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.
A ubiquitously-expressed cysteine protease that plays an enzymatic role in POST-TRANSLATIONAL PROTEIN PROCESSING of proteins within SECRETORY GRANULES.
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.
A serine protease found in the azurophil granules of NEUTROPHILS. It has an enzyme specificity similar to that of chymotrypsin C.
An ubiquitously-expressed lysosomal cysteine protease that is involved in protein processing. The enzyme has both endopeptidase and aminopeptidase activities.
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 lysosomal papain-related cysteine proteinase that is expressed in a broad variety of cell types.
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.
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.
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 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 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.
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.
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.
Peptides composed of two amino acid units.
Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.
Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).
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.
A subclass of peptide hydrolases that depend on a CYSTEINE residue for their activity.
Physiologically inactive substances that can be converted to active enzymes.
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.
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 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.
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.
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)
Rare, autosomal recessive disorder occurring between the first and fifth years of life. It is characterized by palmoplantar keratoderma with periodontitis followed by the premature shedding of both deciduous and permanent teeth. Mutations in the gene for CATHEPSIN C have been associated with this disease.
An extracellular cystatin subtype that is abundantly expressed in bodily fluids. It may play a role in the inhibition of interstitial CYSTEINE PROTEASES.
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 characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
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.
The rate dynamics in chemical or physical systems.
Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.
The process of cleaving a chemical compound by the addition of a molecule of water.
A subclass of exopeptidases that includes enzymes which cleave either two or three AMINO ACIDS from the end of a peptide chain.
An essential branched-chain amino acid important for hemoglobin formation.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
Proteins prepared by recombinant DNA technology.
Phosphoric acid esters of mannose.
Peptides composed of between two and twelve amino acids.

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. (1/1976)

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)

Bile duct epithelial cells exposed to alpha-naphthylisothiocyanate produce a factor that causes neutrophil-dependent hepatocellular injury in vitro. (2/1976)

The acute hepatotoxicity induced by alpha-naphthylisothiocyanate (ANIT) in rats is manifested as neutrophil-dependent necrosis of bile duct epithelial cells (BDECs) and hepatic parenchymal cells. This hepatotoxicity mirrors that of drug-induced cholangiolitic hepatitis in humans. Since BDECs are primary targets of ANIT-induced toxicity, we hypothesized that after exposure to ANIT, BDECs produce a factor(s) that causes neutrophil chemotaxis and neutrophil-dependent hepatocellular injury. To test this hypothesis BDECs were isolated from male Sprague Dawley rats and incubated with ANIT (6.25, 12.5, 25, or 50 microM) or vehicle for 24 h. The conditioned medium (CM) was collected and placed in the bottom chamber of a two-chambered chemotaxis system, while isolated neutrophils were placed in the top chamber. Chemotaxis was indicated by neutrophil migration through a membrane to the bottom chamber. CM from BDECs exposed to each concentration of ANIT was chemotactic, whereas CM from vehicle-treated BDECs was not. ANIT alone caused a modest degree of chemotaxis at 50 microM. The conditioned media were added to isolated hepatocytes or to hepatocyte-neutrophil cocultures and incubated for 24 h. Hepatocyte toxicity was indicated by alanine aminotransferase release into the culture medium. CM from vehicle-treated BDECs did not cause hepatocyte killing in either hepatocyte-neutrophil cocultures or hepatocyte cultures. In contrast, the addition of CM from ANIT-treated BDECs (CM-BDEC-A) to hepatocyte-neutrophil cocultures resulted in hepatocyte killing. The same CM was not cytotoxic to hepatocyte cultures devoid of neutrophils. The hepatocyte killing could not be explained by residual ANIT in the CM, which was below the limit of detection (< or = 0.5 microM). The addition of antiproteases afforded protection against neutrophil-dependent hepatocellular injury induced by CM-BDEC-A. These results indicate that ANIT causes BDECs to release a factor(s) that attracts neutrophils and stimulates them to injure hepatocytes in vitro.  (+info)

Crystal structure of wild-type human procathepsin K. (3/1976)

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)

The intracellular serpin proteinase inhibitor 6 is expressed in monocytes and granulocytes and is a potent inhibitor of the azurophilic granule protease, cathepsin G. (4/1976)

The monocyte and granulocyte azurophilic granule proteinases elastase, proteinase 3, and cathepsin G are implicated in acute and chronic diseases thought to result from an imbalance between the secreted proteinase(s) and circulating serpins such as alpha1-proteinase inhibitor and alpha1-antichymotrypsin. We show here that the intracellular serpin, proteinase inhibitor 6 (PI-6), is present in monocytes, granulocytes, and myelomonocytic cell lines. In extracts from these cells, PI-6 bound an endogenous membrane-associated serine proteinase to form an sodium dodecyl sulfate (SDS)-stable complex. Using antibodies to urokinase, elastase, proteinase 3, or cathepsin G, we demonstrated that the complex contains cathepsin G. Native cathepsin G and recombinant PI-6 formed an SDS-stable complex in vitro similar in size to that observed in the extracts. Further kinetic analysis demonstrated that cathepsin G and PI-6 rapidly form a tight 1:1 complex (ka = 6.8 +/- 0.2 x 10(6) mol/L-1s-1 at 17 degrees C; Ki = 9.2 +/- 0.04 x 10(-10) mol/L). We propose that PI-6 complements alpha1-proteinase inhibitor and alpha1-antichymotrypsin (which control extracellular proteolysis) by neutralizing cathepsin G that leaks into the cytoplasm of monocytes or granulocytes during biosynthesis or phagocytosis. Control of intracellular cathepsin G may be particularly important, because it has recently been shown to activate the proapoptotic proteinase, caspase-7.  (+info)

Cathepsin S required for normal MHC class II peptide loading and germinal center development. (5/1976)

Major histocompatibility complex (MHC) class II molecules acquire antigenic peptides after degradation of the invariant chain (Ii), an MHC class II-associated protein that otherwise blocks peptide binding. Antigen-presenting cells of mice that lack the protease cathepsin S fail to process Ii beyond a 10 kDa fragment, resulting in delayed peptide loading and accumulation of cell surface MHC class II/10 kDa Ii complexes. Although cathepsin S-deficient mice have normal numbers of B and T cells and normal IgE responses, they show markedly impaired antibody class switching to IgG2a and IgG3. These results indicate cathepsin S is a major Ii-processing enzyme in splenocytes and dendritic cells. Its role in humoral immunity critically depends on how antigens access the immune system.  (+info)

Impaired invariant chain degradation and antigen presentation and diminished collagen-induced arthritis in cathepsin S null mice. (6/1976)

Cathepsins have been implicated in the degradation of proteins destined for the MHC class II processing pathway and in the proteolytic removal of invariant chain (Ii), a critical regulator of MHC class II function. Mice lacking the lysosomal cysteine proteinase cathepsin S (catS) demonstrated a profound inhibition of Ii degradation in professional APC in vivo. A marked variation in the generation of MHC class II-bound Ii fragments and presentation of exogenous proteins was observed between B cells, dendritic cells, and macrophages lacking catS. CatS-deficient mice showed diminished susceptibility to collagen-induced arthritis, suggesting a potential therapeutic target for regulation of immune responsiveness.  (+info)

Characterization of novel cathepsin K mutations in the pro and mature polypeptide regions causing pycnodysostosis. (7/1976)

Cathepsin K, a lysosomal cysteine protease critical for bone remodeling by osteoclasts, was recently identified as the deficient enzyme causing pycnodysostosis, an autosomal recessive osteosclerotic skeletal dysplasia. To investigate the nature of molecular lesions causing this disease, mutations in the cathepsin K gene from eight families were determined, identifying seven novel mutations (K52X, G79E, Q190X, Y212C, A277E, A277V, and R312G). Expression of the first pro region missense mutation in a cysteine protease, G79E, in Pichia pastoris resulted in an unstable precursor protein, consistent with misfolding of the proenzyme. Expression of five mature region missense defects revealed that G146R, A277E, A277V, and R312G precursors were unstable, and no mature proteins or protease activity were detected. The Y212C precursor was activated to its mature form in a manner similar to that of the wild-type cathepsin K. The mature Y212C enzyme retained its dipeptide substrate specificity and gelatinolytic activity, but it had markedly decreased activity toward type I collagen and a cathepsin K-specific tripeptide substrate, indicating that it was unable to bind collagen triple helix. These studies demonstrated the molecular heterogeneity of mutations causing pycnodysostosis, indicated that pro region conformation directs proper folding of the proenzyme, and suggested that the cathepsin K active site contains a critical collagen-binding domain.  (+info)

Vaccination with cathepsin L proteinases and with leucine aminopeptidase induces high levels of protection against fascioliasis in sheep. (8/1976)

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)

The main symptoms of PLD include:

* Skin manifestations: The disease typically presents with thickened, scaly skin on the palms and soles, as well as on the fingers and toes. The skin may also be darkly pigmented and have a characteristic "café-au-lait" appearance.
* Nervous system abnormalities: PLD can cause neurological symptoms such as intellectual disability, seizures, and difficulty with coordination and balance.
* Eye problems: The disease may also cause vision loss due to cataracts or other eye defects.

PLD is usually diagnosed through a combination of clinical evaluation, skin biopsy, and genetic testing. There is no cure for the disease, but treatment options are available to manage the symptoms. These may include:

* Medications: To control seizures and other neurological symptoms, medications such as anticonvulsants and anti-epileptic drugs may be prescribed.
* Surgery: In some cases, surgery may be necessary to remove affected skin or to correct eye defects.
* Physical therapy: To help improve coordination and balance, physical therapy may be recommended.

The prognosis for PLD is generally poor, with many individuals experiencing significant developmental delays and intellectual disability. However, with appropriate management and supportive care, some individuals with the disease may lead relatively normal lives.

... 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 ...
"Cathepsins as transcriptional activators? Developmental Cell 2004, 6(5):610-1. Goulet B, and Nepveu A. "Complete and Limited ...
... , Histones & Cathepsin; PMAP The Proteolysis Map-animation Nature journal: recent chromatin publications and news ...
... there are 11 cysteine cathepsins: B, C, F, H, K, L, O, S, V, X, and W. Most cathepsins are expressed throughout the body, but ... gene duplications have produced over 20 paralogs of a cathepsin L-like enzyme. Cysteine cathepsins are also part of the normal ... Cathepsin K has a role in bone resorption and has been studied as a drug target for osteoporosis. A number of parasites, ... Cysteine cathepsins have been associated with cancer and tumor progression, cardiovascular disease, autoimmune disease, and ...
BACE1, BACE2 Cathepsin D Cathepsin E Chymosin (or "rennin") Napsin-A Nepenthesin Pepsin Presenilin Renin BACE1; BACE2; CTSD; ... Eukaryotic aspartic proteases include pepsins, cathepsins, and renins. They have a two-domain structure, arising from ancestral ... Cathepsin D". In Rawlings ND, Salvesen G (eds.). Handbook of Proteolytic Enzymes (Third ed.). Academic Press. pp. 54-63. doi: ...
... 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, ...
Hook G, Yu J, Toneff T, Kindy M, Hook V (2014). "Brain pyroglutamate amyloid-β is produced by cathepsin B and is reduced by the ... Kumar P, Nachagari D, Fields C, Franks J, Albritton LM (October 2007). "Host cell cathepsins potentiate Moloney murine leukemia ... reduces brain amyloid-β and improves memory deficits in Alzheimer's disease animal models by inhibiting cathepsin B, but not ... and Structure-Activity Relationship Study of Epoxysuccinyl-Peptide Derivatives as Cathepsin B Inhibitors". Biological & ...
Im E, Kazlauskas A (March 2007). "The role of cathepsins in ocular physiology and pathology". Experimental Eye Research. 84 (3 ... PMID 17322367.[dead link] Gacko M, Chyczewski L, Chrostek L (1999). "Distribution, activity and concentration of cathepsin B ...
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 ...
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]\ ...
Pro-cathepsin D, Prosaposin, and Progranulin: Lysosomal Networks in Parkinsonism Nahid Tayebi 1 , Grisel Lopez 1 , Jenny Do 1 ... Pro-cathepsin D, Prosaposin, and Progranulin: Lysosomal Networks in Parkinsonism Nahid Tayebi et al. Trends Mol Med. 2020 Oct. ... Recombinant pro-CTSD (cathepsin D) enhances SNCA/α-Synuclein degradation in α-Synucleinopathy models. Prieto Huarcaya S, Drobny ... Once in the lysosome, cathepsin D (CTSD) cleaves PSAP, creating four different activators for enzyme hydrolysis, and PGRN is ...
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 ...
Destabilizing role of cathepsin S in murine atherosclerotic plaques. KJ Rodgers, DJ Watkins, AL Miller, PY Chan, S Karanam, WH ... Destabilizing role of cathepsin S in murine atherosclerotic plaques. / Rodgers, KJ; Watkins, DJ; Miller, AL et al. ... Destabilizing role of cathepsin S in murine atherosclerotic plaques. In: Arteriosclerosis, Thrombosis, and Vascular Biology. ... Destabilizing role of cathepsin S in murine atherosclerotic plaques. Arteriosclerosis, Thrombosis, and Vascular Biology. 2006 ...
Tags: aging, blood type, brown fat, C. diff, cancer, cancer immunotherapy, cathepsin, cathepsin B, Clostridium difficile, ... cathepsin. The Peoples Picks for Best Posts Posted on January 5th, 2021. by Dr. Francis Collins ... In a study in Cell Metabolism, Moon and his team showed that this protein called cathepsin B makes its way into the brain and ...
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 ...
We all know that exercise is important for a strong and healthy body. Less appreciated is that exercise seems also to be important for a strong and healthy mind, boosting memory and learning, while possibly delaying age-related cognitive decline. How is this so? Researchers have assembled a growing body of evidence that suggests skeletal muscle cells secrete proteins and other factors into the blood during exercise that have a regenerative effect on the brain. ...
Strong homology of MEP with human cathepsin L suggests that MEP is the mouse analogue of cathepsin L. Amino acid sequencing of ... Strong homology of MEP with human cathepsin L suggests that MEP is the mouse analogue of cathepsin L. Amino acid sequencing of ... Strong homology of MEP with human cathepsin L suggests that MEP is the mouse analogue of cathepsin L. Amino acid sequencing of ... Strong homology of MEP with human cathepsin L suggests that MEP is the mouse analogue of cathepsin L. Amino acid sequencing of ...
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 ...
We found that the expression of carboxylesterase 1 (CES1) and cathepsin C (CTSC) was downregulated in HCM tissues and ... coexpression network analysis reveals negative regulation of hypertrophic cardiomyopathy by carboxylesterase 1 and cathepsin C ...
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 ...
Crystal Structure of an activation intermediate of Cathepsin E ... Cathepsin E: AD. activation peptide from Cathepsin E: BE. 23- ... Crystal Structure of an activation intermediate of Cathepsin E Coordinates. PDB Format Method. X-RAY DIFFRACTION 2.35 Å. Oligo ... Ostermann, N. et al., Crystal structure of an activation intermediate of cathepsin e. J.Mol.Biol. (2004) Release Date. 2005-07- ...
We first confirmed that CysLT1R and cathepsin B are upregulated by Aβ (1-42) and that CysLT1R activation induces cathepsin B. ... We used in vitro and in vivo models to determine whether 6-shogaol inhibits CysLT1R/cathepsin B in an amyloid-beta (Aβ; 1-42)- ... 6-Shogaol has anti-amyloidogenic activity and ameliorates Alzheimers disease via CysLT1R-mediated inhibition of cathepsin B ... Our results indicate that 6-shogaol is a CysLT1R/cathepsin B inhibitor and is a novel potential therapeutic agent for the ...
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 ...
Antibody Details for Cathepsin L. WBI Title. Validation Status. Band Result. Date. Dilution. ...
Cathepsin-Cleavable BIM BH3 Peptide Amphiphiles Are Potent Inducers of Cellular Apoptosis Joseph Bellairs, Joseph Bellairs * ... apoptosis, cathepsins, peptides, micelles, cancer, tumor cells, malignant, antibodies, cancer therapy, caspase-3, caspases ... Joseph Bellairs, Ravand Samaeekia, Handan Acar, Matthew Tirrell, James LaBelle; Cathepsin-Cleavable BIM BH3 Peptide Amphiphiles ... We further demonstrate that incorporating a cathepsin B-cleavable linker between the BIM BH3 peptide and the hydrophobic tail ...
Deficiency of cathepsin A, see Galactosialidosis. *Deficiency of cytochrome-b5 reductase, see Autosomal recessive congenital ...
Cathepsin K. Cathepsin K is a cysteine protease expressed predominantly in osteoclasts. Search. Main menu. Skip to primary ...
In vitro studies have shown that TAF is metabolized to tenofovir by CES1 in hepatocytes, and by cathepsin A in PBMCs and ...
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: ...
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 ...
Background Cathepsin K, a cysteine protease predominantly expressed in osteoclasts, is. Background Cathepsin K, a cysteine ... Outcomes Lung airway cathepsin K manifestation in wild-type mice continued to be continuous between 1 and six months of age as ... Bottom line This study shows that airway advancement is partly governed by cathepsin K which its appearance plays a part in the ... Lung homogenates of wild-type and cathepsin K-deficient mice had been used to judge their material of collagen, ...
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 * ...
  • 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)
  • 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)
  • Cathepsin G can cleave protease activated receptor-4 (PAR4) and is a potential target for novel anti-thrombotic therapies. (crbdiscovery.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)
  • Moreover, we clarified the relationship between CysLT1R and cathepsin B, a cysteine protease. (nih.gov)
  • Background Cathepsin K, a cysteine protease predominantly expressed in osteoclasts, is a significant drug focus on for the treating osteoporosis. (monossabios.com)
  • solid course="kwd-title" Keywords: lung airway, cathepsin K, TGF-1, extracellular matrix, protease inhibitors Background Cathepsin K (CatK) is certainly a lysosomal cysteine protease with powerful collagenolytic and elastolytic actions. (monossabios.com)
  • In this research, the interactions between specific flavonols and the 2019-nCoV receptor binding domain (RBD), transmembrane protease, serine 2 (TMPRSS2), and cathepsins (CatB and CatL) were analyzed. (afsu.edu.tr)
  • 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)
  • 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)
  • 2018). Caspase-4 activation by a bacterial surface protein is mediated by cathepsin G in human gingival fibroblasts Cell Death Differ . (crbdiscovery.com)
  • It's been reported the fact that secretion of development factors such as for example TGF-1 and changed appearance of matrix degrading enzymes such as for example cathepsins [14] donate to structural adjustments in the ECM. (monossabios.com)
  • The cathepsin B enzymes from NEJ flukes have recently been demonstrated to be crucial to invasion and migration by the parasite. (edu.au)
  • Here we characterize one of the cathepsin B enzymes (recombinant FhcatB1) from NEJ flukes. (edu.au)
  • FhcatB1 has biochemical properties distinct from mammalian cathepsin B enzymes, with an atypical preference for Ile over Leu or Arg residues at the P2 substrate position and an inability to act as an exopeptidase. (edu.au)
  • 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)
  • Cathepsin G is a member of the hematopoietic serine proteinase super family along with elastase and proteinase 3. (arodia.com)
  • We found that the expression of carboxylesterase 1 (CES1) and cathepsin C (CTSC) was downregulated in HCM tissues and negatively correlated with Maxi LVWT. (bvsalud.org)
  • 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)
  • TGF-1 demonstrated a competent substrate of cathepsin K and TGF-1 proteins articles in lung was elevated with a potent cathepsin inhibitor. (monossabios.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)
  • 1996) Cathepsin G in gingival tissue and crevicular fluid in adult periodontosis. (arodia.com)
  • 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)
  • The convenience of TGF-1 to cathepsin K-mediated degradation was identified em in vitro PU-H71 /em and lung fibroblast proliferations in wild-type and cathepsin K-deficient cells had been evaluated. (monossabios.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)
  • Cathepsin L, Human Liver, CAS 60616-82-2, is a native, the most potent of all the lysosomal proteinases. (emdmillipore.com)
  • 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)
  • In subsequent RT-PCR experiments, both P450 and cathepsin genes exhibited tissue-specific or distinct expression patterns which supported their principal roles of detoxification and/or digestion in a particular tissue. (biomedcentral.com)
  • Cathepsin S is a lysosomal enzyme that belongs to the papain family of cysteine proteases. (fagusantibodies.com)
  • 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)
  • 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)
  • 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)
  • 1998) Specificity of human cathepsin G. Biochim. (arodia.com)
  • 2013). Cathepsin G-Dependent Modulation of Platelet Thrombus Formation In Vivo by Blood Neutrophils. (crbdiscovery.com)
  • Lung homogenates of wild-type and cathepsin K-deficient mice had been used to judge their material of collagen, glycosaminoglycans, and TGF-1. (monossabios.com)
  • Outcomes Lung airway cathepsin K manifestation in wild-type mice continued to be continuous between 1 and six months of age as well as the airway integrity was managed. (monossabios.com)
  • Hai, PH , Doh-Ura, K & Nakanishi, H 2007, ' Impairment of microglial responses to facial nerve axotomy in cathepsin S-deficient mice ', Journal of Neuroscience Research , vol. 85, no. 10, pp. 2196-2206. (elsevierpure.com)
  • 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)
  • Inflammasome activation was confirmed using inhibitors of cathepsin B and Caspase-1. (cdc.gov)
  • Independent of its proteinase activity, cathepsin G is a significant broad spectrum anti-microbial agent. (arodia.com)
  • There is published data that ANCA associated antibodies against cathepsin G are found in ulcerative colitis and crohn's disease. (arodia.com)
  • 2000) Anti-cathepsin G antibodies in the sera of patients with ulcerative colitis. (arodia.com)
  • Our analysis into P450 and cathepsin genes in H. halys offers new insights into potential mechanisms for understanding generalist herbivory and adaptation success in invasive habitats. (biomedcentral.com)
  • The expected use of healing cathepsin K inhibitors must take potential adjustments in individual lungs under consideration. (monossabios.com)
  • Bottom line This study shows that airway advancement is partly governed by cathepsin K which its appearance plays a part in the maintenance of the airway structural integrity. (monossabios.com)
  • Weighted gene coexpression network analysis reveals negative regulation of hypertrophic cardiomyopathy by carboxylesterase 1 and cathepsin C. (bvsalud.org)
  • Following a comprehensive transcriptome analysis, H. halys had an expanded suite of cytochrome P450 and cathepsin-L genes compared to other insects. (biomedcentral.com)
  • My work on the cathepsins, the secreted cathepsins, just gradually became less and less important. (nih.gov)