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.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).Cysteine Endopeptidases: ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.Cathepsin 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.Oligodeoxyribonucleotides, Antisense: Short fragments of DNA that are used to alter the function of target RNAs or DNAs to which they hybridize.Cathepsin G: A serine protease found in the azurophil granules of NEUTROPHILS. It has an enzyme specificity similar to that of chymotrypsin C.Cathepsin H: An ubiquitously-expressed lysosomal cysteine protease that is involved in protein processing. The enzyme has both endopeptidase and aminopeptidase activities.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.

Programming for cytotoxic effector function occurs concomitantly with CD4 extinction during CD8(+) T cell differentiation in the thymus. (1/8)

CD4(+) T cells are generally specialized to function as helper cells and CD8(+) T cells are generally specialized to function as cytotoxic effector cells. To explain how such concordance is achieved between co-receptor expression and immune function, we considered two possibilities. In one case, immature CD4(+)CD8(+) thymocyte precursors might first down-regulate expression of one co-receptor molecule, with the remaining co-receptor molecule subsequently activating the appropriate helper or cytotoxic functional program. Alternatively, we considered that the same intrathymic signals that selectively extinguished expression of one or the other co-receptor molecule might simultaneously initiate the appropriate helper or cytotoxic functional program. In the present study, we attempted to distinguish between these alternatives by examining thymocyte precursors of CD8(+) T cells for expression of Cathepsin C and Cathepsin W, molecules important for cytotoxic effector function. We report in developing thymocytes that Cathepsin C and Cathepsin W are expressed coordinately with extinction of CD4 co-receptor expression. We conclude that CD4 extinction and initiation of the cytotoxic functional program occurs simultaneously during differentiation of CD8(+) T cells in the thymus.  (+info)

Human cathepsin W, a cysteine protease predominantly expressed in NK cells, is mainly localized in the endoplasmic reticulum. (2/8)

Human cathepsin W (also called lymphopain) is a recently described papain-like cysteine protease of unknown function whose gene expression was found to be restricted to cytotoxic cells. Here we demonstrate that cathepsin W is expressed predominantly in NK cells and, to a lesser extent, in CTLs. Quantitative RT-PCR revealed that NK cells contained approximately 21 times more cathepsin W transcript than CTLs. The predominant expression of cathepsin W in NK cells was further confirmed by Western blot analysis and immunohistochemistry. IL-2-mediated stimulation of NK cells and CTLs revealed a stronger up-regulation of the cathepsin W gene and protein expression in NK cells (7-fold) than in CTLs (2-fold). Transfection experiments of HeLa cells and biochemical analyses revealed that cathepsin W is exclusively "high mannose-type" glycosylated and is mainly targeted to the endoplasmic reticulum (ER). Interestingly, the ER localization of cathepsin W was also found in NK cells, in which colocalization studies revealed an overlapping staining of cathepsin W and Con A, an ER-specific lectin. Furthermore, subcellular fractionation of cathepsin W-expressing cells confirmed the ER localization and showed that cathepsin W is membrane associated. Based on the results of this study, cathepsin W might represent a putative component of the ER-resident proteolytic machinery. The constitutive expression in NK cells and the stronger up-regulation of cathepsin W by IL-2 in NK cells than CTLs suggest that cathepsin W is not just a marker of cytotoxic cells but is, rather, specifically expressed in NK cells.  (+info)

Functional involvement of cathepsin W in the cytotoxic activity of NK-92 cells. (3/8)

Human cathepsin W (lymphopain) is a papain-like cysteine protease of unknown function that is specifically expressed in natural killer (NK) cells and to a lesser extent in cytotoxic T cells (CTL). In order to analyze the functional importance of cathepsin W for the cytotoxic process, we investigated NK-92 cells that have an NK cell-like phenotype and express cathepsin W. NK-92 cells possess strong cytotoxic activity against Jurkat and K562 cells. The cytotoxic activity of NK-92 cells against K562 was decreased in the presence of antisense phosphorothioate oligonucleotides against the cathepsin W-cDNA. Western blot analysis showed that the impaired cytotoxic activity of NK-92 cells was accompanied by reduced amounts of cathepsin W in the antisense-treated cells. In addition, co-cultivation experiments between NK-92 and K562 cells revealed a time-dependent decrease of cathepsin W by Western blot and immunofluorescence analysis during the cytotoxic attack, whereas CD56 expression of NK-92 cells was not affected. During cytotoxic attack, cathepsin W was neither targeted to K562 cells or other subcellular compartments, as shown by immunofluorescence analysis. The decrease of cathepsin W protein was associated with stable cathepsin W transcript levels. Control experiments using HT-29 cells, which are resistant against NK-92-mediated cytotoxicity, showed no change of cathepsin W expression, implying that the decrease of cathepsin W in the NK-92/K562 assay is linked to the cytotoxic process. Although the exact function of cathepsin W with respect to its enzymatic activity and its site of action still needs to be elucidated, our data demonstrate for the first time that cathepsin W is important for cellular cytotoxicity mediated by NK cells.  (+info)

Characterization of murine cathepsin W and its role in cell-mediated cytotoxicity. (4/8)

Cathepsin W is a member of the papain-like family of cysteine proteases. In this report, we have isolated the cDNA for murine CtsW (mCtsW) from a splenocyte library. The deduced 371-amino-acid sequence shares 68% identity with human CtsW and includes the conserved catalytic triad cysteine, histidine, and asparagine found in all members of this family. In addition to the fulllength form of mCtsW, we have isolated an alternatively spliced form of the mRNA that lacks a complete catalytic triad. An S1 nuclease protection assay and a Western blot analysis showed that mCtsW is mainly restricted to the CD8(+) T cell and natural killer cell compartments. In addition, we confirmed that, like its human homologue, mCtsW is localized mainly to the endoplasmic reticulum and its expression is up-regulated upon activation. We also characterized the mCtsW locus using bacterial artificial chromosome clones. The gene consists of 10 coding exons and 9 introns spanning 3.2 kb. To elucidate the physiologic role of this protease, we generated mice deficient in mCtsW. Our data establish that mCtsW is not required for cytotoxic lymphocyte-induced target cell death in vitro. In addition, mCtsW deficiency does not alter the susceptibility of cytotoxic lymphocytes to suicide or fratricide after degranulation. Thus, mCtsW does not have a unique role in target cell apoptosis or cytotoxic cell survival in vitro.  (+info)

Upregulation of cathepsin W-expressing T cells is specific for autoimmune atrophic gastritis compared to other types of chronic gastritis. (5/8)

AIM: To investigate a pathophysiological role of cathepsin W (CatW), a putative thiol-dependent cysteine protease, which is specifically expressed in cytotoxic lymphocytes, in different types of chronic inflammation of the gastric mucosa. METHODS: Gastric and duodenal biopsies of patients with Helicobacter pylori (H pylori)-associated active gastritis (Hp, n = 19), chemically induced reactive gastritis (CG, n = 17), autoimmune atrophic gastritis (AIG, n = 20), lymphocytic corpus gastritis (LG, n = 29), celiac disease (CD, n = 10), and corresponding controls (n = 24) were analyzed by immunohistochemistry for the expression of CatW and CD45. Furthermore, immunohistochemical double staining with anti-CD3 and anti-cathepsin was performed for the samples of AIG. RESULTS: Median values of CatW-expressing cells among CD45-positive immune cells were between 2% and 6% for normal gastric mucosa, CG, and LG, whereas the corresponding value was significantly increased for AIG (24.7%, P<0.001) and significantly decreased for HP (0.7%, P<0.05). Double staining with anti-CD3 and anti-CatW antibodies revealed that >90% of CatW-expressing cells in gastric mucosa of AIG were T cells. Duodenal mucosa had significantly more CatW/CD45-positive cells than normal gastric mucosa (median: 17.8% vs 2%, P<0.01). The corresponding proportion of CatW/CD45-postive cells was decreased in CD compared to duodenal mucosa (median: 2.1% vs 17.8%, P<0.05). CONCLUSION: The opposite findings regarding the presence of CatW-positive cells in AIG (increase) and CD (decrease) reflects the different cellular composition of immune cells involved in the pathogenesis of these diseases.  (+info)

The peri-islet basement membrane, a barrier to infiltrating leukocytes in type 1 diabetes in mouse and human. (6/8)

 (+info)

Human cathepsin W, a putative cysteine protease predominantly expressed in CD8+ T-lymphocytes. (7/8)

A 750-bp fragment of a novel human cysteine protease has been identified from the dbEST databank. PCR cloning and DNA sequencing yielded a 1.38-kb full-length cDNA which encodes a polypeptide of 376 amino acids. The protein consists of a putative 21-residue signal peptide, a 106-residue propeptide and a 252-residue mature protein. The deduced amino acid sequence contains the highly conserved residues of the catalytic triad of papain-like cysteine proteases: cysteine, histidine, and asparagine. Furthermore, the protein sequence possesses two potential N-glycosylation sites: one in the propeptide and one in the mature protein. Comparison of the amino acid sequence of human cathepsin W with other human thiol-dependent cathepsins revealed a relatively low degree of similarity (21-31%). In contrast to cathepsins L, S, K, B, H and O, cathepsin W contains a 21-amino acid peptide insertion between the putative active site histidine and asparagine residues and an 8-amino acid C-terminal extension. This unique sequence may indicate that cathepsin W belongs in a novel subgroup of papain-like proteases distinct from that of cathepsin L- and B-like proteases. Northern blot analysis indicates a specific expression of cathepsin W in lymphatic tissues. Further analysis revealed predominant levels of expression in T-lymphocytes, and more specifically in CD8+ cells. The expression of the protease in cytotoxic T-lymphocytes may suggest a specific function in the mechanism or regulation of T-cell cytolytic activity.  (+info)

Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization. (8/8)

A cDNA for a novel human papain-like cysteine protease, designated cathepsin F, has been cloned from a lambdagt10-skeletal muscle cDNA library. The nucleotide sequence encoded a polypeptide of 302 amino acids composed of an 88-residue propeptide and a 214-residue mature protein. Protein sequence comparisons revealed 58% homology with cathepsin W; about 42-43% with cathepsins L, K, S, H, and O; and 38% with cathepsin B. Sequence comparisons of the propeptides indicated that cathepsin F and cathepsin W may form a new cathepsin subgroup. Northern blot analysis showed high expression levels in heart, skeletal muscle, brain, testis, and ovary; moderate levels in prostate, placenta, liver, and colon; and no detectable expression in peripheral leukocytes and thymus. The precursor polypeptide of human recombinant cathepsin F, produced in Pichia pastoris, was processed to its active mature form autocatalytically or by incubation with pepsin. Mature cathepsin F was highly active with comparable specific activities toward synthetic substrates as reported for cathepsin L. The protease had a broad pH optimum between 5.2 and 6.8. Similar to cathepsin L, its pH stability at cytosolic pH (7.2) was short, with a half-life of approximately 2 min. This may suggest a function in an acidic cellular compartment. Transient expression of T7-tagged cathepsin F in COS-7 cells revealed a vesicular distribution of the gene product in the juxtanuclear region of the cells. However, contrary to all known cathepsins, the open reading frame of the cathepsin F cDNA did not encode a signal sequence, thus suggesting that the protease is targeted to the lysosomal compartment via an N-terminal signal peptide-independent lysosomal targeting pathway.  (+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, ...
Cathepsin W is a protein that in humans is encoded by the CTSW gene.[5][6][7]. The protein encoded by this gene, a member of the peptidase C1 family, is a cysteine proteinase that may have a specific function in the mechanism or regulation of T-cell cytolytic activity. The encoded protein is found associated with the membrane inside the endoplasmic reticulum of natural killer and cytotoxic T-cells. Expression of this gene is up-regulated by interleukin-2.[7]. ...
Korpos et al. (1) claim that "limited information exists on the nature of the ECM [extracellular matrix] of the pancreas and, in particular, on the composition of peri-islet capsule," and that they provide the "the first comprehensive analysis of the [ECM] composition of peri-islet capsules.". We dispute the strength of these claims. In mice we originally reported in 2008 that a basement membrane (BM) exists around islets, and eight unique components were identified (type IV collagens α1, α2, laminin α2, β1, γ1, nidogen 1, nidogen 2, perlecan) as well as two composite components (laminin Engelbreth-Holm-Swarm, collagen IV) (2). It was also shown that type IV collagens α3, α4, α5, α6 were not present (2). Korpos et al. (1) were able to find a further three unique components (laminin α4, β2, agrin) and one composite component (laminin 322).. In 2008 in humans (3,4), at least four unique components (laminin α1, α5, β1, γ1) were identified and in their Supplementary Figure 1 staining ...
Mouse monoclonal Cathepsin W antibody [BV39-2B]. Validated in WB, IHC and tested in Human. Immunogen corresponding to recombinant full length protein.
The task of tracing visual language in book design is a challenge, but one that is useful to take up in order to help us understand how readers make meaning of what they read. Studying the lineage of some forms of layout also sheds light on how design fits into and contributes to culture in a wider sense. Childrens science books - the highly graphic and colourful ones published over the last 30 years or so in the UK - provide some excellent examples of complex visual language, partly because they tend to be more highly illustrated than books meant for adults. But how do diagrams, illustrations and different forms of text interact to produce content in these books? Meaning does not reside in the book alone, but is dependent on context: the particular conditions of reading, and the wider social and cultural environment. This is an exploration of book design as a medium of communication.. Many changes have occurred in British childrens publishing over the past 30 years. These have had a visible ...
ROZMAN PUNGERČAR, Jerica, KOPITAR-JERALA, Nataša, BOGYO, M., TURK, Dušan, VASILJEVA, Olga, KLEMENČIČ, Ivica, VANDENABEELE, P., BR MME, D., PUIZDAR, Vida, FONOVIĆ, Marko, TRSTENJAK-PREBANDA, Mojca, DOLENC, Iztok, TURK, Vito, TURK, Boris. Inhibition of papain-like cysteine proteases and legumain by caspase-specific inhibitors : when reaction mechanism is more important than specificity. Cell Death Differ, 2003, vol. 10, str. 881-888 ...
Complete information for CTSF gene (Protein Coding), Cathepsin F, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Causes of Abdominal Tumor. Infection by Helicobacter pylori is believed to be the cause of most abdominal tumor while autoimmune atrophic gastritis, intestinal metaplasia and various genetic factors are associated with increased risk levels. Its also states that diet plays no role in the genesis of abdominal tumor. However, there is some research done listed down the following dietary risks, and protective factors, for abdominal tumor: "smoked foods, salted fish and meat, and pickled vegetables (appear to increase the risk of stomach cancer.) Nitrates and nitrites are substances commonly found in cured meats. They can be converted by certain bacteria, such as H. pylori, into compounds that have been found to cause stomach cancer in animals. On the other hand, eating fresh fruits and vegetables that contain antioxidant vitamins (such as A and C) appears to lower the risk of abdominal tumor.. In more detail, H. pylori is the main risk factor in 65-80% of abdominal tumor, but in only 2% of such ...
As highlighted by the similarity of their fold and the superimposition of their active site, we have shown that NsPCS belongs to the papain superfamily of cysteine proteases. It is therefore expected that the peptide hydrolase activity of NsPCS, i.e., the deglycination of GSH, resembles the general and well known mechanism of papain-like cysteine proteases. By analogy with such a mechanism, Cys-70, His-183, and Asp-201 (equivalent to Cys-56, His-162, and Asp-180 in AtPCS1) correspond to the catalytic triad in NsPCS. Moreover, it is also highly probable that Cys-70 and His-183 form a thiolate-imidazolium ion pair, stabilized by Asp-201, and that the nucleophilic attack of Cys-70 on the Cys-Gly peptide bond is favored by the oxyanion hole, made up of Cys-70 and Gln-64. In a second step, the water molecule W153, whose nucleophilicity is enhanced by the proximity of His-183 and Asp-201, is then ideally placed to attack the thioester bond and liberate the γ-glutamylcysteine. We could trap the ...
The propeptide of cruzipain--a potent selective inhibitor of the trypanosomal enzymes cruzipain and brucipain, and of the human enzyme cathepsin F

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 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 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 A (CTSA) AntikörperCathepsin A (CTSA) Antikörper

Am meisten referenzierte anti-Cathepsin A Antikörper. Show all anti-Cathepsin A (CTSA) Antikörper with Pubmed References. * ... Weitere Antikörper gegen Cathepsin A Interaktionspartner. Arabidopsis thaliana Cathepsin A (CTSA) Interaktionspartner ... Zusätzlich bieten wir Ihnen Cathepsin A Proteine (28) und Cathepsin A Kits (27) und viele weitere Produktgruppen zu diesem ... The Cathepsin C releases the glycosidases from complexes formed with cathepsin A, and reinstates their activity. ...
more infohttps://www.antikoerper-online.de/abstract/Cathepsin+A+

Cathepsin Detection Kits - MP BiomedicalsCathepsin Detection Kits - MP Biomedicals

MAGIC RED® CATHEPSIN B KIT. A fluorogenic test kit for Cathepsin B. (Patent# 6,235,493-May 22, 2001). Ref.: 1. Van Noorden, C.J ... MAGIC RED® CATHEPSIN K KIT. A fluorogenic test kit for Cathepsin K. (Patent# 6,235,493-May 22, 2001). Ref.: 1. Van Noorden, C.J ... MAGIC RED® CATHEPSIN L KIT. A fluorogenic test kit for Cathepsin L. (Patent# 6,235,493-May 22, 2001). Ref.: 1. Van Noorden, C.J ...
more infohttp://www.mpbio.com/index.php?cPath=2873_2_1999_2005_2031_2091_2235&country=223

WikiGenes - Ctsl - cathepsin LWikiGenes - Ctsl - cathepsin L

... cathepsin B), Arg-AMC (cathepsin H), and N-benzyloxycarbonyl-Phe-Arg-AMC (cathepsin L), were determined in rat lung throughout ... cathepsin-B and cathepsin-L activities [26].. *Furthermore, cathepsin L may play an important role in the degradation of the ... cathepsin B and cathepsin D. Thus, Ras utilizes different effectors to mediate transformation and to deregulate cathepsin L ... Cathepsin B-like and cathepsin L-like activities fell below control values initially, but from week 8 of the immunosuppressive ...
more infohttps://www.wikigenes.org/e/gene/e/25697.html

WikiGenes - CTSC - cathepsin CWikiGenes - CTSC - cathepsin C

Human recombinant pro-dipeptidyl peptidase I (cathepsin C) can be activated by cathepsins L and S but not by autocatalytic ... The results suggest that cathepsin L could be an important activator of DPPI in vivo and that cathepsin D and possibly the ... The enzymes, except cathepsin C, are endopeptidases (reviewed in Kirschke et al., 1995), although cathepsin B was found also to ... Mutations of the cathepsin C gene are responsible for Papillon-Lefèvre syndrome. Hart, T.C., Hart, P.S., Bowden, D.W., Michalec ...
more infohttps://www.wikigenes.org/e/gene/e/1075.html

Role of Cathepsin S in Periodontal Inflammation and InfectionRole of Cathepsin S in Periodontal Inflammation and Infection

V. Zavanik-Bergant, A. Sekirnik, R. Golouh, V. Turk, and J. Kos, "Immunochemical localisation of cathepsin S, cathepsin L and ... Both stimulants caused a significant cathepsin S upregulation. A significantly elevated cathepsin S expression in gingival ... Role of Cathepsin S in Periodontal Inflammation and Infection. S. Memmert,1,2 A. Damanaki,1 A. V. B. Nogueira,3 S. Eick,4 M. ... "Antimicrobial peptide LL-37 is both a substrate of cathepsins S and K and a selective inhibitor of cathepsin L," Biochemistry, ...
more infohttps://www.hindawi.com/journals/mi/2017/4786170/

Cathepsin Assay KitsCathepsin Assay Kits

BioVision develops and offers a wide variety of products including assay kits, antibodies, recombinant proteins & enzymes, and other innovative research tools for studying Apoptosis, Metabolism, Cell Proliferation, Cellular Stress, Cell Damage and Repair, Diabetes, Obesity and Metabolic Syndrome, Stem Cell Biology, Gene Regulation, Signal Transduction, etc. BioVisions products are currently being sold in more than 60 countries worldwide.
more infohttps://www.biovision.com/products/cancer-research/apoptosis-related-products/non-caspase-proteases/cathepsin/cathepsin-assay-kits.html

CTSB - Cathepsin B - Homo sapiens (Human) - CTSB gene & proteinCTSB - Cathepsin B - Homo sapiens (Human) - CTSB gene & protein

Cathepsin B. Cathepsin B, EC 3.4.22.1 (APP secretase, APPS) (Cathepsin B1) [Cleaved into: Cathepsin B light chain; Cathepsin B ... Cathepsin BImported. ,p>Information which has been imported from another database using automatic procedures.,/p> ,p>,a href="/ ... tr,E9PL32,E9PL32_HUMAN Cathepsin B (Fragment) OS=Homo sapiens OX=9606 GN=CTSB PE=1 SV=2 ...
more infohttps://www.uniprot.org/uniprot/E9PL32

Ctsg - Cathepsin G - Rattus norvegicus (Rat) - Ctsg gene & proteinCtsg - Cathepsin G - Rattus norvegicus (Rat) - Ctsg gene & protein

Cathepsin GAdd BLAST. ›26. Proteomic databases. PaxDb, a database of protein abundance averages across all three domains of ... sp,P17977,CATG_RAT Cathepsin G (Fragment) OS=Rattus norvegicus GN=Ctsg PE=1 SV=1 IIGGREARPNSHPYMAFLLIQSPEGL ...
more infohttp://www.uniprot.org/uniprot/P17977

anti-Cathepsin D Primary Antibodiesanti-Cathepsin D Primary Antibodies

Ausgesuchte Qualitäts-Hersteller für Cathepsin D Antikörper. Hier bestellen. ... Monoklonale und polyklonale Cathepsin D Antikörper für viele Methoden. ... Bezeichner auf Proteinebene für anti-Cathepsin D (CTSD) Antikörper etID16901.18 , cathepsin D , aspartic protease , cathepsin d ... cathepsin D (lysosomal aspartyl peptidase) , cathepsin D (lysosomal aspartyl protease) , prepro-cathepsin D, prepro-CD ...
more infohttps://www.antikoerper-online.de/peptide-hormone-metabolism-pathway-41/cathepsin-d-antibody-2858/

Human Cathepsin Enzyme Products - MP BiomedicalsHuman Cathepsin Enzyme Products - MP Biomedicals

CATHEPSIN L-HUMAN LIVER. Cathepsin L is unstable at neutral pH, but is relatively stable in the range 4.5 to 5.5.. ...
more infohttps://www.mpbio.com/index.php?cPath=2_2009_2882_2923&country=223

Cathepsin A
     Summary Report | CureHunterCathepsin A Summary Report | CureHunter

Cathepsin A: A carboxypeptidase that catalyzes the release of a C-terminal amino acid with a broad specificity. It also plays a ... Cathepsin A. Subscribe to New Research on Cathepsin A A carboxypeptidase that catalyzes the release of a C-terminal amino acid ... 09/01/1987 - "Study of cathepsin A, B and D activities in the skin wound edges. ". 01/01/1984 - "Study of cathepsin A and D ... 02/01/2000 - "Cathepsin A activity in primary and metastatic human melanocytic tumors.". 01/01/1999 - "Cathepsin A activity in ...
more infohttp://www.curehunter.com/public/keywordSummaryD043402.do
  • 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. (oregonstate.edu)
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