutionary separated from the cathepsin B- and L-like ... Wex T, Levy B, Wex H, Brömme D (1999). "Human cathepsins F and W: A new subgroup of cathepsins". Biochem. Biophys. Res. Commun ... 2003). "Characterization of novel anti-cathepsin W antibodies and cellular distribution of cathepsin W in the gastrointestinal ... Cathepsin W is a protein that in humans is encoded by the CTSW gene.[5][6][7] ...
"Entrez Gene: CTSD cathepsin D".. *^ Barrett AJ (April 1970). "Cathepsin D. Purification of isoenzymes from human and chicken ... Cathepsin D is an aspartic endo-protease that is ubiquitously distributed in lysosomes.[7] The main function of cathepsin D is ... The optimum pH for cathepsin D in vitro is 4.5-5.0.[13] Cathepsin-D is an aspartic protease that depends critically on ... Cathepsin D is a protein that in humans is encoded by the CTSD gene.[5][6] This gene encodes a lysosomal aspartyl protease ...
Cathepsin A is an enzyme that is classified both as a cathepsin and a carboxypeptidase. In humans, it is encoded by the CTSA ... Cathepsin A has been shown to interact with NEU1.[7] References[edit]. *^ a b c GRCh38: Ensembl release 89: ENSG00000064601 - ... "Entrez Gene: CTSA cathepsin A".. *^ Mitchell, Richard Sheppard; Kumar, Vinay; Robbins, Stanley L.; Abbas, Abul K.; Fausto, ... 1991). "Human lysosomal protective protein has cathepsin A-like activity distinct from its protective function". J. Biol. Chem ...
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.
Cathepsin A (serine protease) Cathepsin B (cysteine protease) Cathepsin C (cysteine protease) Cathepsin D (aspartyl protease) ... Cathepsin H (cysteine protease) Cathepsin K (cysteine protease) Cathepsin L1 (cysteine protease) Cathepsin L2 (or V) (cysteine ... Cathepsin S (cysteine protease) Cathepsin W (cysteine proteinase) Cathepsin Z (or X) (cysteine protease) Cathepsins have been ... Cathepsin K has also been shown to play a role in arthritis. Mouse cathepsin L is homologous to human cathepsin V. Mouse ...
If you know of any papers that use this antibody, please contact us at antibodies [at] alzforum [dot] org for consideration in the References section.. ...
Cathepsin Cathepsin T at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... Cathepsin T (EC 3.4.22.24) is an enzyme. This enzyme catalyses the following chemical reaction Interconversion of the three ... Pitot, H.C.; Gohda, E. (1987). "Cathepsin T". Methods Enzymol. 142: 279-289. doi:10.1016/s0076-6879(87)42038-7. PMID 2885716. ...
... cathepsin D-like acid proteinase, cathepsin E-like acid proteinase, cathepsin D-type proteinase) is an enzyme. This enzyme ... Cathepsin Cathepsin E Lapresle, C.; Puizdar, V.; Porchon-Bertolotto, C.; Joukoff, E.; Turk, V. (1986). "Structural differences ... Cathepsin E at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology portal. ... Cathepsin E (EC 3.4.23.34, slow-moving proteinase, erythrocyte membrane aspartic proteinase, SMP, EMAP, non-pepsin proteinase, ...
Cathepsin L1, previously called cathepsin L Cathepsin L2 or cathepsin V Barrett, A.J.; Kirschke, H. (1981). "Cathepsin B, ... cathepsin H and cathepsin L". Methods Enzymol. 80: 535-561. doi:10.1016/s0076-6879(81)80043-2. PMID 7043200. Barrett, A.J.; ... Reinheckel T.Human cathepsin L rescues the neurodegeneration and lethality in cathepsin B/L double-deficient mice. Biol Chem. ... Cathepsin L at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology portal. ...
... cathepsin S can be replaced by cathepsin F. Secreted cathepsin S cleaves some extracellular matrix (ECM) proteins. Cathepsin S ... In vitro, cathepsin S retains some enzyme activity in the presence of 3M urea. Cathepsin S is produced as a zymogen and is ... Cathepsin S can function as an elastase over a broad pH range in alveolar macrophages. Cathepsin S is a lysosomal enzyme that ... In tumorogenesis, cathepsin S promotes a tumor growth. Cathepsin S expression and activity has also been shown to be ...
Cathepsin X (EC 3.4.18.1, cathepsin B2, cysteine-type carboxypeptidase, cathepsin IV, cathepsin Z, acid carboxypeptidase, ... Cathepsin Z Cathepsin X at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... Otto, K.; Riesenkönig, H. (1975). "Improved purification of cathepsin B1 and cathepsin B2". Biochim. Biophys. Acta. 379 (2): ... "On the substrate specificity of cathepsins B1 and B2 including a new fluorogenic substrate for cathepsin B1". Life Sci. 17 (8 ...
Cathepsin K is degraded by Cathepsin S, called Controlled Cathepsin Cannibalism. Cathepsin K expression is stimulated by ... Cathepsin K has also been found to be over-expressed in glioblastoma. That the expression of cathepsin K is characteristic for ... Cathepsin K antibodies are marketed for research into expression of this enyzme by various cells. Merck had a cathepsin K ... Other cathepsin K inhbitors are in various stages of development. Medivir has a cathepsin K inhibitor, MIV-711 (L-006235), in ...
Cathepsin V (EC 3.4.22.43, Cathepsin L2, cathepsin U) is an enzyme. This enzyme catalyses the following chemical reaction The ... Cathepsin L2 Brömme, D.; Li, Z.; Barnes, M.; Mehler, E. (1999). "Human cathepsin V functional expression, tissue distribution, ... Cathepsin V at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology portal. ... Santamaría, I.; Velasco, G.; Cazorla, M.; Fueyo, A.; Campo, E.; López-Otín, C. (1998). "Cathepsin L2, a novel human cysteine ...
Cathepsin L1 is a protein that in humans is encoded by the CTSL1 gene. The protein encoded by this gene is a lysosomal cysteine ... Major sites of cleavage by cathepsins B, D, and L". J. Biol. Chem. 266 (30): 20198-204. PMID 1939080. Stearns NA, Dong JM, Pan ... 1991). "Comparison of cathepsin L synthesized by normal and transformed cells at the gene, message, protein, and ... Joseph L, Lapid S, Sukhatme V (1987). "The major ras induced protein in NIH3T3 cells is cathepsin L". Nucleic Acids Res. 15 (7 ...
"Entrez Gene: CTSH cathepsin H". Sawicki G, Warwas M (1990). "Cathepsin H from human placenta". Acta Biochim. Pol. 36 (3-4): 343 ... Cathepsin H is a protein that in humans is encoded by the CTSH gene. The protein encoded by this gene is a lysosomal cysteine ... 2003). "Expression of cathepsins B, H, K, L, and S during human fetal lung development". Dev. Dyn. 225 (1): 14-21. doi:10.1002/ ... 2001). "Expression of cathepsins B, H, K, L, and S and matrix metalloproteinases 9 and 13 during chondrocyte hypertrophy and ...
Cathepsin G is one of those homologous protease that evolved from a common ancestor by gene duplication. Cathepsin G is a 255- ... An upregulation of cathepsin G was reported in studies of keratoconus. Cathepsin G has been found to interact with: SERPINB1 ... "Entrez Gene: CTSG cathepsin G". Shafer WM, Pohl J, Onunka VC, Bangalore N, Travis J (January 1991). "Human lysosomal cathepsin ... "Generation of the neutrophil-activating peptide-2 by cathepsin G and cathepsin G-treated human platelets". The American Journal ...
Cathepsin K detection by zymography Zymographic techniques for detection of cathepsins K, L, S, and V Zymography for detection ... Cathepsin zymography is a technique for quantifying enzymatic activity of the cathepsin family of cysteine proteases. It is ... While the proform of cathepsins are generally stable, once activated, proteases such as cathepsin K are vulnerable to ... After the renaturing period, the gel is then incubated in assay buffer to allow the now active cathepsins to proteolyze the ...
Cathepsin L2, also known as cathepsin V and encoded by the CTSL2 gene, is a human gene. The protein encoded by this gene, a ... 2006). "Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the ... 2007). "Inhibition of cathepsin L-like proteases by cathepsin V propeptide". Biol. Chem. 388 (5): 541-5. doi:10.1515/BC. ... 2005). "The human cysteine protease cathepsin V can compensate for murine cathepsin L in mouse epidermis and hair follicles". ...
  • Cathepsin Z has an exposed integrin-bindign Arg-Gly-Asp motif within the propeptide of the enzyme, through which cathepsin Z has been shown to interact with several integrins during normal homeostasis, immune processes and cancer. (wikipedia.org)
  • The cDNAs encoding rat, human, murine, bovine, dog and two Schistosome cathepsin Cs have been cloned and sequenced and show that the enzyme is highly conserved. (wikipedia.org)
  • The signal peptide is removed during translocation or secretion of the pro-enzyme (pro-cathepsin C) and a large N-terminal proregion fragment (also known as the exclusion domain), which is retained in the mature enzyme, is separated from the catalytic domain by excision of a minor C-terminal part of the pro-region, called the activation peptide. (wikipedia.org)
  • After TMB substrate solution is added, only those wells that contain Cathepsin Z (CTSZ), biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. (biobool.com)
  • Cathepsin Z, also called cathepsin X or cathepsin P, is a protein that in humans is encoded by the CTSZ gene. (wikipedia.org)
  • Cathepsin C catalyses excision of dipeptides from the N-terminus of protein and peptide substrates, except if (i) the amino group of the N-terminus is blocked, (ii) the site of cleavage is on either side of a proline residue, (iii) the N-terminal residue is lysine or arginine, or (iv) the structure of the peptide or protein prevents further digestion from the N-terminus. (wikipedia.org)
  • Unlike the other members of the papain family, mature cathepsin C consists of four subunits, each composed of the N-terminal proregion fragment, the heavy chain and the light chain. (wikipedia.org)
  • The very long (251-amino acid residues) proregion of the cathepsin F precursor contains a C-terminal domain similar to the pro-segment of cathepsin L-like enzymes, a 50-residue flexible linker peptide, and an N-terminal domain predicted to adopt a cystatin-like fold. (wikipedia.org)
  • The primary structure and tissue distribution of cathepsin C". Biological Chemistry Hoppe-Seyler. (wikipedia.org)
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