Geotrichosis: Infection due to the fungus Geotrichum.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.Papillon-Lefevre Disease: Rare, autosomal recessive disorder occurring between the first and fifth years of life. It is characterized by palmoplantar keratoderma with periodontitis followed by the premature shedding of both deciduous and permanent teeth. Mutations in the gene for CATHEPSIN C have been associated with this disease.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).Dipeptidyl-Peptidases and Tripeptidyl-Peptidases: A subclass of exopeptidases that includes enzymes which cleave either two or three AMINO ACIDS from the end of a peptide chain.Cathepsin K: A cysteine protease that is highly expressed in OSTEOCLASTS and plays an essential role in BONE RESORPTION as a potent EXTRACELLULAR MATRIX-degrading enzyme.Cathepsin G: A serine protease found in the azurophil granules of NEUTROPHILS. It has an enzyme specificity similar to that of chymotrypsin C.Cathepsin H: An ubiquitously-expressed lysosomal cysteine protease that is involved in protein processing. The enzyme has both endopeptidase and aminopeptidase activities.Gerbillinae: A subfamily of the Muridae consisting of several genera including Gerbillus, Rhombomys, Tatera, Meriones, and Psammomys.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.Cathepsin F: A lysosomal papain-related cysteine proteinase that is expressed in a broad variety of cell types.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.Hyperkeratosis, Epidermolytic: A form of congenital ichthyosis inherited as an autosomal dominant trait and characterized by ERYTHRODERMA and severe hyperkeratosis. It is manifested at birth by blisters followed by the appearance of thickened, horny, verruciform scales over the entire body, but accentuated in flexural areas. Mutations in the genes that encode KERATIN-1 and KERATIN-10 have been associated with this disorder.Lysosomes: A class of morphologically heterogeneous cytoplasmic particles in animal and plant tissues characterized by their content of hydrolytic enzymes and the structure-linked latency of these enzymes. The intracellular functions of lysosomes depend on their lytic potential. The single unit membrane of the lysosome acts as a barrier between the enzymes enclosed in the lysosome and the external substrate. The activity of the enzymes contained in lysosomes is limited or nil unless the vesicle in which they are enclosed is ruptured. Such rupture is supposed to be under metabolic (hormonal) control. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)Cathepsin Z: A ubiquitously-expressed cysteine peptidase that exhibits carboxypeptidase activity. It is highly expressed in a variety of immune cell types and may play a role in inflammatory processes and immune responses.Protease Inhibitors: Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).Dipeptides: Peptides composed of two amino acid units.Serine Endopeptidases: Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.Endopeptidases: A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.Enzyme Precursors: Physiologically inactive substances that can be converted to active enzymes.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.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 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.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)Authorship: The profession of writing. Also the identity of the writer as the creator of a literary production.Knowledge Bases: Collections of facts, assumptions, beliefs, and heuristics that are used in combination with databases to achieve desired results, such as a diagnosis, an interpretation, or a solution to a problem (From McGraw Hill Dictionary of Scientific and Technical Terms, 6th ed).Microscopic Polyangiitis: A primary systemic vasculitis of small- and some medium-sized vessels. It is characterized by a tropism for kidneys and lungs, positive association with anti-neutrophil cytoplasmic antibodies (ANCA), and a paucity of immunoglobulin deposits in vessel walls.Dipeptidyl Peptidase 4: A serine protease that catalyses the release of an N-terminal dipeptide. Several biologically-active peptides have been identified as dipeptidyl peptidase 4 substrates including INCRETINS; NEUROPEPTIDES; and CHEMOKINES. The protein is also found bound to ADENOSINE DEAMINASE on the T-CELL surface and is believed to play a role in T-cell activation.Wegener Granulomatosis: A multisystemic disease of a complex genetic background. It is characterized by inflammation of the blood vessels (VASCULITIS) leading to damage in any number of organs. The common features include granulomatous inflammation of the RESPIRATORY TRACT and kidneys. Most patients have measurable autoantibodies (ANTINEUTROPHIL CYTOPLASMIC ANTIBODIES) against neutrophil proteinase-3 (WEGENER AUTOANTIGEN).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.Cattle: Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.Antibodies: Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).Pedigree: The record of descent or ancestry, particularly of a particular condition or trait, indicating individual family members, their relationships, and their status with respect to the trait or condition.Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.IndiaExopeptidases: A sub-class of PEPTIDE HYDROLASES that act only near the ends of polypeptide chains.Spectrometry, Mass, Electrospray Ionization: A mass spectrometry technique used for analysis of nonvolatile compounds such as proteins and macromolecules. The technique involves preparing electrically charged droplets from analyte molecules dissolved in solvent. The electrically charged droplets enter a vacuum chamber where the solvent is evaporated. Evaporation of solvent reduces the droplet size, thereby increasing the coulombic repulsion within the droplet. As the charged droplets get smaller, the excess charge within them causes them to disintegrate and release analyte molecules. The volatilized analyte molecules are then analyzed by mass spectrometry.Mass Spectrometry: An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.Amyloid beta-Protein Precursor: A single-pass type I membrane protein. It is cleaved by AMYLOID PRECURSOR PROTEIN SECRETASES to produce peptides of varying amino acid lengths. A 39-42 amino acid peptide, AMYLOID BETA-PEPTIDES is a principal component of the extracellular amyloid in SENILE PLAQUES.Cystatin C: An extracellular cystatin subtype that is abundantly expressed in bodily fluids. It may play a role in the inhibition of interstitial CYSTEINE PROTEASES.Alzheimer Disease: A degenerative disease of the BRAIN characterized by the insidious onset of DEMENTIA. Impairment of MEMORY, judgment, attention span, and problem solving skills are followed by severe APRAXIAS and a global loss of cognitive abilities. The condition primarily occurs after age 60, and is marked pathologically by severe cortical atrophy and the triad of SENILE PLAQUES; NEUROFIBRILLARY TANGLES; and NEUROPIL THREADS. (From Adams et al., Principles of Neurology, 6th ed, pp1049-57)Mice, Transgenic: Laboratory mice that have been produced from a genetically manipulated EGG or EMBRYO, MAMMALIAN.MedlinePlus: NATIONAL LIBRARY OF MEDICINE service for health professionals and consumers. It links extensive information from the National Institutes of Health and other reviewed sources of information on specific diseases and conditions.Keratoderma, Palmoplantar: Group of mostly hereditary disorders characterized by thickening of the palms and soles as a result of excessive keratin formation leading to hypertrophy of the stratum corneum (hyperkeratosis).Tooth Exfoliation: Physiologic loss of the primary dentition. (Zwemer, Boucher's Clinical Dental Terminology, 4th ed)Rotifera: A class of minute animals of the phylum Aschelminthes.Gene Expression Profiling: The determination of the pattern of genes expressed at the level of GENETIC TRANSCRIPTION, under specific circumstances or in a specific cell.Phylogeny: The relationships of groups of organisms as reflected by their genetic makeup.Oligonucleotide Array Sequence Analysis: Hybridization of a nucleic acid sample to a very large set of OLIGONUCLEOTIDE PROBES, which have been attached individually in columns and rows to a solid support, to determine a BASE SEQUENCE, or to detect variations in a gene sequence, GENE EXPRESSION, or for GENE MAPPING.Transcriptome: The pattern of GENE EXPRESSION at the level of genetic transcription in a specific organism or under specific circumstances in specific cells.Genome-Wide Association Study: An analysis comparing the allele frequencies of all available (or a whole GENOME representative set of) polymorphic markers in unrelated patients with a specific symptom or disease condition, and those of healthy controls to identify markers associated with a specific disease or condition.Gene Expression Regulation: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.

Increased collagenase and dipeptidyl peptidase I activity in leucocytes from healthy elderly people. (1/128)

The incidence of infectious diseases increases with ageing. The enzymatic activity of leucocytes may have a relevant role in the morbidity and mortality due to infections in the elderly. In this study we have compared the activity of enzymes involved in the inflammatory response in leucocytes from young and elderly women. A total of 35 healthy females was studied, 20 volunteers aged 78-98 years (mean 89.1 years) and 15 young controls aged 19-34 years (mean 26 years). All of them were in good clinical condition, without any acute or chronic disease. Intracellular enzyme activity was analysed by flow cytometry in leucocytes from young and elderly women. The enzyme substrates employed were for oxidative burst, L-aminopeptidase, collagenase, cathepsin B, C, D and, G and dipeptidyl peptidase I. The intracellular enzyme activity assessed by flow cytometry in leucocytes from young and elderly women was similar, as far as oxidative burst, L-aminopeptidase, cathepsin B, C, D and G are concerned. An increased collagenase activity was detected in granulocytes from elders. The mean fluorescence channels for this enzyme corresponded to 86 +/- 23 and 60 +/- 15 in cells from elders and controls, respectively (P = 0.01224). An increased dipeptidyl peptidase I activity was detected in lymphocytes from elderly women. The corresponding values for this enzyme in elders and the young were 65.9 +/- 43.3 and 17.3 +/- 5, respectively (P = 0. 0036). The proper functional activity of intracellular enzymes involved in inflammatory responses is likely to be determinant for successful ageing.  (+info)

Dipeptidyl peptidase I is required for the processing and activation of granzymes A and B in vivo. (2/128)

Dipeptidyl peptidase I (DPPI) is a lysosomal cysteine protease that has been implicated in the processing of granzymes, which are neutral serine proteases exclusively expressed in the granules of activated cytotoxic lymphocytes. In this report, we show that cytotoxic lymphocytes derived from DPPI-/- mice contain normal amounts of granzymes A and B, but these molecules retain their prodipeptide domains and are inactive. Cytotoxic assays with DPPI-/- effector cells reveal severe defects in the induction of target cell apoptosis (as measured by [(125)I]UdR release) at both early and late time points; this defect is comparable to that detected in perforin-/- or granzyme A-/- x B-/- cytotoxic lymphocytes. DPPI therefore plays an essential role in the in vivo processing and activation of granzymes A and B, which are required for cytotoxic lymphocyte granule-mediated apoptosis.  (+info)

Location of the binding site for chloride ion activation of cathepsin C. (3/128)

Cathepsin C, a tetrameric lysosomal dipeptidyl-peptide hydrolase, is activated by chloride ion. The activation is shown here to be specific and pH-dependent, dissociation constants for chloride being lower at low pH. Bound chloride decreases the Km for the hydrolysis of chromophore labelled substrates without any significant change in Vmax, confirming its involvement in substrate binding. Determination of the kinetic parameters of chloride activation, using unlabelled substrates, has enabled its site of action to be located. The lower Km for the hydrolysis of simple amide substrates in the presence of Cl- shows that the S sites are involved. Possible involvement of the S' sites is excluded by the finding that the Km for the nucleophile in the transferase reaction is unaffected by chloride. The rates of inhibition by E-64 and iodoacetate are both chloride-dependent and, from the structure of the papain-E-64 complex, it is concluded that chloride binds close to the S2 site. The binding of guanidinium ion, a positively charged inhibitor, to the S site is dependent on chloride. Based on these results, a model is proposed to explain the chloride activation of cathepsin C. The possible physiological role of chloride in the regulation of proteolysis in the lysosome is discussed.  (+info)

Mutations of the cathepsin C gene are responsible for Papillon-Lefevre syndrome. (4/128)

Papillon-Lefevre syndrome (PLS) is an autosomal recessive disorder characterised by palmoplantar hyperkeratosis and severe early onset periodontitis that results in the premature loss of the primary and secondary dentitions. A major gene locus for PLS has been mapped to a 2.8 cM interval on chromosome 11q14. Correlation of physical and genetic maps of this interval indicate it includes at least 40 ESTs and six known genes including the lysosomal protease cathepsin C gene (CTSC). The CTSC message is expressed at high levels in a variety of immune cells including polymorphonuclear leucocytes, macrophages, and their precursors. By RT-PCR, we found CTSC is also expressed in epithelial regions commonly affected by PLS, including the palms, soles, knees, and oral keratinised gingiva. The 4.7 kb CTSC gene consists of two exons. Sequence analysis of CTSC from subjects affected with PLS from five consanguineous Turkish families identified four different mutations. An exon 1 nonsense mutation (856C-->T) introduces a premature stop codon at amino acid 286. Three exon 2 mutations were identified, including a single nucleotide deletion (2692delA) of codon 349 introducing a frameshift and premature termination codon, a 2 bp deletion (2673-2674delCT) that results in introduction of a stop codon at amino acid 343, and a G-->A substitution in codon 429 (2931G-->A) introducing a premature termination codon. All PLS patients were homozygous for cathepsin C mutations inherited from a common ancestor. Parents and sibs heterozygous for cathepsin C mutations do not show either the palmoplantar hyperkeratosis or severe early onset periodontitis characteristic of PLS. A more complete understanding of the functional physiology of cathepsin C carries significant implications for understanding normal and abnormal skin development and periodontal disease susceptibility.  (+info)

Haim-Munk syndrome and Papillon-Lefevre syndrome are allelic mutations in cathepsin C. (5/128)

Of the many palmoplantar keratoderma (PPK) conditions, only Papillon-Lefevre syndrome (PLS) and Haim-Munk syndrome (HMS) are associated with premature periodontal destruction. Although both PLS and HMS share the cardinal features of PPK and severe periodontitis, a number of additional findings are reported in HMS including arachnodactyly, acro-osteolysis, atrophic changes of the nails, and a radiographic deformity of the fingers. While PLS cases have been identified throughout the world, HMS has only been described among descendants of a religious isolate originally from Cochin, India. Parental consanguinity is a characteristic of many cases of both conditions. Although autosomal recessive transmission of PLS is evident, a more "complex" autosomal recessive pattern of inheritance with phenotypic influences from a closely linked modifying locus has been hypothesised for HMS. Recently, mutations of the cathepsin C gene have been identified as the underlying genetic defect in PLS. To determine if a cathepsin C mutation is also responsible for HMS, we sequenced the gene in affected and unaffected subjects from the Cochin isolate in which both the PLS and HMS phenotypes appear. Here we report identification of a mutation of cathepsin C (exon 6, 2127A--> G) that changes a highly conserved amino acid in the cathepsin C peptide. This mutation segregates with HMS in four nuclear families. Additionally, the existence of a shared common haplotype for genetic loci flanking the cathepsin C gene suggests that affected subjects descended from the Cochin isolate are homozygous for a mutation inherited "identical by descent" from a common ancestor. This finding supports simple autosomal recessive inheritance for HMS in these families. We also report a mutation of the same exon 6 CTSC codon (2126C-->T) in a Turkish family with classical PLS. These findings provide evidence that PLS and HMS are allelic variants of cathepsin C gene mutations.  (+info)

Localisation of a gene for prepubertal periodontitis to chromosome 11q14 and identification of a cathepsin C gene mutation. (6/128)

Prepubertal periodontitis (PPP) is a rare and rapidly progressive disease of young children that results in destruction of the periodontal support of the primary dentition. The condition may occur as part of a recognised syndrome or may occur as an isolated finding. Both autosomal dominant and recessive forms of Mendelian transmission have been reported for PPP. We report a consanguineous Jordanian family with four members affected by PPP in two nuclear sibships. The parents of the affected subjects are first cousins. We have localised a gene of major effect for PPP in this kindred (Zmax=3.55 for D11S901 at theta=0.00) to a 14 cM genetic interval on chromosome 11q14 flanked by D11S916 and D11S1367. This PPP candidate interval overlaps the region of chromosome 11q14 that contains the cathepsin C gene responsible for Papillon-Lefevre and Haim-Munk syndromes. Sequence analysis of the cathepsin C gene from PPP affected subjects from this Jordanian family indicated that all were homozygous for a missense mutation (1040A-->G) that changes a tyrosine to a cysteine. All four parents were heterozygous carriers of this Tyr347Cys cathepsin C mutation. None of the family members who were heterozygous carriers for this mutation showed any clinical findings of PPP. None of the 50 controls tested were found to have this Tyr347Cys mutation. This is the first reported gene mutation for non-syndromic periodontitis and shows that non-syndromic PPP is an allelic variant of the type IV palmoplantar ectodermal dysplasias.  (+info)

Arginine-based structures are specific inhibitors of cathepsin C. Application of peptide combinatorial libraries. (7/128)

Novel synthetic peptide inhibitors of lysosomal cysteine proteinase cathepsin C have been designed through the use of soluble peptide combinatorial libraries. The uncovered structural inhibitory module consists of the N-terminal cluster of L-arginine residues. Its modification with D-amino acids or arginine derivatives did not increase the inhibition strength. Inhibitory potency of oligoarginines improves with the elongation of peptide chain reaching a maximum for octa-L-arginine. The oligoarginines specifically interact with the cathepsin C active site as shown by competitive-type inhibition kinetics (Ki approximately 10-5 M) and intrinsic fluorescence measurements. The inhibitory interaction of oligoarginines is established through the specific spatial contact of a net of guanidino groups in the arginine side-chains, as indicated by comparison with inhibitory action of low molecular mass guanidine derivatives (Ki approximately 10-3 M). Nonarginine polyionic compounds cannot mimic the inhibitory effect of oligoarginines. The arginine-based peptide inhibitors were selective towards cathepsin C among other cysteine proteinases tested.  (+info)

Programming for cytotoxic effector function occurs concomitantly with CD4 extinction during CD8(+) T cell differentiation in the thymus. (8/128)

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)

*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 C (CTSC) also known as dipeptidyl peptidase I (DPP-I) is a lysosomal exo-cysteine protease belonging to the peptidase C1 family. In humans, it is encoded by the CTSC gene. Cathepsin C appears to be a central coordinator for activation of many serine proteases in immune/inflammatory cells. Cathepsin C catalyses excision of dipeptides from the N-terminus of protein and peptide substrates, except if (i) the amino group of the N-terminus is blocked, (ii) the site of cleavage is on either side of a proline residue, (iii) the N-terminal residue is lysine or arginine, or (iv) the structure of the peptide or protein prevents further digestion from the N-terminus. The cDNAs encoding rat, human, murine, bovine, dog and two Schistosome cathepsin Cs have been cloned and sequenced and show that the enzyme is highly conserved. The human and rat cathepsin C cDNAs encode precursors (prepro-cathepsin C) comprising signal peptides of 24 residues, pro-regions of 205 (rat cathepsin C) or 206 (human ...
Background: PLS is a rare autosomal recessive disorder characterized by early onset periodontopathia and palmar plantar keratosis. PLS is caused by mutations in the cathepsin C (CTSC) gene. Dipeptidyl-peptidase I encoded by the CTSC gene removes dipeptides from the aminoterminus of protein substrates and mainly plays an immune and inflammatory role. Several mutations have been reported in this gene in patients from several ethnic groups. We report here mutation analysis of the CTSC gene in three Indian families with PLS. Methods: Peripheral blood samples were obtained from individuals belonging to three Indian families with PLS for genomic DNA isolation. Exon-specific intronic primers were used to amplify DNA samples from individuals. PCR products were subsequently sequenced to detect mutations.PCR-SCCP and ASOH analyses were used to determine if mutations were present in normal control individuals. Results: All patients from three families had a classic PLS phenotype, which included ...
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
Buy anti-CTSC antibody, Rabbit anti-Bovine Cathepsin C Polyclonal Antibody-AAQ08887.1 (MBS573038) product datasheet at MyBioSource, Primary Antibodies. Application: Immunoprecipitation (IP)
Dadkhah E, Moghaddasian M, Arab H, Bustani Farkoush H, Kazemi Noughabi M, Abbaszadegan MR. Novel mutation in cathepsin C gene(CTSC) and modeling of mutated protein in three Iranian families with Papillon Lefever Syndrome. European Human Genetics Conference 2012.Nurnberg, Germany, 2012.. Abbaszadegan MR, Forghanifard MM. Impact of cancer testis antigens crosstalk with self renewal cell signaling pathways in esophageal squamous cell carcinoma. European Human Genetics Conference 2012.Nurnberg, Germany. June 23-26-2012. (Poster presentation).. ...
Dadkhah E, Moghaddasian M, Arab H, Bustani Farkoush H, Kazemi Noughabi M, Abbaszadegan MR. Novel mutation in cathepsin C gene(CTSC) and modeling of mutated protein in three Iranian families with Papillon Lefever Syndrome. European Human Genetics Conference 2012.Nurnberg, Germany, 2012.. Abbaszadegan MR, Forghanifard MM. Impact of cancer testis antigens crosstalk with self renewal cell signaling pathways in esophageal squamous cell carcinoma. European Human Genetics Conference 2012.Nurnberg, Germany. June 23-26-2012. (Poster presentation).. ...
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The mechanism of toxicity for cytolytic lymphocytes of Leu-Leu-OMe and related dipeptide derivatives was examined. Selective inhibition of dipeptidyl peptidase I (DPPI), a lysosomal thiol protease highly enriched in cytotoxic lymphocytes, prevented all natural killer (NK) toxic effects of such agents. However, many DPPI substrates were found to possess no NK toxic properties. For some such agents, this lack of NK toxicity appeared to be related to the lack of uptake by lymphocytes. In this regard, Leu-Leu-OMe was found to be incorporated by lymphocytes and monocytes via a saturable facilitated transport mechanism with characteristics distinct from previously characterized mammalian dipeptide transport processes. This novel transport process was found to be specific for dipeptides composed of selective L-stereoisomer amino acids and enhanced by hydrophobic ester or amide additions to the COOH terminus of dipeptides. Maximal rates of Leu-Leu-OMe uptake by T8 and NK cell-enriched peripheral blood ...
Heike Wulff. "Seed grants like the CTSC award are very important because they allow us to generate preliminary data for larger NIH grants, which are typically not awarded without existing data showing that the project is feasible," said Heike Wulff, professor of pharmacology and one of this years awardees. "Our CTSC grant will allow us to test whether a novel therapeutic principle, the activation of a particular neuronal potassium channel, can indeed reduce neuronal excitability and thus prevent epileptic seizures.". The CTSC awarded seven UC Davis investigators for investigations in three broad categories: highly innovative research, new approaches to neurodevelopmental disorders and mini-biorepositories from clinical research projects. The recipients are working closely with CTSC leadership for additional resources to support their collaborative research projects.. Highly innovative research. ...
Yveline Hamon, Monika Łęgowska, Patricia Fergelot, Sandrine Dallet-Choisy, Louise Newell, Lise Vanderlynden, Ali Kord Valeshabad, Karina Acrich, Hadi Kord, Tsamakis Charalampos, Fanny Morice-Picard, Ian Surplice, Jerome Zoidakis, Karen David, Antonia Vlahou, Shivanna Ragunatha, Nikoletta Nagy, Katalin Farkas, Márta Széll, Cyril Goizet, Beate Schacher, Maurizio Battino, Abdullah Al Farraj Aldosari, Xinwen Wang, Yang Liu, Sylvain Marchand-Adam, Adam Lesner, Elodie Kara, Sevil Korkmaz-Icöz, Celia Moss, Peter Eickholz, Alain Taieb, Salih Kavukcu, Dieter E. Jenne, Francis Gauthier, Brice Korkmaz, Analysis of urinary cathepsin C for diagnosing Papillon-Lefèvre syndrome, The FEBS Journal, 2016, Vol. 283, iss. 3, 498-509, IF: ...
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Papillon-Lefevre syndrome. Coloured transmission electron micrograph (TEM) of a cell affected by Papillon-Lefevre syndrome, a rare inherited condition. Plaques of the protein keratin (blue) are seen within the cell. The disease causes hyperkeratosis (thickening of the skin) and severe periodontitis, an inflammation of the tissue that surrounds and supports the teeth. The inflammation results in bone and tooth loss. Magnification: x16,600 when printed at 10 centimetres wide. - Stock Image C020/8722
Papillon-Lefevre Disease: Rare, autosomal recessive disorder occurring between the first and fifth years of life. It is characterized by palmoplantar keratoderma with periodontitis followed by the premature shedding of both deciduous and permanent teeth. Mutations in the gene for CATHEPSIN C have been associated with this disease.
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 ...
People make mistakes and poor choices; Vision Zero says those mistakes dont have to cost lives. Working together, we can eliminate deaths and serious injuries on our streets. The CTSC focused on Vision Zero for their 2016-2018 work plan, committing to making Santa Cruz County safer for all road users. Click here to read our 2017 report, The Impact of Traffic Violence On Santa Cruz County, explore interactive maps showing our high-injury corridors and other crash data, and view our Vision Zero workplan.. Our Mission. The mission of the Community Traffic Safety Coalition is to reduce traffic-related injuries while promoting the use of alternative modes of transportation. The primary focus is on bicycle and pedestrian safety issues. The CTSC educates all road users in safety practices to decrease the risk and severity of collisions, and advocates for improved conditions to make all methods of transportation safer.. About the Community Traffic Safety Coalition. The CTSC is a creative and ...
Congratulations to our KL2 Scholars-Nicole Kucine, MD, and Danielle Novetsky Friedman, MD-on presenting their theses before the Masters Examining Committee in April. Nicole, a WCMC Assistant Professor of Pediatrics, presented on her CTSC KL2 research, Evaluation of Myeloproliferative Neoplasms in Pediatric Patients. Danielle, an MSK Instructor of Pediatrics, presented on her CTSC KL2 research, Chronic Conditions in Adult Survivors of Retinoblastoma. Wed also like to thank their mentors (Drs. Ross Levine, James Bussel, Kevin Oeffinger, Erika Abramson, and Chaya Moskowitz) and our Associate Program Directors (Drs. Yuan-Shan Zhu and Dean Bajorin) for attending and showing tremendous support for their mentees.. CTSC Research in Progress Luncheon ...
Upon stimulation, polymorphonuclear leucocytes (PMNs) release potent serine proteases, i.e. elastase, cathepsin C and proteinase 3, which contribute to the degradation of tissue and plasma components. Here, we describe the development of a plasma test to assess PMN-mediated fibrinogenolysis as a biochemical marker for actual PMN-derived proteolysis in vivo, useful for monitoring therapeutic efficacy, i.e. of elastase inhibitors. We generated a monoclonal antibody (MAb), designated 1-1/B3, with a high affinity for elastase-degraded fibrinogen (EDF). The epitope for 1-1/B3 becomes exposed in a time-dependent manner during digestion of fibrinogen with purified PMN-derived serine proteases and with isolated PMNs in vitro. However, 1-1/B3 does not react with plasma fibrinogen or with fibrin(ogen) degradation products generated by plasmin or by other active proteases that may occur locally, i.e. metalloproteases and lysosomal cathepsins. On the basis of MAb 1-1/B3, we developed a plasma test for the ...
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From NCBI Gene:. This gene encodes a member of the peptidase C1 family and lysosomal cysteine proteinase that appears to be a central coordinator for activation of many serine proteinases in cells of the immune system. Alternative splicing results in multiple transcript variants, at least one of which encodes a preproprotein that is proteolytically processed to generate heavy and light chains that form a disulfide-linked dimer. A portion of the propeptide acts as an intramolecular chaperone for the folding and stabilization of the mature enzyme. This enzyme requires chloride ions for activity and can degrade glucagon. Defects in the encoded protein have been shown to be a cause of Papillon-Lefevre syndrome, an autosomal recessive disorder characterized by palmoplantar keratosis and periodontitis. [provided by RefSeq, Nov 2015]. From UniProt: ...
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Glutamine supplementation has been advocated for patients requiring parenteral nutritional support. However, the direct effect of glutamine on neoplastic cells is poorly understood. We therefore investigated the effects of glutamine on the proliferation, differentiation, and cell-matrix interactions of two human colon carcinoma cell lines (Caco-2 and SW620) adapted to glutamine-free media. Doubling times were calculated by logarithmic transformation of serial cell counts. Alkaline phosphatase, cathepsin C (dipeptidyl peptidase), lactase, and isomaltase expression (markers of differentiation) were assayed by digestion of synthetic substrates. Adhesion to matrix proteins was assessed by colorimetric quantitation of toluidine blue staining of adherent cells. Surface expression of Caco-2 receptors for matrix proteins (integrins) was studied by biotinylation and immunoprecipitation with specific antibodies. Glutamine (1-10 mm) dose-dependently stimulated Caco-2 proliferation on all matrices studied ...
The UC Davis Clinical and Translational Science Center (CTSC) and the wide array of services that have supported innovative biomedical research and led to the development of new treatments for diseases during the past 10 years will continue, thanks to a $27.8 million grant from the National Center for Accelerating Translational Science and the ongoing support from the School of Medicine.
Apoptose er programmert celledød for å fjerne uønskede celler og er en felles egenskap for alle flercellede organismer. Caspase-3 er involvert i intracellulære signalkaskader ved apoptose. En ubalanse i regulering av apoptose kan føre til kreftutvikling. Apoptose spiller en viktig rolle i flere andre sykdommer som immunologisk, iskemiske, og nevrodegenerative sykdommer. For å undersøke betydningen av proteasen legumain og proteaseinhibitoren cystatin E/M for caspase-3 aktivitet, ble det brukt HEK293 (normale kontroll celler), M38L (overutrykker legumain) og M4C (overutrykker cystatin E/M) celler. Cellene ble stimulert med dødsstimulerende stoffer som staurosporin og Leu-Leu-OMe. Staurosporin er kjent for å være en kinasehemmer. Leu-Leu-OMe øker lysosomal membranpermeabilitet. Proteaser som er involvert i apoptose vil dermed frigjøres fra lysosomer til cytosol. Legumain som befinner seg i lysosomene, kan frigjøres til cytosol og dermed påvirke aktiviteten av caspase-3 eller andre ...
Cathepsin B is an enzymatic protein belonging to the peptidase (or protease) families. In humans, it is coded by the CTSB gene. The protein encoded by this gene is a lysosomal cysteine protease composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. It is a member of the peptidase C1 family. At least five transcript variants encoding the same protein have been found for this gene.
Complexes of gold( I) have long been used to treat rheumatoid arthritis although the precise biological targets of gold are not well understood. One intriguing therapeutic target of Au( I) is the cathepsin family of lysosomal cysteine proteases. Here, we present the inhibition of cathepsin B by a known Au( I)-based drug and a series of derivatives. The complexes investigated were reversible, competitive inhibitors with IC50 values ranging from 0.3 to 250 mu M, depending on the substituents around the Au( I). ...
Dipeptidyl-peptidase 3 is an enzyme that in humans is encoded by the DPP3 gene. This gene encodes a protein that is a member of the S9B family in clan SC of the serine proteases. This cytoplasmic protein binds a single zinc ion with its zinc-binding motif (HELLGH) and has post-proline dipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from the N-termini of proteins. Increased activity of this protein is associated with endometrial and ovarian cancers. Alternate transcriptional splice variants have been characterized. GRCh38: Ensembl release 89: ENSG00000254986 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000063904 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse PubMed Reference:". Fukasawa KM, Fukasawa K, Harada M (Jun 2000). "Assignment of the dipeptidyl peptidase III gene (DPP3) to human chromosome 11 band q12→q13.1 by in situ hybridization". Cytogenet Cell Genet. 88 (1-2): 99-100. doi:10.1159/000015498. PMID 10773679. "Entrez Gene: DPP3 dipeptidyl-peptidase ...
YSCH2B1 J01327 M25040 M25041 V01307 607bp ds-DNA PLN 23-AUG-1994 Yeast (S.cerevisiae) histone H2B-1 gene. histone; histone H2B. YSCH2B2 J01328 V01308 589bp ds-DNA PLN 23-AUG-1994 Yeast (S.cerevisiae) histone H2B-2 gene. histone; histone H2B. YSCLTG3 D16304 1779bp ds-DNA PLN 24-AUG-1994 Yeast LTG3 gene. . YSCSTEYCI L21944 3136bp ds-DNA PLN 23-AUG-1994 Saccharomyces cerevisiae dipeptidyl aminopeptidase (STE13 or YCI1) gene, complete cds. dipeptidyl aminopeptidase ...
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CD26 antibody [M-A261] (dipeptidyl peptidase 4) for FACS, IHC-Fr, IP. Anti-CD26 mAb (GTX74879) is tested in Human samples. 100% Ab-Assurance.
Human CTSB full-length ORF (NP_001899.1, 1 a.a. - 339 a.a.) recombinant protein with GST-tag at N-terminal. (H00001508-P02) - Products - Abnova
TY - JOUR. T1 - Increased muscle proteolysis after local trauma mainly reflects macrophage-associated lysosomal proteolysis. AU - Farges, M C AU - Balcerzak, Denis Pierre. AU - Fisher, B D AU - Attaix, D AU - Bechet, D AU - Ferrara, M AU - Baracos, V E PY - 2002/2. Y1 - 2002/2. N2 - Rat gastrocnemius showed increased protein degradation (+75-115%) at 48 h after traumatic injury. Injured muscle showed increased cathepsin B activity (+327%) and mRNA encoding cathepsin B (+670%), cathepsin L (+298%), cathepsin H (+159%), and cathepsin C (+268%). In in situ hybridization, cathepsin B mRNA localized to the mononuclear cell infiltrate in injured muscle, and only background levels of hybridization were observed either over muscle cells in injured tissue or in uninjured muscle. Immunogold/electron microscopy showed specific staining for cathepsin B only in lysosome-like structures in cells of the mononuclear cell infiltrate in injured muscle. Muscle cells were uniformly negative in the ...
The Center for Sudden Unexpected Death in Epilepsy (SUDEP) Research seeks novel pilot projects in human SUDEP Research that will address the goal of understanding its pathophysiology.. In collaboration with the Center for SUDEP Research (CSR), the Clinical and Translational Science Collaborative (CTSC) will grant funding for this the one-year CSR-themed pilot grant award.. One $25,000 grant will be awarded. In addition, $10,000 is available for the use of one CTSC Core per pilot grant award when used in support of the primary grant.. The primary investigator is required to be a full-time CWRU faculty member with a primary appointment at Case Western Reserve University, University Hospitals Case Medical Center or the Louis Stokes VA Medical Center.. The application must be received by Friday, April 28, at 11:59 p.m. to be considered for review. Any applications received after this deadline will not be reviewed.. Learn more about the requirements and application process at ...
The presence of DPPII (dipeptidyl peptidase II; E.C. 3.4.14.2) has been demonstrated in various mammalian tissues. However, a profound molecular and catalytic characterization, including substrate selectivity, kinetics and pH-dependence, has not been conducted. In the present study, DPPII was purified from human seminal plasma to apparent homogeneity with a high yield (40%) purification scheme, including an inhibitor-based affinity chromatographic step. The inhibitor lysyl-piperidide (Ki~0.9 μM at pH 5.5) was chosen, as it provided a favourable affinity/recovery ratio. The human enzyme appeared as a 120 kDa homodimer. Mass spectrometric analysis after tryptic digestion together with a kinetic comparison indicate strongly its identity with QPP (quiescent cell proline dipeptidase), also called dipeptidyl peptidase 7. pH profiles of both kcat and kcat/Km clearly demonstrated that DPPII/QPP possesses an acidic and not a neutral optimum as was reported for QPP. Kinetic parameters of the human ...
Purpose: The olfm1 gene encodes a secreted glycoprotein highly conserved in vertebrates. There are two olfm1 genes in zebrafish, olfm1a and olfm1b. Both of these genes are expressed in the brain and retina starting from 16 h post fertilization to adults. We generated a null mutant of both olfm1a and olfm1b genes and analyzed its retinal structure and visual function.. Methods: Olfm1a and olfm1b mutant alleles with nonsense point mutations were obtained from the Wellcome Trust Sanger Institute. Olfm1a and olfm1b null mutants were bred to generate double null mutant (olfm1a/b null). Spontaneous movement, optokinetic and optomotor responses, behavioral responses to light increments and decrements and electroretinogram (ERG) to increased (ON) and decreased (OFF) illumination were compared between olfm1a/b null and wild-type larvae 7 days post fertilization (dpf). The retinal morphology was examined by immunostaining of frozen sections. Total RNA was isolated from 3 and 7 dpf larvae for RNA ...
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 ...
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Lamin A/C gene (LMNA) associated cardiomyopathy is a form of dilated cardiomyopathy with poor prognosis and high mortality, and a rapid evolution toward end-stage heart failure and malignant ventricular arrhythmias associated with increased risk of sudden cardiac death. It is transmitted in a autosomal dominant manner and is characterized by age-dependent high penetrance and variable expression. Screening of first degree relatives of proband patients by means of clinical evaluation, electrocardiogram, echocardiography and genetic analysis is useful for the early diagnosis of the disease. Drug therapy and non-pharmacological measures in the early stages of the disease seem to improve the prognosis of these patients.. ...
The Community-Based Clinical Research Centers are supported by the William T. Dahms, MD Clinical Research Unit (DCRU) and utilize the research network of the Cleveland Clinical & Translational Science Collaborative of Cleveland (CTSC), UL1TR000439, from the National Center of Advancing Translational Sciences (NCATS) component of the National Institutes of Health, to expand clinical/translational research resources available to both academic and community-based research programs. The Dahms Clinical Research Unit is a joint effort with the Case Western Reserve University School of Medicine ...
Fibroblast Activation Protein (FAP) is a cellXsurface anchored dimeric protease, closely related to Dipeptidyl Peptidase (DPP) 4. This atypical serine protease has both dipeptidyl peptidase and endopeptidase activities, cleaving substrates at a postXproline bond. FAP expression is difficult to detect in nonXdiseased adult organs, but is greatly up regulated in sites of tissue remodelling, which includes liver fibrosis, lung fibrosis, atherosclerosis, arthritis, tumours and embryonic tissues. Due to its restricted expression pattern and dual enzymatic activities, FAP is emerging as a unique therapeutic target. However, methods to exploit and target this protease are advancing more rapidly than knowledge of the fundamental biology of FAP. This thesis aims to rectify this imbalance, emphasising the need to better define the substrate repertoire and downstream effects of FAP enzyme activity to elucidate the role of this protease in biological and pathological processes. In this study, primary mouse ...
This unit describes an assay for the direct and selective detection of the four cathepsins B, H, K, and L in adherently growing cells
Inhibition of dipeptidyl peptidase IV is a promising new approach for the treatment of type 2 diabetes. The dipeptidyl peptidase IV inhibitor LAF237 preven
... is a comprehensive digestive enzyme formula containing all the necessary digestive enzymes including dipeptidyl peptidase IV (DPP-IV), lactase and alpha-galactosidase that assist in the proper digestion of proteins, fats, starch, dairy, and glut
... is a comprehensive digestive enzyme formula containing all the necessary digestive enzymes including dipeptidyl peptidase IV (DPP-IV), lactase and alpha-galactosidase that assist in the proper digestion of proteins, fats, starch, dairy, and glut
Monoclonal antibodies to dipeptidyl aminopeptidase IV (DAP IV, EC 3.4.14.5) were raised and selectively applied to paraffin-embedded sections of thyroid carcinoma. Five monoclonal antibodies were found to stain paraffin sections of thyroid carcinomas. Using one of these antibodies (44-4), we studied retrospectively aberrant expression of DAP IV in thyroid carcinoma to determine whether immunohistochemical staining with DAP IV antibody is useful in pathological diagnosis.. In almost all cases of thyroid follicular and papillary carcinoma, tumour cells were positive (99.0 per cent) with DAP IV, whereas the cases of follicular adenoma showed a low incidence (27.1 per cent) of positive staining. Follicular adenoma with incomplete capsular invasion had a higher positive incidence (50 per cent) than follicular adenoma without incomplete capsular invasion (9.6 per cent).. In positive staining cases previously diagnosed as benign tumours, 11 benign cases reacting positively with DAP IV were rediagnosed ...
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IUID of items is accomplished by marking each qualifying item with a permanent 2-dimensional data matrix. The data matrix is encoded with the data elements necessary to construct a Unique Item Identifier (UII) which is globally unique and unambiguous. The data elements required to form a UII include the manufacturers identification (i.e. cage code) and the items serial number. If the manufacturer serializes within part number, that data element will also be encoded.. Because the data matrix is machine-readable, IUID marking greatly reduces human error and improves the accuracy of inventory and acquisition records.. UIIs are stored in comprehensive IUID Registry, which allows easy access to information such as acquisition cost and life-cycle data. The IUID Registry is maintained by the Defense Logistics Information Service (DLIS).. Every IUID delivery includes the required data elements describing the end item and the "pedigree" of embedded items. This data is captured during the acceptance ...
Results In Caco-2 cells an ∼ 18-fold increase (p,0.0001) in DP IV protein expression was seen after incubation with TNFα at a concentration of 25 ng/μl for 48 h, as compared to untreated cells. This change is mirrored at the mRNA level with a twofold increase in DP IV expression at similar TNFα concentration and time course. Similar changes were noted in human tissue with a significant 4.5-fold DP IV upregulation (p=0.02) in CD compared to normal controls. However, results at the protein level in human tissue showed an opposite trend, with a ∼2.7-fold decrease in DP IV expression in CD tissue compared to controls (p=0.05). The highest DP IV fasting plasma levels were noted in the control group (558.5±39.98 ng/ml). Levels in CD were significantly less (p=0.0028) both in large bowel CD (406.2±48.10 ng/ml) and more so in the small bowel CD group (361.3±38.83 ng/ml; p,0.01). There was no significant difference in plasma DP IV between active and inactive disease.. ...
This page includes the following topics and synonyms: Gliptin, DPP-4 Inhibitor, Dipeptidyl Peptidase-4 Inhibitor, Dipeptidyl-Peptidase IV Inhibitor, DPP-4, Sitagliptin, Januvia, Saxagliptin, Onglyza, Linagliptin, Tradjenta, Alogliptin, Nesina.
This page includes the following topics and synonyms: Gliptin, DPP-4 Inhibitor, Dipeptidyl Peptidase-4 Inhibitor, Dipeptidyl-Peptidase IV Inhibitor, DPP-4, Sitagliptin, Januvia, Saxagliptin, Onglyza, Linagliptin, Tradjenta, Alogliptin, Nesina.
Abcam provides specific protocols for Cathepsin H overexpression 293T lysate (whole cell) (ab94088) : Transfected Lysate Preparation Notes
2BGN: Crystal Structures of HIV-1 Tat-Derived Nonapeptides Tat-(1-9) and Trp2-Tat-(1-9) Bound to the Active Site of Dipeptidyl-Peptidase Iv (Cd26)
TY - JOUR. T1 - N-terminal His(7)-modification of glucagon-like peptide-1(7-36) amide generates dipeptidyl peptidase IV-stable analogues with potent antihyperglycaemic activity. AU - Green, BD. AU - Mooney, MH. AU - Gault, Victor. AU - Irwin, Nigel. AU - Bailey, CJ. AU - Harriott, P. AU - Greer, B. AU - OHarte, Finbarr. AU - Flatt, Peter. PY - 2004/3. Y1 - 2004/3. N2 - Glucagon-like peptide-1(7-36)amide (GLP-1) possesses several unique and beneficial effects for the potential treatment of type 2 diabetes. However, the rapid in-activation of GLP-1 by dipeptidyl peptidase IV (DPP IV) results in a short half-life in vivo (less than 2 min) hindering therapeutic development. In the present study, a novel His(7)-modified analogue of GLP-1, N-pyroglutamyl-GLP-1, as well as N-acetyl-GLP-1 were synthesised and tested for DPP IV stability and biological activity. Incubation of GLP-1 with either DPP IV or human plasma resulted in rapid degradation of native GLP-1 to GLP-1 (9-36),amide, while ...
l-Asparaginase is a key therapeutic agent for treatment of childhood acute lymphoblastic leukemia (ALL). There is wide individual variation in pharmacokinetics, and little is known about its metabolism. The mechanisms of therapeutic failure with l-asparaginase remain speculative. Here, we now report that 2 lysosomal cysteine proteases present in lymphoblasts are able to degrade l-asparaginase. Cathepsin B (CTSB), which is produced constitutively by normal and leukemic cells, degraded asparaginase produced by Escherichia coli (ASNase) and Erwinia chrysanthemi. Asparaginyl endopeptidase (AEP), which is overexpressed predominantly in high-risk subsets of ALL, specifically degraded ASNase. AEP thereby destroys ASNase activity and may also potentiate antigen processing, leading to allergic reactions. Using AEP-mediated cleavage sequences, we modeled the effects of the protease on ASNase and created a number of recombinant ASNase products. The N24 residue on the flexible active loop was identified as ...
Dipeptidyl peptidase IV is a glycoprotein which removes N-terminal dipeptides from physiologically relevant polypeptides. An homologous series of...
The Community-Based Clinical Research Centers are supported by the William T. Dahms, MD Clinical Research Unit (DCRU) and utilize the research network of the Cleveland Clinical & Translational Science Collaborative of Cleveland (CTSC), UL1TR000439, from the National Center of Advancing Translational Sciences (NCATS) component of the National Institutes of Health, to expand clinical/translational research resources available to both academic and community-based research programs. The Dahms Clinical Research Unit is a joint effort with the Case Western Reserve University School of Medicine ...
Affiliation:日本歯科大学,生命歯学部,教授, Research Field:Morphological basic dentistry,Morphological basic dentistry,Bacteriology (including Mycology),Social dentistry, Keywords:シアル酸,Streptococcus gordonii,口腔レンサ球菌,遺伝子クローニング,DPPIV,感染症,Porphyromonas gingivalis,感染性心内膜炎,dipeptidyl aminopeptidase IV,virulence, # of Research Projects:8, # of Research Products:34, Ongoing Project:免疫抑制剤服用小児における歯肉増殖症の発症メカニズムの解明と予防プロトコルの確立
Gentaur molecular products has all kinds of products like :search , Assaypro \ Cathepsin G, anti_human \ 11654-05021 for more molecular products just contact us
Patients, Treatment, B-cell, Cell, Lymphomas, B-cells, Cells, Cells, Epithelial, Dipeptidyl Peptidase Iv, Diseases, Endothelial Cells, Flow Cytometry, Future, Multiple Myelomas, Plays, Role, Therapeutic, Time, Tissues, Follicular Lymphoma
The cytotoxic cell granule secretory pathway is essential for immune defence. How the pore-forming protein perforin (PFN) facilitates the cytosolic delivery of granule-associated proteases (granzymes) remains enigmatic. Here we show that PFN is able to induce invaginations and formation of complete ...
**9.5367431640625E-7**

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 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
**1.0593159198761**
**1.0595169067383**
  • The microtiter plate provided in this kit has been pre-coated with an antibody specific to Cathepsin Z (CTSZ). (biobool.com)
  • Standards or samples are then added to the appropriate microtiter plate wells with a biotin-conjugated antibody specific to Cathepsin Z (CTSZ). (biobool.com)
  • The concentration of Cathepsin Z (CTSZ) in the samples is then determined by comparing the O.D. of the samples to the standard curve. (biobool.com)
  • These results suggest that the ecdysone response elements are vital for activation of the promoter by 20-hydroxyecdysone (20E) in the larval fat body and further support the crucial role of ecdysone signaling to control cathepsin D gene transcription. (antibodies-online.com)
  • Schwartz-Roberts, Shajahan, Cook, Wärri, Abu-Asab, Clarke: GX15-070 (obatoclax) induces apoptosis and inhibits cathepsin D- and L-mediated autophagosomal lysis in antiestrogen-resistant breast cancer cells. (antibodies-online.com)
  • The requirement for cathepsin L proteolysis identifies a previously uncharacterized class of inhibitor for SARS-CoV infection. (pnas.org)
  • To test this, we used an immunocompetent endometriosis mouse model and found that endometriotic lesions exhibited a greater than 5-fold increase in active cathepsins compared to tissue from peritoneal wall or eutopic endometrium, with cathepsins L and K specifically implicated. (nih.gov)
  • Human endometriosis lesions also exhibited greater cathepsin activity than adjacent peritoneum tissue, supporting the mouse results. (nih.gov)
  • Platt's long-term research has focused on cathepsins, including the development of sensitive tools and assays to quantify their activity in cells and tissue, as well as potential diagnostic applications for breast, lung and cervical cancer. (innovations-report.com)
  • IHC image of Cathepsin D staining in Human Lung formalin fixed paraffin embedded tissue section, performed on a Leica Bond™ system using the standard protocol F. The section was pre-treated using heat mediated antigen retrieval with sodium citrate buffer (pH6, epitope retrieval solution 1) for 20 mins. (abcam.com)
  • Cathepsin L-deficient mice were shown to have less adipose tissue, lower serum glucose and insulin levels, more insulin receptor subunits, more glucose transporter (GLUT4) and more fibronectin than wild type controls. (wikipedia.org)
  • Keilová, H.: On the specificity and inhibition of cathepsins D and B. In: Tissue proteinases, ed. by A. J. Barrett and J. T. Dingle, p. 45-65. (springer.com)
  • Our results are consistent with a model in which SARS-CoV employs a unique three-step method for membrane fusion, involving receptor-binding and induced conformational changes in S glycoprotein followed by cathepsin L (CTSL) proteolysis and activation of membrane fusion within endosomes. (pnas.org)
  • Because cathepsins have harmful effects on critical proteins such as collagen and elastin, pharmaceutical companies have been developing drugs to inhibit activity of the enzymes, but so far these compounds have had too many side effects to be useful and have failed clinical trials. (innovations-report.com)
  • Determination of cathepsin V activity and intracellular trafficking by N-glycosylation. (nih.gov)
  • E-64 blocks all cathepsin proteolytic activity in murine endometriotic lesions. (nih.gov)
  • Mouse endometriotic lesions exhibit elevated cathepsin proteolytic activity. (nih.gov)
  • Cathepsin-D is an aspartic protease that depends critically on protonation of its active site Asp residue. (wikipedia.org)
  • A significantly elevated cathepsin S expression in gingival biopsies from rats with experimental periodontitis was found in vivo , as compared to that from control. (hindawi.com)
  • Gingival biopsies from periodontitis patients showed a significantly higher cathepsin S expression than those from healthy gingiva. (hindawi.com)
  • Cathepsin D enzymatic activity induces hydrolytic modification of apolipoprotein B-100-containing lipoproteins, including LDL, which means it may be involved in atherosclerosis as well. (wikipedia.org)
  • Cathepsin D (an aspartyl protease) appears to cleave a variety of substrates such as fibronectin and laminin. (wikipedia.org)
  • Along with Asp-protonation, lower pH also leads to conformational switch in cathepsin-D : the N-terminal segment of the protease moves out of the active site as pH drops. (wikipedia.org)