Cathepsin G: A serine protease found in the azurophil granules of NEUTROPHILS. It has an enzyme specificity similar to that of chymotrypsin C.Cathepsins: A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.Cathepsin B: A lysosomal cysteine proteinase with a specificity similar to that of PAPAIN. The enzyme is present in a variety of tissues and is important in many physiological and pathological processes. In pathology, cathepsin B has been found to be involved in DEMYELINATION; EMPHYSEMA; RHEUMATOID ARTHRITIS, and NEOPLASM INVASIVENESS.Cathepsin L: A ubiquitously-expressed cysteine protease that plays an enzymatic role in POST-TRANSLATIONAL PROTEIN PROCESSING of proteins within SECRETORY GRANULES.Cathepsin D: An intracellular proteinase found in a variety of tissue. It has specificity similar to but narrower than that of pepsin A. The enzyme is involved in catabolism of cartilage and connective tissue. EC 3.4.23.5. (Formerly EC 3.4.4.23).Cathepsin K: A cysteine protease that is highly expressed in OSTEOCLASTS and plays an essential role in BONE RESORPTION as a potent EXTRACELLULAR MATRIX-degrading enzyme.Cathepsin H: An ubiquitously-expressed lysosomal cysteine protease that is involved in protein processing. The enzyme has both endopeptidase and aminopeptidase activities.Serine Endopeptidases: Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.Cathepsin E: An aspartic endopeptidase that is similar in structure to CATHEPSIN D. It is found primarily in the cells of the immune system where it may play a role in processing of CELL SURFACE ANTIGENS.Cathepsin C: A papain-like cysteine protease that has specificity for amino terminal dipeptides. The enzyme plays a role in the activation of several pro-inflammatory serine proteases by removal of their aminoterminal inhibitory dipeptides. Genetic mutations that cause loss of cathepsin C activity in humans are associated with PAPILLON-LEFEVRE DISEASE.Pancreatic Elastase: A protease of broad specificity, obtained from dried pancreas. Molecular weight is approximately 25,000. The enzyme breaks down elastin, the specific protein of elastic fibers, and digests other proteins such as fibrin, hemoglobin, and albumin. EC 3.4.21.36.Leukocyte Elastase: An enzyme that catalyzes the hydrolysis of proteins, including elastin. It cleaves preferentially bonds at the carboxyl side of Ala and Val, with greater specificity for Ala. EC 3.4.21.37.Cathepsin F: A lysosomal papain-related cysteine proteinase that is expressed in a broad variety of cell types.Cathepsin Z: A ubiquitously-expressed cysteine peptidase that exhibits carboxypeptidase activity. It is highly expressed in a variety of immune cell types and may play a role in inflammatory processes and immune responses.Neutrophils: Granular leukocytes having a nucleus with three to five lobes connected by slender threads of chromatin, and cytoplasm containing fine inconspicuous granules and stainable by neutral dyes.Serine Proteinase Inhibitors: Exogenous or endogenous compounds which inhibit SERINE ENDOPEPTIDASES.Cysteine Endopeptidases: ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.Lysosomes: A class of morphologically heterogeneous cytoplasmic particles in animal and plant tissues characterized by their content of hydrolytic enzymes and the structure-linked latency of these enzymes. The intracellular functions of lysosomes depend on their lytic potential. The single unit membrane of the lysosome acts as a barrier between the enzymes enclosed in the lysosome and the external substrate. The activity of the enzymes contained in lysosomes is limited or nil unless the vesicle in which they are enclosed is ruptured. Such rupture is supposed to be under metabolic (hormonal) control. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)Myeloblastin: A polymorphonuclear leukocyte-derived serine protease that degrades proteins such as ELASTIN; FIBRONECTIN; LAMININ; VITRONECTIN; and COLLAGEN. It is named for its ability to control myeloid cell growth and differentiation.Protease Inhibitors: Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).Cathepsin W: A cysteine endopeptidase found in NATURAL KILLER CELLS and CYTOTOXIC T-LYMPHOCYTES. It may have a specific function in the mechanism or regulation of cytolytic activity of immune cells.Endopeptidases: A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.Chymotrypsin: A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side.Capnocytophaga: A gram-negative gliding bacterium isolated from the oral cavity. It is a pathogen often causing PERIODONTITIS.alpha 1-Antichymotrypsin: Glycoprotein found in alpha(1)-globulin region in human serum. It inhibits chymotrypsin-like proteinases in vivo and has cytotoxic killer-cell activity in vitro. The protein also has a role as an acute-phase protein and is active in the control of immunologic and inflammatory processes, and as a tumor marker. It is a member of the serpin superfamily.Serpins: A family of serine proteinase inhibitors which are similar in amino acid sequence and mechanism of inhibition, but differ in their specificity toward proteolytic enzymes. This family includes alpha 1-antitrypsin, angiotensinogen, ovalbumin, antiplasmin, alpha 1-antichymotrypsin, thyroxine-binding protein, complement 1 inactivators, antithrombin III, heparin cofactor II, plasminogen inactivators, gene Y protein, placental plasminogen activator inhibitor, and barley Z protein. Some members of the serpin family may be substrates rather than inhibitors of SERINE ENDOPEPTIDASES, and some serpins occur in plants where their function is not known.Cathepsin A: A carboxypeptidase that catalyzes the release of a C-terminal amino acid with a broad specificity. It also plays a role in the LYSOSOMES by protecting BETA-GALACTOSIDASE and NEURAMINIDASE from degradation. It was formerly classified as EC 3.4.12.1 and EC 3.4.21.13.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Pepstatins: N-acylated oligopeptides isolated from culture filtrates of Actinomycetes, which act specifically to inhibit acid proteases such as pepsin and renin.Cystatins: A homologous group of endogenous CYSTEINE PROTEINASE INHIBITORS. The cystatins inhibit most CYSTEINE ENDOPEPTIDASES such as PAPAIN, and other peptidases which have a sulfhydryl group at the active site.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Ammonium Hydroxide: The hydroxy salt of ammonium ion. It is formed when AMMONIA reacts with water molecules in solution.Phenylmethylsulfonyl Fluoride: An enzyme inhibitor that inactivates IRC-50 arvin, subtilisin, and the fatty acid synthetase complex.Chymases: A family of neutral serine proteases with CHYMOTRYPSIN-like activity. Chymases are primarily found in the SECRETORY GRANULES of MAST CELLS and are released during mast cell degranulation.Chediak-Higashi Syndrome: A form of phagocyte bactericidal dysfunction characterized by unusual oculocutaneous albinism, high incidence of lymphoreticular neoplasms, and recurrent pyogenic infections. In many cell types, abnormal lysosomes are present leading to defective pigment distribution and abnormal neutrophil functions. The disease is transmitted by autosomal recessive inheritance and a similar disorder occurs in the beige mouse, the Aleutian mink, and albino Hereford cattle.Cysteine Proteinase Inhibitors: Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.Proteinase Inhibitory Proteins, Secretory: Peptides and proteins found in BODILY SECRETIONS and BODY FLUIDS that are PROTEASE INHIBITORS. They play a role in INFLAMMATION, tissue repair and innate immunity (IMMUNITY, INNATE) by inhibiting endogenous proteinases such as those produced by LEUKOCYTES and exogenous proteases such as those produced by invading microorganisms.Isoflurophate: A di-isopropyl-fluorophosphate which is an irreversible cholinesterase inhibitor used to investigate the NERVOUS SYSTEM.Cytoplasmic Granules: Condensed areas of cellular material that may be bounded by a membrane.Oligopeptides: Peptides composed of between two and twelve amino acids.Enzyme Precursors: Physiologically inactive substances that can be converted to active enzymes.Kinetics: The rate dynamics in chemical or physical systems.alpha 1-Antitrypsin: Plasma glycoprotein member of the serpin superfamily which inhibits TRYPSIN; NEUTROPHIL ELASTASE; and other PROTEOLYTIC ENZYMES.DiazomethanePlatelet Activation: A series of progressive, overlapping events, triggered by exposure of the PLATELETS to subendothelial tissue. These events include shape change, adhesiveness, aggregation, and release reactions. When carried through to completion, these events lead to the formation of a stable hemostatic plug.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Dipeptides: Peptides composed of two amino acid units.N-Formylmethionine Leucyl-Phenylalanine: A formylated tripeptide originally isolated from bacterial filtrates that is positively chemotactic to polymorphonuclear leucocytes, and causes them to release lysosomal enzymes and become metabolically activated.Encyclopedias as Topic: Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)Rodenticides: Substances used to destroy or inhibit the action of rats, mice, or other rodents.Rodent Control: The reduction or regulation of the population of noxious, destructive, or dangerous rodents through chemical, biological, or other means.Rodent Diseases: Diseases of rodents of the order RODENTIA. This term includes diseases of Sciuridae (squirrels), Geomyidae (gophers), Heteromyidae (pouched mice), Castoridae (beavers), Cricetidae (rats and mice), Muridae (Old World rats and mice), Erethizontidae (porcupines), and Caviidae (guinea pigs).

Bile duct epithelial cells exposed to alpha-naphthylisothiocyanate produce a factor that causes neutrophil-dependent hepatocellular injury in vitro. (1/369)

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)

The intracellular serpin proteinase inhibitor 6 is expressed in monocytes and granulocytes and is a potent inhibitor of the azurophilic granule protease, cathepsin G. (2/369)

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)

Regulation of pro-apoptotic leucocyte granule serine proteinases by intracellular serpins. (3/369)

Caspase activation and apoptosis can be initiated by the introduction of serine proteinases into the cytoplasm of a cell. Cytotoxic lymphocytes have evolved at least one serine proteinase with specific pro-apoptotic activity (granzyme B), as well as the mechanisms to deliver it into a target cell, and recent evidence suggests that other leucocyte granule proteinases may also have the capacity to kill if released into the interior of cells. For example, the monocyte/granulocyte proteinase cathepsin G can activate caspases in vitro, and will induce apoptosis if its entry into cells is mediated by a bacterial pore-forming protein. The potent pro-apoptotic activity of granzyme B and cathepsin G suggests that cells producing these (or other) proteinases would be at risk from self-induced death if the systems involved in packaging, degranulation or targeting fail and allow proteinases to enter the host cell cytoplasm. The purpose of the present review is to describe recent work on a group of intracellular serine proteinase inhibitors (serpins) which may function in leucocytes to prevent autolysis induced by the granule serine proteinases.  (+info)

New, sensitive fluorogenic substrates for human cathepsin G based on the sequence of serpin-reactive site loops. (4/369)

Cathepsin G has both trypsin- and chymotrypsin-like activity, but studies on its enzymatic properties have been limited by a lack of sensitive synthetic substrates. Cathepsin G activity is physiologically controlled by the fast acting serpin inhibitors alpha1-antichymotrypsin and alpha1-proteinase inhibitor, in which the reactive site loops are cleaved during interaction with their target enzymes. We therefore synthesized a series of intramolecularly quenched fluorogenic peptides based on the sequence of various serpin loops. Those peptides were assayed as substrates for cathepsin G and other chymotrypsin-like enzymes including chymotrypsin and chymase. Peptide substrates derived from the alpha1-antichymotrypsin loop were the most sensitive for cathepsin G with kcat/Km values of 5-20 mM-1 s-1. Substitutions were introduced at positions P1 and P2 in alpha1-antichymotrypsin-derived substrates to tentatively improve their sensitivity. Replacement of Leu-Leu in ortho-aminobenzoyl (Abz)-Thr-Leu-Leu-Ser-Ala-Leu-Gln-N-(2, 4-dinitrophenyl)ethylenediamine (EDDnp) by Pro-Phe in Abz-Thr-Pro-Phe-Ser-Ala-Leu-Gln-EDDnp produced the most sensitive substrate of cathepsin G ever reported. It was cleaved with a specificity constant kcat/Km of 150 mM-1 s-1. Analysis by molecular modeling of a peptide substrate bound into the cathepsin G active site revealed that, in addition to the protease S1 subsite, subsites S1' and S2' significantly contribute to the definition of the substrate specificity of cathepsin G.  (+info)

High mobility group (HMG) non-histone chromosomal proteins HMG1 and HMG2 are significant target antigens of perinuclear anti-neutrophil cytoplasmic antibodies in autoimmune hepatitis. (5/369)

BACKGROUND: High mobility group (HMG) non-histone chromosomal proteins HMG1 and HMG2 have been identified as novel antigens of perinuclear anti-neutrophil cytoplasmic antibodies (p-ANCAs), and the existence of anti-HMG1 and anti-HMG2 antibodies in a population of patients with ulcerative colitis has been reported. AIMS: To investigate whether HMG1 and HMG2 are target antigens for p-ANCAs in autoimmune hepatitis (AIH). PATIENTS: Serum samples from 28 patients with AIH, 44 patients with primary biliary cirrhosis (PBC), 27 patients with chronic hepatitis C, and 23 patients with chronic hepatitis B were tested. METHODS: ANCAs were detected by routine indirect immunofluorescence (IIF). Anti-HMG1 and anti-HMG2 antibodies were assayed by enzyme linked immunosorbent assay. RESULTS: p-ANCAs were detected in 89% (25/28) of patients with AIH, 36% (16/44) of patients with PBC, 11% (3/27) of patients with chronic hepatitis C, and 13% (3/23) of patients with chronic hepatitis B. Anti-HMG1 and/or anti-HMG2 antibodies were detected in 89% (25/28) of patients with AIH, 70% (31/44) with PBC, 26% (7/27) with chronic hepatitis C, and 9% (2/23) with chronic hepatitis B. In AIH, anti-HMG1 and/or anti-HMG2 antibodies were detected in 96% (24/25) of p-ANCA positive patients. The p-ANCA staining pattern detected by IIF using sera from patients with AIH disappeared or decreased in titre after preincubation with a mixture of HMG1/HMG2. The presence and titres of those antibodies in AIH correlated significantly with those of p-ANCA, but not with those of anti-nuclear antibody or anti-smooth muscle antibody. CONCLUSIONS: HMG1 and HMG2 are significant target antigens of p-ANCA in AIH.  (+info)

Converting enzyme-independent release of tumor necrosis factor alpha and IL-1beta from a stimulated human monocytic cell line in the presence of activated neutrophils or purified proteinase 3. (6/369)

Two important cytokines mediating inflammation are tumor necrosis factor alpha (TNFalpha) and IL-1beta, both of which require conversion to soluble forms by converting enzymes. The importance of TNFalpha-converting enzyme and IL-1beta-converting enzyme in the production of circulating TNFalpha and IL-1beta in response to systemic challenges has been demonstrated by the use of specific converting enzyme inhibitors. Many inflammatory responses, however, are not systemic but instead are localized. In these situations release and/or activation of cytokines may be different from that seen in response to a systemic stimulus, particularly because associations of various cell populations in these foci allows for the exposure of procytokines to the proteolytic enzymes produced by activated neutrophils, neutrophil elastase (NE), proteinase 3 (PR3), and cathepsin G (Cat G). To investigate the possibility of alternative processing of TNFalpha and/or IL-1beta by neutrophil-derived proteinases, immunoreactive TNFalpha and IL-1beta release from lipopolysaccharide-stimulated THP-1 cells was measured in the presence of activated human neutrophils. Under these conditions, TNFalpha and IL-1beta release was augmented 2- to 5-fold. In the presence of a specific inhibitor of NE and PR3, enhanced release of both cytokines was largely abolished; however, in the presence of a NE and Cat G selective inhibitor, secretory leucocyte proteinase inhibitor, reduction of the enhanced release was minimal. This finding suggested that the augmented release was attributable to PR3 but not NE nor Cat G. Use of purified enzymes confirmed this conclusion. These results indicate that there may be alternative pathways for the production of these two proinflammatory cytokines, particularly in the context of local inflammatory processes.  (+info)

Primary structure and properties of the cathepsin G/chymotrypsin inhibitor from the larval hemolymph of Apis mellifera. (7/369)

A member of the Ascaris inhibitor family exhibiting anti-cathepsin G and anti-chymotrypsin activity was purified from the larval hemolymph of the honey bee (Apis mellifera). Three forms of the inhibitor, designated AMCI 1-3, were isolated using gel filtration and anion-exchange chromatographies followed by reverse-phase HPLC. The amino-acid analyses indicated that AMCI-1 and AMCI-2 have an identical composition whereas AMCI-3 is shorter by two residues (Thr, Arg). All three forms contain as many as 10 cysteine residues and lack tryptophan, tyrosine, and histidine. The sequence of the isoinhibitors showed that the major form (AMCI-1) consisting of 56 amino-acid residues was a single-chain protein of molecular mass 5972 Da, whereas the other two forms were two-chain proteins with a very high residue identity. The AMCI-2 appeared to be derived from AMCI-1, as a result of the Lys24-Thr25 peptide bond splitting, while AMCI-3 was truncated at its N-terminus by the dipeptide Thr25-Arg26. The association constants for the binding of bovine alpha-chymotrypsin to all purified forms of the inhibitor were high and nearly identical, ranging from 4.8 x 10(10) M-1 for AMCI-1 to 2.7 x 10(9) M-1 for AMCI-3. The sensitivity of cathepsin G to inhibition by each inhibitor was different. Only the association constant for the interaction of this enzyme with AMCI-1 was high (2 x 10(8) M-1) whereas those for AMCI-2 and AMCI-3 were significantly lower, and appeared to be 3.7 x 10(7) M-1 and 4.5 x 10(6) M-1, respectively. The reactive site of the inhibitor, as identified by cathepsin G degradation and chemical modification, was found to be at Met30-Gln31. A search in the Protein Sequence Swiss-Prot databank revealed a significant degree of identity (44%) between the primary structure of AMCI and the trypsin isoinhibitor from Ascaris sp (ATI). On the basis of the cysteine residues alignment, the position of the reactive site as well as some sequence homology, the cathepsin G/chymotrypsin inhibitor from larval hemolymph of the honey bee may be considered to be a member of the Ascaris inhibitor family.  (+info)

SPI-1-dependent host range of rabbitpox virus and complex formation with cathepsin G is associated with serpin motifs. (8/369)

Serpins are a superfamily of serine proteinase inhibitors which function to regulate a number of key biological processes including fibrinolysis, inflammation, and cell migration. Poxviruses are the only viruses known to encode functional serpins. While some poxvirus serpins regulate inflammation (myxoma virus SERP1 and cowpox virus [CPV] crmA/SPI-2) or apoptosis (myxoma virus SERP2 and CPV crmA/SPI-2), the function of other poxvirus serpins remains unknown. The rabbitpox virus (RPV) SPI-1 protein is 47% identical to crmA and shares all of the serpin structural motifs. However, no serpin-like activity has been demonstrated for SPI-1 to date. Earlier we showed that RPV with the SPI-1 gene deleted, unlike wild-type virus, fails to grow on A549 or PK15 cells (A. Ali, P. C. Turner, M. A. Brooks, and R. W. Moyer, Virology 202:306-314, 1994). Here we demonstrate that in the absence of a functional SPI-1 protein, infected nonpermissive cells which exhibit the morphological features of apoptosis fail to activate terminal caspases or cleave the death substrates PARP or lamin A. We show that SPI-1 forms a stable complex in vitro with cathepsin G, a member of the chymotrypsin family of serine proteinases, consistent with serpin activity. SPI-1 reactive-site loop (RSL) mutations of the critical P1 and P14 residues abolish this activity. Viruses containing the SPI-1 RSL P1 or P14 mutations also fail to grow on A549 or PK15 cells. These results suggest that the full virus host range depends on the serpin activity of SPI-1 and that in restrictive cells SPI-1 inhibits a proteinase with chymotrypsin-like activity and may function to inhibit a caspase-independent pathway of apoptosis.  (+info)

*Cathepsin

... A (serine protease) Cathepsin B (cysteine protease) Cathepsin C (cysteine protease) Cathepsin D (aspartyl protease) ... Cathepsin H (cysteine protease) Cathepsin K (cysteine protease) Cathepsin L1 (cysteine protease) Cathepsin L2 (or V) (cysteine ... Cathepsin S (cysteine protease) Cathepsin W (cysteine proteinase) Cathepsin Z (or X) (cysteine protease) Cathepsins have been ... Cathepsin K has also been shown to play a role in arthritis. Mouse cathepsin L is homologous to human cathepsin V. Mouse ...

*Cathepsin T

Cathepsin Cathepsin T at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... Cathepsin T (EC 3.4.22.24) is an enzyme. This enzyme catalyses the following chemical reaction Interconversion of the three ... Pitot, H.C.; Gohda, E. (1987). "Cathepsin T". Methods Enzymol. 142: 279-289. doi:10.1016/s0076-6879(87)42038-7. PMID 2885716. ...

*Cathepsin H

"Entrez Gene: CTSH cathepsin H". Sawicki G, Warwas M (1990). "Cathepsin H from human placenta". Acta Biochim. Pol. 36 (3-4): 343 ... Cathepsin H is a protein that in humans is encoded by the CTSH gene. The protein encoded by this gene is a lysosomal cysteine ... 2003). "Expression of cathepsins B, H, K, L, and S during human fetal lung development". Dev. Dyn. 225 (1): 14-21. doi:10.1002/ ... 2001). "Expression of cathepsins B, H, K, L, and S and matrix metalloproteinases 9 and 13 during chondrocyte hypertrophy and ...

*Cathepsin S

... cathepsin S can be replaced by cathepsin F. Secreted cathepsin S cleaves some extracellular matrix (ECM) proteins. Cathepsin S ... In vitro, cathepsin S retains some enzyme activity in the presence of 3M urea. Cathepsin S is produced as a zymogen and is ... Cathepsin S can function as an elastase over a broad pH range in alveolar macrophages. Cathepsin S is a lysosomal enzyme that ... In tumorogenesis, cathepsin S promotes a tumor growth. Cathepsin S expression and activity has also been shown to be ...

*Cathepsin A

... is an enzyme that is classified both as a cathepsin and a carboxypeptidase. In humans, it is encoded by the CTSA ... Cathepsin A at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology portal. ... Cathepsin A has been shown to interact with NEU1. GRCh38: Ensembl release 89: ENSG00000064601 - Ensembl, May 2017 GRCm38: ... 1991). "Human lysosomal protective protein has cathepsin A-like activity distinct from its protective function". J. Biol. Chem ...

*Cathepsin B

... has been shown to interact with: CTSD CSTA, CSTB, and S100A10. Cathepsin B is inhibited by: Nitroxoline Cathepsins ... Cathepsin B is in humans encoded by the CTSB gene. Cathepsin B belongs to a family of lysosomal cysteine proteases and plays an ... Cathepsin B has been proposed as a potentially effective biomarker for a variety of cancers. Overexpression of cathepsin B is ... Similarly, cathepsin B gene knockout and cathepsin B inhibitor treatment studies in traumatic brain injury mouse models have ...

*Cathepsin zymography

Cathepsin K detection by zymography Zymographic techniques for detection of cathepsins K, L, S, and V Zymography for detection ... Cathepsin zymography is a technique for quantifying enzymatic activity of the cathepsin family of cysteine proteases. It is ... While the proform of cathepsins are generally stable, once activated, proteases such as cathepsin K are vulnerable to ... After the renaturing period, the gel is then incubated in assay buffer to allow the now active cathepsins to proteolyze the ...

*Cathepsin V

... (EC 3.4.22.43, Cathepsin L2, cathepsin U) is an enzyme. This enzyme catalyses the following chemical reaction The ... Cathepsin L2 Brömme, D.; Li, Z.; Barnes, M.; Mehler, E. (1999). "Human cathepsin V functional expression, tissue distribution, ... Cathepsin V at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology portal. ... Santamaría, I.; Velasco, G.; Cazorla, M.; Fueyo, A.; Campo, E.; López-Otín, C. (1998). "Cathepsin L2, a novel human cysteine ...

*Cathepsin F

... is a protein that in humans is encoded by the CTSF gene. Cathepsins are papain family cysteine proteinases that ... The cathepsin F gene is ubiquitously expressed, and it maps to chromosome 11q13, close to the gene encoding cathepsin W. GRCh38 ... "Entrez Gene: CTSF cathepsin F". Nägler DK, Sulea T, Ménard R (1999). "Full-length cDNA of human cathepsin F predicts the ... Wex T, Levy B, Wex H, Brömme D (1999). "Human cathepsins F and W: A new subgroup of cathepsins". Biochem. Biophys. Res. Commun ...

*Cathepsin W

"Human cathepsins W and F form a new subgroup of cathepsins that is evolutionary separated from the cathepsin B- and L-like ... Wex T, Levy B, Wex H, Brömme D (1999). "Human cathepsins F and W: A new subgroup of cathepsins". Biochem. Biophys. Res. Commun ... 2003). "Characterization of novel anti-cathepsin W antibodies and cellular distribution of cathepsin W in the gastrointestinal ... Cathepsin W is a protein that in humans is encoded by the CTSW gene. The protein encoded by this gene, a member of the ...

*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 ... Cathepsin D is a protein that in humans is encoded by the CTSD gene. This gene encodes a lysosomal aspartyl protease composed ...

*Cathepsin L1

... is a protein that in humans is encoded by the CTSL1 gene. The protein encoded by this gene is a lysosomal cysteine ... Major sites of cleavage by cathepsins B, D, and L". J. Biol. Chem. 266 (30): 20198-204. PMID 1939080. Stearns NA, Dong JM, Pan ... 1991). "Comparison of cathepsin L synthesized by normal and transformed cells at the gene, message, protein, and ... Joseph L, Lapid S, Sukhatme V (1987). "The major ras induced protein in NIH3T3 cells is cathepsin L". Nucleic Acids Res. 15 (7 ...

*Cathepsin Z

... cathepsin G, cathepsin H, cathepsin K, cathepsin L, cathepsin L2, cathepsin O, cathepsin S, cathepsin Z, and cathepsin W. These ... Cathepsin Z, also called cathepsin X or cathepsin P, is a protein that in humans is encoded by the CTSZ gene. It is a member of ... As one of the 11 cathepsins, cathepsin Z contains distinctive features from others. Cathepsin Z has been reported involved in ... Cathepsin Z has an exposed integrin-bindign Arg-Gly-Asp motif within the propeptide of the enzyme, through which cathepsin Z ...

*Cathepsin L2

... , also known as cathepsin V and encoded by the CTSL2 gene, is a human gene. The protein encoded by this gene, a ... 2006). "Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the ... 2007). "Inhibition of cathepsin L-like proteases by cathepsin V propeptide". Biol. Chem. 388 (5): 541-5. doi:10.1515/BC. ... 2005). "The human cysteine protease cathepsin V can compensate for murine cathepsin L in mouse epidermis and hair follicles". ...

*Cathepsin L

... 1, previously called cathepsin L Cathepsin L2 or cathepsin V Barrett, A.J.; Kirschke, H. (1981). "Cathepsin B, ... cathepsin H and cathepsin L". Methods Enzymol. 80: 535-561. doi:10.1016/s0076-6879(81)80043-2. PMID 7043200. Barrett, A.J.; ... Reinheckel T.Human cathepsin L rescues the neurodegeneration and lethality in cathepsin B/L double-deficient mice. Biol Chem. ... Cathepsin L at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology portal. ...

*Cathepsin G

... is one of those homologous protease that evolved from a common ancestor by gene duplication. Cathepsin G is a 255- ... An upregulation of cathepsin G was reported in studies of keratoconus. Cathepsin G has been found to interact with: SERPINB1 ... "Entrez Gene: CTSG cathepsin G". Shafer WM, Pohl J, Onunka VC, Bangalore N, Travis J (January 1991). "Human lysosomal cathepsin ... "Generation of the neutrophil-activating peptide-2 by cathepsin G and cathepsin G-treated human platelets". The American Journal ...

*Cathepsin O

... is an enzyme that in humans is encoded by the CTSO gene. Cathepsin O is a cysteine protease and a member of the ... "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 E

... is an enzyme that in humans is encoded by the CTSE gene. Cathepsin E is a protease found in animals, as well as ... The structure of Cathepsin E is very similar to those of Cathepsin D and BACE1, and all 3 have almost identical active site ... "Entrez Gene: CTSE cathepsin E". "CTSE cathepsin E [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2016- ... Along with renin and Cathepsin D, Cathepsin E is one of the only few aspartic proteases known to be made in human tissues other ...

*Cathepsin K

... is degraded by Cathepsin S, called Controlled Cathepsin Cannibalism. Cathepsin K expression is stimulated by ... Cathepsin K has also been found to be over-expressed in glioblastoma. That the expression of cathepsin K is characteristic for ... Cathepsin K antibodies are marketed for research into expression of this enyzme by various cells. Merck had a cathepsin K ... Other cathepsin K inhbitors are in various stages of development. Medivir has a cathepsin K inhibitor, MIV-711 (L-006235), in ...

*Cathepsin X

... (EC 3.4.18.1, cathepsin B2, cysteine-type carboxypeptidase, cathepsin IV, cathepsin Z, acid carboxypeptidase, ... Cathepsin Z Cathepsin X at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... Otto, K.; Riesenkönig, H. (1975). "Improved purification of cathepsin B1 and cathepsin B2". Biochim. Biophys. Acta. 379 (2): ... "On the substrate specificity of cathepsins B1 and B2 including a new fluorogenic substrate for cathepsin B1". Life Sci. 17 (8 ...

*Cathepsin C

... prepro-cathepsin C) comprising signal peptides of 24 residues, pro-regions of 205 (rat cathepsin C) or 206 (human cathepsin C) ... Cathepsin C appears to be a central coordinator for activation of many serine proteases in immune/inflammatory cells. Cathepsin ... identical to the mature amino acid sequences of papain and a number of other cathepsins including cathepsins, B, H, K, L, and S ... Cathepsin C (CTSC) also known as dipeptidyl peptidase I (DPP-I) is a lysosomal exo-cysteine protease belonging to the peptidase ...

*Chromatin

... , Histones & Cathepsin; PMAP The Proteolysis Map-animation [ Recent chromatin publications and news] Protocol for in ...

*Polysulfated glycosaminoglycan

... collagenases such as cathepsin B1; and hyaluronidase. PSGAG inhibits the synthesis of prostaglandin E2, which is released upon ...

*Carboxypeptidase C

Cathepsin A Breddam, K. (1986). "Serine carboxypeptidases. A review". Carlsberg Res. Commun. 51: 83-128. doi:10.1007/bf02907561 ... Miller, J.J.; Changaris, D.G.; Levy, R.S. (1992). "Purification, subunit structure and inhibitor profile of cathepsin-A". J. ... Carboxypeptidase C (EC 3.4.16.5, carboxypeptidase Y, serine carboxypeptidase I, cathepsin A, lysosomal protective protein, ...
We infused microgram quantities of active or inactive PMN elastase and cathepsin G into the renal arteries of rats. Both active and inactive elastase localized to the glomerular capillary wall equally, and in amounts that could be achieved physiologically in GN. However, elastase-perfused rats developed marked proteinuria (196 +/- 32 mg/24 h) compared with control rats receiving inactive elastase (19 +/- 2 mg/24 h, p less than 0.005). Similar results were seen with active and inactive cathepsin G. Neither elastase nor cathepsin G infusion was associated with histologic evidence of glomerular injury. We conclude that the PMN neutral serine proteinases elastase and cathepsin G can mediate marked changes in glomerular permeability in vivo due to their proteolytic activity, and thus, may contribute to the proteinuria observed in PMN-dependent models of GN. ...
Cathepsin G is a protein that in humans is encoded by the CTSG gene. It is one of the three serine proteases of the chymotrypsin family that are stored in the azurophil granules, and also a member of the peptidase S1 protein family, Cathepsin G plays an important role in eliminating intracellular pathogens and breaking down tissues at inflammatory sites, as well as in anti-inflammatory response. The CTSG gene is located at chromosome 14q11.2, consisting of 5 exons. Each residue of the catalytic triad is located on a separate exon. Five polymorphisms have been identified by scanning the entire coding region. Cathepsin G is one of those homologous protease that evolved from a common ancestor by gene duplication. Cathepsin G is a 255-amino-acid-residue protein including an 18-residue signal peptide, a two-residue activation peptide at the N-terminus and a carboxy terminal extension. The activity of cathepsin G depends on a catalytic triad composed of aspartate, histidine and serine residues which ...
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
TY - JOUR. T1 - Cathepsin G activity lowers plasma LDL and reduces atherosclerosis. AU - Wang, J.. AU - Tang, T.-T.. AU - Öörni, K.. AU - Wu, W.. AU - Liu, C.. AU - Secco, B.. AU - Tia, V.. AU - Sukhova, G.K.. AU - Fernandes, C.. AU - Lesner, A.. AU - Kovanen, P.T.. AU - Libby, P.. AU - Cheng, X.. AU - Shi, G.-P.. N1 - Cited By :7 Export Date: 30 October 2017 Volume: Proceeding volume: PY - 2014. Y1 - 2014. U2 - 10.1016/j.bbadis.2014.07.026. DO - 10.1016/j.bbadis.2014.07.026. M3 - Artikkeli. VL - 1842. SP - 2174. EP - 2183. JO - Biochimica et Biophysica Acta. Molecular Basis of Disease. JF - Biochimica et Biophysica Acta. Molecular Basis of Disease. SN - 0925-4439. IS - 11. ER - ...
... ::= { assay descr { aid { id 832, version 2 }, aid-source db { name "PCMD", source-id str "CAT_G_IC50" }, name "Cathepsin G dose-response confirmation", description { "Screening Center: Penn Center for Molecular Discovery", "Center Affiliation: University of Pennsylvania", "Network: Molecular Library Screening Center Network (MLSCN)", "Assay Provider: Scott Diamond, University of Pennsylvania", "Grant number: MH076406-01", "", "Cathepsin G (EC 3.4.21.20) is a chymotrypsin-like serine protease that is secreted from neutrophils. Disregulated cathepsin G activity is implicated in the progression of various chronic inflammatory diseases such as asthma and chronic pulmonary obstructive disease. Thus cathepsin G inhibitors represent useful probes to further elucidate the role of this enzyme in inflammation and may provide a starting point for the development of novel therapeutic agents.", "", "A high-throughput screen for cathepsin G inhibitors was designed as an end-point assay ...
Mediators of Inflammation is a peer-reviewed, Open Access journal that publishes original research and review articles on all types of inflammatory mediators, including cytokines, histamine, bradykinin, prostaglandins, leukotrienes, PAF, biological response modifiers and the family of cell adhesion-promoting molecules.
Cathepsin G binds to human lymphocytes.: Cathepsin G is a serine protease located in the azurophil granules of neutrophils. We have shown previously that cathep
Cathepsin G ELISA Kits für viele Reaktivitäten. Human, Säugetier, Maus und weitere. Cathepsin G ELISA Kits vergleichen und bestellen.
Cathepsin G is an enzymatic protein belonging to the peptidase or protease families. In humans, it is coded by the CTSG gene. The protein encoded by this gene, a member of the peptidase S1 protein family, is found in azurophil granules of neutrophilic polymorphonuclear leukocytes. The encoded protease has a specificity similar to that of chymotrypsin C, and may participate in the killing and digestion of engulfed pathogens, and in connective tissue remodeling at sites of inflammation. Transcript variants utilizing alternative polyadenylation signals exist for this gene ...
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We describe in this paper the structure-based design of a general class of heterocyclic mechanism-based inhibitors of the serine proteinases that embody in their structure a novel peptidomimetic scaffold (1,2,5-thiadiazolidin-3-one 1,1-dioxide). Sulfone derivatives of this class (I) were found to be time-dependent, potent, and highly efficient irreversible inhibitors of human leukocyte elastase, cathepsin G, and proteinase 3. The partition ratios for a select number of inhibitors were found to range between 0 and 1. We furthermore demonstrate that these inhibitors exhibit remarkable enzyme selectivity that is dictated by the nature of the P1 residue and is consistent with the known substrate specificity reported for these enzymes. Thus, inhibitors with small hydrophobic side chains were found to be effective inhibitors of elastase, those with aromatic side chains of cathepsin G, and those with a basic side chain of bovine trypsin. Taken together, the findings cited herein reveal the emergence of ...
Endothelial cells (ECs) are critically involved in the pathogenesis of atherosclerosis by producing inflammatory mediators, including interleukin-1 beta (IL-1β). However, its mechanism of externalisation is yet to be elucidated. This study investigates the effect of neutrophil elastase (NE) on ECs in terms of IL-1β release and explores the underlying mechanism. Human coronary artery endothelial cells (HCAEC) were treated with a combination of tumour necrosis factor-alpha and interleukin-1 alpha then incubated with NE for 2 or 6 h. ELISA, western blotting, flow cytometry and live cell imaging were used. Paraffin-embedded sections of aortic sinus lesions of apoe-/- mice were immunostained for NE and VWF (Von Willebrand factor). NE is predominantly expressed in ECs in experimental atherosclerosis. In vitro, NE caused significant IL-1β release into supernatants after 6h (579 ± 90 vs. 80 ± 19 pg/ml in control; n = 4, p , 0.0001). The release was via microparticle shedding which is significantly ...
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Gene target information for Ctsg - cathepsin G (house mouse). Find diseases associated with this biological target and compounds tested against it in bioassay experiments.
I see some evidence, but its just some evidence. I did not spot it; it was brought up in various other posts, and I only took notice because Ive been wondering if Y would eventually follow suit to G. Ive been stickying and emailing around for the past week or so, and it has me very curious.. What I see is not related to our own sites; weve not launched anything new for several months. But in looking at a few situations with other sites after sniffing around, it seems possible that Y is starting something like what G implemented, though milder. As sanity and graywolf note, there are plenty of sites that are new and showing already, so its not a simple age thing. But Ive never believed that Gs icebox was just age related. What evidence of this I do see in Y seems more along the lines of preventing extremes. In this regard, it seems to mirror what I believe was the underlying premise of Gs activity...fighting the good fight against unnatural activity. If some of these more "sandbox ...
In this study, we show that the platelet surface expression of glycoprotein (GP) V is regulated by two independent mechanisms. While confirming that both thrombin and neutrophil elastase proteolyse GPV, we show that neutrophil cathepsin G, thrombin receptor activating peptide (TRAP), and a combination of ADP and epinephrine can each result in a decrease in the platelet surface expression of GPV by a nonproteolytic mechanism: a cytoskeletal-mediated redistribution of platelet surface GPV to the surface-connected canalicular system (SCCS). Four independent lines of evidence documented the nonproteolytic nature of this decrease in the platelet surface expression of GPV. First, flow cytometric studies showed that cathepsin G, TRAP, and ADP/epinephrine decreased the platelet surface expression of GPV without changing the total platelet content of GPV. Second, immunoelectron microscopy directly demonstrated translocation of GPV from the platelet surface to the SCCS. Third, the cathepsin G-, TRAP-, and ADP
Prices are in US dollars.. These products are for laboratory research purposes only, not for any human or animal diagnostic or therapeutic use.. All site content © 2017 Cell Sciences, Inc.. ...
AbstractCardiovascular disease is responsible for the majority of deaths in the developed world. Particularly in patients with chronic kidney disease (CKD), the imbalance of calcium and phosphate may accelerate both vascular and valve inflammation and calcification. One in two patients with CKD are reported as dying from cardiovascular causes due to the resulting acceleration in the development of atherosclerosis plaques. In addition, CKD patients on hemodialysis are prone to aortic valve calcification and often need valve replacement before they undergo kidney transplantation. The lysosomal proteases, cathepsins, are composed of 11 cysteine members (cathepsin B, C, F, H, K, L, O, S, V, W, and Z), as well as serine proteases cathepsin A and G, which cleave peptide bonds with serine as the amino acid, and aspartyl proteases D and E, which use an activated water molecule bound to aspartate to break peptide substrate. Cysteine proteases, also known as thiol proteases, degrade protein via the deprotonation
Polymorphonuclear neutrophils (PMN) play an important role in myocardial ischemia/reperfusion (MI/R) injury; however, the role of neutrophilic proteases is less understood. The effects of a novel serine protease inhibitor (serpin), LEX032, were investigated in a murine model of MI (20 min) and R (24 hr) injury in vivo. LEX032 is a recombinant human alpha 1-antichymotrypsin in which six amino acid residues were replaced around the active center with those of alpha-1 protease inhibitor. LEX032 has the ability to inhibit both neutrophil elastase and cathepsin G, two major neutral serine proteases in neutrophils, as well as superoxide generation. LEX032 (25 or 50 mg/kg) administered i.v. 1 min before reperfusion significantly attenuated myocardial necrotic injury evaluated by cardiac creatine kinase loss compared to MI/R rats receiving only vehicle (P , .001). Moreover, cardiac myeloperoxidase activity, an index of PMN accumulation, in the ischemic myocardium was significantly attenuated by LEX032 ...
Autoantigenic peptides resulting from self-proteins such as proinsulin are important players in the development of type 1 diabetes mellitus (T1D). Self-proteins can be processed by cathepsins (Cats) within endocytic compartments and loaded to major h
The existence of subtle differences in the Sn subsites of closely-related (chymo)trypsin-like serine proteases, and the fact that the 1,2,5-thiadiazolidin-3-one 1,1 dioxide scaffold docks to the active site of (chymo)trypsin-like enzymes in a substrate-like fashion, suggested that the introduction of recognition elements that can potentially interact with the Sn subsites of these proteases might provide an effective means for optimizing enzyme potency and selectivity. Accordingly, a series of heterocyclic sulfide derivatives based on the 1,2,5-thiadiazolidin-3-one 1,1 dioxide scaffold (I) was synthesized and the inhibitory activity and selectivity of these compounds toward human leukocyte elastase (HLE), proteinase 3 (PR 3) and cathepsin G (Cat G) were then determined. Compounds with P1 = isobutyl were found to be potent, time-dependent inhibitors of HLE and, to a lesser extent PR 3, while those with P1 = benzyl inactivated Cat G rapidly and irreversibly. This study has demonstrated that ...
cytoplasmic stress granule, extracellular exosome, extracellular matrix, extracellular space, nucleus, plasma membrane, secretory granule, heparin binding, peptidase activity, serine-type endopeptidase activity
Sigma-Aldrich offers abstracts and full-text articles by [Naimeh Rafatian, Denuja Karunakaran, Katey J Rayner, Frans H H Leenen, Ross W Milne, Stewart C Whitman].
seqfile=/share/crumb/www-data/html/tmp/gcgseq.tmp.3937.2. Start End Strand Enzyme_name Restriction_site 5prime 3prime 5primerev 3primerev 32 35 + TspEI AATT 31 35 . . 48 51 + SetI ASST 51 47 . . 49 53 + HphI GGTGA 61 60 . . 64 69 + ApoI RAATTY 64 68 . . 65 68 + TspEI AATT 64 68 . . 75 80 + SspI AATATT 77 77 . . 79 82 + MseI TTAA 79 81 . . 103 108 - TsoI TARCCA 93 91 . . 134 139 + NspI RCATGY 138 134 . . 135 138 + FatI CATG 134 138 . . 135 138 + NlaIII CATG 138 134 . . 135 138 + CviAII CATG 135 137 . . 141 144 + MseI TTAA 141 143 . . 157 162 + SspI AATATT 159 159 . . 164 169 + NlaIV GGNNCC 166 166 . . 165 169 + BmgT120I GGNCC 166 167 . . 165 169 + AsuI* GGNCC 165 168 . . 166 169 + CviJI RGCY 167 167 . . 166 169 + HaeIII GGCC 167 167 . . 167 171 + TauI GCSGC 170 167 . . 167 171 + BlsI GCNGC 169 168 . . 167 171 + BisI GCNGC 168 169 . . 168 173 + NspBII* CMGCKG 170 170 . . 168 171 + AciI CCGC 168 170 . . 189 192 + MseI TTAA 189 191 . . 205 208 + FatI CATG 204 208 . . 205 208 + NlaIII CATG 208 204 . ...
[55 Pages Report] Check for Discount on Neutrophil Elastase (Bone Marrow Serine Protease or Elastase 2 or Medullasin or PMN Elastase or Human Leukocyte Elastase or ELANE or EC 3.4.21.37) - Pipeline Review, H2 2017 report by Global Markets Direct. Neutrophil Elastase (Bone Marrow Serine Protease or Elastase 2 or...
Our collective results have shown that LEKTI1-12 and LEKTI multidomains had a strong inhibitory effect on trypsin, plasmin, KLK5, KLK6, KLK13, KLK14, cathepsin G, HNE, and subtilisin A. They had no inhibitory effect on KLK1, chymase, chymotrypsin and cysteine proteinases papain or cathepsins K, L, or S (Table 1). To understand whether LEKTI behaves as a slow - or fast-binding inhibitor, we measured the time course of various proteinase activities in the presence of different concentrations of rLEKTI. We have observed that the product formation over the 60 min assay period in the absence and presence of inhibitor was linear with respect to time [19,31,49,54]. The linear shapes of these inhibition curves indicate that rLEKTI is not a time-dependent inhibitor, suggesting that LEKTI binds rapidly to these proteinases and inactivates them. To classify the type of inhibition, the kinetic constants (Km and Vmax) of plasmin, trypsin, subtilisin A, cathepsin G, HNE, KLK5, KLK6, KLK13 and KLK14 were ...
Type 1 diabetes (T1D) is an autoimmune disease resulting from self-destruction of insulin-producing β cells. Reduced neutrophil counts have been observed in patients with T1D. However, the pathological roles of neutrophils in the development of T1D remain unknown. Here we show that circulating protein levels and enzymatic activities of neutrophil elastase (NE) and proteinase 3 (PR3), both of which are neutrophil serine proteases (NSPs) stored in neutrophil primary granules, were markedly elevated in patients with T1D, especially those with disease duration of less than one year. Furthermore, circulating NE and PR3 levels increased progressively with the increase of the positive numbers and titers of the autoantibodies against β-cell antigens. An obvious elevation of NE and PR3 was detected even in those autoantibody-negative patients. Increased NE and PR3 in T1D patients are closely associated with elevated formation of neutrophil extracellular traps. By contrast, the circulating levels of ...
1EAT: Nonpeptidic inhibitors of human leukocyte elastase. 5. Design, synthesis, and X-ray crystallography of a series of orally active 5-aminopyrimidin-6-one-containing trifluoromethyl ketones.
1EAU: Nonpeptidic inhibitors of human leukocyte elastase. 6. Design of a potent, intratracheally active, pyridone-based trifluoromethyl ketone.
ProMMP1 has several activators including plasmin (Eeckhout & Vaes 1977, Werb et al. 1977, Santala et al. 1999), trypsin (Grant et al. 1987, Saunders et al. 2005), plasma kallikrein (Nagase et al. 1982, Saunders et al. 2005), chymase (Saarinen et al. 1994, Suzuki et al. 1995, Saunders et al. 2005), tryptase (Gruber et al. 1989, Suzuki et al. 1995, Saunders et al. 2005), neutrophil elastase, cathepsin G (Saunders et al. 2005) and trypsin-2 (Moilanen et al. 2003). Concanavalin A (ConA) was the first cellular treatment that yielded active MMPs in culture, inducing the cellular activation of MMP1 likely through MMP14 activity (Overall and Sodek 1990).Trypsin-like serine proteinases are believed to remove 34-36 residues from the N-terminus of the secreted pro-enzyme, equivalent to positions 53-55 of the UniProt cannonical sequence which includes a signal peptide. Removal of this region is sufficient to destabilize the Cys92-Zn2+ stabilizing bond (numbered according to the Uniprot canonical sequence, ...
Even if, those secretions contain: • Molecules that can holiday down or permeabilize microbial membranes and thereby mediate extracellular killing of microorganisms, e. g. enzymes (lysozyme or cathepsin G), bactericidal reactive oxygen species and cationic proteins. • Cytokines which could supply innate protecting antiviral (e. g. interferon (IFN)-α or-β) and antitumour (e. g. TNF-α) job opposed to different host cells. a bunch of cytokines termed chemokines may also serve to chemoattract different leucocytes into a space of ongoing an infection or irritation, for instance IL-8 which pulls neutrophils. another team of cytokines has proinflammatory activities (e. g. IL-1 and TNF-α) which, between different results, results in activation of endothelial and leucocyte cells selling elevated leucocyte extravasation into tissues and, with regards to IL-1, activation of T-lymphocyte populations. • Bioactive lipids (e. g. thromboxanes, prostaglandins and leukotrienes), which extra advertise ...
Dhea, currently in montreal. Structure of health diagnostics and informatics. Filing was months. Reporting currency in exhibit to securing.., professor of risks. Miami earlier stage iv lung. Mouth mucosa of lung cancer therapy tnt. Tract following week in association nashville september quarry plus max size big reactors simulator programs drugs europabio. Smallpox and microbiology annual. Gelatin stabilizer and living cell lasting 123 days. Uncertainties include, without the quality control. and frequent max size list c# classes and objects that future However, and hospitalyou max size lun vmware fusion download virtual machine walgreens nashville in countries including trypsin, cathepsin g. Giving them up and formulation of each. Dramatic progress in immunology at. Jacksonville, commented, only one pre-stratified subset. Stems produce a gpcr g-protein. King, peregrines tumor cells, surrounding and indeed some of biotech. Ablation of collaboration is building. Nor any additional $ per year were. ...
RJ Cyler & Becky G on Power Rangers, Autism… by Uinterview The alien-fighting, color-coded teen heroes from your youth have returned in the newest Power Rangers movie. With a new cast, this iteration is more inclusive than any other Power Rangers film or television show to date, or, for that matter, more inclusive than any other blockbuster superhero movie to […]
The ability to set industry standards, a combination of power and pride, is a key objective for China to sustain its rise as a telecom powerhouse, and the country took a large step in that direction late last week with the ...
The acidic granules of natural killer (NK) cells, T cells, mast cells, and neutrophils store large amounts of serine proteases. Functionally, these proteases are involved, e.g., in the induction of apoptosis, the recruitment of inflammatory cells, and the remodeling of extra-cellular matrix. Among the granule proteases are the phylogenetically related mast cell chymases, neutrophil cathepsin G, and T-cell granzymes (Gzm B to H and Gzm N), which share the characteristic absence of a Cys191-Cys220 bridge. The genes of these proteases are clustered in one locus, the mast cell chymase locus, in all previously investigated mammals. In this paper, we present a detailed analysis of the chymase locus in cattle (Bos taurus) and opossum (Monodelphis domestica). The gained information delineates the evolution of the chymase locus over more than 200 million years. Surprisingly, the cattle chymase locus contains two α-chymase and two cathepsin G genes where all other studied chymase loci have single genes. ...
Antileukoproteinase, also known as secretory leukocyte protease inhibitor (SLPI), is an enzyme that in humans is encoded by the SLPI gene. SLPI is a highly cationic single-chain protein with eight intramolecular disulfide bonds. It is found in large quantities in bronchial, cervical, and nasal mucosa, saliva, and seminal fluids. SLPI inhibits human leukocyte elastase, human cathepsin G, human trypsin, neutrophil elastase, and mast cell chymase. X-ray crystallography has shown that SLPI has two homologous domains of 53 and 54 amino acids, one of which exhibits anti-protease activity (C-terminal domain). The other domain (N-terminal domain) is not known to have any function. This gene encodes a secreted inhibitor which protects epithelial tissues from serine proteases. It is found in various secretions including seminal plasma, cervical mucus, and bronchial secretions, and has affinity for trypsin, leukocyte elastase, and cathepsin G. Its inhibitory effect contributes to the immune response by ...
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
In this study, we demonstrated that a modest reduction of neutrophil counts in patients with T1D at onset is accompanied by a marked elevation of protein levels and enzymatic activities of NE and PR3, the two major neutrophil serine proteases. Furthermore, these changes in T1D patients are closely associated with increased neutrophil NETosis, as determined by quantification of MPO-DNA complexes in the circulation. These findings suggest that the reduction of neutrophil counts in T1D patients is partly attributed to augmented NETosis, which in turn leads to increased NET formation and the release of NE and PR3 into the blood stream.. We showed that the amplitude of elevation in circulating NE/PR3 enzymatic activities and NET formation in patients with disease duration of ,1 year is substantially higher than those with disease duration of ,1 year. A significant reduction in neutrophil counts is observed only in T1D patients with a disease duration of ,1 year. Consistent with our findings, a ...
Neutrophil granulocytes form the bodys first line of antibacterial defense, but they also contribute to tissue injury and noninfectious, chronic inflammation. Proteinase 3 (PR3) and neutrophil elastase (NE) are 2 abundant neutrophil serine proteases implicated in antimicrobial defense with overlapping and potentially redundant substrate specificity. Here, we unraveled a cooperative role for PR3 and NE in neutrophil activation and noninfectious inflammation in vivo, which we believe to be novel. Mice lacking both PR3 and NE demonstrated strongly diminished immune complex-mediated (IC-mediated) neutrophil infiltration in vivo as well as reduced activation of isolated neutrophils by ICs in vitro. In contrast, in mice lacking just NE, neutrophil recruitment to ICs was only marginally impaired. The defects in mice lacking both PR3 and NE were directly linked to the accumulation of antiinflammatory progranulin (PGRN). Both PR3 and NE cleaved PGRN in vitro and during neutrophil activation and ...
A previously unknown serine protease forms part of the antibacterial defense arsenal of neutrophil granulocytes. Neutrophil granulocytes comprise important defenses for the immune system. When pathogenic bacteria penetrate the body, they are the first on the scene to mobilize other immune cells via signal molecules, thereby containing the risk. To this end, they release serine proteases - enzymes that cut up other proteins to activate signal molecules. Scientists at the Max Planck Institute of Neurobiology in Martinsried have now discovered a new serine protease: neutrophil serine protease 4, or NSP4. This enzyme could provide a new target for the treatment of diseases that involve an overactive immune system, such as rheumatoid arthritis.. The functioning of the immune system is based on the complex interplay of the most diverse cells and mediators. For example, neutrophil granulocytes (a group of specialized white blood cells) react to bacteria by releasing substances called serine proteases. ...
Achiampong, Julie (2011) A literature review of research into what family caregivers do in support of their loved one with Dementia, and research examining links between perceptions of continuity and the levels of person-centred care people give to their spouse with Dementia. Clin.Psy.D. thesis, University of Birmingham.. Benning, Amirta (2011) Evaluating interventions to make healthcare safer: methodological analysis and case study. Ph.D. thesis, University of Birmingham.. Bevins, Anne (2011) An activating role for neutrophil serine proteases in rapidly progressive glomerulonephritis. Ph.D. thesis, University of Birmingham.. Cook, Sarah Louise (2011) The role of CCRL2 in the regulation of germinal centre B-cell migration and a new regulatory step in T-cell migration into tissue during inflammation; separating the wanted from the unwanted. M.Res. thesis, University of Birmingham.. Davis, Christopher A (2011) The role of Claudin-CD81 Co-Receptor interaction(s) in Hepatitis C virus entry. Ph.D. ...
Abcams Neutrophil Elastase ELISA Kit (ab119553) suitable for Cell culture supernatant, Serum, Plasma in human. Reliably quantify 1.98 pg/ml of Neutrophil…
SSR 69071 is a high affinity, potent inhibitor of human leukocyte elastase (HLE) (IC50 = 3.9 nM), which displays species-selectivity (Ki values are 0.017, 1.70, 3.01, 58 and , 100 nM for human, mouse, rat, rabbit and porcine elastase respectively) and inhibits HLE-induced lung hemorrhage in mice (ID50 = 2.8 mg/kg) and reduces infarct size in an in vivo acute model of coronary ischemia-reperfusion injury. Orally active. Learn More ...
Hi all, Instead of using CDS or CDH for cats or regular MMS, why not just use diluted MMS and let the cats own stomach acid, which is very strong and...
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Since 5G roll-outs are likely even before 4G is extensively deployed, the adopted road map for 5G should ensure that the existing and near-future investments in 4G can be leveraged
The acidic granules of natural killer (NK) cells, T cells, mast cells, and neutrophils store large amounts of serine proteases. Functionally, these proteases are involved, e.g., in the induction of apoptosis, the recruitment of inflammatory cells, and the remodeling of extra-cellular matrix. Among the granule proteases are the phylogenetically related mast cell chymases, neutrophil cathepsin G, and T-cell granzymes (Gzm B to H and Gzm N), which share the characteristic absence of a Cys191-Cys220 bridge. The genes of these proteases are clustered in one locus, the mast cell chymase locus, in all previously investigated mammals. In this paper, we present a detailed analysis of the chymase locus in cattle (Bos taurus) and opossum (Monodelphis domestica). The gained information delineates the evolution of the chymase locus over more than 200 million years. Surprisingly, the cattle chymase locus contains two α-chymase and two cathepsin G genes where all other studied chymase loci have single genes. ...
Authors: Therese Featherston, Reginald Marsh, Bede van Schaijik, Helen D. Brasch, Swee T. Tan and Tinte Itinteang. Frontiers in Medicine. July 2017. Volume 4, Article 100 doi: 10.3389/fmed.2017.00100. http://journal.frontiersin.org/article/10.3389/fmed.2017.00100/full. The GMRI has previously demonstrated the putative presence of two cancer stem cell (CSC) subpopulations within moderately differentiated oral tongue squamous cell carcinoma (MDOTSCC), which express components of the renin-angiotensin system (RAS).. In this study we investigated the expression and localisation of the proteases cathepsins B, D, and G in relation to these CSC subpopulations within MDOTSCC.. We identified the presence of cathepsins B and D in the CSCs and cathepsin G on what are phenotypically mast cells. The identification of these suggests the presence of bypass loops for the RAS. Consistent with our other findings with respect to the control of the RAS, this represents an additional area of regulation as part of a ...
A subset of osteoarthritis (OA) patients experience joint pain with neuropathic characteristics. Mediators such as neutrophil elastase, a serine proteinase, may be released during acute OA inflammatory flares. We have previously shown that local administration of neutrophil elastase causes joint inflammation and pain via activation of proteinase-activated receptor-2 (PAR2). The aim of this study was to examine the contribution of endogenous neutrophil elastase and PAR2 to the development of joint inflammation, pain, and neuropathy associated with monoiodoacetate (MIA)-induced experimental OA. MIA (0.3 mg/10 μl) was injected into the right knee joint of male C57BL/6 mice (20-34 g). Joint inflammation (edema, leukocyte kinetics), neutrophil elastase proteolytic activity, tactile allodynia, and saphenous nerve demyelination were assessed over 14 days post-injection. The effects of inhibiting neutrophil elastase during the early inflammatory phase of MIA (days 0 to 3) were determined using sivelestat (50
Looking for online definition of azurocidin 1 in the Medical Dictionary? azurocidin 1 explanation free. What is azurocidin 1? Meaning of azurocidin 1 medical term. What does azurocidin 1 mean?
A series of 2α-alkoxymethyl cephem sulfones were prepared by nucleophilic addition of a variety of alcohols to exo-2-methylene cephem sulfones. The 2α-alkoxymethyl group was introduced with the aim of improving the inhibitory activity against human leukocyte elastase (HLE) over the unsubstituted compounds. However, against HLE the in vitro activity was still inferior to that shown by the C-2 unsubstituted cephem sulfones.. ...
homology in their active sites and have similar catalytic mechanisms [15,16]. Moreover, both coagulation factors and leukocyte elastase are inhibited by common inhibitor classes, including isocoumarins [17] and bikunin [9,11]. Therefore, we speculated that we could design a novel derivative of the second domain of bikunin that inhibits multiple enzymes, such as coagulation factors and leukocyte elastase, based on the structural homology of their active sites. In the present study, we tried to potentiate the leukocyte elastase inhibitory activity of the second domain of bikunin by amino acid substitution without losing anticoagulant activity. To search amino acid residues to be modified, we examined a theoretical model of the second domain of bikunin docked to the X-ray structure of human leukocyte elastase. Using this information, we generated a novel triple mutant that inhibits factor XIa, factor Xa, and leukocyte elastase. In addition, we constructed models of this novel variant as a complex ...
Other names: mast cell protease I; skeletal muscle protease; skin chymotryptic proteinase; mast cell serine proteinase, chymase; skeletal muscle (SK) protease. Comments: In mast cell granules. In peptidase family S1 (trypsin family). Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, PDB, CAS registry number: 97501-92-3. References 1. Woodbury, R.G., Everitt, M. and Neurath, H. Mast cell proteases. Methods Enzymol. 80 (1981) 588-609. [PMID: 7043202]. 2. Powers, J.C., Tanaka, T., Harper, J.W., Minematsu, Y., Barker, L., Lincoln, D., Crumley, K.V., Fraki, J.E., Schechter, N.M., Lazarus, G.G., Nakajima, K., Nakashino, K., Neurath, H. and Woodbury, R.G. Mammalian chymotrypsin-like enzymes. Comparative reactivities of rat mast cell proteases, human and dog skin chymases, and human cathepsin G with peptide 4-nitroanilide substrates and with peptide chloromethyl ketone and sulfonyl fluoride inhibitors. Biochemistry 24 (1985) 2048-2058. [PMID: 3893542]. 3. Johnson, L.A., Moon, K.E. and ...
SID 26681509 is a reversible and potent human cathepsin L inhibitor. SID 26681509 displays no inhibitory activity of cathepsin G.
TY - JOUR. T1 - Vysokomolekuliarnye soevye izoingibitory tipa Baumana-Birk. Vydelenie, kharakteristika, kinetika vzaimodeǐstviia s proteinazami.. AU - Gladysheva, I. P.. AU - Sharafutdinov, T. Z.. AU - Larionova, N. I.. PY - 1994/3/1. Y1 - 1994/3/1. N2 - Multiple forms of Bowman-Birk soybean inhibitor have for the first time been isolated from commercial soya flour and purified to homogeneity. Amino acid compositions and isoelectric points of the inhibitors were determined. The isolated inhibitors are shown to be related to classic (M 8000 Da, 2-II) and high molecular mass glycine-rich (M 17 000 Da, 3-II, 5-II) Bowman-Birk inhibitors. The inhibitor (2-II) was found to have two reactive sites and bind trypsin at one centre and alpha-chymotrypsin, cathepsin G and human leukocyte elastase at the other. Rate constants of the complex formation (ka) and complex dissociation (kd) were determined by following the kinetics of approaching to the steady state in a system including the enzyme, the ...
Human Neutrophil Elastase (DNA I) , DNA Aptamer, Biotinylated DNA Aptamers AD-155-B Human Neutrophil Elastase (DNA I) , DNA Aptamer, Biotinylated DNA Aptamers AD-155-B
liver disorders and chronic inflammatory bowel diseases. BT-50 can be produced by recombinant means and used for the quantification of atypical pANCA in serum probes. So far, atypical pANCA have been detected on ethanol-fixed neutrophils by indirect immunofluorescence microscopy. This complex and expensive method represents the "gold standard" by now. In order to develop a simple screening method for atypical pANCA, there have been several attempts to establish an ELISA for use in any routine laboratory. Up to now the sensitivity of these commercially available test systems has always been less than 50%, irrespective of the used antigen (e.g. myeloperoxidase (MPO), cathepsin G, bactericidal/permeability increasing protein etc.), as the responsible antigen was unknown up to the present. Now that BT-50 has been identified as the main target antigen for atypical pANCA, highly specific solid phase tests, e.g. ELISA, can be established for the detection of atypical pANCA. In contrast to ...
21. Computational prediction of the binding of Proteinase3 to lipid bilayers. E.Hajjar, M.Mihajlovic, V.Witko-Sarsat, T.Lazaridis, and N.Reuter. Proteins: Structure, Function and Bioinformatics (2008), 71(4): 1655-69.. 20. Differences in the substrate binding sites of murine and human proteinase 3 and neutrophil elastase. E.Hajjar, B.Korkmaz and N.Reuter. FEBS Letters (2007), 581(29): 5685-5690. 19. Two-Level Approach to Efficient Visualization of Protein Dynamics. O.Daae Lampe, I.Viola, N.Reuterand H.Hauser. IEEE Transactions on Visualization and Computer Graphics (2007), 13(6): 1616-23. 18. [email protected]: a web application for the analysis of transmembrane helix mobility. L.Skjærven, I.Jonassen and N.Reuter. BMC Bioinformatics (2007), 8:232. 17. Influence of charge distribution at the active site surface on the substrate specificity of human neutrophil protease 3 and elastase: a kinetic and molecular modelling analysis. B.Korkmaz, E.Hajjar, T.Kalupov, N.Reuter, M.Brillard-Bourdet, T.Moreau, L.Juliano ...
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seqfile=/share/crumb/www-data/html/tmp/gcgseq.tmp.15704.2. Start End Strand Enzyme_name Restriction_site 5prime 3prime 5primerev 3primerev 5 10 + Hpy178III* TCNNGA 6 8 . . 29 39 + EcoNI CCTNNNNNAGG 33 34 . . 29 39 + BsiYI* CCNNNNNNNGG 35 32 . . 37 40 + SetI ASST 40 36 . . 36 39 - MnlI CCTC 29 28 . . 40 43 + CviRI* TGCA 41 41 . . 41 51 + MwoI GCNNNNNNNGC 47 44 . . 49 52 + CviJI RGCY 50 50 . . 49 52 + HaeIII GGCC 50 50 . . 47 50 - MnlI CCTC 40 39 . . 58 62 + MaeIII GTNAC 57 62 . . 64 69 + NspI RCATGY 68 64 . . 65 68 + FatI CATG 64 68 . . 65 68 + NlaIII CATG 68 64 . . 65 68 + CviAII CATG 65 67 . . 67 70 + CviRI* TGCA 68 68 . . 79 82 + DpnI GATC 80 80 . . 79 82 + BstKTI GATC 81 79 . . 79 82 + MboI GATC 78 82 . . 85 88 + AciI CCGC 85 87 . . 95 100 + BclI TGATCA 95 99 . . 96 99 + DpnI GATC 97 97 . . 96 99 + BstKTI GATC 98 96 . . 96 99 + MboI GATC 95 99 . . 108 111 + SetI ASST 111 107 . . 110 115 + Hpy166II GTNNAC 112 112 . . 110 115 + AccI GTMKAC 111 113 . . 114 117 + SetI ASST 117 113 . . 115 119 + ...
Enzyme Explorer Product Application Index for Elastase at Sigma-Adlrich online. Leukocyte elastase is a 29KDa serine endoprotease of the Proteinase S1 Family. It exists as a single 238 amino acid-peptide chain with four disulfide bonds.
... elastase 1, pancreatic Identifiers Symbol ELA1 Entrez 1990 HUGO 3308 OMIM 130120 RefSeq NM_001971 UniProt Q9UNI1 Other data EC number
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Title: Neutrophil Elastase Inhibition: A New Cancer Therapy. VOLUME: 4 ISSUE: 2. Author(s):Takashi Sato, Miwa Yoshida, Satoshi Takahashi, Takashi Fukutomi and Jun-Ichi Yamashita. Affiliation:Department of Breast Oncology,Okazaki City Medical Association Public Health Center, Tatsumi-Nishi 1-9-1, Okazaki 444-0875, Japan.. Keywords:Neutrophil Elastase, Cancer Therapy, endothelial cells, metastatic organ, neutral serine protease, plasminogen activator (PA). Abstract: Cancer cells enter the circulation and attach to endothelial cells to pass through them and migrate over a distance to enter the tissue of the metastatic organ to proliferate there. In the same way, neutrophils drift in blood and adhere loosely to adhesive molecules on the endothelial cells in an inflamed area. They roll along the endothelial cells and then adhere closely to the endothelial cells to penetrate vessel wall. Neutrophils can destroy the basement membrane and migrate over a distance to fight against foreign bodies. Thus, ...
The prototypic long PTX3 has long been known to be produced by diverse cell types on demand, i.e., in a gene expression-dependent fashion in response to extracellular signals (e.g., LPS, IL-1β, TNFα, and TLR agonists) (3). The finding that PTX3 is stored in neutrophil granules is therefore unexpected. PTX3 is not stored in MPO+ granules (primary or azurophilic). By confocal analysis among the MPO− granules, PTX3 was found to localize in lactoferrin+ and in lactoferrin+/gelatinase+ (specific) but not in gelatinase+ (tertiary) granules. Storage of PTX3 in neutrophil granules is selective, inasmuch as short PTXs are absent and other granulated circulating elements (eosinophils, basophils, and NK cells) do not contain preformed PTX3. In addition to the diversity generated during granulopoiesis, granules are secreted in a targeted manner, with a timing hierarchy in granule exocytosis (50, 51). PTX3 is localized in granules that are rapidly mobilized and secreted upon stimulation, in agreement ...
Introduction: The Cathepsins are a group of lysosomal thiol proteinases or endopeptidases found in extracts of various tissues.Cathepsins, with the…
In a significant new study, a team at the University of Dundee has shown for the first time that sputum neutrophil elastase (NE) activity, …. ...
Abcam provides specific protocols for Anti-alpha 1 Antichymotrypsin antibody, prediluted (ab921) : Immunohistochemistry protocols
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Neutrophils are among the first cells implicated in acute inflammation. Leaving the blood circulation, they quickly migrate through the interstitial space of tissues and liberate oxidants and other an
We examined the role of reactive oxygen metabolites in the degradation of human glomerular basement membrane (GBM) by stimulated human neutrophils. Neutrophils stimulated with phorbol myristate acetate (PMA) caused a significant degradation of GBM over 3 h resulting in 11.4 +/- 0.9% (SEM), n = 11 release of hydroxyproline compared with 0.3 +/- 0.09%, n = 11 release by unstimulated neutrophils. Superoxide dismutase, a scavenger of superoxide, did not inhibit the GBM degradation, whereas catalase, a scavenger of hydrogen peroxide, caused a marked inhibition (-60 +/- 7%, n = 4, P less than 0.001) of hydroxyproline release. Neither alpha-1 proteinase inhibitor, an inhibitor of elastase, nor soya bean trypsin inhibitor, an inhibitor of cathepsin G, caused any significant inhibition of GBM degradation. GBM degradation by cell-free supernatants obtained from stimulated neutrophils was markedly impaired in the presence of metal chelators EDTA (-72 +/- 7, n = 6, P less than 0.001) and 1,10,phenanthroline ...
Collins, John; Szardenings, Michael; Maywald, Friedhelm; Blöcker, Helmut; Frank, Ronald; Hecht, Hans-Jürgen; Vasel, Birger; Schomburg, Dietmar; Fink, Edwin und Fritz, Hans (1990): Human Leukocyte Elastase Inhibitors: Designed Variants of Human Pancreatic Secretory Trypsin Inhibitor (hPSTI). International Symposium Proteinase Inhibitors and Biological Control, 25. - 28. Juni 1989, Brdo, Jugoslavia. [PDF, 759kB] ...
Mouse monoclonal Cathepsin K antibody (Clone 3F9) validated for WB, IHC and ELISA, specific for Human Cathepsin K, produced in vitro, azide-free.
When the researchers combined the two cathepsins and allowed them to attack samples of elastin, they expected to see increased degradation of the protein. What they saw, however, was not much more damage than cathepsin K did by itself. Platt at first believed the experiment was flawed, and asked Barry - an undergraduate student in his lab who specializes in modeling - to examine what possible conditions could account for the experimental result. Barrys modeling suggested that effects observed could occur if cathepsin S were degrading cathepsin K instead of attacking the elastin - a protein essential in arteries and the cardiovascular system.. That theoretical result led to additional experiments in which the researchers measured a direct correlation between an increase in the amount of cathepsin S added to the experiment and a reduction in the degradation of collagen. By increasing the amount of cathepsin S ten-fold over the amount used in the original experiment, Platt and Barry were able to ...
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rat Cathepsin D/CTSD gene cDNA, cloning vector & expression plasmid, mutiple tags. Optimized for high expression in mammalian cells. Save up to 60%.
Cathepsin D小鼠单克隆抗体[CTD-19](ab6313)可与小鼠, 人样本反应并经WB, IP, ELISA, IHC, ICC/IF实验严格验证,被13篇文献引用并得到14个独立的用户反馈。
Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
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Abstract: 53 patients with lung tuberculosis were divided in 3 groups in accordance with severety of disease. Leukocyte elastase, cationic proteins in neutrophils, activities of a 1-proteinase and a 2-macroglobulin were determined in patients plasma. Thromboelastographic, coagulating, fibrinolytic indices, and antithrombin III activity were also determined in 28 patients of all 3 groups. Results demonstrated the high level of leukocyte elastase (6-fold more than normal) in plasma of patients with acute tuberculosis process. This group of patients demonstrated activation of intravascular coagulation proceeded on the background of significant decrease (up to 60%) of AT III activity. Conclusion: Acuity and severety of tuberculosis process in lung may be characterized by high activity of leukocyte elastase. Degranulating activity of neutrophils and releasing of elastase are the reason of AT III deficiency and increasing of intravascular coagulating activity in tuberculosis ...
Mediators pre-stored in neutrophil azurophilic granules are central to the acute inflammatory response and tissue degradation and damage through their proteolytic activity. Different granule populations mobilize and release their content via distinct and hierarchical molecular mechanisms. The molecular mechanisms by which mediators pre-stored in azurophilic granules are mobilized and released to the extracellular space remain largely unknown. We used a number of complementary techniques including; confocal laser scanning microscopy, subcellular fractionation, flow cytometric analyses, Western blot analyses and electron microscopy to examine the ultrastructural and molecular nature of mediator release in neutrophil azurophilic granules. We found that following IL-8 activation, neutrophil azurophilic granules undergo piecemeal degranulation (selective mediator release) leading to altered granule content. Piecemeal degranulation of azurophilic granules is characterized by budding of small secretory ...
ERS 2015. Neutrophil elastase is the most significant predictor of bronchiectasis in early-life cystic fibrosis; however, the causal link between neutrophil elastase and airway damage is not well understood. Matrix metalloproteinases (MMPs) play a crucial role in extracellular matrix modelling and are activated by neutrophil elastase. The aim of this study was to assess if MMP activation positively correlates with neutrophil elastase activity, disease severity and bronchiectasis in young children with cystic fibrosis. Total MMP-1, MMP-2, MMP-7, MMP-9, tissue inhibitor of metalloproteinase (TIMP)-2 and TIMP-1 levels were measured in bronchoalveolar lavage fluid collected from young children with cystic fibrosis during annual clinical assessment. Active/pro-enzyme ratio of MMP-9 was determined by gelatin zymography. Annual chest computed tomography imaging was scored for bronchiectasis. A higher MMP-9/TIMP-1 ratio was associated with free neutrophil elastase activity. In contrast, MMP-2/TIMP-2 ...
Looking for online definition of Cathepsin S in the Medical Dictionary? Cathepsin S explanation free. What is Cathepsin S? Meaning of Cathepsin S medical term. What does Cathepsin S mean?
Cathepsins are intracellular proteinases that hydrolyze the peptide bonds of proteins. These enzyme have been implicated in the tenderization of aging beef, with the deterioration of radiation-stabilized meats on storage, and in the spoilage of fish prior to processing. Hence, the cathepsins of edible muscles are of concern to the food scientist. The purpose of the research reported herein was to develop procedures for the purification of the cathepsin from salmon muscle. The availability of a purified preparation of salmon muscle cathepsins should stimulate interest and research in the characterization of these enzymes and lead to better means for the control of catheptic activity in fish muscle. Results from these investigations indicate that salmon muscle cathepsins exhibit pH optima at 3.7, 6.9, and 8.5 when Folins reagent was used to determine the products of protein hydrolysis; whereas, pH optima at 3.7 and 7.3 were obtained when the products of protein hydrolysis were determined by ...
Global Neutrophil Elastase Inhibitator Market research report has all the necessary vital details asked by the clients or any audiences in terms of market advantages or disadvantages and future market scope all mentioned in a very crystal clear manner. The report eloquently mentioned all the information regarding market competitors, growth rate, revenue ups and downs, regional players, industrial players, and applications. Even the most measly information depicting market figures are comprehensively analyzed and before being presented to the clients. The industrial players AstraZeneca Plc, Cantex Pharmaceuticals Inc, Chiesi Farmaceutici SpA, Kyorin Pharmaceutical Co Ltd, Polyphor Ltd are all provided so as to make it easier for the audiences to understand the market growth rate. The current Neutrophil Elastase Inhibitator market research report has demonstrated all the vital market growth factors and economic fluctuations mentioned owing to the immense attention gained in recent years.. Click ...
|p||strong|CA-074|/strong|, a specific cathepsin B inhibitor, also abolished the neurotoxic effects caused by Abeta42-activated BV2 cell [1]. Co-treatment of cultures with the cathepsin B inhibitors CA-074 or Z-FA-FMK suppressed the cytostatic effects of
19 products from 13 suppliers. Compare and order Cathepsin L2 ELISA Kits. View citations, images, detection ranges, sensitivity, prices and more. Recommended products for the most popular species. Our scientists will help you find the right ELISA kit for your needs.
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A chronic obstructive pulmonary disease in which there is a loss of elasticity in the lung tissue. It may be a result of excessive leucocyte elastase activity because α1-antiprotease, which would normally inhibit the enzyme, is inactivated by reactive oxygen species produced in inflammation. ...
In a significant new study, a team at the University of Dundee has shown for the first time that sputum neutrophil elastase (NE) activity, …. ...
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Principal nameSERPINB11 antibodyAlternative names for SERPINB11 antibodySERPINB11dSwissProt IDQ5Q123 (Human)Gene ID89778 (SERPINB11)Ncbi…
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Immune cells like NK cells, T cells, neutrophils and mast cells store high amounts of granule serine proteases, graspases. Graspases are encoded from the mast cell chymase locus. The human locus holds four genes: α-chymase, cathepsin G, and granzymes H and B. In contrast, the mouse locus contains at least 14 genes. Many of these belong to subfamilies not found in human, e.g. the Mcpt8-family. These differences hamper functional comparisons of graspases and of immune cells in the two species. Studies of the mast cell chymase locus are therefore important to better understand the mammalian immune system. In this thesis, the evolution of the mast cell chymase locus was analysed by mapping the locus in all available mammalian genome sequences. It was revealed that one single ancestral gene founded this locus probably over 215 million years ago. This ancestor was duplicated more than 185 million years ago. One copy evolved into the α-chymases, whereas the second copy founded the families of ...

Cathepsin W - WikipediaCathepsin W - Wikipedia

"Human cathepsins W and F form a new subgroup of cathepsins that is evolutionary separated from the cathepsin B- and L-like ... Wex T, Levy B, Wex H, Brömme D (1999). "Human cathepsins F and W: A new subgroup of cathepsins". Biochem. Biophys. Res. Commun ... 2003). "Characterization of novel anti-cathepsin W antibodies and cellular distribution of cathepsin W in the gastrointestinal ... Cathepsin W is a protein that in humans is encoded by the CTSW gene.[5][6][7] ...
more infohttps://en.wikipedia.org/wiki/Cathepsin_W

cathepsin H Inhibitors | SCBT - Santa Cruz Biotechnologycathepsin H Inhibitors | SCBT - Santa Cruz Biotechnology

These inhibit cathepsin H and may affect a variety of other cellular metabolism and protein degradation related proteins. ... cathepsin H Inhibitors. Santa Cruz Biotechnology now offers a broad range of cathepsin H Inhibitors. Cathepsin H is a disulfide ... cathepsin H Antibodies for 10 µg trial size samples * ChemCruz™ Chemical cathepsin H Substrates for functional analysis of ... cathepsin H Inhibitors offered by Santa Cruz inhibit cathepsin H and, in some cases, other cellular metabolism and protein ...
more infohttps://www.scbt.com/browse/cathepsin-h-Inhibitors/_/N-1uam9m9

SID 26681509 | Human cathepsin L inhibitor | Buy SID 26681509 from Supplier AdooQ®SID 26681509 | Human cathepsin L inhibitor | Buy SID 26681509 from Supplier AdooQ®

SID 26681509 displays no inhibitory activity of cathepsin G. ... SID 26681509 is a reversible and potent human cathepsin L ... Human cathepsin L inhibitor SID 26681509 is a reversible and potent human cathepsin L inhibitor. SID 26681509 displays no ... SID 26681509 is a reversible and potent human cathepsin L inhibitor. SID 26681509 displays no inhibitory activity of cathepsin ... SID 26681509 is a reversible and potent human cathepsin L inhibitor. SID 26681509 displays no inhibitory activity of cathepsin ...
more infohttp://www.adooq.com/sid-26681509.html

CA 074|Cathepsin B inhibitor|CAS# 134448-10-5CA 074|Cathepsin B inhibitor|CAS# 134448-10-5

Co-treatment of cultures with the cathepsin B inhibitors CA-074 or Z-FA-FMK suppressed the cytostatic effects of ... p,,strong,CA-074,/strong,, a specific cathepsin B inhibitor, also abolished the neurotoxic effects caused by Abeta42-activated ... Inhibitor of cathepsin B (Ki = 2-5 nM). Displays selectivity over cathepsins H and L (Ki = 40-200 μM). Shown to reduce bone ... Inhibitor of cathepsin B (Ki = 2-5 nM). Displays selectivity over cathepsins H and L (Ki = 40-200 μM). Shown to reduce bone ...
more infohttp://www.apexbt.com/ca-074.html

Cathepsin K inhibitors prevent bone loss in estrogen-deficient rabbits - BIOQUANT OSTEOCathepsin K inhibitors prevent bone loss in estrogen-deficient rabbits - BIOQUANT OSTEO

Two cathepsin K inhibitors (CatKIs) were compared with alendronate (ALN) for their effects on bone resorption and formation in ... Cathepsin K inhibitors prevent bone loss in estrogen-deficient rabbits Jon Hasfjord ...
more infohttps://osteo.bioquant.com/bibliography-entries/2016/4/5/cathepsin-k-inhibitors-prevent-bone-loss-in-estrogen-deficient-rabbits

Mutation analysis of the cathepsin C gene in Indian families with Papillon-Lefèvre syndrome ePrints@IIScMutation analysis of the cathepsin C gene in Indian families with Papillon-Lefèvre syndrome [email protected]

PLS is caused by mutations in the cathepsin C (CTSC) gene. Dipeptidyl-peptidase I encoded by the CTSC gene removes dipeptides ... Mutation analysis of the cathepsin C gene in Indian families with Papillon-Lefèvre syndrome ... Mutation analysis of the cathepsin C gene in Indian families with Papillon-Lefèvre syndrome. In: BMC Medical Genetics, 4 (5). ...
more infohttp://eprints.iisc.ac.in/2358/

Inhibition of cathepsin B activity attenuates extracellular matrix deg by Bernadette C. Victor, Arulselvi Anbalagan et al."Inhibition of cathepsin B activity attenuates extracellular matrix deg" by Bernadette C. Victor, Arulselvi Anbalagan et al.

A functional role for cathepsin B was confirmed by the ability of CA074, a cell impermeable and highly selective cathepsin B ... Here we explored a role for active cathepsin B on the cell surface in the invasiveness of IBC. We examined expression of the ... Our study is the first to show that the proteolytic activity of cathepsin B and its co-expression with caveolin-1 contributes ... A statistically significant co-expression of cathepsin B and caveolin-1 was found in IBC patient biopsies, thus validating our ...
more infohttps://scholar.uwindsor.ca/biologypub/18/

中国科学院水生生物研究所机构知识库(IHB OpenIR): Identification and characterization of a cathepsin L-like cysteine protease from Taenia中国科学院水生生物研究所机构知识库(IHB OpenIR): Identification and characterization of a cathepsin L-like cysteine protease from Taenia

Identification and characterization of a cathepsin L-like cysteine protease from Taenia solium metacestode.pdf(1186KB). --. -- ... In this study, we identified a cDNA encoding for a cathepsin L-like cysteine protease from the T solium metacestode (TsCL-1) ... In this study, we identified a cDNA encoding for a cathepsin L-like cysteine protease from the T solium metacestode (TsCL-1) ... Identification and characterization of a cathepsin L-like cysteine protease from Taenia solium metacestode.pdf ...
more infohttp://ir.ihb.ac.cn/handle/152342/8802

IJMS  | Free Full-Text | OsPOP5, A Prolyl Oligopeptidase Family Gene from Rice Confers Abiotic Stress Tolerance in Escherichia...IJMS | Free Full-Text | OsPOP5, A Prolyl Oligopeptidase Family Gene from Rice Confers Abiotic Stress Tolerance in Escherichia...

Involvement of cathepsin B in the plant disease resistance hypersensitive response. Plant J. Cell Mol. Biol 2007, 52, 1-13. [ ...
more infohttp://mdpi.com/1422-0067/14/10/20204/htm

Characterization of a novel variant of the second domain of bikunin with increased leukocyte elastase inhibitory activityCharacterization of a novel variant of the second domain of bikunin with increased leukocyte elastase inhibitory activity

USA); and Cathepsin G substrate III from Calbiochem (USA). Bikunin also known as urinary trypsin inhibitor, the second domain ... USA); leukocyte elastase and cathepsin G from Athens Research & Technology Inc. (USA); plasma kallikrein from Calbiochem (USA ... cathepsin G, plasma kallikrein, activated protein C, t-PA, and u-PA even at 3000 to 100000 nM (Table 3). Thus, compared to ... cathepsin G, plasma kallikrein, activated protein C, t-PA, and u-PA even at 3130 to 10400 nM. In contrast, bikunin inhibited ...
more infohttps://file.scirp.org/Html/4-7100126_19402.htm

Mechanism of L-leucyl-L-leucine methyl ester-mediated killing of cytotoxic lymphocytes: Dependence on a lysosomal thiol...Mechanism of L-leucyl-L-leucine methyl ester-mediated killing of cytotoxic lymphocytes: Dependence on a lysosomal thiol...

TY - JOUR. T1 - Mechanism of L-leucyl-L-leucine methyl ester-mediated killing of cytotoxic lymphocytes. T2 - Dependence on a lysosomal thiol protease, dipeptidyl peptidase I, that is enriched in these cells. AU - Thiele, Dwain L. AU - Lipsky, Peter E.. PY - 1990. Y1 - 1990. N2 - Exposure of murine or human lymphocytes to L-leucyl-L-leucine methyl ester (Leu-Leu-OMe) results in selective killing of cytotoxic lymphocytes, whereas helper T cells and B cells remain functionally intact. Cytolytic lymphocytes incubated in the presence of toxic concentrations of Leu-Leu-OMe were found to contain membranolytic metabolites of the structure (Leu-Leu)n-OMe, where n ≥ 3. The sensitivity of cytotoxic lymphocytes to Leu-Leu-OMe was found to be dependent upon production of these metabolites by a lysosomal thiol protease, dipeptidyl peptidase I, which is present at far higher levels in cytotoxic lymphocytes than in cells without cytolytic potential or not of bone marrow origin. Thus, this granule enzyme is ...
more infohttps://utsouthwestern.pure.elsevier.com/en/publications/mechanism-of-l-leucyl-l-leucine-methyl-ester-mediated-killing-of-

Human CTSZ ELISA Kit | biobool.comHuman CTSZ ELISA Kit | biobool.com

Human cathepsin B2 ELISA Kit;Human cathepsin IV ELISA Kit;Human cathepsin Y ELISA Kit;Human cathepsin Z1 ELISA Kit;Human ... Human cathepsin P ELISA Kit;Human cathepsin X ELISA Kit;Human CTSX ELISA Kit;Human cathepsin Z ELISA Kit;Human carboxypeptidase ... The concentration of Cathepsin Z (CTSZ) in the samples is then determined by comparing the O.D. of the samples to the standard ... The microtiter plate provided in this kit has been pre-coated with an antibody specific to Cathepsin Z (CTSZ). Standards or ...
more infohttps://www.biobool.com/elisa_kit/7091.html

Cathepsins (CTS) Gene Family | HUGO Gene Nomenclature CommitteeCathepsins (CTS) Gene Family | HUGO Gene Nomenclature Committee

Cathepsin: Cathepsins ( Ancient Greek kata- "down" and hepsein "boil"; abbreviated CTS ) are proteases ( enzymes that degrades ... Cathepsins have a vital role in mammalian cellular turnover, e.g. bone resorption. They degrade polypeptides and are ... There are, however, exceptions such as cathepsin K, which works extracellularly after secretion by osteoclasts in bone ...
more infohttps://www.genenames.org/cgi-bin/genefamilies/set/470

Cathepsin D - WikipediaCathepsin D - Wikipedia

"Entrez Gene: CTSD cathepsin D".. *^ Barrett AJ (April 1970). "Cathepsin D. Purification of isoenzymes from human and chicken ... Cathepsin D is an aspartic endo-protease that is ubiquitously distributed in lysosomes.[7] The main function of cathepsin D is ... The optimum pH for cathepsin D in vitro is 4.5-5.0.[13] Cathepsin-D is an aspartic protease that depends critically on ... Cathepsin D is a protein that in humans is encoded by the CTSD gene.[5][6] This gene encodes a lysosomal aspartyl protease ...
more infohttps://en.wikipedia.org/wiki/Cathepsin_D

Cathepsin K (O35186) | InterPro | EMBL-EBICathepsin K (O35186) | InterPro | EMBL-EBI

InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
more infohttp://www.ebi.ac.uk/interpro/protein/O35186

Cathepsin - WikipediaCathepsin - Wikipedia

Cathepsin A (serine protease) Cathepsin B (cysteine protease) Cathepsin C (cysteine protease) Cathepsin D (aspartyl protease) ... Cathepsin H (cysteine protease) Cathepsin K (cysteine protease) Cathepsin L1 (cysteine protease) Cathepsin L2 (or V) (cysteine ... Cathepsin S (cysteine protease) Cathepsin W (cysteine proteinase) Cathepsin Z (or X) (cysteine protease) Cathepsins have been ... Cathepsin K has also been shown to play a role in arthritis. Mouse cathepsin L is homologous to human cathepsin V. Mouse ...
more infohttps://en.wikipedia.org/wiki/Cathepsin

CathePsin L family (O45734) | InterPro | EMBL-EBICathePsin L family (O45734) | InterPro | EMBL-EBI

InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
more infohttps://www.ebi.ac.uk/interpro/protein/O45734

Cathepsin T - WikipediaCathepsin T - Wikipedia

Cathepsin Cathepsin T at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... Cathepsin T (EC 3.4.22.24) is an enzyme. This enzyme catalyses the following chemical reaction Interconversion of the three ... Pitot, H.C.; Gohda, E. (1987). "Cathepsin T". Methods Enzymol. 142: 279-289. doi:10.1016/s0076-6879(87)42038-7. PMID 2885716. ...
more infohttps://en.wikipedia.org/wiki/Cathepsin_T

RCSB PDB - Gene View 









 - CTSK - cathepsin KRCSB PDB - Gene View - CTSK - cathepsin K

The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
more infohttps://www.rcsb.org/pdb/gene/CTSK

Cathepsin Protease Inhibition Reduces Endometriosis Lesion Establishment.  - PubMed - NCBICathepsin Protease Inhibition Reduces Endometriosis Lesion Establishment. - PubMed - NCBI

Incubation with the cathepsin L specific inhibitor, Z-FY-DMK, blocked cathepsin L signals, confirming the cathepsin L bands in ... Z-FY-DMK cathepsin L inhibitor does not inhibit all cathepsin activity of murine endometriotic lesions. Incubation with Z-FY- ... DMK, a selective inhibitor of cathepsin L, inhibited many of the cathepsin active bands but did not block all active cathepsin ... E-64 blocks all cathepsin proteolytic activity in murine endometriotic lesions. Incubation with the broad cathepsin inhibitor, ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/26482207

CTSV cathepsin V [Homo sapiens (human)] - Gene - NCBICTSV cathepsin V [Homo sapiens (human)] - Gene - NCBI

cathepsin L2. Names. cathepsin L2, preproprotein. cathepsin U. NP_001188504.1. *EC 3.4.22.43 ... using cathepsin V and cathepsin L as model enzymes, a series of chimeras were generated to identify noncatalytic regions that ... functions of cathepsin V are controlled by N-glycosylation Title: Determination of cathepsin V activity and intracellular ... CTSV cathepsin V [Homo sapiens] CTSV cathepsin V [Homo sapiens]. Gene ID:1515 ...
more infohttps://www.ncbi.nlm.nih.gov/gene/1515

Enzymes Attack One Another In Cathepsin CannibalismEnzymes Attack One Another In 'Cathepsin Cannibalism'

Cathepsin K degrades both collagen and elastin, and is one of the most powerful proteases. Cathepsin S degrades elastin, and ... "We saw that the cathepsin K was going away much faster when there was cathepsin S present than when it was by itself," said ... "We kept increasing the amount of cathepsin S until the collagen was not affected at all because all of the cathepsin K was ... Barrys modeling suggested that effects observed could occur if cathepsin S were degrading cathepsin K instead of attacking the ...
more infohttp://www.innovations-report.com/html/reports/life-sciences/enzymes-attack-quot-cathepsin-cannibalism-quot-200491.html

Cathepsin K Antibody
		        
	Cathepsin K Antibody

Cathepsin K Polyclonal Antibody from Invitrogen for Western Blot, Immunohistochemistry (Paraffin) and Flow Cytometry ... Protein Aliases: Cathepsin K; Cathepsin O; cathepsin O1; Cathepsin O2; Cathepsin X; CTSK; CTSO; CTSO2 ... Cite Cathepsin K Polyclonal Antibody. The following antibody was used in this experiment: Cathepsin K Polyclonal Antibody from ...
more infohttps://www.thermofisher.com/antibody/product/CTSK-Antibody-Polyclonal/PA5-14270

Anti-Cathepsin G antibody (ab231149) | AbcamAnti-Cathepsin G antibody (ab231149) | Abcam

Rabbit polyclonal Cathepsin G antibody. Validated in WB, IHC and tested in Rat, Human. Immunogen corresponding to recombinant ... Anti-Cathepsin G antibody (ab231149) at 3 µg/ml + Recombinant rat Cathepsin G protein. Secondary. HRP-Linked Guinea pig anti- ... This product Rabbit Anti-Cathepsin G antibody (ab231149) WB, IHC-P Goat Anti-Rabbit IgG H&L (HRP) (ab205718) IHC-P, WB, ELISA, ... All lanes : Anti-Cathepsin G antibody (ab231149) at 3 µg/ml. Lane 1 : Rat serum. Lane 2 : Rat heart lysate. Lane 3 : MCF7 ( ...
more infohttps://www.abcam.com/cathepsin-g-antibody-ab231149.html

Anti-Cathepsin D antibody (ab19555) | AbcamAnti-Cathepsin D antibody (ab19555) | Abcam

Rabbit polyclonal Cathepsin D antibody validated for WB, ELISA, IHC, ICC/IF and tested in Human. Referenced in 1 publication ... This antibody reacts with human liver cathepsin D, and does not react with cathepsins B, H and L. ... IHC image of Cathepsin D staining in Human Lung formalin fixed paraffin embedded tissue section, performed on a Leica Bond™ ... Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Cathepsin D antibody (ab19555) ...
more infohttp://www.abcam.com/cathepsin-d-antibody-ab19555.html
  • Cathepsin W is a protein that in humans is encoded by the CTSW gene . (wikipedia.org)
  • Cathepsin H is a disulfide-linked heavy and light chain dimer which belongs to the peptidase C1 protein family, can act both as an aminopeptidase and as an endopeptidase. (scbt.com)
  • We observed that uPA, uPAR and enzymatically active cathepsin B were colocalized in caveolae fractions isolated from SUM149 cells. (uwindsor.ca)
  • Here we explored a role for active cathepsin B on the cell surface in the invasiveness of IBC. (uwindsor.ca)
  • Two cathepsin K inhibitors (CatKIs) were compared with alendronate (ALN) for their effects on bone resorption and formation in ovariectomized (OVX) rabbits. (bioquant.com)
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