AnatomyOrganismsChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesInformation Science
Cathepsin BCathepsinsCathepsin LCathepsin DCathepsin HCathepsin KCathepsin GCathepsin ECathepsin CCysteine EndopeptidasesCathepsin FCystatinsLysosomesCathepsin ZCysteine Proteinase InhibitorsDiazomethaneEndopeptidasesDipeptidesCystatin ACathepsin WCystatin BPapainBenzoylarginine-2-NaphthylamidePepstatinsProtease InhibitorsCysteine ProteasesCathepsin AEnzyme PrecursorsCystatin CHydrogen-Ion ConcentrationExopeptidasesAmino Acid SequenceMolecular Sequence DataSerine EndopeptidasesTrypsinogenPancreatic ElastaseSubstrate SpecificityHydrolysisKineticsLeucineLeukocyte ElastaseReceptors, Urokinase Plasminogen ActivatorElectrophoresis, Polyacrylamide GelPeptide HydrolasesOligopeptides2,2'-DipyridylFasciola hepaticaLiver
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.
Diazomethane
Endopeptidases
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.

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)

Inhibition of cathepsin B activity attenuates extracellular matrix deg by Bernadette C. Victor, Arulselvi Anbalagan et al.Inhibition of cathepsin B activity attenuates extracellular matrix deg by Bernadette C. Victor, Arulselvi Anbalagan et al.
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
https://scholar.uwindsor.ca/biologypub/18/
Demonstration by electrospray mass spectrometry that the peptidyldipeptidase activity of cathepsin B is capable of rat...Demonstration by electrospray mass spectrometry that the peptidyldipeptidase activity of cathepsin B is capable of rat...
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. ...
http://www.biochemj.org/content/294/3/923
CA 074|Cathepsin B inhibitor|CAS# 134448-10-5CA 074|Cathepsin B inhibitor|CAS# 134448-10-5
|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
http://www.apexbt.com/ca-074.html
Interleukin-4 downregulates the cyclic tensile stress-induced matrix metalloproteinases-13 and cathepsin b expression by rat...
Mechanical stress plays a key role in the pathogenesis of cartilage destruction seen in osteoarthritis (OA). We investigated the effect of cyclic tensile stress (CTS) on the anabolic and catabolic gene expression of rat cultured normal chondrocytes using the Flexercell strain unit. The effects of interleukin (IL)-4, a chondroprotective cytokine, on the changes in gene expression induced by CTS were also investigated. CTS (7% elongation at 0.5 Hz) for 24 h did not affect the expression of aggrecan and type II collagen, whereas CTS significantly upregulated matrix metalloproteinase (MMP)-13 and cathepsin B mRNA expression by chondrocytes. IL-1beta expression was also signifi cantly upregulated by CTS up to 12 h. The upregulation of MMP-13 was observed at 3 h, which was earlier than that of IL-1beta. Furthermore, pre-treatment with IL-4 (10 ng/ml) suppressed both MMP-13 and cathepsin B induction by mechanical stress, as well as CTS-induced IL-1beta expression. Our results suggest that IL-4 might ...
http://ousar.lib.okayama-u.ac.jp/ja/list/ou_authors/T/e5f780c6b21d999674506e4da22f6611/item/30956
RCSB PDB - 1CPJ: CRYSTAL STRUCTURES OF RECOMBINANT RAT CATHEPSIN B AND A CATHEPSIN B-INHIBITOR COMPLEX: IMPLICATIONS FOR...RCSB PDB - 1CPJ: CRYSTAL STRUCTURES OF RECOMBINANT RAT CATHEPSIN B AND A CATHEPSIN B-INHIBITOR COMPLEX: IMPLICATIONS FOR...
1CPJ: CRYSTAL STRUCTURES OF RECOMBINANT RAT CATHEPSIN B AND A CATHEPSIN B-INHIBITOR COMPLEX: IMPLICATIONS FOR STRUCTURE-BASED INHIBITOR DESIGN
https://www.rcsb.org/structure/1CPJ
CA-074 Methyl Ester | ≥99%(HPLC) | Cathepsin B inhibitor | AdooQ®CA-074 Methyl Ester | ≥99%(HPLC) | Cathepsin B inhibitor | AdooQ®
CA-074 methyl ester is a cell-permeable analog of CA-074 that acts as an irreversible cathepsin B inhibitor. CA-074 methyl ester is reported to inhibit bone resorption in rodent models and shown to inhibit B16 melanoma cell invasion in vitro.
https://www.adooq.com/ca-074-methyl-ester.html
A two-hybrid screen identifies cathepsins B and L as uncoating factors for adeno-associated virus 2 and 8. - Semantic ScholarA two-hybrid screen identifies cathepsins B and L as uncoating factors for adeno-associated virus 2 and 8. - Semantic Scholar
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
https://www.semanticscholar.org/paper/A-two-hybrid-screen-identifies-cathepsins-B-and-L-Akache-Grimm/9f109afff4f407e8bd3f49f41c84c45f482ad521
Lysosomal cathepsin B participates in the podosome-mediated extracellu by Chun Tu, Ceasar F. Ortega-Cava et al.Lysosomal cathepsin B participates in the podosome-mediated extracellu by Chun Tu, Ceasar F. Ortega-Cava et al.
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.
https://scholar.uwindsor.ca/biologypub/23/
Selective Targeting of Tumor and Stromal Cells By a Nanocarrier System Displaying Lipidated Cathepsin B Inhibitor
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 ...
https://pub.uni-bielefeld.de/publication/2703442
Changes in Activity of Cysteine Cathepsins B and L in Brain Structures of Mice with Aggressive and Depressive-Like Behavior...
TY - JOUR. T1 - Changes in Activity of Cysteine Cathepsins B and L in Brain Structures of Mice with Aggressive and Depressive-Like Behavior Formed under Conditions of Social Stress. AU - Zhanaeva, S. Ya. AU - Rogozhnikova, A. A.. AU - Alperina, E. L.. AU - Gevorgyan, M. M.. AU - Idov, G. V.. PY - 2018/3/1. Y1 - 2018/3/1. N2 - We studied activity of lysosomal cysteine proteases, cathepsins B and L, in brain structures (frontal cortex, caudate nucleus, hippocampus, and hypothalamus) of C57Bl/6J mice with aggressive and depressive-like behavior formed under conditions of chronic social stress (repeated experience of victories and defeats within 20 days). Mice with depressive-like behavior showed increased activity of cathepsin В in the hypothalamus and nucleus caudatus and increased activity of cathepsin L in the hippocampus compared to control animals not subjected to agonistic confrontations. In mice with aggressive behavior, protease activity in the studied brain structures was not changed. In ...
https://research.nsu.ru/ru/publications/changes-in-activity-of-cysteine-cathepsins-b-and-l-in-brain-struc
British Library EThOS: Involvement of cathepsin B-like genes in disease resistance in Arabidopsis thalianaBritish Library EThOS: Involvement of cathepsin B-like genes in disease resistance in Arabidopsis thaliana
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 ...
http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.657047
Recombinant Human Cathepsin B /CTSB Protein, His Tag, 1mgRecombinant Human Cathepsin B /CTSB Protein, His Tag, 1mg
Recombinant Human Cathepsin B /CTSB Protein, APP secretase (APPS), belongs to peptidase C1 family, produced in human 293 cells (HEK293).
https://www.proteinkinase.biz/-recombinant-proteins/2318-recombinant-human-cathepsin-b-ctsb-protein-his-tag-1mg.html
ScholarWorks: Multiple cell death pathways are independently activated by lethal hypertonicity in renal epithelial cellsScholarWorks: Multiple cell death pathways are independently activated by lethal hypertonicity in renal epithelial cells
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 ...
http://scholarworks.unist.ac.kr/handle/201301/4120
Synthesis and hydrolysis by cathepsin B of fluorogenic substrates with the general structure benzoyl-X-ARG-MCA containing non...
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 ...
http://www.repositorio.unifesp.br/handle/11600/26549
Increased muscle proteolysis after local trauma mainly reflects macrophage-associated lysosomal proteolysis<...Increased muscle proteolysis after local trauma mainly reflects macrophage-associated lysosomal proteolysis<...
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 ...
https://abdn.pure.elsevier.com/en/publications/increased-muscle-proteolysis-after-local-trauma-mainly-reflects-m
MDL 28170|Calpain and cathepsin B inhibitor, selective|CAS# 88191-84-8MDL 28170|Calpain and cathepsin B inhibitor, selective|CAS# 88191-84-8
|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
http://www.apexbt.com/mdl-28170.html
VisEn Introduces New Fluorescence Molecular Imaging Agent - NS Medical DevicesVisEn Introduces New Fluorescence Molecular Imaging Agent - NS Medical Devices
VisEn Medical (VisEn), a provider of fluorescence in vivo imaging from research through medicine, has launched its new Cat B 680 FAST imaging agent. It is meant for measuring and monitoring cathepsin B activity associated with disease progression and therapeutic response in vivo. Cathepsin B expression is a key biomarker and therapeutic target in a range of diseases, including atherosclerosis, oncology, and arthritis. The new agent is designed to complement the companys existing in vivo agent product lines, providing early imaging time points and an additional reporting wavelength for more multiplexing choices in cell-based and in vivo research study designs.. The fluorescence imaging agents and labels are designed to provide a range of biologically-specific imaging readouts in vivo. The company offers over 30 different fluorescence molecular agents for imaging key disease-associated biologic targets, processes and pathways, said the company. The agents are designed for in vivo biomarker ...
https://www.nsmedicaldevices.com/news/visen_introduces_new_fluorescence_molecular_imaging_agent_100120/
Enzymatic activity of cathepsin B, cathepsin B and L, plasmin, trypsin and collagenase in hepatocellular carcinoma]. | Harvard...Enzymatic activity of cathepsin B, cathepsin B and L, plasmin, trypsin and collagenase in hepatocellular carcinoma]. | Harvard...
Enzymatic activity of cathepsin B, cathepsin B and L, plasmin, trypsin and collagenase in hepatocellular carcinoma]. Pol Arch Med Wewn. 2002 Jul; 108(1):653-62 ...
https://connects.catalyst.harvard.edu/Profiles/display/797302
Angiotensin-Converting Enzyme - Proteopedia, life in 3DAngiotensin-Converting Enzyme - Proteopedia, life in 3D
3d0g), namely at residues 31, 35, 38, & 353 in ACE2 or residues 479 and 487 in the SARS-CoV RBD, are what allowed for SARS transmission from Civets to Humans. In fact, in those SARS strains which were determined to be most infectious, the unfavorable electrostatic interactions at the binding interface were removed via mutations at the critical residues 479 and 487. [16] In 2020 Zhou et al. (Nature. 2020; 579: 270-273) and Hoffmann et al. (Cell. 2020; 181: 271-280) showed that SARS-CoV-2, the COVID-19 coronavirus causing the global 2019-2020 pandemia, uses ACE2 as a receptor protein to enter and infect cells, just as SARS-CoV does. Cell entry requires the binding of the S1 region of the virus spike (S) protein to ACE2 followed by the fusion of the viral and cellular membranes produced by the S2 subunit of the S protein. Beforehand, this process requires priming of the S protein by host cell proteases, which is performed by TMPRSS2 and the endosomal cysteine proteases cathepsin B and L (CatB/L). ...
http://proteopedia.org/wiki/index.php/Angiotensin-Converting_Enzyme
GMS | 27th German Cancer Congress Berlin 2006 | Expression of cathepsin B in gastric adenocarcinomas represents a prognostic...
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 ...
http://www.egms.de/static/en/meetings/dkk2006/06dkk309.shtml
Structure Cluster - 1CPJ: CRYSTAL STRUCTURES OF RECOMBINANT RAT CATHEPSIN B AND A CATHEPSIN B-INHIBITOR COMPLEX:...Structure Cluster - 1CPJ: CRYSTAL STRUCTURES OF RECOMBINANT RAT CATHEPSIN B AND A CATHEPSIN B-INHIBITOR COMPLEX:...
1CPJ: Crystal structures of recombinant rat cathepsin B and a cathepsin B-inhibitor complex. Implications for structure-based inhibitor design.
http://www.rcsb.org/pdb/explore/structureCluster.do?structureId=1CPJ
ctsb Protein, cathepsin B - Creative BioMart
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.
https://www.creativebiomart.net/symbolsearch_CTSB.htm
PDB: 3AI8
HEADER HYDROLASE/HYDROLASE INHIBITOR 11-MAY-10 3AI8 TITLE CATHEPSIN B IN COMPLEX WITH THE NITROXOLINE COMPND MOL_ID: 1; COMPND 2 MOLECULE: CATHEPSIN B; COMPND 3 CHAIN: B, A; COMPND 4 SYNONYM: CATHEPSIN B1, APP SECRETASE, APPS, CATHEPSIN B LIGHT CHAIN, COMPND 5 CATHEPSIN B HEAVY CHAIN; COMPND 6 EC: 3.4.22.1; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: CTSB; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21DE3; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3A KEYWDS CATHEPSIN B, REVERSIBLE INHIBITOR, NITROXOLINE, 8-HYDROXY-5- KEYWDS 2 NITROQUINOLINE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR M.RENKO,B.MIRKOVIC,S.GOBEC,J.KOS,D.TURK REVDAT 3 29-JAN-14 3AI8 1 JRNL VERSN REVDAT 2 08-JUN-11 3AI8 1 JRNL REVDAT 1 18-MAY-11 3AI8 0 JRNL AUTH ...
https://www.genome.jp/entry/pdb:3AI8
SCKL | Cathepsin B Inhibitor, z-FA-FMK Induces IκBα DegradationSCKL | Cathepsin B Inhibitor, z-FA-FMK Induces IκBα Degradation
OBJECTIVE To measure the cardiovascular threat of diabetic subject matter with chronic kidney disease (CKD) predicated on different approximated glomerular filtration rate (eGFR) equations also to evaluate which definition of CKD best improves cardiovascular risk prediction from the Framingham Cardiovascular Risk Score (Framingham-CV-RS). Outcomes During 5 many years of follow-up, 95 people had a major cardiovascular event. Crude HRs had been increased for many CKD definitions. Nevertheless, after CI-1040 modifying for founded cardiovascular risk elements, HRs for both creatinine-based CKD meanings had been attenuated to stage estimates of just one 1.03, whereas the HRs for the cystatin CCbased CKD description continued to be significantly increased (HR 1.75 [95% CI 1.07C2.87]). Expansion of the research model by the various CKD definitions led to a rise in the statistic only once SCKL adding CKD-CysC (from 0.638 to 0.644) plus a net CI-1040 reclassification improvement of 8.9%. CONCLUSIONS Just ...
https://z-fa-fmk.net/tag/sckl/
Myosin | Cathepsin B Inhibitor, z-FA-FMK Induces IκBα DegradationMyosin | Cathepsin B Inhibitor, z-FA-FMK Induces IκBα Degradation
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 ...
http://z-fa-fmk.net/category/myosin/
Journal: Chemical communications / Publication Year: 2020 / Source: 2020 v.56 no.14 - PubAg Search ResultsJournal: Chemical communications / Publication Year: 2020 / Source: 2020 v.56 no.14 - PubAg Search Results
We develop a simple fluorescence method for the sensitive detection of cathepsin B activity based on the integration of a peptide-DNA conjugate with multiple cyclic signal amplification. This method can detect cathepsin B activity with an extremely low detection limit of 8.1 × 10⁻¹² g mL⁻¹ and a large dynamic range of 4 orders of magnitude from 1 × 10⁻¹¹ to 1 × 10⁻⁷ g mL⁻¹, and it can even measure ...
https://pubag.nal.usda.gov/?f%5Bjournal_name%5D%5B%5D=Chemical+communications&f%5Bpublication_year_rev%5D%5B%5D=7980-2020&f%5Bsource%5D%5B%5D=2020+v.56+no.14
Evidence That Inhibition of Cathepsin-B Contributes to the Neuroprotective Properties of Caspase Inhibitor Tyr-Val-Ala-Asp...
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https://www.ndmrb.ox.ac.uk/research/our-research/publications/625263/
Defects in COG-Mediated Golgi Trafficking Alter Endo-Lysosoma System in Human Cells
The conserved oligomeric complex (COG) is a multi-subunit vesicle tethering complex that functions in retrograde trafficking at the Golgi. We have previously demonstrated that the formation of enlarged endo-lysosomal structures (EELSs) is one of the major glycosylation-independent phenotypes of cells depleted for individual COG complex subunits. Here, we characterize the EELSs in HEK293T cells using microscopy and biochemical approaches. Our analysis revealed that the EELSs are highly acidic and that vATPase-dependent acidification is essential for the maintenance of this enlarged compartment. The EELSs are accessible to both trans-Golgi enzymes and endocytic cargo. Moreover, the EELSs specifically accumulate endolysosomal proteins Lamp2, CD63, Rab7, Rab9, Rab39, Vamp7, and STX8 on their surface. The EELSs are distinct from lysosomes and do not accumulate active Cathepsin B. Retention using selective hooks (RUSH) experiments revealed that biosynthetic cargo mCherry-Lampl reaches the EELSs much ...
https://ir.vanderbilt.edu/handle/1803/9575
Cathepsin B-mediated autophagy flux facilitates the anthrax toxin receptor 2-mediated delivery of anthrax lethal factor into...Cathepsin B-mediated autophagy flux facilitates the anthrax toxin receptor 2-mediated delivery of anthrax lethal factor into...
Sigma-Aldrich offers abstracts and full-text articles by [Soon-Duck Ha, Boram Ham, Jeremy Mogridge, Paul Saftig, Shengcai Lin, Sung Ouk Kim].
https://www.sigmaaldrich.com/catalog/papers/19858192
OriGene - CTSB (NM 147783) Human ORF cDNA CloneOriGene - CTSB (NM 147783) Human ORF cDNA Clone
CTSB - CTSB (GFP-tagged) - Human cathepsin B (CTSB), transcript variant 5 available for purchase from OriGene - Your Gene Company.
http://www.origene.com/Human_ORF_Clone/RG210578.aspx
sst Receptors | PI3-kinase inhibitors in lymphomasst Receptors | PI3-kinase inhibitors in lymphoma
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 ...
http://mirc-undernet.org/category/sst-receptors/
Gentaur Molecular :BPS Bioscience \ Cathepsin B \ 80001Gentaur Molecular :BPS Bioscience \ Cathepsin B \ 80001
Gentaur molecular products has all kinds of products like :search , BPS Bioscience \ Cathepsin B \ 80001 for more molecular products just contact us
http://www.antibody-antibodies.com/product_det.php?id=190591&supplier=search&name=Cathepsin%20B
Silica crystals and aluminum salts activate the NALP3 inflammasome thr by Veit Hornung, Franz G. Bauernfeind et al.Silica crystals and aluminum salts activate the NALP3 inflammasome thr by Veit Hornung, Franz G. Bauernfeind et al.
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.
https://escholarship.umassmed.edu/infdis_pp/73/
Anti-Cathepsin B Picoband™ AntibodyAnti-Cathepsin B Picoband™ Antibody
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
https://www.bosterbio.com/anti-cathepsin-b-picoband-trade-antibody-pb9046.html
116(1)116(1)
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. ...
https://www.jci.org/116/1
Prosense | Application Support Knowledgebase | Lab Products & Services | PerkinElmerProsense | Application Support Knowledgebase | Lab Products & Services | PerkinElmer
Traditional mouse models of cancer rely primarily on ex vivo measurements of disease morphology and histologic analysis for the assessment of tumors. These measurements of disease may be distant from the actual biological targets of interest and can be time consuming, expensive, and impractical. By using NIR (Near-Infrared) in vivo imaging probes in combination with FMT, the biological processes that change with disease progression and therapeutic response can be visualized non-invasively over time.. ProSense™ agents were developed to specifically look at the expression and activity of key disease associated proteases. ProSense agents are optically silent until in the presence of these proteases and can be used to easily monitor the activity of these proteases in real time. PerkinElmer offers three different ProSense activatable agents. ProSense 680 is activated by Cathepsin B, L, S and Plasmin. ProSense 750 FAST is activated by Cathepsin B, L, S, K, V and D. ProSense 750 EX is activated by ...
https://www.perkinelmer.com/lab-products-and-services/application-support-knowledgebase/in-vivo-preclinical-imaging/ProSense-ASK.html
CTSB (Human) Recombinant Protein (P02) - (H00001508-P02) - Products - Abnova
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
http://www.abnova.com/products/products_detail.asp?catalog_id=H00001508-P02
JoVE Author Search: Lakka S
Apoptosis, Autophagy, Caspase-3, Cathepsin, Cathepsin B, Cdna, Cell Death, Cysteine, Cytochrome, Cytochrome C, Death, Glycoprotein, Inhibition, Light, Medulloblastoma, Membrane, Microtubule, Mitochondria, Neoplasms, Neuroblastoma
http://labindex.jove.com/author/Lakka-S
Cysteine cathepsin activity suppresses osteoclastogenesis of myeloid-derived suppressor cells in breast cancerCysteine cathepsin activity suppresses osteoclastogenesis of myeloid-derived suppressor cells in breast cancer
Cysteine cathepsin proteases contribute to many normal cellular functions, and their aberrant activity within various cell types can contribute to many diseases, including breast cancer. It is now well accepted that cathepsin proteases have numerous cell-specific functions within the tumor microenvironment that function to promote tumor growth and invasion, such that they may be valid targets for anti-metastatic therapeutic approaches. Using activity-based probes, we have examined the activity and expression of cysteine cathepsins in a mouse model of breast cancer metastasis to bone. In mice bearing highly metastatic tumors, we detected abundant cysteine cathepsin expression and activity in myeloid-derived suppressor cells (MDSCs). These immature immune cells have known metastasis-promoting roles, including immunosuppression and osteoclastogenesis, and we assessed the contribution of cysteine cathepsins to these functions. Blocking cysteine cathepsin activity with multiple small-molecule ...
https://scholars.latrobe.edu.au/display/publication26065
Modulation of cathepsin L expression and NF-kB signalling pathway effectors by advanced glycation end-products in retinal...Modulation of cathepsin L expression and NF-kB signalling pathway effectors by advanced glycation end-products in retinal...
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 ...
http://iovs.arvojournals.org/article.aspx?articleid=2560302
Molecular characterization of cathepsin B from Clonorchis sinensis excretory/secretory products and assessment of its potential...Molecular characterization of cathepsin B from Clonorchis sinensis excretory/secretory products and assessment of its potential...
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 ...
https://parasitesandvectors.biomedcentral.com/articles/10.1186/1756-3305-4-149
L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including...L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including...
1. L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) at a concentration of 0.5 mM had no effect on the serine proteinases plasma kallikrein and leucocyte elastase or the metalloproteinases thermolysin and clostridial collagenase. In contrast, 10 muM-E-64 rapidly inactivated the cysteine proteinases cathepsins B, H and L and papain (t0.5 = 0.1-17.3s). The streptococcal cysteine proteinase reacted much more slowly, and there was no irreversible inactivation of clostripain. The cysteine-dependent exopeptidase dipeptidyl peptidase I was very slowly inactivated by E-64. 2. the active-site-directed nature of the interaction of cathepsin B and papain with E-64 was established by protection of the enzyme in the presence of the reversible competitive inhibitor leupeptin and by the stereospecificity for inhibition by the L as opposed to the D compound. 3. It was shown that the rapid stoichiometric reaction of the cysteine proteinases related to papain can be used to determine the operational molarity of
https://www.bioseek.eu/us/eng/research/pubmed/L_trans_Epoxysuccinyl_leucylamido_4_guanidino_butane_E_64_and_its_analogues_as_inhibitors_of_cysteine_proteinases_including_cathepsins_B_H_and_L_7044372
Inhibition of lysosomal cysteine proteases by a series of Au(I) complexes - Research Portal - Converis Standard ConfigInhibition of lysosomal cysteine proteases by a series of Au(I) complexes - Research Portal - Converis Standard Config
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). ...
https://converis.upt.pt/converis/portal/detail/Publication/4906004?auxfun=&lang=de_DE
admin | Gillies McIndoe Research Instituteadmin | Gillies McIndoe Research Institute
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 ...
http://gmri.org.nz/cms/author/admin/page/2/
N-substituted peptidyl nitriles as cysteine cathepsin inhibitors - Patent # 6812237 - PatentGenius
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##
http://www.patentgenius.com/patent/6812237.html
Role of cathepsin B in the pathogenesis of acute pancreatitis<...Role of cathepsin B in the pathogenesis of acute pancreatitis<...
TY - JOUR. T1 - Role of cathepsin B in the pathogenesis of acute pancreatitis. AU - Gumaste, Vivek V.. PY - 1994/4. Y1 - 1994/4. UR - http://www.scopus.com/inward/record.url?scp=0028301772&partnerID=8YFLogxK. UR - http://www.scopus.com/inward/citedby.url?scp=0028301772&partnerID=8YFLogxK. M3 - Article. C2 - 8143984. VL - 106. SP - 1123. EP - 1125. JO - Gastroenterology. JF - Gastroenterology. SN - 0016-5085. IS - 4. ER - ...
https://einstein.pure.elsevier.com/en/publications/role-of-cathepsin-b-in-the-pathogenesis-of-acute-pancreatitis-2
Elevated levels of cathepsin B in human glioblastoma cell lines. - Fingerprint - University of Illinois at Urbana-ChampaignElevated levels of cathepsin B in human glioblastoma cell lines. - Fingerprint - University of Illinois at Urbana-Champaign
Fingerprint Dive into the research topics of Elevated levels of cathepsin B in human glioblastoma cell lines.. Together they form a unique fingerprint. ...
https://experts.illinois.edu/en/publications/elevated-levels-of-cathepsin-b-in-human-glioblastoma-cell-lines/fingerprints/
Natively inhibited trypanosoma brucei cathepsin B structure determined by using an x-ray laser<...
TY - JOUR. T1 - Natively inhibited trypanosoma brucei cathepsin B structure determined by using an x-ray laser. AU - Redecke, Lars. AU - Nass, Karol. AU - DePonte, Daniel P.. AU - White, Thomas A.. AU - Rehders, Dirk. AU - Barty, Anton. AU - Stellato, Francesco. AU - Liang, Mengning. AU - Barends, Thomas R M. AU - Boutet, Sébastien. AU - Williams, Garth J.. AU - Messerschmidt, Marc. AU - Seibert, M. Marvin. AU - Aquila, Andrew. AU - Arnlund, David. AU - Bajt, Sasa. AU - Barth, Torsten B.. AU - Bogan, Michael J.. AU - Caleman, Carl. AU - Chao, Tzu Chiao. AU - Doak, R. Bruce. AU - Fleckenstein, Holger. AU - Frank, Matthias. AU - Fromme, Raimund. AU - Galli, Lorenzo. AU - Grotjohann, Ingo. AU - Hunter, Mark S.. AU - Johansson, Linda C.. AU - Kassemeyer, Stephan. AU - Katona, Gergely. AU - Kirian, Richard A.. AU - Koopmann, Rudolf. AU - Kupitz, Chris. AU - Lomb, Lukas. AU - Martin, Andrew V.. AU - Mogk, Stefan. AU - Neutze, Richard. AU - Shoeman, Robert L.. AU - Steinbrener, Jan. AU - Timneanu, ...
https://ucdavis.pure.elsevier.com/en/publications/natively-inhibited-trypanosoma-brucei-cathepsin-b-structure-deter
Antibody Panel to Cathepsin Protease Family - Product Review 26 | acris-antibodies.com
Introduction: The Cathepsins are a group of lysosomal thiol proteinases or endopeptidases found in extracts of various tissues.Cathepsins, with the…
https://us.acris-antibodies.com/reviews/antibody-panel-cathepsin-protease-family.htm
JCI - A dyad of lymphoblastic lysosomal cysteine proteases degrades the antileukemic drug l-asparaginaseJCI - A dyad of lymphoblastic lysosomal cysteine proteases degrades the antileukemic drug l-asparaginase
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 ...
https://www.jci.org/articles/view/37977/sd/1
New Therapeutic Target Discovered for Alzheimers DiseaseNew Therapeutic Target Discovered for Alzheimers Disease
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.
https://health.ucsd.edu/news/releases/Pages/2014-03-17-17-new-therapeutic-alzheimers-target.aspx
Fluorescent probes towards selective cathepsin B detection and visualization in cancer cells and patient samplesFluorescent probes towards selective cathepsin B detection and visualization in cancer cells and patient samples
Human cysteine cathepsins constitute an 11-membered family of proteases responsible for degradation of proteins in cellular endosomal-lysosomal compartments as such, they play important roles in antigen processing, cellular stress signaling, autophagy, and senescence. Moreover, for many years these …
https://pubmed.ncbi.nlm.nih.gov/31803426/
Cathepsin S Is Involved in Th17 Differentiation Through the Upregulation of IL-6 by Activating PAR-2 after Systemic Exposure to...
TY - JOUR. T1 - Cathepsin S Is Involved in Th17 Differentiation Through the Upregulation of IL-6 by Activating PAR-2 after Systemic Exposure to Lipopolysaccharide from Porphyromonas gingivalis. AU - Dekita, Masato. AU - Wu, Zhou. AU - Ni, Junjun. AU - Zhang, Xinwen. AU - Liu, Yicong. AU - Yan, Xu. AU - Nakanishi, Hiroshi. AU - Takahashi, Ichiro. PY - 2017. Y1 - 2017. N2 - Positive links have been found between periodontitis and numerous diseases in humans via persistent inflammation throughout the body. However, the main factors responsible for maintaining this pro-inflammatory condition are poorly understood. The spleen, the largest secondary immune organ, is a central hub regulating the immune response/inflammation due to the dendritic cell (DC) response to CD4(+) T cell subtype differentiation, and lysosomal proteinase cathepsin S (CatS) is known to be involved in DC functions. In the present study, we found that CatS-induced IL-6 production by splenic DCs subsequently promotes Th17 ...
https://kyushu-u.pure.elsevier.com/en/publications/cathepsin-s-is-involved-in-th17-differentiation-through-the-upreg
KAKEN - Research Projects | Involvement of Cathepsins in Osteoporosis and Allergy and Cathepsin Inhibitors as the New...KAKEN - Research Projects | Involvement of Cathepsins in Osteoporosis and Allergy and Cathepsin Inhibitors as the New...
Principal Investigator：KATUNUMA Nobuhiko, Project Period (FY)：1989 - 1990, Research Category：Grant-in-Aid for Developmental Scientific Research (B)., Research Field：Pathological medical chemistry
https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-01870018/
JCI - Extracellular matrix proteomics identifies molecular signature of symptomatic carotid plaquesJCI - Extracellular matrix proteomics identifies molecular signature of symptomatic carotid plaques
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.. ...
https://j8k9.com.www.mobile.jci.org/articles/view/86924/pdf
JCI - Extracellular matrix proteomics identifies molecular signature of symptomatic carotid plaquesJCI - Extracellular matrix proteomics identifies molecular signature of symptomatic carotid plaques
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.. ...
https://j8k9.com.www.mobile.jci.org/articles/view/86924/figure/1
CST - Microglia Neurodegeneration Module Antibody Sampler KitCST - Microglia Neurodegeneration Module Antibody Sampler Kit
Antibody Sampler Kit for studying ASC mouse/Axl/Cathepsin B/CD68/galectin-3/HIF1A/HIF1A (Pro564) hydroxylate/HS1 in the Neuroscience research area.
https://www.cellsignal.com/products/primary-antibodies/microglia-neurodegeneration-module-antibody-sampler-kit/93195
LSHTM Research OnlineLSHTM Research Online
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 ...
https://researchonline.lshtm.ac.uk/view/creators/eadmhwhi.type.html
Browsing ICR Divisions by subject Cysteine Endopeptidases
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 ...
https://repository.icr.ac.uk/handle/internal/1/browse?value=Cysteine+Endopeptidases&type=subject
CathepsinCathepsin
... 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 are ... Cathepsin K has also been shown to play a role in arthritis. Mouse cathepsin L is homologous to human cathepsin V. Mouse ...
https://en.wikipedia.org/wiki/Cathepsin
Cathepsin TCathepsin T
... (EC 3.4.22.24) is an enzyme. This enzyme catalyses the following chemical reaction: Interconversion of the three ... Cathepsin+T at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.22). ... Cathepsin Gohda E, Pitot HC (May 1981). "Purification and characterization of a new thiol proteinase from rat kidney". ... Pitot HC, Gohda E (1987). "Cathepsin T". Methods in Enzymology. 142: 279-89. doi:10.1016/s0076-6879(87)42038-7. PMID 2885716. ...
https://en.wikipedia.org/wiki/Cathepsin_T
Cathepsin FCathepsin F
... is a protein that in humans is encoded by the CTSF gene. Cysteine cathepsins are a family of cysteine proteases ... The cathepsin F gene is ubiquitously expressed, and it maps to chromosome 11q13, close to the gene encoding cathepsin W. ... Wex T, Levy B, Wex H, Brömme D (1999). "Human cathepsins F and W: A new subgroup of cathepsins". Biochem. Biophys. Res. Commun ... Wex T, Wex H, Brömme D (2000). "The human cathepsin F gene--a fusion product between an ancestral cathepsin and cystatin gene ...
https://en.wikipedia.org/wiki/Cathepsin_F
Cathepsin LCathepsin L
... may refer to: Cathepsin L1, a human protease enzyme encoded by the CTSL gene and known for its role in viral entry ... Cathepsin L2, a human protease enzyme encoded by the CTSV gene and also known as cathepsin V This disambiguation page lists ... articles associated with the title Cathepsin L. If an internal link led you here, you may wish to change the link to point ...
https://en.wikipedia.org/wiki/Cathepsin_L
Cathepsin WCathepsin W
"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 ... The protein encoded by this gene, a member of the peptidase C1 family of cysteine cathepsins, is a cysteine protease cathepsin ... 2003). "Characterization of novel anti-cathepsin W antibodies and cellular distribution of cathepsin W in the gastrointestinal ...
https://en.wikipedia.org/wiki/Cathepsin_W
Cathepsin SCathepsin S
... cathepsin S can be replaced by cathepsin F. Secreted cathepsin S cleaves some extracellular matrix (ECM) proteins. Cathepsin S ... "Engineering the S2 subsite specificity of human cathepsin S to a cathepsin L- and cathepsin B-like specificity". The Journal of ... 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 ...
https://en.wikipedia.org/wiki/Cathepsin_S
Cathepsin XCathepsin X
... (EC 3.4.18.1, cathepsin B2, cysteine-type carboxypeptidase, cathepsin IV, cathepsin Z, acid carboxypeptidase, ... Shows weak endopeptidase activity Cathepsin X is a cysteine cathepsin, a lysosomal cysteine peptidase of family C1 (papain ... Otto K, Riesenkönig H (February 1975). "Improved purification of cathepsin B1 and cathepsin B2". Biochimica et Biophysica Acta ... "On the substrate specificity of cathepsins B1 and B2 including a new fluorogenic substrate for cathepsin B1". Life Sciences. 17 ...
https://en.wikipedia.org/wiki/Cathepsin_X
Cathepsin DCathepsin D
... can also be found in the extracellular space and it is one of the few cathepsins, that shows some activity at ... Cathepsin D is an aspartic endo-protease that is ubiquitously distributed in lysosomes. The main function of cathepsin D is to ... "Entrez Gene: CTSD cathepsin D". Barrett AJ (April 1970). "Cathepsin D. Purification of isoenzymes from human and chicken liver ... The optimum pH for cathepsin D in vitro is 4.5-5.0. Cathepsin-D is an aspartic protease that depends critically on protonation ...
https://en.wikipedia.org/wiki/Cathepsin_D
Cathepsin KCathepsin K
... is degraded by Cathepsin S, in a process referred to as Controlled Cathepsin Cannibalism. Cathepsin K expression is ... 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 enzyme by various cells. Merck had a cathepsin K ... Other cathepsin K inhibitors are in various stages of development. Medivir has a cathepsin K inhibitor, MIV-711 (L-006235), in ...
https://en.wikipedia.org/wiki/Cathepsin_K
Cathepsin ZCathepsin Z
... cathepsin C, cathepsin F, cathepsin H, cathepsin K, cathepsin L, cathepsin L2 or V, cathepsin O, cathepsin S, cathepsin Z, and ... 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-binding Arg-Gly-Asp motif within the propeptide of the enzyme, through which cathepsin Z ...
https://en.wikipedia.org/wiki/Cathepsin_Z
Cathepsin L1Cathepsin L1
"Entrez Gene: CTSL1 cathepsin L1". Barrett AJ, Kirschke H (1981). "Cathepsin B, Cathepsin H, and cathepsin L". Methods in ... or by cathepsins (primarily cathepsin L) in endolysosomes. Hydroxychloroquine inhibits the action of cathepsin L in ... Cathepsin L1 is a protein that in humans is encoded by the CTSL1 gene. The protein is a cysteine cathepsin, a lysosomal ... Cathepsin L1 is a member of the Peptidase C1 (cathepsin) MEROPS family, which plays an important role in diverse processes ...
https://en.wikipedia.org/wiki/Cathepsin_L1
Cathepsin HCathepsin H
... is a protein that in humans is encoded by the CTSH gene. The protein encoded by this gene is a cysteine cathepsin, ... "Entrez Gene: CTSH cathepsin H". Sawicki G, Warwas M (1990). "Cathepsin H from human placenta". Acta Biochim. Pol. 36 (3-4): 343 ... 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 ...
https://en.wikipedia.org/wiki/Cathepsin_H
Cathepsin GCathepsin 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 ...
https://en.wikipedia.org/wiki/Cathepsin_G
Cathepsin CCathepsin C
... 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 ... "Entrez Gene: CTSC cathepsin C". Paris A, Strukelj B, Pungercar J, Renko M, Dolenc I, Turk V (Aug 1995). "Molecular cloning and ...
https://en.wikipedia.org/wiki/Cathepsin_C
Cathepsin zymographyCathepsin zymography
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 ...
https://en.wikipedia.org/wiki/Cathepsin_zymography
Cathepsin L2Cathepsin L2
... , (EC 3.4.22.43, also known as cathepsin V or cathepsin U), is a protein encoded in humans by the CTSV gene. The ... "Entrez Gene: CTSL2 cathepsin L2". Brömme D, Li Z, Barnes M, Mehler E (February 1999). "Human cathepsin V functional expression ... 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. ...
https://en.wikipedia.org/wiki/Cathepsin_L2
Cathepsin ACathepsin A
... is an enzyme that is classified both as a cathepsin and a carboxypeptidase. In humans, it is encoded by the CTSA ... Cathepsin+A at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology v t e (Genes on human ... "Entrez Gene: CTSA cathepsin A". Mitchell, Richard Sheppard; Kumar, Vinay; Robbins, Stanley L.; Abbas, Abul K.; Fausto, Nelson ( ... Cathepsin A has been shown to interact with NEU1. GRCh38: Ensembl release 89: ENSG00000064601 - Ensembl, May 2017 GRCm38: ...
https://en.wikipedia.org/wiki/Cathepsin_A
Cathepsin OCathepsin O
... is an enzyme that in humans is encoded by the CTSO gene. Cathepsin O is a cysteine cathepsin, a cysteine protease ... "Entrez Gene: cathepsin O". Shi GP, Chapman HA, Bhairi SM, et al. (1995). "Molecular cloning of human cathepsin O, a novel ... 1994). "Human cathepsin O. Molecular cloning from a breast carcinoma, production of the active enzyme in Escherichia coli, and ... "Genomic structure and chromosomal localization of the human cathepsin O gene (CTSO)". Genomics. 53 (2): 231-4. doi:10.1006/geno ...
https://en.wikipedia.org/wiki/Cathepsin_O
Cathepsin ECathepsin E
... cathepsin D-like acid proteinase, cathepsin E-like acid proteinase, cathepsin D-type proteinase) is an enzyme. Cathepsin E is a ... The structure of Cathepsin E is very similar to those of Cathepsin D and BACE1, and all 3 have almost identical active site ... Along with renin and Cathepsin D, Cathepsin E is one of the only few aspartic proteases known to be made in human tissues other ... A distinguishing factor of Cathepsin E in comparison with the structure of Cathepsin D and BACE1 can be seen at the formation ...
https://en.wikipedia.org/wiki/Cathepsin_E
Cathepsin BCathepsin B
In humans, cathepsin B is encoded by the CTSB gene. Cathepsin B is upregulated in certain cancers, in pre-malignant lesions, ... Cathepsin B belongs to a family of lysosomal cysteine proteases known as the cysteine cathepsins and plays an important role in ... Cathepsin B has been shown to interact with: CTSD CSTA, CSTB, and S100A10. Cathepsin B is inhibited by: Nitroxoline CA-074 ... Cathepsin B has been proposed as a potentially effective biomarker for a variety of cancers. Overexpression of cathepsin B is ...
https://en.wikipedia.org/wiki/Cathepsin_B
ChromatinChromatin
... , Histones & Cathepsin; PMAP The Proteolysis Map-animation Nature journal: recent chromatin publications and news ...
https://en.wikipedia.org/wiki/Chromatin
Polysulfated glycosaminoglycanPolysulfated glycosaminoglycan
... collagenases such as cathepsin B1; and hyaluronidase. PSGAG inhibits the synthesis of prostaglandin E2, which is released upon ...
https://en.wikipedia.org/wiki/Polysulfated_glycosaminoglycan
Carboxypeptidase CCarboxypeptidase C
Cathepsin A Breddam, K. (1986). "Serine carboxypeptidases. A review". Carlsberg Res. Commun. 51: 83-128. doi:10.1007/bf02907561 ... Miller JJ, Changaris DG, Levy RS (December 1992). "Purification, subunit structure and inhibitor profile of cathepsin A". ... Carboxypeptidase C (EC 3.4.16.5, carboxypeptidase Y, serine carboxypeptidase I, cathepsin A, lysosomal protective protein, ...
https://en.wikipedia.org/wiki/Carboxypeptidase_C
KeratinocyteKeratinocyte
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. ...
https://en.wikipedia.org/wiki/Keratinocyte
Batten diseaseBatten disease
Cathepsin D is involved in CLN10. DNA analysis can be used to help confirm the diagnosis of Batten disease. When the mutation ...
https://en.wikipedia.org/wiki/Batten_disease
MedivirMedivir
Miv-711 Cathepsin K inhibitor for osteoarthritis. Fast track (FDA) MALT1 "Swedish pharma firm Medivir partners Aragen Life ...
https://en.wikipedia.org/wiki/Medivir
Protease inhibitor (biology)Protease inhibitor (biology)
... these include cathepsin L, papain, and procaricain. It forms an alpha-helical domain that runs through the substrate-binding ...
https://en.wikipedia.org/wiki/Protease_inhibitor_(biology)
CUX1CUX1
"Cathepsins as transcriptional activators? Developmental Cell 2004, 6(5):610-1. Goulet B, and Nepveu A. "Complete and Limited ...
https://en.wikipedia.org/wiki/CUX1
HistolysainHistolysain
Lushbaugh WB, Hofbauer AF, Pittman FE (June 1985). "Entamoeba histolytica: purification of cathepsin B". Experimental ...
https://en.wikipedia.org/wiki/Histolysain
Cystatin BCystatin B
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 ...
https://en.wikipedia.org/wiki/Cystatin_B
4P6E: Crystal Structure Of Human Cathepsin S Bound To A Non-covalent Inhibitor4P6E: Crystal Structure Of Human Cathepsin S Bound To A Non-covalent Inhibitor
CATHEPSIN SN-[(8r)-8-(Benzoylamino)-5,6,7,8-Tetrahydronaphthalen-2-Yl]-4-Methylpiperazine-1-CarboxamideSulfate Ion ... 4P6E: Crystal Structure Of Human Cathepsin S Bound To A Non-covalent Inhibitor. ...
https://www.ncbi.nlm.nih.gov/Structure/pdb/4P6E
Inhibiting Cathepsin G to Protect Against Photoaging and Infraaging | Cosmetics & ToiletriesInhibiting Cathepsin G to Protect Against Photoaging and Infra'aging | Cosmetics & Toiletries
Polygonum aviculare extract is a cathepsin G inhibitor, and is shown here to oppose photoaging and infraaging by improving ... Cathepsin G activity: The effect of Polygonum aviculare extracta on cathepsin G activity was evaluated using an enzymatic assay ... In addition, cathepsin G has been shown in vitro to degrade elastin into fragments that can be further processed by elastase.9 ... The cathepsin G inhibitor phosphonic acid served as a positive control. Results presented in Figure 2 show a neat inhibition of ...
https://www.cosmeticsandtoiletries.com/cosmetic-ingredients/actives/article/21835979/inhibiting-cathepsin-g-to-protect-against-photoaging-and-infraaging
Rat Cathepsin S (CTSS) ELISA kit | CSB-EL006204RA | CusabioRat Cathepsin S (CTSS) ELISA kit | CSB-EL006204RA | Cusabio
Rat Cathepsin S (CTSS) ELISA kit from Cusabio. Cat#: CSB-EL006204RA. US, UK & Europe Distribution. Online Order or Request ... Rat Cathepsin S (CTSS) ELISA kit , CSB-EL006204RA Cusabio Elisa Rat Cathepsin S (CTSS) ELISA kit , CSB-EL006204RA. (No reviews ... Recombinant Human Cathepsin S (CTSS) , CSB-EP006204HU , CusabioAlternative Name(s): Cathepsin S; CathepsinS; CATS_HUMAN; ... Human Cathepsin S (CTSS) ELISA Kit , CSB-E13722h , CusabioHuman Cathepsin S (CTSS) ELISA Kit is Available at Gentaur Genprice ...
https://joplink.net/rat-cathepsin-s-ctss-elisa-kit-csb-el006204ra/
Peripheral Role of Cathepsin S in Th1 Cell-Dependent Transition of Nerve Injury-Induced Acute Pain to a Chronic Pain State |...Peripheral Role of Cathepsin S in Th1 Cell-Dependent Transition of Nerve Injury-Induced Acute Pain to a Chronic Pain State |...
Peripheral Role of Cathepsin S in Th1 Cell-Dependent Transition of Nerve Injury-Induced Acute Pain to a Chronic Pain State. ... Peripheral Role of Cathepsin S in Th1 Cell-Dependent Transition of Nerve Injury-Induced Acute Pain to a Chronic Pain State ... Peripheral Role of Cathepsin S in Th1 Cell-Dependent Transition of Nerve Injury-Induced Acute Pain to a Chronic Pain State ... Peripheral Role of Cathepsin S in Th1 Cell-Dependent Transition of Nerve Injury-Induced Acute Pain to a Chronic Pain State ...
https://www.jneurosci.org/content/34/8/3013/tab-e-letters
Peptide synthesis by recombinant Fasciola hepatica cathepsin L1 - DORASPeptide synthesis by recombinant Fasciola hepatica cathepsin L1 - DORAS
Ruth, Deborah M., McMahon, Gillian and Ó Fágáin, Ciarán (2006) Peptide synthesis by recombinant Fasciola hepatica cathepsin L1. ... fasciola hepatica cathepsin L1; recombinant; enzymatic peptide synthesis; cysteine proteinase;. Subjects:. Biological Sciences ... Synthesis of the tripeptide Z-Phe-Arg-SerNH2 has been accomplished by a recombinant cysteine protease, cathepsin L1 from liver ...
https://doras.dcu.ie/78/
Cathepsins - Proteases - Proteins and Enzymes - ProductsCathepsins - Proteases - Proteins and Enzymes - Products
... but it is currently unclear how cathepsins mediate apoptosis. Cathepsins are lysosomal enzymes that are also used as sensitive ... The cathepsin assays are simple, straightforward, and can be adapted to 96-well plate assays. Assay conditions have been ... BioVisions newly developed Cathepsin Activity Assay kits are fluorescence-based assays that utilize the preferred substrate ... Cell lysates or other samples that contain cathepsins will cleave the synthetic substrate to release free AFC. The released ...
https://www.biovision.com/products/proteins-and-enzymes/proteases/cathepsins.html
Ward, C., Kuehn, D., Burden, R.E., et al. (2010) Antibody targeting of cathepsin S inhibits angiogenesis and synergistically...Ward, C., Kuehn, D., Burden, R.E., et al. (2010) Antibody targeting of cathepsin S inhibits angiogenesis and synergistically...
2010) Antibody targeting of cathepsin S inhibits angiogenesis and synergistically enhances anti-VEGF. PLoS One, 5, Article ID ... TITLE: Antibody research targeting Cathepsin S for cancer therapy AUTHORS: Hang Fai Kwok KEYWORDS: Cathepsin S; Tumor; ... ABSTRACT: Cathepsin S is a cysteine protease highly expressed in many type of cancers including colorectal, prostate, breast, ... Immunoexpression of Cathepsin D and S100A4 Protein and Their Molecular Subtyptes in Canine Mammary Carcinomas ...
https://scirp.org/reference/referencespapers.aspx?referenceid=786161
Investigating the role of cathepsin S in the pathogenesis of cystic fibrosis-like lung disease | European Respiratory SocietyInvestigating the role of cathepsin S in the pathogenesis of cystic fibrosis-like lung disease | European Respiratory Society
Investigating the role of cathepsin S in the pathogenesis of cystic fibrosis-like lung disease. Ryan Brown, Donna Small, ... Elevated levels of the cysteine protease cathepsin S (cat S) are found in cystic fibrosis (CF) lung secretions, however, the ... Investigating the role of cathepsin S in the pathogenesis of cystic fibrosis-like lung disease ... Investigating the role of cathepsin S in the pathogenesis of cystic fibrosis-like lung disease ...
https://erj.ersjournals.com/content/46/suppl_59/PA3903
Human Cathepsin D ELISA Kit Price PicoKine® | BosterBioHuman Cathepsin D ELISA Kit Price PicoKine® | BosterBio
Human Cathepsin D ELISA Kit PicoKine™ (96 Tests). Quantitate Human CTSD in cell culture supernatants, cell lysates, serum ... More Cathepsin D Products. *Mouse Cathepsin D ELISA Kit PicoKine® (EK0673). *Human Cathepsin D PicoKine® Quick ELISA Kit ( ... Human Cathepsin D ELISA Kit PicoKine®. Cathepsin D ELISA kit for Human. Human Cathepsin D ELISA Kit PicoKine™ (96 Tests). ... Background of Cathepsin D. Cathepsin D is a protein that in humans is encoded by the CTSD gene. This proteinase is a member of ...
https://www.bosterbio.com/human-cathepsin-d-picokine-trade-elisa-kit-ek0672-boster.html
Two-step mechanism of inhibition of cathepsin B by cystatin C, due to the inhibitor displacing the occluding loop of the enzyme...Two-step mechanism of inhibition of cathepsin B by cystatin C, due to the inhibitor displacing the occluding loop of the enzyme...
Cysteine proteinase, Cysteine proteinase inhibitor, Cathepsin, Cystatin, Kinetics. in FEBS Letters. volume. 422. issue. 1. ... Two-step mechanism of inhibition of cathepsin B by cystatin C, due to the inhibitor displacing the occluding loop of the enzyme ... Stopped-flow kinetics showed that the inhibition of the lysosomal cysteine proteinase, cathepsin B, by its endogenous inhibitor ... Stopped-flow kinetics showed that the inhibition of the lysosomal cysteine proteinase, cathepsin B, by its endogenous inhibitor ...
https://lup.lub.lu.se/search/publication/1113877
Expression of the elastolytic cathepsins S and K in human atheroma and regulation of their production in smooth muscle cellsExpression of the elastolytic cathepsins S and K in human atheroma and regulation of their production in smooth muscle cells
A selective inhibitor of cathepsin S blocked , 80% of this elastolytic activity. The presence of cathepsins K and S at sites of ... Expression of the elastolytic cathepsins S and K in human atheroma and regulation of their production in smooth muscle cells. ... Expression of the elastolytic cathepsins S and K in human atheroma and regulation of their production in smooth muscle cells. ... "Expression of the Elastolytic Cathepsins S and K in Human Atheroma and Regulation of Their Production in Smooth Muscle Cells." ...
https://dash.harvard.edu/handle/1/13506487?show=full
Cathepsin H, Human Liver | Athens Research & Technology
A more basic protein than Cathepsin B or L. Functions as both an aminopeptidase and endopeptidase. Cathepsin H, like cathepsin ... Gel Scan of Cathepsin H, Human Liver. This information is representative of the product ART prepares, but is not lot specific. ... "Cathepsin H functions as an aminopeptidase in secretory vesicles for production of enkephalin and galanin peptide ...
https://www.athensresearch.com/products/all/cathepsin-h-human-liver
Disruption of the Cathepsin K gene reduces atherosclerosis progression and induces plaque fibrosis but accelerates macrophage...
BACKGROUND-: Cathepsin K (catK), a lysosomal cysteine protease, was identified in a gene-profiling experiment that compared ... abstract = "BACKGROUND-: Cathepsin K (catK), a lysosomal cysteine protease, was identified in a gene-profiling experiment that ... keywords = "Atherosclerosis, Cathepsins, Lipids, Pathology, Proteases",. author = "E. Lutgens and Lutgens, {S. P.M.} and Faber ... N2 - BACKGROUND-: Cathepsin K (catK), a lysosomal cysteine protease, was identified in a gene-profiling experiment that ...
https://mayoclinic.pure.elsevier.com/en/publications/disruption-of-the-cathepsin-k-gene-reduces-atherosclerosis-progre
Differential expression of Cathepsin E in transthyretin amyloidosis: from neuropathology to the immune system | Journal of...Differential expression of Cathepsin E in transthyretin amyloidosis: from neuropathology to the immune system | Journal of...
Cathepsin E (CtsE) is an important intermediate for antigen presentation and chemotaxis, but its role in the pathogenesis of ... Cathepsin E (CtsE) is an important intermediate for antigen presentation and chemotaxis, but its role in the pathogenesis of ... Cathepsin E (CtsE) is an aspartic protease mainly located at the endosomal compartment but also found in the endoplasmic ... Expression of Cathepsin E is downregulated in injured nerves from V30M animals. We have previously performed a transcriptomic ...
https://jneuroinflammation.biomedcentral.com/articles/10.1186/s12974-017-0891-9
Matrix-metalloproteinase-9 is cleaved and activated by Cathepsin K | BMC Research Notes | Full TextMatrix-metalloproteinase-9 is cleaved and activated by Cathepsin K | BMC Research Notes | Full Text
... treatment of recombinant proMMP-9 with recombinant cathepsin K (CTSK) at pH 5 yielded a fragment that corresponded to the ... Drake FH, Dodds RA, James IE, Connor JR, Debouck C, Richardson S et al (1996) Cathepsin K, but not cathepsins B, L, or S, is ... Lysosomal cysteine cathepsin (LCC) is a subgroup of the family of cathepsin proteases that requires an acidic environment for ... Activators of MMP-9 include MMP-2 [14, 15], MMP-3 [14, 16], MMP-7 [17], MMP-10 [18], MMP-13 [19], cathepsin G [20] and ...
https://bmcresnotes.biomedcentral.com/articles/10.1186/s13104-015-1284-8
Cathepsin K (CTSK) Antibody | Abbexa LtdCathepsin K (CTSK) Antibody | Abbexa Ltd
Cathepsin K Antibody is a Mouse Monoclonal against Cathepsin K. ... Anti-Cathepsin O, Anti-Cathepsin O antibody, Cathepsin O ... Anti-Cathepsin X, Anti-Cathepsin X antibody, Cathepsin X antibody, Antibody against Cathepsin X ... Cathepsin K Antibody is a Mouse Monoclonal against Cathepsin K. Target. Cathepsin K (CTSK). ... CTS-K, CTS02, CTSO, CTSO1, CTSO2, PKND, PYCD, Pycnodysostosis, Cathepsin O, Cathepsin X, Anti-CTS-K, Anti-CTS-K antibody, CTS-K ...
https://www.abbexa.com/cathepsin-k-antibody-6
InnoZyme™ Cathepsin B Activity Assay Kit, Fluorogenic | CBA001InnoZyme™ Cathepsin B Activity Assay Kit, Fluorogenic | CBA001
Cathepsin B Activity Assay Kit, Fluorogenic - Find MSDS or SDS, a COA, data sheets and more information. ... Table 2: Cathepsin B activity in cell lysates. Cathepsin B activity in five human cell line lysates as measured with Cathepsin ... Cathepsin B Inhibitor, Reduction Reagent, Cathepsin B Substrate, and Calibration Standard at -20°C. Control Cathepsin B(aliquot ... Cathepsin B Inhibitor, Reduction Reagent, Cathepsin B Substrate, and Calibration Standard at -20°C. Control Cathepsin B(aliquot ...
https://www.emdmillipore.com/PR/en/product/InnoZyme-Cathepsin-B-Activity-Assay-Kit-Fluorogenic,EMD_BIO-CBA001
Cathepsin S-mediated autophagic flux in tumor-associated macrophages accelerate tumor development by promoting M2 polarization ...Cathepsin S-mediated autophagic flux in tumor-associated macrophages accelerate tumor development by promoting M2 polarization ...
Cathepsin S (Cat S) expression was analyzed in human colon carcinoma and normal colon tissues. In vivo effects were evaluated ... Cathepsin S (Cat S), unlike the ubiquitous cathepsin B (Cat B) and cathepsin L (Cat L), exhibits a restricted tissue expression ... cathepsins are now recognized that cysteine proteases play pivotal roles in cancer progression[20]. Of the cysteine cathepsins ... Cathepsin S (Cat S) expression was analyzed in human colon carcinoma and normal colon tissues. In vivo effects were evaluated ...
https://molecular-cancer.biomedcentral.com/articles/10.1186/1476-4598-13-43
Cathepsin S dominates autoantigen processing in human thymic dendritic cellsCathepsin S dominates autoantigen processing in human thymic dendritic cells
... Author: Stoeckle, Christina; Quecke, Paula; ... Cathepsin S dominates autoantigen processing in human thymic dendritic cells. DSpace Repository. Login ...
https://publikationen.uni-tuebingen.de/xmlui/handle/10900/50952
Cathepsin | 组织蛋白酶 | 抑制剂 | MCECathepsin | 组织蛋白酶 | 抑制剂 | MCE
There are about 15 classes of cathepsins in humans (Cathepsin A, B, C, D, E, F, G, H, K, L, O, S, V, W, and Z). ... Cathepsins are vital for digestion, coagulation, immune response, adipogenesis, hormone liberation, peptide synthesis, among a ... Cathepsins are proteases with serine, cysteine, or aspartic acid residues as the nucleophiles. ... Cathepsin X-IN-1 Inhibitor 98.81% Cathepsin X-IN-1 (compound 25) 是一种有效的 组织蛋白酶 X 抑制剂，IC50 为 7.13 µM。Cathepsin X-IN-1 降低 PC-3 细胞迁 ...
https://www.medchemexpress.cn/Targets/Cathepsin.html
Cathepsin H › PeptaNovaCathepsin H › PeptaNova
SKU: 3113-v Category: Cathepsin and Thiol Protease Substrates Tags: Cathepsin H, substrate ...
https://peptanova.de/product-tag/cathepsin-h/
Inhibition of cathepsin B activity attenuates extracellular matrix degradation and inflammatory breast cancer invasion | Breast...Inhibition of cathepsin B activity attenuates extracellular matrix degradation and inflammatory breast cancer invasion | Breast...
A functional role for cathepsin B was confirmed by the ability of CA074, a cell impermeable and highly selective cathepsin B ... Here we explored a role for active cathepsin B on the cell surface in the invasiveness of IBC. We examined expression of the ... Our study is the first to show that the proteolytic activity of cathepsin B and its co-expression with caveolin-1 contributes ... A statistically significant co-expression of cathepsin B and caveolin-1 was found in IBC patient biopsies, thus validating our ...
https://breast-cancer-research.biomedcentral.com/articles/10.1186/bcr3058
November | 2015 | Cathepsin K
Cathepsin K. Cathepsin K is a cysteine protease expressed predominantly in osteoclasts. Search. Main menu. Skip to primary ...
https://cathepsink.com/2015/11
Cathepsin D - MRM ProteomicsCathepsin D - MRM Proteomics
MRM Proteomics Inc. was established in 2010 as a spin-out company to commercialize the cutting-edge proteomics technologies, tools and know-how developed at the University of Victoria-Genome BC Proteomics Centre.. ...
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Cathepsin-K immunoreactivity distinguishes MiTF/TFE family renal translocation carcinomas from other renal carcinomasCathepsin-K immunoreactivity distinguishes MiTF/TFE family renal translocation carcinomas from other renal carcinomas
None of the other renal neoplasms expressed cathepsin-K. We conclude the following: (1) cathepsin-K is consistently and ... 2) Cathepsin-K immunolabeling in both TFE3 and TFEB translocation renal cell carcinomas distinguishes these neoplasms from the ... Cathepsin-K immunoreactivity distinguishes MiTF/TFE family renal translocation carcinomas from other renal carcinomas Academic ... We studied cathepsin-K in 17 cytogenetically confirmed microphthalmia transcription factor/TFE-family translocation renal cell ...
http://scholars.uab.edu/display/pub2040920
Cathepsin C is a tissue-specific regulator of squamous carcinogenesis<...Cathepsin C is a tissue-specific regulator of squamous carcinogenesis<...
title = "Cathepsin C is a tissue-specific regulator of squamous carcinogenesis",. abstract = "Serine and cysteine cathepsin ( ... Cathepsin C is a tissue-specific regulator of squamous carcinogenesis. In: Genes and Development. 2013 ; Vol. 27, No. 19. pp. ... Cathepsin C is a tissue-specific regulator of squamous carcinogenesis. Genes and Development. 2013 Oct 1;27(19):2086-2098. doi ... Cathepsin C is a tissue-specific regulator of squamous carcinogenesis. Brian Ruffell, Nesrine I. Affara, Lucia Cottone, Simon ...
https://ohsu.pure.elsevier.com/en/publications/cathepsin-c-is-a-tissue-specific-regulator-of-squamous-carcinogen-2
IMSEAR at SEARO: Isolation, purification and properties of cathepsin B from buffalo liver.
The amino acid composition of buffalo cathepsin B was found to be similar to that of human liver cathepsin B. The optical ... Isolation, purification and properties of cathepsin B from buffalo liver.. Authors: Salahuddin, A. Siddiqui, F A. Salahuddin, P ... Cathepsin B was isolated from buffalo liver by salt fractionation, ion-exchange resin treatment, gel filtration and repeated ... The results showed buffalo cathepsin B to be a single-chain molecule. The N- and C-terminal amino acids of the enzyme were ...
https://imsear.searo.who.int/handle/123456789/28679
March, 2018 | http://cathepsin-s.comMarch, 2018 | http://cathepsin-s.com
Hat also tested the things PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/22913204 verb type and canonicity, the statistical analyses ...
https://cathepsin-s.com/2018/03/
Recombinant Human Cathepsin L/CTSL (C-6His)Recombinant Human Cathepsin L/CTSL (C-6His)
... Shipped on dry ice. Store product at -20°C after arrival. Laboratory research use ...
https://www.pelobiotech.com/product-details/recombinant-human-cathepsin-l-ctsl-c-6his.html
Recombinant Human Cathepsin E(CTSE) (Active) - CusabioRecombinant Human Cathepsin E(CTSE) (Active) - Cusabio
Purchase Recombinant Human Cathepsin E(CTSE) (Active). It is produced in Mammalian cell. High purity. Good price. ... CATE; CATE_HUMAN; Cathepsin E; Cathepsin E form II; CTSE; Erythrocyte membrane aspartic proteinase ; Slow moving proteinase. ... Three-dimensional structure of cathepsin-E. PMID: 15845357. *the human cathepsin E gene is regulated by the constitutive ... Emerging roles of cathepsin E in immune system cells and skin keratinocytes, and in host defense against cancer cells. PMID: ...
https://www.cusabio.com/Other/Recombinant-Human-Cathepsin-E-CTSE--12923698.html
ProteasesInhibitorInhibitorsProteaseEnzymesEnzymePresence of cathepsinsCtsEProteinsFluorescenceAntibodyPeptideTumorAssayELISA KitXenopusExpressionCleavesRecombinantSubstrateMacrophagesGeneActivitySequenceAmino acidPathogenesisHomoDegradationCytokinesMechanismActiveDegrade elastinContrastMoleculePurificationInflammatory breast
Proteases9
  • There is growing recognition that alternative proteolytic enzymes such as the lysosomal cathepsin proteases may initiate or propagate proapoptotic signals, but it is currently unclear how cathepsins mediate apoptosis. (biovision.com)
  • Here, we explore the proteases Cathepsins L and D for forming protein fragments from three IgG1s, one IgG2, and one bispecific, knob-and-hole IgG1. (uu.nl)
  • Lysosomal cysteine cathepsin (LCC) is a subgroup of the family of cathepsin proteases that requires an acidic environment for optimal activation, and is found mainly in the acidic lysosomes where they participate in protein turnover and degradation of internalized ECM [ 25 ]. (biomedcentral.com)
  • CTSS is one of 11 cysteine cathepsin proteases, which is the largest cathepsin subclass. (biomedcentral.com)
  • Serine and cysteine cathepsin (Cts) proteases are an important class of intracellular and pericellular enzymes mediating multiple aspects of tumor development. (elsevier.com)
  • As well as activity in lysosomal protein degradation, cathepsin C also plays a key role in the activation of granule serine proteases in cytotoxic T cells, natural killer cells (granzymes A and B), mast cells (chymase and tryptase) and neutrophils (cathepsin G, neutrophil elastase, proteinase 3). (guidetoimmunopharmacology.org)
  • Cathepsins B and B-like proteases are identified in various species [ 3 ]. (ijbs.com)
  • Cathepsins B-like and L-like cysteine proteases are found in Caenorhabditis elegans [ 4 , 5 ]. (ijbs.com)
  • Moreover, several cathepsins and cathepsin-like proteases are revealed through functional and structural analyses in fishes, amphibians, reptiles, and birds in addition to mammals [ 11 ]. (ijbs.com)
Inhibitor6
  • 6, 7 Further, in one animal model of photoaging, a cathepsin G inhibitor prevented UVB-induced ECM degradation, suggesting activation of the enzyme by UVB as well. (cosmeticsandtoiletries.com)
  • Once activated, cathepsin G degrades fibronectin (FN) into fragments that induce and up-regulate the expression and activity of matrix metalloproteinase (MMP-1 and MMP-2) while simultaneously inhibiting the expression of tissue inhibitor of metalloproteinase-1 (TIMP-1)-the natural inhibitor of MMPs. (cosmeticsandtoiletries.com)
  • Stopped-flow kinetics showed that the inhibition of the lysosomal cysteine proteinase, cathepsin B, by its endogenous inhibitor, cystatin C, occurs by a two-step mechanism, in which an initial, weak interaction is followed by a conformational change. (lu.se)
  • article{d5c1ff8e-0690-4d5e-85b5-097b38cc0bdd, abstract = {{Stopped-flow kinetics showed that the inhibition of the lysosomal cysteine proteinase, cathepsin B, by its endogenous inhibitor, cystatin C, occurs by a two-step mechanism, in which an initial, weak interaction is followed by a conformational change. (lu.se)
  • A functional role for cathepsin B was confirmed by the ability of CA074, a cell impermeable and highly selective cathepsin B inhibitor, to significantly reduce pericellular proteolysis and invasion by SUM149 cells. (biomedcentral.com)
  • 100 muM for cathepsin B). This compound could act as a new lead for the further development of improved inhibitors within this inhibitor type. (canada.ca)
Inhibitors9
  • Active cathepsins, cathepsin inhibitors and cathepsin antibodies are also available. (biovision.com)
  • The Calbiochem ® Cathepsin B Activity Assay Kit, Fluorogenic is designed to measure cathepsin B activity in tissues extracts and cell lysates, and for screening cathepsin B inhibitors. (emdmillipore.com)
  • Exploration of the P1 SAR of aldehyde cathepsin K inhibitors. (expasy.org)
  • By screening a combinatorial pentapeptide amide collection in an inhibition assay, we systematically evaluated the potential of 19 proteinogenic amino acids and seven nonproteinogenic amino acids to serve as building blocks for inhibitors of human cathepsin L. Particularly efficient were aromatic, bulky, hydrophobic amino-acid residues, especially leucine, and positively charged residues, especially arginine. (uni-bielefeld.de)
  • This random approach for the design of inhibitors was introduced to compensate for the inaccuracy induced by shifted docking of combinatorial compound collections at the active center of cathepsin L. Thereby, we obtained structurally defined pentapeptide amides which inhibited human cathepsin L at nanomolar concentrations. (uni-bielefeld.de)
  • Among the most potent novel inhibitors, one peptide, RKLLW-NH2, shares the amphiphilic character of the nonamer fragment VMNGLQNRK of the autoinhibitory, substrate-like, but reverse-binding prosegment of human cathepsin L which blocks the active center of the enzyme. (uni-bielefeld.de)
  • Highly potent inhibitors of human cathepsin L identified by screening combinatorial pentapeptide amide collections", EUROPEAN JOURNAL OF BIOCHEMISTRY , vol. 267, 2000, pp. 5085-5092. (uni-bielefeld.de)
  • In a search for selective cathepsin L inhibitors as anticancer agents, a series of 2-cyanoprrolidine peptidomimetics, carrying a nitrile group as warhead, were designed. (canada.ca)
  • Inflammasome activation was confirmed using inhibitors of cathepsin B and Caspase-1. (cdc.gov)
Protease15
  • Synthesis of the tripeptide Z-Phe-Arg-SerNH2 has been accomplished by a recombinant cysteine protease, cathepsin L1 from liver fluke (Fasciola hepatica), using Z-Phe-Arg-OMe as acyl acceptor and SerNH2 as nucleophile in 0.1 M ammonium acetate pH 9.0-12.5% v/v acetonitrile at 37 °C. LC-MS detection indicated tripeptide formation after 10 min, continuing up to 5.5 h. (dcu.ie)
  • ABSTRACT: Cathepsin S is a cysteine protease highly expressed in many type of cancers including colorectal, prostate, breast, and glioblastoma's. (scirp.org)
  • Elevated levels of the cysteine protease cathepsin S (cat S) are found in cystic fibrosis (CF) lung secretions, however, the role of cat S in CF lung disease is unclear. (ersjournals.com)
  • Cathepsin G, a serine protease found in polymorphonuclear neutrophils (PMNs), functions in inflammation. (enzolifesciences.com)
  • BACKGROUND-: Cathepsin K (catK), a lysosomal cysteine protease, was identified in a gene-profiling experiment that compared human early plaques, advanced stable plaques, and advanced atherosclerotic plaques containing a thrombus, where it was highly upregulated in advanced stable plaques. (elsevier.com)
  • Cathepsin D is an estrogen-regulated, lysosomal acidic protease associated with tissue breakdown. (scrippslabs.com)
  • Cathepsins are protease enzymes, categorized into multiple families. (medchemexpress.cn)
  • Cathepsins can be serine protease, cysteine protease, or aspartyl protease. (medchemexpress.cn)
  • Dysregulated expression and activity of cathepsin S (CTSS), a lysosomal protease and a member of the cysteine cathepsin protease family, is linked to the pathogenesis of multiple diseases, including a number of conditions affecting the lungs. (biomedcentral.com)
  • In this review, we will focus on one cysteine protease in particular, cathepsin S (CTSS), and outline the research supporting its growing importance in pulmonary diseases and the potential of targeting of CTSS as a therapeutic option. (biomedcentral.com)
  • 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. (biomedcentral.com)
  • The Magic Red Cathepsin K Kit uses a quick and easy method to analyze intracellular cathepsin K protease activity in whole living cells. (bio-rad-antibodies.com)
  • Cathepsin Magic Red Kits measure cathepsin K protease activity by detecting active cathepsins in whole, living cells. (bio-rad-antibodies.com)
  • Cathepsin C (CatC) is a lysosomal cysteine protease that is constitutively expressed at high levels in lung, kidney, liver and spleen. (guidetoimmunopharmacology.org)
  • Cathepsin L superfamily is a multifunctional cysteine protease enzyme and widely distributed in most animals. (ijbs.com)
Enzymes5
  • Cathepsins are lysosomal enzymes that are also used as sensitive markers in various toxicological investigations. (biovision.com)
  • Normal arteries contained little or no cathepsin K or S. In contrast, macrophages in atheroma contained abundant immunoreactive cathepsins K and S. Intimal smooth muscle cells (SMC), especially cells appearing to traverse the internal elastic laminae, also contained these enzymes. (harvard.edu)
  • The presence of cathepsins K and S at sites of vascular matrix remodeling and the ability of SMC and macrophages to use these enzymes to degrade elastin supports a role for elastolytic cathepsins in vessel wall remodeling and identifies novel therapeutic targets in regulating plaque stability. (harvard.edu)
  • ENZYMES: Cathepsin L-EC 3.4.22.15, Cathepsin D-EC 3.4.23.5. (uu.nl)
  • As multifunctional enzymes, cysteine cathepsins widely exist particularly in lysosomes. (ijbs.com)
Enzyme5
  • Fifty plants initially were screened for activity against the cathepsin G enzyme to find the best botanical extract to inhibit its activity (data not shown). (cosmeticsandtoiletries.com)
  • The presence of this loop, which allows the enzyme to function as an exopeptidase, thus complicates the inhibition mechanism, rendering cathepsin B much less susceptible than other cysteine. (lu.se)
  • The amino acid composition of buffalo cathepsin B was found to be similar to that of human liver cathepsin B. The optical properties of the buffalo enzyme were found consistent with its aromatic amino acid content. (who.int)
  • Severe positive selection was also observed in cathepsin V (L2) of primates, indicating that this enzyme had some special functions. (ijbs.com)
  • Measurements of cell-associated enzyme activities showed that lactate dehydrogenase, acid phosphatase, and cathepsin D were significantly increased. (aai.org)
Presence of cathepsins1
  • Instead, their methodology is based on a cell-permeable and non-cytotoxic reagent which is cleaved in the presence of cathepsins to produce a fluorescent product. (bio-rad-antibodies.com)
CtsE1
  • Cathepsin E (CtsE) is an important intermediate for antigen presentation and chemotaxis, but its role in the pathogenesis of FAP disease remains unknown. (biomedcentral.com)
Proteins3
  • Cathepsin H, like cathepsin L and B, is involved in the catabolism of proteins in the lysosomal system. (athensresearch.com)
  • Rodents contain 10 cysteine cathepsins and carry additional genes that express other cathepsins and cathepsin-like proteins [ 10 ]. (ijbs.com)
  • Western blotting showed increased Cox-2, Cyclin E, KLF4 and c-myc proteins and decreased expression of Cathepsin D. In addition, the KLF4 protein was higher in the chemically-induced cell strains compared to the spontaneously-occurring cell strains while COX-2 was higher in the spontaneously-occurring cell strains. (cdc.gov)
Fluorescence2
  • BioVision's newly developed Cathepsin Activity Assay kits are fluorescence-based assays that utilize the preferred substrate sequence for each cathepsin, labeled with AFC (amino-4-trifluoromethyl coumarin). (biovision.com)
  • The CB-NP could accumulate in tumor tissues, enter into tumor cells, and generate fluorescent signals in cytosol in response to cathepsin B. The results of non-invasive fluorescence imaging in a tumor-bearing mouse model demonstrated the potential of CB-NP for tumor diagnosis in clinical fields. (elsevier.com)
Antibody4
  • 2010) Antibody targeting of cathepsin S inhibits angiogenesis and synergistically enhances anti-VEGF. (scirp.org)
  • In recent years, antibody research specifically targeting Cathepsin S to block/inhibit tumorigenic effects were generated some positive preclinical data. (scirp.org)
  • This mini-review provides an overview of therapeutic antibody targeting Cathepsin S strategies in the last half decade, focusing on the rationale of cell-surface Cathepsin S targeted and their potential clinical application. (scirp.org)
  • Cathepsin K Antibody is a Mouse Monoclonal against Cathepsin K. (abbexa.com)
Peptide4
  • Cathepsin H functions as an aminopeptidase in secretory vesicles for production of enkephalin and galanin peptide neurotransmitters. (athensresearch.com)
  • The Magic Red reagent contains a cathepsin K target sequence peptide (LR) 2 linked to a red (Cresyl Violet) fluorescent probe. (bio-rad-antibodies.com)
  • We developed a cathepsin B-sensitive nanoprobe (CB-NP) with a cathepsin B substrate peptide probe and tumor-targeting glycol chitosan nanoparticles. (elsevier.com)
  • Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes. (bioss.com.cn)
Tumor1
  • Expression array and real time PCR analysis demonstrated increased expression of the cell cycle inhibitory factor p16 and the apoptotic factor Cathepsin D in all of the tumor cell strains. (cdc.gov)
Assay1
  • The effect of Polygonum aviculare extract a on cathepsin G activity was evaluated using an enzymatic assay. (cosmeticsandtoiletries.com)
ELISA Kit4
  • Rat Cathepsin S (CTSS) ELISA kit is Available at Gentaur Genprice with the fastest delivery. (joplink.net)
  • CusabioHuman Cathepsin S (CTSS) ELISA Kit is Available at Gentaur Genprice with the fastest delivery.Online Order Payment is possible or send. (joplink.net)
  • CusabioRat Cathepsin L1 (CTSL1) ELISA kit is Available at Gentaur Genprice with the fastest delivery.Online Order Payment is possible or send. (joplink.net)
  • Human Cathepsin D ELISA Kit PicoKine™ (96 Tests). (bosterbio.com)
Xenopus1
  • Cathepsin L in zebrafish, cathepsins S and K in xenopus, and cathepsin L in mice and rats underwent evident tandem-repeat events. (ijbs.com)
Expression9
  • This study examined the expression of the potent elastases cathepsins S and K in human atheroma. (harvard.edu)
  • Over-expression of Cathepsin D is also linked to tumorigenesis in prostate cancer and to aggressive forms of colorectal cancer and lung adenocarcinoma. (scrippslabs.com)
  • Cathepsin S (Cat S) expression was analyzed in human colon carcinoma and normal colon tissues. (biomedcentral.com)
  • IBC patient biopsies were examined for expression of cathepsin B and caveolin-1. (biomedcentral.com)
  • A statistically significant co-expression of cathepsin B and caveolin-1 was found in IBC patient biopsies, thus validating our in vitro data. (biomedcentral.com)
  • Our study is the first to show that the proteolytic activity of cathepsin B and its co-expression with caveolin-1 contributes to the aggressiveness of IBC. (biomedcentral.com)
  • High Expression of Cathepsin E is associated with Tissues but Not Blood of Patients with Barrett's Esophagus and Adenocarcinoma. (cusabio.com)
  • In this work , we reveal the relationship between the expression of cathepsins and radioresistance in GBM. (bvsalud.org)
  • 18. Hie M, Shimono M, Fujii K, Tsukamoto I. Increased cathepsin K and tartrate-resistant acid phosphatase expression in bone of streptozotocin-induced diabetic rats. (bvsalud.org)
Cleaves1
  • Cathepsin cleaves prolactin into a 16kDa prolactin. (medscape.com)
Recombinant1
  • Also, treatment of recombinant proMMP-9 with recombinant cathepsin K (CTSK) at pH 5 yielded a fragment that corresponded to the molecular weight of active MMP-9, and showed MMP-9 activity. (biomedcentral.com)
Substrate1
  • Cell lysates or other samples that contain cathepsins will cleave the synthetic substrate to release free AFC. (biovision.com)
Macrophages1
  • Decreased activity of cathepsin E produced by decidual macrophages might be responsible for the induction of miscarriages in some recurrent miscarriage patients. (cusabio.com)
Gene2
  • Cathepsin D is a protein that in humans is encoded by the CTSD gene. (bosterbio.com)
  • Positive selection was the specific cause of differentiation of cathepsin L family genes, confirming that gene function variation after expansion events was related to interactions with the environment and adaptability. (ijbs.com)
Activity3
  • Cultured human SMC displayed no immunoreactive cathepsins K and S and exhibited little or no elastolytic activity when incubated with insoluble elastin. (harvard.edu)
  • A comparative structure model of splice variant 2 was computed based on its alignment to the known structure of cathepsin E intermediate (Protein Data Bank code 1TZS) and used to rationalize its conformational properties and loss of activity. (cusabio.com)
  • VGCFTM-H caused dose- and time-dependent increases in cathepsin activity and cytokines in the acellular lavage fluid, indicating activation of the NLRP3 inflammasome by VGCFTM-H may contribute to lung inflammation. (cdc.gov)
Sequence2
  • A DNA sequence encoding the Homo sapiens (Human) Cathepsin F, was expressed in the hosts and tags indicated. (enquirebio.com)
  • See the reference protein sequence for cathepsin E precursor (NP_001120469.1). (beds.ac.uk)
Amino acid1
  • Positive selection was detected in cathepsin L-like members in mice and rats, and amino acid sites under positive selection pressure were calculated. (ijbs.com)
Pathogenesis1
  • Cathepsin E, mitochondrial fission, and caspase activation/apoptosis are linked in the pathogenesis of pulmonary emphysema. (cusabio.com)
Homo1
  • All 11 cysteine cathepsins are detected in Homo sapiens (human) through a bioinformatic study on the human genome [ 9 ]. (ijbs.com)
Degradation2
  • Cathepsin G has recently emerged as an important mediator of proteolytic ECM degradation in photoaging. (cosmeticsandtoiletries.com)
  • Downregulation of caveolin-1, the structural protein of caveolae, reduces the cell surface association of cathepsin B and decreases degradation of type IV collagen and invasion by the colon cancer cells, consistent with a functional role for caveolae-associated cathepsin B in invasion [ 12 ]. (biomedcentral.com)
Cytokines1
  • SMC stimulated with the atheroma-associated cytokines IL-1beta or IFN-gamma secreted active cathepsin S and degraded substantial insoluble elastin (15-20 microg/10(6) cells/24 h). (harvard.edu)
Mechanism1
  • Increased reactive oxygen species lead to secretion of cathepsin D by an mechanism that is currently not well understood. (medscape.com)
Active2
  • Here we explored a role for active cathepsin B on the cell surface in the invasiveness of IBC. (biomedcentral.com)
  • We observed that uPA, uPAR and enzymatically active cathepsin B were colocalized in caveolae fractions isolated from SUM149 cells. (biomedcentral.com)
Degrade elastin1
  • In addition, cathepsin G has been shown in vitro to degrade elastin into fragments that can be further processed by elastase. (cosmeticsandtoiletries.com)
Contrast1
  • Cysteine peptidases of Eudiplozoon nipponicum: a broad repertoire of structurally assorted cathepsins L in contrast to the scarcity of cathepsins B in an invasive species of haematophagous monogenean of common carp. (uni-bielefeld.de)
Molecule1
  • The results showed buffalo cathepsin B to be a single-chain molecule. (who.int)
Purification2
  • IMSEAR at SEARO: Isolation, purification and properties of cathepsin B from buffalo liver. (who.int)
  • Salahuddin A, Siddiqui FA, Salahuddin P. Isolation, purification and properties of cathepsin B from buffalo liver. (who.int)
Inflammatory breast1
  • Cathepsin B: a potential prognostic marker for inflammatory breast cancer. (bvsalud.org)
MedlinePlus: Genes: C
MedlinePlus: Genes: C (medlineplus.gov)
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