A ubiquitously-expressed cysteine protease that plays an enzymatic role in POST-TRANSLATIONAL PROTEIN PROCESSING of proteins within SECRETORY GRANULES.
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.
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.
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).
A cysteine protease that is highly expressed in OSTEOCLASTS and plays an essential role in BONE RESORPTION as a potent EXTRACELLULAR MATRIX-degrading enzyme.
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.
An ubiquitously-expressed lysosomal cysteine protease that is involved in protein processing. The enzyme has both endopeptidase and aminopeptidase activities.
A serine protease found in the azurophil granules of NEUTROPHILS. It has an enzyme specificity similar to that of chymotrypsin C.
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.
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.
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
A lysosomal papain-related cysteine proteinase that is expressed in a broad variety of cell types.
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.
Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.
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.
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.
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)
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.
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.
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.
Physiologically inactive substances that can be converted to active enzymes.
Peptides composed of two amino acid units.
Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).
A subclass of peptide hydrolases that depend on a CYSTEINE residue for their activity.
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.
Liver disease caused by infections with parasitic flukes of the genus FASCIOLA, such as FASCIOLA HEPATICA.
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.
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.
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.
N-acylated oligopeptides isolated from culture filtrates of Actinomycetes, which act specifically to inhibit acid proteases such as pepsin and renin.
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)
A cystatin subtype that has a diverse tissue distribution, target specificity, and functions as an endogenous inhibitor of lysosomal cysteine proteases.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
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.
An extracellular cystatin subtype that is abundantly expressed in bodily fluids. It may play a role in the inhibition of interstitial CYSTEINE PROTEASES.
Vesicles derived from the GOLGI APPARATUS containing material to be released at the cell surface.

Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S. (1/644)

The lysosomal cysteine proteases cathepsins S and L play crucial roles in the degradation of the invariant chain during maturation of MHC class II molecules and antigen processing. The p41 form of the invariant chain includes a fragment which specifically inhibits cathepsin L but not S. The crystal structure of the p41 fragment, a homologue of the thyroglobulin type-1 domains, has been determined at 2.0 A resolution in complex with cathepsin L. The structure of the p41 fragment demonstrates a novel fold, consisting of two subdomains, each stabilized by disulfide bridges. The first subdomain is an alpha-helix-beta-strand arrangement, whereas the second subdomain has a predominantly beta-strand arrangement. The wedge shape and three-loop arrangement of the p41 fragment bound to the active site cleft of cathepsin L are reminiscent of the inhibitory edge of cystatins, thus demonstrating the first example of convergent evolution observed in cysteine protease inhibitors. However, the different fold of the p41 fragment results in additional contacts with the top of the R-domain of the enzymes, which defines the specificity-determining S2 and S1' substrate-binding sites. This enables inhibitors based on the thyroglobulin type-1 domain fold, in contrast to the rather non-selective cystatins, to exhibit specificity for their target enzymes.  (+info)

Crystal structure of wild-type human procathepsin K. (2/644)

Cathepsin K is a lysosomal cysteine protease belonging to the papain superfamily. It has been implicated as a major mediator of osteoclastic bone resorption. Wild-type human procathepsin K has been crystallized in a glycosylated and a deglycosylated form. The latter crystals diffract better, to 3.2 A resolution, and contain four molecules in the asymmetric unit. The structure was solved by molecular replacement and refined to an R-factor of 0.194. The N-terminal fragment of the proregion forms a globular domain while the C-terminal segment is extended and shows substantial flexibility. The proregion interacts with the enzyme along the substrate binding groove and along the proregion binding loop (residues Ser138-Asn156). It binds to the active site in the opposite direction to that of natural substrates. The overall binding mode of the proregion to cathepsin K is similar to that observed in cathepsin L, caricain, and cathepsin B, but there are local differences that likely contribute to the specificity of these proregions for their cognate enzymes. The main observed difference is in the position of the short helix alpha3p (67p-75p), which occupies the S' subsites. As in the other proenzymes, the proregion utilizes the S2 subsite for anchoring by placing a leucine side chain there, according to the specificity of cathepsin K toward its substrate.  (+info)

Vaccination with cathepsin L proteinases and with leucine aminopeptidase induces high levels of protection against fascioliasis in sheep. (3/644)

The potential of different parasite proteinases for use as vaccine candidates against fascioliasis in sheep was studied by vaccinating animals with the cathepsin L proteinases CL1 and CL2 and with leucine aminopeptidase (LAP) purified from adult flukes. In the first trial, sheep were immunized with CL1 or CL2 and the mean protection levels obtained were 33 and 34%, respectively. Furthermore, a significant reduction in egg output was observed in sheep vaccinated either with CL1 (71%) or with CL2 (81%). The second trial was performed to determine the protective potential of the two cathepsin L proteinases assayed together, as well as in combination with LAP, and of LAP alone. The combination of CL1 and CL2 induced higher levels of protection (60%) than those produced when these enzymes were administered separately. Those sheep that received the cocktail vaccine including CL1, CL2, and LAP were significantly protected (78%) against metacercarial challenge, but vaccination with LAP alone elicited the highest level of protection (89%). All vaccine preparations induced high immunoglobulin G titers which were boosted after the challenge infection, but no correlations between antibody titers and worm burdens were found. However, the sera of those animals vaccinated with LAP contained LAP-neutralizing antibodies. Reduced liver damage, as assessed by the level of the liver enzyme gamma-glutamyl transferase, was observed in the groups vaccinated with CL1, CL2, and LAP or with LAP alone.  (+info)

Acidic pH as a physiological regulator of human cathepsin L activity. (4/644)

Human cysteine protease cathepsin L was inactivated at acid pH by a first-order process. The inactivation rate decreased with increasing concentrations of a small synthetic substrate, suggesting that substrates stabilize the active conformation. The substrate-independent inactivation rate constant increased with organic solvent content of the buffer, consistent with internal hydrophobic interactions, disrupted by the organic solvent, also stabilizing the enzyme. Circular dichroism showed that the inactivation is accompanied by large structural changes, a decrease in alpha-helix content being especially pronounced. The high activation energy of the reaction at pH 3.0 (200 kJ.mol-1) supported such a major conformational change occurring. The acid inactivation of cathepsin L was irreversible, consistent with the propeptide being needed for proper folding of the enzyme. Aspartic protease cathepsin D was shown to cleave denatured, but not active cathepsin L, suggesting a potential mechanism for in-vivo regulation and turnover of cathepsin L inside lysosomes.  (+info)

A novel egg-derived tyrosine phosphatase, EDTP, that participates in the embryogenesis of Sarcophaga peregrina (flesh fly). (5/644)

We have previously reported that cathepsin L mRNA is present in unfertilized eggs of Sarcophaga peregrina (flesh fly) as a maternal mRNA, which suggests that cathepsin L is required for embryogenesis. Now we have identified an egg protein, with a molecular mass of 100 kDa, that is extremely susceptible to cathepsin L digestion and which disappears rapidly as the embryos develop. We purified this protein to homogeneity, cloned its cDNA, and found that it contained a consensus sequence for the active site of tyrosine phosphatase. In fact this protein showed tyrosine phosphatase activity, indicating that it is a novel tyrosine phosphatase. The expression and subsequent disappearance of this protein, which we have named egg-derived tyrosine phosphatase (EDTP), may be indispensable for embryogenesis of Sarcophaga.  (+info)

Collagenase, cathepsin B and cathepsin L gene expression in the synovial membrane of patients with early inflammatory arthritis. (6/644)

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)

Short report: Diagnosis of human fascioliasis: detection of anti-cathepsin L antibodies in blood samples collected on filter paper. (7/644)

We have developed an ELISA for the diagnosis of human fascioliasis based on the detection of IgG4 antibodies to Fasciola hepatica cathepsin LI cysteine protease. Use of this assay in the Bolivian Altiplano, a region with a high prevalence of the disease, was hampered by the reluctance of the indigenous population to provide blood. To overcome this problem, we have investigated the method of collecting small quantities of blood from the finger onto filter paper, followed by the elution of antibodies for use in the diagnostic assay. Serum samples and blood samples collected onto filter paper were obtained from 57 individuals living in the village of Cutusuma in 1987 and from 11 individuals in Chijipata in 1996. Analysis of the IgG4-ELISA results revealed that there is highly significant linear relationship (P < 0.001) between the two methods of sampling. Most importantly, a reliable diagnosis was made with the blood-filter samples from Cutusuma, which had been stored for 10 years at 40 degrees C. While some deterioration of the blood-filter samples from Cutusuma had occurred over the 10-year storage period, no deterioration occurred with the Chijipata samples, which were stored for one year. Therefore, the method of collecting blood onto filter paper should prove useful for large-scale epidemiologic studies on human fascioliasis in the Bolivian Altiplano and in other regions where this disease is prevalent.  (+info)

Short report: Immunodiagnosis of human fascioliasis using recombinant Fasciola hepatica cathepsin L1 cysteine proteinase. (8/644)

Our laboratory recently developed a diagnostic test (ELISA) for human fascioliasis based on the detection of serum IgG4 antibodies reactive with Fasciola hepatica cathepsin L1 (CL1). In the present study, we have used recombinant CL1, generated by functional expression of the cDNA in Saccharomyces cerevisiae, in this immunodiagnostic test and compared its performance with native CL1. Sera obtained from 64 individuals living in Cutusuma village in the northern Altiplano of Bolivia, a region with a high prevalence of human fascioliasis, were analyzed by the IgG4-ELISA. A highly statistically significant correlation (r2 = 0.751, P < 0.001) was demonstrated between the absorbances obtained using the recombinant and native proteins. These assays showed that 38 (59%) of the individuals tested were seropositive for fascioliasis, whereas only 26 of them were coprologically positive for F. hepatica eggs. All seronegative patients were also coprologically negative. Serum from individuals infected with schistosomiasis mansoni, cysticercosis, hydatidosis, and Chagas disease did not contain antibodies reactive with the recombinant or native CL1. Therefore, recombinant CL1 shows excellent potential for the development of the first standardized assay for the sensitive and specific diagnosis of human fascioliasis. Finally, our data supports earlier reports on the high prevalence of human fascioliasis in the Bolivian Altiplano, which collectively suggest that the disease has been endemic there for more than a decade.  (+info)

Symptoms of fascioliasis can vary depending on the severity of the infection and may include:

1. Abdominal pain
2. Diarrhea
3. Vomiting
4. Fatigue
5. Weight loss
6. Anemia
7. Elevated liver enzymes
8. Inflammation of the liver, bile ducts, or pancreas

If left untreated, fascioliasis can lead to serious complications such as:

1. Cholangiohepatitis (inflammation of the bile ducts and liver)
2. Hepatic cysts or cirrhosis (scarring of the liver)
3. Biliary obstruction or pancreatitis (inflammation of the pancreas)

Diagnosis of fascioliasis typically involves a combination of physical examination, medical history, and laboratory tests such as:

1. Blood tests to detect antibodies against the parasite
2. Detection of the parasite in stool or bile samples
3. Imaging studies such as ultrasound or CT scans to visualize the liver and bile ducts

Treatment of fascioliasis usually involves the use of antiparasitic drugs, such as triclabendazole or nitazoxanide, to eliminate the parasite from the body. Supportive care may also be provided to manage symptoms and prevent complications.

Prevention of fascioliasis primarily involves measures to avoid ingesting contaminated food or water, such as:

1. Avoiding consumption of raw or undercooked meat, particularly pork or lamb
2. Properly cooking and storing food
3. Avoiding consumption of untreated water
4. Using proper sanitation and hygiene practices
5. Avoiding contact with contaminated soil or water

In areas where fascioliasis is common, it is important to be aware of the risk and take appropriate precautions to prevent infection. Early detection and treatment can help prevent complications and improve outcomes for patients with fascioliasis.

... 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 ...
... (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. ...
... 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 ...
... 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 ...
"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 ...
... 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 ...
... (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 ...
... 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 ...
... 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 ...
... 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 ...
"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 ...
... 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 ...
... 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 ...
... 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 ...
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 ...
... , (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. ...
... 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: ...
... 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 ...
... 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 ...
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 ...
... , Histones & Cathepsin; PMAP The Proteolysis Map-animation Nature journal: recent chromatin publications and news ...
... collagenases such as cathepsin B1; and hyaluronidase. PSGAG inhibits the synthesis of prostaglandin E2, which is released upon ...
Cathepsin A Breddam, K. (1986). "Serine carboxypeptidases. A review". Carlsberg Res. Commun. 51: 83-128. doi:10.1007/bf02907561 ... Miller 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, ...
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. ...
Cathepsin D is involved in CLN10. DNA analysis can be used to help confirm the diagnosis of Batten disease. When the mutation ...
Miv-711 Cathepsin K inhibitor for osteoarthritis. Fast track (FDA) MALT1 "Swedish pharma firm Medivir partners Aragen Life ...
... these include cathepsin L, papain, and procaricain. It forms an alpha-helical domain that runs through the substrate-binding ...
"Cathepsins as transcriptional activators? Developmental Cell 2004, 6(5):610-1. Goulet B, and Nepveu A. "Complete and Limited ...
Lushbaugh WB, Hofbauer AF, Pittman FE (June 1985). "Entamoeba histolytica: purification of cathepsin B". Experimental ...
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 ...
Cathepsins - A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal ... ... CATHEPSINS \kˈaθɪpsˌɪnz], \kˈaθɪpsˌɪnz], \k_ˈa_θ_ɪ_p_s_ˌɪ_n_z]\ ...
Buy Cathepsin G, Inflammatory Bowel Disease online from Arotec; leading supplier of premium antigens and antibodies for ... Cathepsin G is a member of the hematopoietic serine proteinase super family along with elastase and proteinase 3. Cathepsin G, ... Cathepsin G datasheet. Primary Sclerosing Cholangitis. Crohns disease. Ulcerative Colitis. Cathepsin G is implicated in ... Cathepsin G is also present in some vasculitic diseases but is not as specific or as prevalent a marker as MPO and PR3. ...
Cathepsin L regulates pathogenic CD4 T cells in experimental autoimmune encephalomyelitis Shibamura-Fujiogi, M;Yuki, K;Hou, L; ... most prominently cathepsin L (CtsL). Since CtsL also mediates invariant chain processing in thymic epithelial cells, deficiency ... were increased in mice lacking the protease inhibitor SerpinB1 and several SerpinB1-inhibitable cysteine cathepsins were ...
Cathepsin S Cleavage of Protease-Activated Receptor-2 on Endothelial Cells Promotes Microvascular Diabetes Complications. ... Dive into the research topics of Cathepsin S Cleavage of Protease-Activated Receptor-2 on Endothelial Cells Promotes ...
Cathepsin B activity assay:. The activity was measured using a Cathepsin B Activity Assay Kit (ab65300; Abcam) according to the ... Cathepsin D activity assay:. The activity was measured using a Cathepsin D Activity Assay Kit (ab65302; Abcam) according to the ... In situ Cathepsin D activity assay:. Cells were treated with a 1 μg/mL BODYPY-FL-pepstatin A probe (P12271; Thermo Fisher ... Cathepsin B (219408) was obtained from Calbiochem (San Diego, CA, USA), SQSTM1/p62 (GP62-C) from Abnova (Taipei, Taiwan), β- ...
Cathepsin L, Human Liver, CAS 60616-82-2, is a native, the most potent of all the lysosomal proteinases. Plays a major role in ... Native cathepsin L from human liver. The most potent of the lysosomal proteinases, having a higher activity than cathepsins B ... More,, Cathepsin L, Human Liver, CAS 60616-82-2, is a native, the most potent of all the lysosomal proteinases. Plays a major ... Cathepsin L, Human Liver, CAS 60616-82-2, is a native, the most potent of all the lysosomal proteinases. Plays a major role in ...
SDS-PAGE - Cathepsin G 293T Transfected Lysate (ab94086) All lanes : Anti-Cathepsin G antibody (ab89593) at 1/500 dilution Lane ... Product datasheet Cathepsin G 293T Transfected Lysate - (positive control) ab94086 2 Images Overview Product name Cathepsin G ... Western blot - Cathepsin G 293T Transfected Lysate (ab94086) Secondary Goat Anti-mouse IgG (H and L) HRP conjugated at 1/2500 ... Cathepsin G 293T Transfected Lysate - (positive control) images 1 ab94086 at 15µg/lane on an SDS-PAGE gel. ...
Faraday et al., (2013). Cathepsin G-Dependent Modulation of Platelet Thrombus Formation In Vivo by Blood Neutrophils. PLoS One ... Cathepsin G FRET substrate [5-FAM]/[6-TAMRA]. Cat No.. Pack Size. Price. Qty. ... Cathepsin G can cleave protease activated receptor-4 (PAR4) and is a potential target for novel anti-thrombotic therapies. ... Substrate peptide for Cathepsin G, a serine protease belonging to the chymotrypsin superfamily which acts as a physiologic ...
Moreover, cathepsin S is expressed in some epithelial cells. Compared with the abundant cathepsins B, L and H, cathepsin S ... Cathepsin S is a lysosomal enzyme that belongs to the papain family of cysteine proteases. This protein is expressed by antigen ... Moreover, cathepsin S is expressed in some epithelial cells. Compared with the abundant cathepsins B, L and H, cathepsin S ... Cathepsin S is a lysosomal enzyme that belongs to the papain family of cysteine proteases. This protein is expressed by antigen ...
However, in N. fowleri cathepsin B (UniProt ID X5D761) and putative cathepsin B (UniProt ID M1HE19) enzymes, eleven and fifteen ... Thus, it is concluded that N. fowleri cathepsin B and putative cathepsin B enzymes lack exopeptidase activity but possess ... this mutation is believed to affect cathepsin B targeting inside the cell and make cathepsin B available in the extracellular ... The present study is the first to predict the three-dimensional folds of N. fowleri cathepsin B paralogous enzymes, including a ...
keywords = "Cathepsin B, Cathepsin S-deficient mice, Facial nerve axotomy, Microglia, Motoneuron survival, Transmigration", ... Hai PH, Doh-Ura K, Nakanishi H. Impairment of microglial responses to facial nerve axotomy in cathepsin S-deficient mice. ... Hai, P. H., Doh-Ura, K., & Nakanishi, H. (2007). Impairment of microglial responses to facial nerve axotomy in cathepsin S- ... Cathepsin S (CS) is a lysosomal/endosomal cysteine protease especially expressed in cells of a mononuclear lineage including ...
Cathepsin-S Levels and Survival among Patients with Non-ST Elevation Acute Coronary Syndromes. ... Cathepsin-S Levels and Survival among Patients with Non-ST Elevation Acute Coronary Syndromes ...
Cathepsin K. Cathepsin K is a cysteine protease expressed predominantly in osteoclasts. Search. Main menu. Skip to primary ...
Following a comprehensive transcriptome analysis, H. halys had an expanded suite of cytochrome P450 and cathepsin-L genes ... Our analysis into P450 and cathepsin genes in H. halys offers new insights into potential mechanisms for understanding ... In subsequent RT-PCR experiments, both P450 and cathepsin genes exhibited tissue-specific or distinct expression patterns which ... A phylogenetic tree generated using cathepsins (Cathepsin-B and Cathepsin-L) in H. halys along with corresponding cathepsins in ...
Cathepsin G (CTSG)]Product Name Synonyme: N/AOther Names: [cathepsin G preproprotein; Cathepsin G; cathepsin G;... ... Human Cathepsin G (CTSG) ELISA Kit , MBS167220 , MybiosourceProduct Short Name: [ ...
Cathepsin K-deficient osteocytes prevent lactation-induced bone loss and parathyroid hormone suppression journal, June 2019 * ... Cathepsin K-deficient osteocytes prevent lactation-induced bone loss and parathyroid hormone suppression journal, June 2019 * ...
... cathepsin B and cathepsin L, and glycosidic and aglycon forms of some flavonols. Turkish Journal of Biology, 45(4), 484-502. ... cathepsin B and cathepsin L, and glycosidic and aglycon forms of some flavonols. ... and cathepsins (CatB and CatL) were analyzed. According to the relative binding capacity index (RBCI) calculated based on the ...
A major cathepsin B protease from the liver fluke Fasciola hepatica has atypical active site features and a potential role in ... A major cathepsin B protease from the liver fluke Fasciola hepatica has atypical active site features and a potential role in ... A major cathepsin B protease from the liver fluke Fasciola hepatica has atypical active site features and a potential role in ... A major cathepsin B protease from the liver fluke Fasciola hepatica has atypical active site features and a potential role in ...
abm , Anti-Cathepsin L Antibody , Y300530Immunogen:Human Cathepsin L recombinant proteinIsotype:IgG1Storage Buffer:0.2 μm ...
Polymerization of IgA-RF and IgG into an immune complex can stimulate neutrophil release of elastase, cathepsin, lysozyme, and ... cathepsin k: enzyme controlling bone remodeling; ROS: reactive oxygen species; NO: nitric oxide; IL-4: interleukin-4; IL-10: ...
Description: A sandwich ELISA for quantitative measurement of Goat Cathepsin Antibodies in samples from blood, plasma, serum, ...
Cathepsin L1 0.9028 6 3hl5 Baculoviral IAP repeat-containing protein 4 0.8946 ...
Endoglycosidase F1, Elizabethkingia meningosepticum, Recombinant, E. coli Endoglycosidase F1, Elizabethkingia meningosepticum, Recombinant, E. coli cleaves asparagine-linked or free oligomannose and hybrid. Suitable for deglycosylation of native proteins.; Synonyms: Endo-β-N-acetylglucosaminidase F1, Endo F1; find Sigma-Aldrich-324725 MSDS, related peer-reviewed papers, technical documents, similar products & more at Sigma-Aldrich
Cathepsin-D. - Chromogranin A and B. - Cluster 1 Antigen. - Cluster-5/5A Antigen. - CTA. - CU18. - DR-70. - DU-PAN-2. - ... Cathepsin Test Volume and Diagnostics Sales Forecast. CEA Test Volume and Diagnostics Sales Forecast. Chromogranin Test Volume ... ACTH, AFP, Beta-2 Microglobulin, CA 15-3/27.29, CA 19-9, CA 125, Calcitonin, Cathepsin, CEA, Chromogranin, Colon-Specific ...
Cited in 1 publications. View Goat Polyclonal anti-SNX16 Antibody (NB100-1211). Validated Applications: WB, IHC, IHC-P, PEP-ELISA. Validated Species: Human, Mouse, Rat + more.
CTSA: cathepsin A. *CTSD: cathepsin D. *CUBN: cubilin. *CUL3: cullin 3. *CUL7: cullin 7 ...
PDB Description: Cathepsin K complexed with a constrained ketoamide inhibitor. PDB Compounds: (A:) cathepsin k. SCOP Domain ... d1yt7a1 d.3.1.1 (A:2-215) (Pro)cathepsin K {Human (Homo sapiens) [TaxId: 9606]} ...
Measurement of free and membrane-bound cathepsin G in human neutrophils using new sensitive fluorogenic substrates. Biochem J. ... E) r4C3 does not increase cathepsin G activity. Purified neutrophils from three independent healthy donors were primed with TNF ... Supernatants were harvested and incubated with fluorescent substrate of cathepsin G (ABZ-TPFSGQ-YNO2 from GeneCust) (46) for 30 ... Neutrophil proteinase 3 and dipeptidyl peptidase I (cathepsin C) as pharmacological targets in granulomatosis with polyangiitis ...
  • Cathepsin G, a 225 amino acid residue protein with an 18 residue signal peptide and a 2 residue activation peptide at the N-terminus, is a ubiquitous enzyme secreted by neutrophils. (arodia.com)
  • 2003) Bactericidal/permeability-increasing protein and cathepsin G are the major antigenic targets of antineutrophil cytoplasmic autoantibodies in systemic sclerosis. (arodia.com)
  • cathepsin K enzyme plays a key role in breaking down the protein in bone. (salesandmarketingnetwork.com)
  • Sequence and expression of the cDNA for MEP (major excreted protein), a transformation-regulated secreted cathepsin. (elsevier.com)
  • Dive into the research topics of 'Sequence and expression of the cDNA for MEP (major excreted protein), a transformation-regulated secreted cathepsin. (elsevier.com)
  • The most potent of the lysosomal proteinases, having a higher activity than cathepsins B and H in the degradation of a variety of physiological protein substrates. (emdmillipore.com)
  • Vitellogenin, zona radiata protein, cathepsin D and heat shock protein 70 as biomarkers of exposure to xenobiotics. (bvsalud.org)
  • Among the biomarkers analysed, vitellogenin (VTG) and zona radiata proteins (ZRP) are key molecules involved in reproduction , widely used to detect the presence of pollutants in the marine environment , while heat shock protein 70 (HSP70) and cathepsin D (CATD) have recently been introduced as bioindicators of endocrine disruption. (bvsalud.org)
  • 2018). Caspase-4 activation by a bacterial surface protein is mediated by cathepsin G in human gingival fibroblasts Cell Death Differ . (crbdiscovery.com)
  • The CSTB gene provides instructions for making a protein called cystatin B. This protein reduces the activity of enzymes called cathepsins. (nih.gov)
  • Furthermore, cathepsin K and S inhibitors showed effectiveness in (pre) clinical evaluation for the treatment of osteoporosis and osteoarthritis, suggesting that cathepsin inhibitors may also have therapeutic effects for the treatment of atherosclerosis. (nih.gov)
  • We report the crystal structures of three noncovalent retrobinding inhibitors in complex with mature cathepsin L up to resolutions of 2.5, 1.8, and 2.5 A, respectively. (rcsb.org)
  • In addition, responses to other markers of bone turnover, including the marker of bone resorption urinary deoxpyridinoline (uDPD), the marker of bone formation serum bone-specific alkaline phosphatase (sBSAP) and the marker of cathepsin K activity serum crosslinked C-terminal peptide (s1CTP) were evaluated in the study. (salesandmarketingnetwork.com)
  • Substrate peptide for Cathepsin G, a serine protease belonging to the chymotrypsin superfamily which acts as a physiologic regulator of platelet activation and thrombus formation. (crbdiscovery.com)
  • We further demonstrate that incorporating a cathepsin B-cleavable linker between the BIM BH3 peptide and the hydrophobic tail within individual amphiphiles results in increased binding to recombinant BCL-2 proteins while also allowing for increased cellular uptake and mitochondrial localization leading to faster and more potent dose-dependent cytotoxicity and caspase activation in malignant cells. (ashpublications.org)
  • Chemotherapy-triggered IL-1β secretion relied on lysosomal permeabilization and the release of cathepsin B, which bound to Nlrp3 and drove caspase-1 activation. (nih.gov)
  • Cathepsin L, Human Liver, CAS 60616-82-2, is a native, the most potent of all the lysosomal proteinases. (emdmillipore.com)
  • Cathepsin S is a lysosomal enzyme that belongs to the papain family of cysteine proteases. (fagusantibodies.com)
  • In addition, evidences indicated that cathepsin S generates A beta from amyloidogenic fragments of beta APP in the endosomal/lysosomal compartment, and is implicated in the pathogenesis of Alzheimer's disease (AD) and Down Syndrome (DS). (fagusantibodies.com)
  • Cathepsin S (CS) is a lysosomal/endosomal cysteine protease especially expressed in cells of a mononuclear lineage including microglia. (elsevierpure.com)
  • Interestingly, cathepsin B, a typical lysosomal cysteine protease, was markedly expressed on the axotomized side in CS-/- but not in wild-type microglia. (elsevierpure.com)
  • Cathepsin G is a member of the hematopoietic serine proteinase super family along with elastase and proteinase 3. (arodia.com)
  • Moreover, we clarified the relationship between CysLT1R and cathepsin B, a cysteine protease. (nih.gov)
  • Cathepsin cysteine proteases have a central role in ECM remodeling and have been implicated in the development and progression of cardiovascular diseases. (nih.gov)
  • Lysosomes contain many well-characterized proteases, and cathepsin B has previously been utilized to release chemotherapeutics in the context of targetable antibody-based treatments. (ashpublications.org)
  • Evaluation of the feasibility of cathepsins as a diagnostic tool revealed that serum levels of cathepsins L and S seem to be promising as biomarkers in the diagnosis of atherosclerosis, whereas cathepsin B shows potential as an imaging tool. (nih.gov)
  • Description: A sandwich quantitative ELISA assay kit for detection of Mouse Cathepsin A (CTSA) in samples from serum, plasma, tissue homogenates, cell lysates or other biological fluids. (wannabe-anthropologist.com)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Cathepsin A (CTSA) in serum, plasma, tissue homogenates and other biological fluids. (wannabe-anthropologist.com)
  • Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human Cathepsin A (CTSA) in samples from serum, plasma, tissue homogenates and other biological fluids with no significant corss-reactivity with analogues from other species. (wannabe-anthropologist.com)
  • 1997) Anti-neutrophil cytoplasmic antibody (ANCA) in malaria is directed against cathepsin G. Clin. (arodia.com)
  • SDS-PAGE - Cathepsin G 293T Transfected Lysate (ab94086) All lanes : Anti-Cathepsin G antibody (ab89593) at 1/500 dilution Lane 1 : Cathepsin G 293T Transfected Lysate - (positive control) (ab94086) Lane 2 : 293T non-transfected lysate Lysates/proteins at 25 µg per lane. (studylib.net)
  • 1996) Cathepsin G in gingival tissue and crevicular fluid in adult periodontosis. (arodia.com)
  • Independent of its proteinase activity, cathepsin G is a significant broad spectrum anti-microbial agent. (arodia.com)
  • 1996) The 8 A crystal structure of human cathepsin G in complex with Suc-Val-Pro-PheP-(OPh)2: a Janus-faced proteinase with two opposite specificities. (arodia.com)
  • EDINBURGH, Scotland--(HSMN NewsFeed)--Merck & Co., Inc, Whitehouse Station, NJ, USA, which operates in many countries as Merck Sharp & Dohme or MSD, announced results of a new study in which its investigational selective cathepsin K inhibitor odanacatib reduced measures of bone turnover (breakdown and rebuilding of bone) in women with breast cancer that has spread to the bones (bone metastases). (salesandmarketingnetwork.com)
  • Previously we reported that IL-17-producing CD4 T cells (Th17) were increased in mice lacking the protease inhibitor SerpinB1 and several SerpinB1-inhibitable cysteine cathepsins were induced in the Th17 cells, most prominently cathepsin L (CtsL). (listlabs.com)
  • Our results indicate that 6-shogaol is a CysLT1R/cathepsin B inhibitor and is a novel potential therapeutic agent for the treatment of various neurodegenerative diseases, including AD. (nih.gov)
  • Reduced Cathepsin L expression and secretion into the extracellular milieu contribute to lung fibrosis in systemic sclerosis. (nih.gov)
  • Cathepsin G also has antimicrobial activity and is involved in chemotaxis, apoptosis, the immune response and inflammation and hydrolysis of extracellular matrix proteins. (crbdiscovery.com)
  • Product datasheet Cathepsin G 293T Transfected Lysate - (positive control) ab94086 2 Images Overview Product name Cathepsin G 293T Transfected Lysate - (positive control) General notes ab94086 is a 293T cell transfected lysate in which Human Cathepsin G has been transiently over-expressed using a pCMV-Cathepsin G plasmid. (studylib.net)
  • Crystalline silica also was reported to cause adverse renal effects in test animals and to inhibit some enzymes (e.g., cathepsin B) while inducing others (CYP1A1). (nih.gov)
  • Compared with the abundant cathepsins B, L and H, cathepsin S shows a restricted tissue distribution, with highest levels in spleen, heart, and lung. (fagusantibodies.com)
  • Strong homology of MEP with human cathepsin L suggests that MEP is the mouse analogue of cathepsin L. Amino acid sequencing of the N-terminus of the secreted form of MEP indicates that, during secretion, the polypeptide is cleaved between amino acids 17 and 18. (elsevier.com)
  • By inhibiting cathepsin K activity, odanacatib represents a potential novel therapeutic approach for metastatic bone disease that works differently from other commonly used medicines. (salesandmarketingnetwork.com)
  • Although expression studies also demonstrated differential expression of cathepsins in cardiovascular diseases like aneurysm formation, neointima formation, and neovascularization, in vivo studies to define the exact role of cathepsins in these processes are lacking. (nih.gov)
  • Cathepsins also show differential expression in various stages of atherosclerosis, and in vivo knockout studies revealed that deficiency of cathepsin K or S reduces atherosclerosis. (nih.gov)
  • 2013). Cathepsin G-Dependent Modulation of Platelet Thrombus Formation In Vivo by Blood Neutrophils. (crbdiscovery.com)
  • We first confirmed that CysLT1R and cathepsin B are upregulated by Aβ (1-42) and that CysLT1R activation induces cathepsin B. In contrast, we found that 6-shogaol-mediated inhibition of CysLT1R downregulates cathepsin B in both in vitro and in vivo models. (nih.gov)
  • While the specific function of cystatin B is unclear, it may help protect the cells' proteins from cathepsins that leak out of the lysosomes. (nih.gov)
  • Furthermore, we found that 6-shogaol-mediated inhibition of CysLT1R/cathepsin B reduces Aβ deposition in the brain and ameliorates behavioral deficits in APPSw/PS1-dE9 Tg mice. (nih.gov)
  • Recombinant Mouse Cathepsin S is produced by our Mammalian expression system and the target gene encoding Val18-Ile340 is expressed with a 6His tag at the C-terminus. (fagusantibodies.com)
  • 1998) Specificity of human cathepsin G. Biochim. (arodia.com)
  • Levels of cystatin B in affected individuals are only 5 to 10 percent of normal, and cathepsin levels are significantly increased. (nih.gov)
  • 1992) Antineutrophil cytoplasmic antibodies (ANCA) directed against cathepsin G in ulcerative colitis, Crohn's disease and primary sclerosing cholangitis. (arodia.com)
  • 2000) Anti-cathepsin G antibodies in the sera of patients with ulcerative colitis. (arodia.com)
  • There is published data that ANCA associated antibodies against cathepsin G are found in ulcerative colitis and crohn's disease. (arodia.com)
  • Cathepsins have the capability to degrade low-density lipoprotein and reduce cholesterol efflux from macrophages, aggravating foam cell formation. (nih.gov)