A lysosomal cysteine proteinase with a specificity similar to that of PAPAIN. The enzyme is present in a variety of tissues and is important in many physiological and pathological processes. In pathology, cathepsin B has been found to be involved in DEMYELINATION; EMPHYSEMA; RHEUMATOID ARTHRITIS, and NEOPLASM INVASIVENESS.
A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.
A ubiquitously-expressed cysteine protease that plays an enzymatic role in POST-TRANSLATIONAL PROTEIN PROCESSING of proteins within SECRETORY GRANULES.
An intracellular proteinase found in a variety of tissue. It has specificity similar to but narrower than that of pepsin A. The enzyme is involved in catabolism of cartilage and connective tissue. EC 3.4.23.5. (Formerly EC 3.4.4.23).
An ubiquitously-expressed lysosomal cysteine protease that is involved in protein processing. The enzyme has both endopeptidase and aminopeptidase activities.
A cysteine protease that is highly expressed in OSTEOCLASTS and plays an essential role in BONE RESORPTION as a potent EXTRACELLULAR MATRIX-degrading enzyme.
A serine protease found in the azurophil granules of NEUTROPHILS. It has an enzyme specificity similar to that of chymotrypsin C.
An aspartic endopeptidase that is similar in structure to CATHEPSIN D. It is found primarily in the cells of the immune system where it may play a role in processing of CELL SURFACE ANTIGENS.
A papain-like cysteine protease that has specificity for amino terminal dipeptides. The enzyme plays a role in the activation of several pro-inflammatory serine proteases by removal of their aminoterminal inhibitory dipeptides. Genetic mutations that cause loss of cathepsin C activity in humans are associated with PAPILLON-LEFEVRE DISEASE.
ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.
A lysosomal papain-related cysteine proteinase that is expressed in a broad variety of cell types.
A homologous group of endogenous CYSTEINE PROTEINASE INHIBITORS. The cystatins inhibit most CYSTEINE ENDOPEPTIDASES such as PAPAIN, and other peptidases which have a sulfhydryl group at the active site.
A class of morphologically heterogeneous cytoplasmic particles in animal and plant tissues characterized by their content of hydrolytic enzymes and the structure-linked latency of these enzymes. The intracellular functions of lysosomes depend on their lytic potential. The single unit membrane of the lysosome acts as a barrier between the enzymes enclosed in the lysosome and the external substrate. The activity of the enzymes contained in lysosomes is limited or nil unless the vesicle in which they are enclosed is ruptured. Such rupture is supposed to be under metabolic (hormonal) control. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)
A 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.
Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.
Diazomethane is an extremely hazardous and unstable organic compound, (CH2)N=N=O, with a methane substituted diazo group, that is highly explosive when heated, shocked or contaminated, and used as a powerful methylating agent in chemical syntheses, but its production and handling require special expertise and equipment due to the high risks involved.
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
Peptides composed of two amino acid units.
A cytastin subtype found at high levels in the SKIN and in BLOOD CELLS. Cystatin A incorporates into the cornified cell envelope of stratified squamous epithelial cells and may play a role in bacteriostatic properties of skin.
A 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.
An intracellular cystatin subtype that is found in a broad variety of cell types. It is a cytosolic enzyme inhibitor that protects the cell against the proteolytic action of lysosomal enzymes such as CATHEPSINS.
A proteolytic enzyme obtained from Carica papaya. It is also the name used for a purified mixture of papain and CHYMOPAPAIN that is used as a topical enzymatic debriding agent. EC 3.4.22.2.
An enzyme substrate which permits the measurement of peptide hydrolase activity, e.g. trypsin and thrombin. The enzymes liberate 2-naphthylamine, which is measured by colorimetric procedures.
N-acylated oligopeptides isolated from culture filtrates of Actinomycetes, which act specifically to inhibit acid proteases such as pepsin and renin.
Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).
A subclass of peptide hydrolases that depend on a CYSTEINE residue for their activity.
A carboxypeptidase that catalyzes the release of a C-terminal amino acid with a broad specificity. It also plays a role in the LYSOSOMES by protecting BETA-GALACTOSIDASE and NEURAMINIDASE from degradation. It was formerly classified as EC 3.4.12.1 and EC 3.4.21.13.
Physiologically inactive substances that can be converted to active enzymes.
An extracellular cystatin subtype that is abundantly expressed in bodily fluids. It may play a role in the inhibition of interstitial CYSTEINE PROTEASES.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
A sub-class of PEPTIDE HYDROLASES that act only near the ends of polypeptide chains.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.
The inactive proenzyme of trypsin secreted by the pancreas, activated in the duodenum via cleavage by enteropeptidase. (Stedman, 25th ed)
A protease of broad specificity, obtained from dried pancreas. Molecular weight is approximately 25,000. The enzyme breaks down elastin, the specific protein of elastic fibers, and digests other proteins such as fibrin, hemoglobin, and albumin. EC 3.4.21.36.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
The process of cleaving a chemical compound by the addition of a molecule of water.
The rate dynamics in chemical or physical systems.
An essential branched-chain amino acid important for hemoglobin formation.
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.
An extracellular receptor specific for UROKINASE-TYPE PLASMINOGEN ACTIVATOR. It is attached to the cell membrane via a GLYCOSYLPHOSPHATIDYLINOSITOL LINKAGE and plays a role in the co-localization of urokinase-type plasminogen activator with PLASMINOGEN.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.
Peptides composed of between two and twelve amino acids.
A reagent used for the determination of iron.
A species of helminth commonly called the sheep liver fluke. It occurs in the biliary passages, liver, and gallbladder during various stages of development. Snails and aquatic vegetation are the intermediate hosts. Occasionally seen in man, it is most common in sheep and cattle.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.

Activation of Xenopus eggs by proteases: possible involvement of a sperm protease in fertilization. (1/980)

Egg activation in cross-fertilization between Xenopus eggs and Cynops sperm may be caused by a protease activity against Boc-Gly-Arg-Arg-MCA in the sperm acrosome. To determine the role of the sperm protease in fertilization, the protease was purified from Cynops sperm using several chromatographic techniques. We found that purified sperm protease readily hydrolyzes Boc-Gly-Arg-Arg-MCA and Z-Arg-Arg-MCA, that protease activity was inhibited by the trypsin inhibitors aprotinin and leupeptin, and that not only the purified protease, but also cathepsin B, induces activation in Xenopus eggs. We inseminated unfertilized Xenopus eggs with homologous sperm in the presence of various peptidyl MCA substrates or protease inhibitors and demonstrated that trypsin inhibitors or MCA substrates containing Arg-Arg-MCA reversibly inhibited fertilization of both fully jellied and denuded eggs. Sperm motility was not affected by the reagents. An extract obtained from Xenopus sperm showed hydrolytic activity against Boc-Gly-Arg-Arg-MCA, Z-Arg-Arg-MCA, and Arg-MCA. These results suggest that the tryptic protease in Xenopus sperm is involved in fertilization, most likely by participating in egg activation.  (+info)

Cathepsin B immunohistochemical staining in tumor and endothelial cells is a new prognostic factor for survival in patients with brain tumors. (2/980)

The cysteine endopeptidase, cathepsin (Cat) B, and its endogenous inhibitor, stefin A, were found relevant for cancer progression of many neoplasms, including human brain tumors. Histological sections of 100 primary brain tumors, 27 benign and 73 malignant, were stained immunohistochemically for Cat B and stefin A. The immunohistochemical staining of Cat B in tumor cells, endothelial cells, and macrophages was scored separately from 0-12. The score in tumor and endothelial cells was significantly higher in malignant tumors compared with benign tumors (P<0.000). A significant correlation between immunostaining of Cat B (scored together for tumor and endothelial cells) and clinical parameters, such as duration of symptoms, Karnofsky score, psycho-organic symptoms, and histological score was demonstrated. Univariate survival analysis indicated that total Cat B score above 8 was a significant predictor for shorter overall survival (P = 0.003). In glioblastoma multiforme, intense Cat B staining of endothelial cells was a significant predictor for shorter survival (P = 0.003). Stefin A immunostaining was weak and detected only in a few benign and some malignant tumors, suggesting that this inhibitor alone is not sufficient in balancing proteolytic activity of Cat B. We conclude that specific immunostaining of Cat B in tumor and endothelial cells can be used to predict the risk of death in patients with primary tumors of the central nervous system.  (+info)

Expression and alteration of the S2 subsite of the Leishmania major cathepsin B-like cysteine protease. (3/980)

The mature form of the cathepsin B-like protease of Leishmania major (LmajcatB) is a 243 amino acid protein belonging to the papain family of cysteine proteases and is 54% identical to human-liver cathepsin B. Despite the high identity and structural similarity with cathepsin B, LmajcatB does not readily hydrolyse benzyloxycarbonyl-Arg-Arg-7-amino-4-methyl coumarin (Z-Arg-Arg-AMC), which is cleaved by cathepsin B enzymes. It does, however, hydrolyse Z-Phe-Arg-AMC, a substrate typically cleaved by cathepsin L and B enzymes. Based upon computer generated protein models of LmajcatB and mammalian cathepsin B, it was predicted that this variation in substrate specificity was attributed to Gly234 at the S2 subsite of LmajcatB, which forms a larger, more hydrophobic pocket compared with mammalian cathepsin B. To test this hypothesis, recombinant LmajcatB was expressed in the Pichia pastoris yeast expression system. The quality of the recombinant enzyme was confirmed by kinetic characterization, N-terminal sequencing, and Western blot analysis. Alteration of Gly234 to Glu, which is found at the corresponding site in mammalian cathepsin B, increased recombinant LmajcatB (rLmajcatB) activity toward Z-Arg-Arg-AMC 8-fold over the wild-type recombinant enzyme (kcat/Km=3740+/-413 M-1.s-1 versus 472+/-72.4 M-1.s-1). The results of inhibition assays of rLmajcatB with an inhibitor of cathepsin L enzymes, K11002 (morpholine urea-Phe-homoPhe-vinylsulphonylphenyl, kinact/Ki=208200+/-36000 M-1. s-1), and a cathepsin B specific inhibitor, CA074 [N-(L-3-trans-propylcarbamoyloxirane-2-carbonyl)-l-isoleucyl-l- prolin e, kinact/Ki=199200+/-32900 M-1.s-1], support the findings that this protozoan protease has the P2 specificity of cathepsin L-like enzymes while retaining structural homology to mammalian cathepsin B.  (+info)

Kappa light chain-associated Fanconi's syndrome: molecular analysis of monoclonal immunoglobulin light chains from patients with and without intracellular crystals. (4/980)

Plasma cell dyscrasias may be responsible for Fanconi's syndrome, due to the toxicity of a free monoclonal kappa light chain toward kidney proximal tubules. Eight cases of Fanconi's syndrome were analyzed. We compared the structures of VkappaI variability subgroup V domains from five cases of Fanconi's syndrome and one myeloma without renal involvement. Among Fanconi cases, four putative structures were obtained after molecular modeling by homology, and the other had previously been refined by X-ray crystallography. The complete sequences of one VkappaI, one VkappaIII and N-terminal sequences of two VkappaI light chains, from patients with different forms of Fanconi's syndrome, were compared with four previously studied sequences. All three kappa chains responsible for a 'classical' form with intralysosomal crystals and a low mass myeloma, were encoded by the LCO2/O12 germline gene and had an unusual non-polar residue exposed to the solvent in the CDR-L1 loop. Of both VkappaI light chains from patients with Fanconi's syndrome without intracellular crystals, one derived from LCO2/O12 and the other from LCO8/O18 gene. Another feature that could be related to non-crystallization was the absence of accessible side chains in the CDR-L3 loop which is known to be implicated in dimer formation.  (+info)

Collagenase, cathepsin B and cathepsin L gene expression in the synovial membrane of patients with early inflammatory arthritis. (5/980)

OBJECTIVE: To examine the expression of the matrix metalloproteinase, MMP-1, and the cysteine proteases, cathepsin B (CB) and cathepsin L (CL), in the synovial membrane (SM) of patients with early inflammatory arthritis. METHODS: Samples of SM were obtained by blind needle biopsy or needle arthroscopy from inflamed knees of 28 patients with early inflammatory arthritis (mean disease duration 10.2 months, range 2 weeks-18 months). Sixteen patients had rheumatoid arthritis (RA), nine psoriatic arthritis and there was one each with ankylosing spondylitis, gout and an undifferentiated arthritis. Comparison was made with tissue from two patients with established erosive RA and three normal synovial tissue samples. In situ hybridization was performed using digoxigenin-labelled RNA probes. RESULTS: MMP-1, CB and CL were expressed in all patients with early arthritis and in established erosive RA, whereas normal synovium showed only scanty expression. The three proteases were prominent in perivascular infiltrates and endothelial cells of early arthritis tissue. MMP-1 was observed primarily in the lining layer, but was also evident in the sublining area. CB and CL were expressed to a lesser extent in the lining layer, and were present mainly in the subintima. The three proteases were not found in lymphoid aggregrates. No differences were observed between the disease categories. CONCLUSIONS: The detection of MMP-1, CB and CL in the synovium shortly after symptom onset implies that the potential for joint destruction exists at a very early stage in the disease. In addition, the perivascular and endothelial cell expression suggests a role for these proteases in mononuclear cell influx to the inflamed synovium and in angiogenesis.  (+info)

Antigen secreted from noncytosolic Listeria monocytogenes is processed by the classical MHC class I processing pathway. (6/980)

Intracellular bacteria can reside in a vacuolar compartment, or they can escape the vacuole and become free living in the cytoplasm. The presentation of Ag by class I MHC molecules has been defined primarily for Ag present in the cytoplasm. It was therefore thought that Ags from bacteria that remain in a vacuole would not be presented by MHC class I molecules. Although some studies have provided data to support this idea, it is not necessarily true for all intracellular bacteria. For example, we have previously demonstrated that an epitope from the p60 protein secreted by LLO- Listeria monocytogenes, which does not reside in the cytoplasm, can be presented by MHC class I molecules to a T cell clone specific for the epitope, p60217-225. We have further examined the route by which Ag secreted by LLO- L. monocytogenes is presented by MHC class I molecules. Using pharmacological inhibitors, we demonstrate that MHC class I presentation of the p60 epitope derived from by LLO- L. monocytogenes requires phagolysosome fusion and processing by the proteasome. Lysosomal cathepsins, however, are not required for processing of the p60 epitope. Similarly, processing of the AttM epitope, secreted by LLO- L. monocytogenes and presented by H2-M3, also requires phagolysosome fusion and cleavage by the proteasome. Thus, p60 and AttM secreted by LLO- L. monocytogenes are processed via the classical class I pathway for presentation by MHC class I molecules.  (+info)

The affinity and kinetics of inhibition of cysteine proteinases by intact recombinant bovine cystatin C. (7/980)

Recent studies have shown that the bovine cysteine proteinase inhibitor, cystatin C, is synthesized as a preprotein containing a 118-residue mature protein. However, the forms of the inhibitor isolated previously from bovine tissues had shorter N-terminal regions than expected from these results, and also lower affinity for proteinases than human cystatin C. In this work, we report the properties of recombinant, full-length bovine cystatin C having a complete N-terminal region. The general characteristics of this form of the inhibitor, as reflected by the isoelectric point, the far-ultraviolet circular dichroism spectrum, the thermal stability and the changes of tryptophan fluorescence on interaction with papain, resembled those of human cystatin C. The affinity and kinetics of inhibition of papain and cathepsins B, H and L by the bovine inhibitor were also comparable with those of the human inhibitor, although certain differences were apparent. Notably, the affinity of bovine cystatin C for cathepsin H was somewhat weaker than that of human cystatin C, and bovine cystatin C bound to cathepsin L with about a four-fold higher association rate constant than the human inhibitor. This rate constant is comparable with the highest values reported previously for cystatin-cysteine proteinase reactions. The full-length, recombinant bovine cystatin C bound appreciably more tightly to proteinases than the shorter form characterized previously. Digestion of the recombinant inhibitor with neutrophil elastase resulted in forms with truncated N-terminal regions and appreciably decreased affinity for papain, consistent with the forms of bovine cystatin C isolated previously having arisen by proteolytic cleavage of a mature, full-length inhibitor.  (+info)

Accumulation of sialic acid in endocytic compartments interferes with the formation of mature lysosomes. Impaired proteolytic processing of cathepsin B in fibroblasts of patients with lysosomal sialic acid storage disease. (8/980)

The impact of an altered endocytic environment on the biogenesis of lysosomes was studied in fibroblasts of patients suffering from sialic acid storage disease (SASD). This inherited disorder is characterized by the accumulation of acidic monosaccharides in lysosomal compartments and a concomitant decrease of their buoyant density. We demonstrate that C-terminal trimming of the lysosomal cysteine proteinase cathepsin B is inhibited in SASD fibroblasts. This late event in the biosynthesis of cathepsin B normally takes place in mature lysosomes, suggesting an impaired biogenesis of these organelles in SASD cells. When normal fibroblasts are loaded with sucrose, which inhibits transport from late endosomes to lysosomes, C-terminal cathepsin B processing is prevented to the same extent. Further characterization of the terminal endocytic compartments of SASD cells revealed properties usually associated with late endosomes/prelysosomes. In addition to a decreased buoyant density, SASD "lysosomes" show a reduced acidification capacity and appear smaller than their normal counterparts. We conclude that the accumulation of small non-diffusible compounds within endocytic compartments interferes with the formation of mature lysosomes and that the acidic environment of the latter organelles is a prerequisite for C-terminal processing of lysosomal hydrolases.  (+info)

Cathepsin B is a lysosomal cysteine protease that plays a role in various physiological processes, including intracellular protein degradation, antigen presentation, and extracellular matrix remodeling. It is produced as an inactive precursor (procathepsin B) and activated upon cleavage of the propeptide by other proteases or autocatalytically. Cathepsin B has a wide range of substrates, including collagen, elastin, and various intracellular proteins. Its dysregulation has been implicated in several pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders.

Cathepsins are a type of proteolytic enzymes, which are found in lysosomes and are responsible for breaking down proteins inside the cell. They are classified as papain-like cysteine proteases and play important roles in various physiological processes, including tissue remodeling, antigen presentation, and apoptosis (programmed cell death). There are several different types of cathepsins, including cathepsin B, C, D, F, H, K, L, S, V, and X/Z, each with distinct substrate specificities and functions.

Dysregulation of cathepsins has been implicated in various pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders. For example, overexpression or hyperactivation of certain cathepsins has been shown to contribute to tumor invasion and metastasis, while their inhibition has been explored as a potential therapeutic strategy in cancer treatment. Similarly, abnormal levels of cathepsins have been linked to the progression of neurodegenerative diseases like Alzheimer's and Parkinson's, making them attractive targets for drug development.

Cathepsin L is a lysosomal cysteine protease that plays a role in various physiological processes, including protein degradation, antigen presentation, and extracellular matrix remodeling. It is produced as an inactive precursor and activated by cleavage of its propeptide domain. Cathepsin L has a broad specificity for peptide bonds and can cleave both intracellular and extracellular proteins, making it an important player in various pathological conditions such as cancer, neurodegenerative diseases, and infectious diseases. Inhibition of cathepsin L has been explored as a potential therapeutic strategy for these conditions.

Cathepsin D is a lysosomal aspartic protease that plays a role in intracellular protein degradation and turnover. It is produced as an inactive precursor and is activated by cleavage into two subunits within the acidic environment of the lysosome. Cathepsin D is also known to be secreted by certain cells, where it can contribute to extracellular matrix remodeling and tissue degradation. In addition, abnormal levels or activity of cathepsin D have been implicated in various diseases, including cancer, neurodegenerative disorders, and infectious diseases.

Cathepsin H is a lysosomal cysteine protease that plays a role in intracellular protein degradation and turnover. It is expressed in various tissues, including the spleen, thymus, lungs, and immune cells. Cathepsin H has been implicated in several physiological processes, such as antigen presentation, bone resorption, and extracellular matrix remodeling. Additionally, its dysregulation has been associated with various pathological conditions, including cancer, neurodegenerative disorders, and infectious diseases.

The enzyme's active site contains a catalytic triad composed of cysteine, histidine, and aspartic acid residues, which facilitates the proteolytic activity. Cathepsin H exhibits specificity for peptide bonds containing hydrophobic or aromatic amino acids, making it an important player in processing and degrading various cellular proteins.

In summary, Cathepsin H is a lysosomal cysteine protease involved in protein turnover and degradation with potential implications in several pathological conditions when dysregulated.

Cathepsin K is a proteolytic enzyme, which belongs to the family of papain-like cysteine proteases. It is primarily produced by osteoclasts, which are specialized cells responsible for bone resorption. Cathepsin K plays a crucial role in the degradation and remodeling of the extracellular matrix, particularly in bone tissue.

This enzyme is capable of breaking down various proteins, including collagen, elastin, and proteoglycans, which are major components of the bone matrix. By doing so, cathepsin K helps osteoclasts to dissolve and remove mineralized and non-mineralized bone matrix during the process of bone resorption.

Apart from its function in bone metabolism, cathepsin K has also been implicated in several pathological conditions, such as osteoporosis, rheumatoid arthritis, and tumor metastasis to bones. Inhibitors of cathepsin K are being investigated as potential therapeutic agents for the treatment of these disorders.

Cathepsin G is a serine protease, which is a type of enzyme that breaks down other proteins. It is produced and released by neutrophils, a type of white blood cell that plays an important role in the body's immune response to infection. Cathepsin G helps to digest and kill microorganisms that have invaded the body. It can also contribute to tissue damage and inflammation in certain diseases, such as rheumatoid arthritis and cystic fibrosis.

Cathepsin E is a type of proteolytic enzyme, which belongs to the family of papain-like cysteine proteases. It is primarily located in the lysosomes of cells and plays a role in intracellular protein degradation. Cathepsin E is unique among the cathepsins because it is predominantly expressed in immune cells, such as macrophages and dendritic cells, where it functions as a protease involved in antigen presentation.

The enzyme has a molecular weight of approximately 42 kDa and is synthesized as an inactive precursor that undergoes proteolytic processing to generate the mature, active enzyme. Cathepsin E can cleave various substrates, including peptides and proteins, and has been implicated in several physiological and pathological processes, such as inflammation, immune response, and cancer.

In summary, Cathepsin E is a lysosomal cysteine protease that plays a crucial role in antigen presentation and protein degradation, primarily expressed in immune cells.

Cathepsin C is a lysosomal cysteine protease that plays a role in intracellular protein degradation and activation of other proteases. It is also known as dipeptidyl peptidase I (DPP I) because of its ability to remove dipeptides from the N-terminus of polypeptides. Cathepsin C is widely expressed in many tissues, including immune cells, and has been implicated in various physiological and pathological processes such as antigen presentation, bone resorption, and tumor cell invasion. Defects in the gene encoding cathepsin C have been associated with several genetic disorders, including Papillon-Lefèvre syndrome and Haim-Munk syndrome, which are characterized by severe periodontal disease and skin abnormalities.

Cysteine endopeptidases are a type of enzymes that cleave peptide bonds within proteins. They are also known as cysteine proteases or cysteine proteinases. These enzymes contain a catalytic triad consisting of three amino acids: cysteine, histidine, and aspartate. The thiol group (-SH) of the cysteine residue acts as a nucleophile and attacks the carbonyl carbon of the peptide bond, leading to its cleavage.

Cysteine endopeptidases play important roles in various biological processes, including protein degradation, cell signaling, and inflammation. They are involved in many physiological and pathological conditions, such as apoptosis, immune response, and cancer. Some examples of cysteine endopeptidases include cathepsins, caspases, and calpains.

It is important to note that these enzymes require a reducing environment to maintain the reduced state of their active site cysteine residue. Therefore, they are sensitive to oxidizing agents and inhibitors that target the thiol group. Understanding the structure and function of cysteine endopeptidases is crucial for developing therapeutic strategies that target these enzymes in various diseases.

Cathepsin F is a lysosomal cysteine protease that belongs to the papain family. It is primarily expressed in hematopoietic cells, including monocytes, macrophages, and dendritic cells. Cathepsin F plays a role in various physiological processes, such as antigen presentation, bone remodeling, and extracellular matrix degradation. It is also implicated in several pathological conditions, such as cancer, neurodegenerative disorders, and infectious diseases.

Cathepsin F has a broad substrate specificity and can cleave various proteins, including collagen, elastin, and casein. Its activity is tightly regulated by endogenous inhibitors, such as cystatins and stefins, to prevent excessive protein degradation and tissue damage.

In summary, Cathepsin F is a lysosomal enzyme involved in various physiological and pathological processes, with a broad substrate specificity and regulatory mechanisms.

Cystatins are a group of proteins that inhibit cysteine proteases, which are enzymes that break down other proteins. Cystatins are found in various biological fluids and tissues, including tears, saliva, seminal plasma, and urine. They play an important role in regulating protein catabolism and protecting cells from excessive protease activity. There are three main types of cystatins: type 1 (cystatin C), type 2 (cystatin M, cystatin N, and fetuin), and type 3 (kininogens). Abnormal levels of cystatins have been associated with various pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders.

Lysosomes are membrane-bound organelles found in the cytoplasm of eukaryotic cells. They are responsible for breaking down and recycling various materials, such as waste products, foreign substances, and damaged cellular components, through a process called autophagy or phagocytosis. Lysosomes contain hydrolytic enzymes that can break down biomolecules like proteins, nucleic acids, lipids, and carbohydrates into their basic building blocks, which can then be reused by the cell. They play a crucial role in maintaining cellular homeostasis and are often referred to as the "garbage disposal system" of the cell.

Cathepsin Z is a lysosomal protease, also known as cathepsin X or peptidyl-dipeptidase I. It is a cysteine proteinase that plays a role in intracellular protein degradation and turnover. Cathepsin Z is expressed in various tissues, including the spleen, thymus, liver, and lungs. It has been found to be involved in several physiological processes, such as antigen presentation, bone resorption, and extracellular matrix remodeling. Additionally, cathepsin Z may contribute to some pathological conditions, like cancer, atherosclerosis, and neurodegenerative disorders.

The enzyme's primary function is to cleave peptide bonds, particularly after hydrophobic residues, in the process of protein degradation. Cathepsin Z has an optimal pH range between 5.0 and 6.5, which is typical for lysosomal enzymes. Its activity can be regulated by endogenous inhibitors, such as cystatins, to maintain a balance in proteolytic processes within the cell.

In summary, Cathepsin Z is a lysosomal cysteine protease involved in intracellular protein degradation and turnover, with potential roles in various physiological and pathological conditions.

Cysteine proteinase inhibitors are a type of molecule that bind to and inhibit the activity of cysteine proteases, which are enzymes that cleave proteins at specific sites containing the amino acid cysteine. These inhibitors play important roles in regulating various biological processes, including inflammation, immune response, and programmed cell death (apoptosis). They can also have potential therapeutic applications in diseases where excessive protease activity contributes to pathology, such as cancer, arthritis, and neurodegenerative disorders. Examples of cysteine proteinase inhibitors include cystatins, kininogens, and serpins.

Diazomethane is a highly reactive, explosive organic compound with the chemical formula CH2N2. It is a colorless gas or pale yellow liquid that is used as a methylating agent in organic synthesis. Diazomethane is prepared by the reaction of nitrosomethane with a base such as potassium hydroxide.

It is important to handle diazomethane with care, as it can be explosive and toxic. It should only be used in well-ventilated areas, and protective equipment such as gloves and safety glasses should be worn. Diazomethane should not be stored for long periods of time, as it can decompose spontaneously and release nitrogen gas.

Diazomethane is used to introduce methyl groups into organic molecules in a process called methylation. It reacts with carboxylic acids to form methyl esters, and with phenols to form methyl ethers. Diazomethane is also used to synthesize other organic compounds such as pyrazoles and triazoles.

It is important to note that the use of diazomethane in the laboratory has declined due to its hazardous nature, and safer alternatives are now available for many of its applications.

Endopeptidases are a type of enzyme that breaks down proteins by cleaving peptide bonds inside the polypeptide chain. They are also known as proteinases or endoproteinases. These enzymes work within the interior of the protein molecule, cutting it at specific points along its length, as opposed to exopeptidases, which remove individual amino acids from the ends of the protein chain.

Endopeptidases play a crucial role in various biological processes, such as digestion, blood coagulation, and programmed cell death (apoptosis). They are classified based on their catalytic mechanism and the structure of their active site. Some examples of endopeptidase families include serine proteases, cysteine proteases, aspartic proteases, and metalloproteases.

It is important to note that while endopeptidases are essential for normal physiological functions, they can also contribute to disease processes when their activity is unregulated or misdirected. For instance, excessive endopeptidase activity has been implicated in the pathogenesis of neurodegenerative disorders, cancer, and inflammatory conditions.

A dipeptide is a type of molecule that is formed by the condensation of two amino acids. In this process, the carboxyl group (-COOH) of one amino acid combines with the amino group (-NH2) of another amino acid, releasing a water molecule and forming a peptide bond.

The resulting molecule contains two amino acids joined together by a single peptide bond, which is a type of covalent bond that forms between the carboxyl group of one amino acid and the amino group of another. Dipeptides are relatively simple molecules compared to larger polypeptides or proteins, which can contain hundreds or even thousands of amino acids linked together by multiple peptide bonds.

Dipeptides have a variety of biological functions in the body, including serving as building blocks for larger proteins and playing important roles in various physiological processes. Some dipeptides also have potential therapeutic uses, such as in the treatment of hypertension or muscle wasting disorders.

Cystatin A is a type of cysteine protease inhibitor that is primarily produced by cells of the immune system. It is a small protein consisting of 120 amino acids and is encoded by the CSTA gene in humans. Cystatin A functions to regulate the activity of cathepsins, which are enzymes that break down proteins in the body.

Cystatin A is mainly found inside cells, where it helps to maintain the balance of cathepsins and prevent excessive protein degradation. However, it can also be released into extracellular spaces under certain conditions, such as inflammation or cell damage. In the extracellular space, cystatin A may help to regulate the activity of cathepsins in the surrounding tissue and contribute to the regulation of immune responses.

Abnormal levels of cystatin A have been associated with various diseases, including cancer, autoimmune disorders, and neurodegenerative diseases. However, more research is needed to fully understand the role of cystatin A in these conditions and its potential as a therapeutic target.

Cathepsin W is a lysosomal cysteine protease that is primarily expressed in cells of the immune system, such as natural killer (NK) cells and cytotoxic T lymphocytes (CTLs). It is also known as lysosomal thiol protease or NK-lysin.

Cathepsin W plays a role in the immune response by contributing to the destruction of target cells during the process of cell-mediated cytotoxicity. It is stored in the lysosomes of NK cells and CTLs, and upon activation, it is released into the immunological synapse between the effector and target cells.

Once released, cathepsin W can cleave various proteins, including cytoskeletal components, adhesion molecules, and signaling proteins, leading to the disruption of the target cell's membrane and ultimately its death. Dysregulation of cathepsin W has been implicated in several diseases, including autoimmune disorders, neurodegenerative diseases, and cancer.

Cystatin B is a type of protease inhibitor that belongs to the cystatin superfamily. It is primarily produced in the central nervous system and is found in various body fluids, including cerebrospinal fluid and urine. Cystatin B plays a crucial role in regulating protein catabolism by inhibiting lysosomal cysteine proteases, which are enzymes that break down proteins.

Defects or mutations in the gene that encodes for cystatin B have been associated with a rare inherited neurodegenerative disorder known as Uner Tan Syndrome (UTS). UTS is characterized by language impairment, mental retardation, and distinctive facial features. The exact mechanism by which cystatin B deficiency leads to this disorder is not fully understood, but it is thought to involve the dysregulation of protein catabolism in neurons, leading to neurotoxicity and neurodegeneration.

Papain is defined as a proteolytic enzyme that is derived from the latex of the papaya tree (Carica papaya). It has the ability to break down other proteins into smaller peptides or individual amino acids. Papain is widely used in various industries, including the food industry for tenderizing meat and brewing beer, as well as in the medical field for its digestive and anti-inflammatory properties.

In medicine, papain is sometimes used topically to help heal burns, wounds, and skin ulcers. It can also be taken orally to treat indigestion, parasitic infections, and other gastrointestinal disorders. However, its use as a medical treatment is not widely accepted and more research is needed to establish its safety and efficacy.

Benzoylarginine-2-Naphthylamide is a synthetic substance that is used in laboratory settings as a reagent for the detection and measurement of certain enzymes, specifically proteases such as trypsin. It is a colorless to pale yellow crystalline powder that is soluble in water and alcohol. When treated with an enzyme that can cleave it, such as trypsin, it produces a colored product that can be measured and used to quantify the enzyme's activity. This compound is not used for medical purposes in humans or animals.

Pepstatins are a group of naturally occurring cyclic peptides that inhibit aspartic proteases, a type of enzyme that breaks down proteins. They are isolated from various actinomycete species of Streptomyces and Actinosynnema. Pepstatins are often used in laboratory research to study the function of aspartic proteases and as tools to probe the mechanism of action of these enzymes. In addition, pepstatins have been explored for their potential therapeutic use in various diseases, including cancer, viral infections, and cardiovascular disease. However, they have not yet been approved for clinical use.

Protease inhibitors are a class of antiviral drugs that are used to treat infections caused by retroviruses, such as the human immunodeficiency virus (HIV), which is responsible for causing AIDS. These drugs work by blocking the activity of protease enzymes, which are necessary for the replication and multiplication of the virus within infected cells.

Protease enzymes play a crucial role in the life cycle of retroviruses by cleaving viral polyproteins into functional units that are required for the assembly of new viral particles. By inhibiting the activity of these enzymes, protease inhibitors prevent the virus from replicating and spreading to other cells, thereby slowing down the progression of the infection.

Protease inhibitors are often used in combination with other antiretroviral drugs as part of highly active antiretroviral therapy (HAART) for the treatment of HIV/AIDS. Common examples of protease inhibitors include saquinavir, ritonavir, indinavir, and atazanavir. While these drugs have been successful in improving the outcomes of people living with HIV/AIDS, they can also cause side effects such as nausea, diarrhea, headaches, and lipodystrophy (changes in body fat distribution).

Cysteine proteases are a type of enzymes that cleave peptide bonds in proteins, and they require a cysteine residue in their active site to do so. These enzymes play important roles in various biological processes, including protein degradation, cell signaling, and inflammation. They can be found in various tissues and organisms, including humans, where they are involved in many physiological and pathological conditions.

Cysteine proteases are characterized by a conserved catalytic mechanism that involves a nucleophilic attack on the peptide bond carbonyl carbon by the thiolate anion of the cysteine residue, resulting in the formation of an acyl-enzyme intermediate. This intermediate is then hydrolyzed to release the cleaved protein fragments.

Some examples of cysteine proteases include cathepsins, caspases, and calpains, which are involved in various cellular processes such as apoptosis, autophagy, and signal transduction. Dysregulation of these enzymes has been implicated in several diseases, including cancer, neurodegenerative disorders, and infectious diseases. Therefore, cysteine proteases have emerged as important therapeutic targets for the development of new drugs to treat these conditions.

Cathepsin A is a lysosomal protein that belongs to the peptidase family. It plays a role in various biological processes, including protein degradation and activation, cell signaling, and inflammation. Cathepsin A has both endopeptidase and exopeptidase activities, which allow it to cleave and process a wide range of substrates.

In addition to its enzymatic functions, cathepsin A also plays a structural role in the formation and stability of the protective protein complex called the "serglycin-cathepsin A proteoglycan complex." This complex protects certain proteases from degradation and helps regulate their activity within the lysosome.

Deficiencies or mutations in cathepsin A have been linked to several diseases, including a rare genetic disorder called galactosialidosis, which is characterized by developmental delays, coarse facial features, and progressive neurological deterioration.

Enzyme precursors are typically referred to as zymogens or proenzymes. These are inactive forms of enzymes that can be activated under specific conditions. When the need for the enzyme's function arises, the proenzyme is converted into its active form through a process called proteolysis, where it is cleaved by another enzyme. This mechanism helps control and regulate the activation of certain enzymes in the body, preventing unwanted or premature reactions. A well-known example of an enzyme precursor is trypsinogen, which is converted into its active form, trypsin, in the digestive system.

Cystatin C is a protein produced by many cells in the body, including all types of nucleated cells. It is a member of the cysteine protease inhibitor family and functions as an endogenous inhibitor of cathepsins, which are proteases involved in various physiological and pathological processes such as extracellular matrix degradation, antigen presentation, and cell death.

Cystatin C is freely filtered by the glomeruli in the kidneys and almost completely reabsorbed and catabolized by the proximal tubules. Therefore, its serum concentration is a reliable marker of glomerular filtration rate (GFR) and can be used to estimate kidney function.

Increased levels of cystatin C in the blood may indicate impaired kidney function or kidney disease, while decreased levels are less common and may be associated with hyperfiltration or overproduction of cystatin C. Measuring cystatin C levels can complement or supplement traditional methods for assessing kidney function, such as estimating GFR based on serum creatinine levels.

Hydrogen-ion concentration, also known as pH, is a measure of the acidity or basicity of a solution. It is defined as the negative logarithm (to the base 10) of the hydrogen ion activity in a solution. The standard unit of measurement is the pH unit. A pH of 7 is neutral, less than 7 is acidic, and greater than 7 is basic.

In medical terms, hydrogen-ion concentration is important for maintaining homeostasis within the body. For example, in the stomach, a high hydrogen-ion concentration (low pH) is necessary for the digestion of food. However, in other parts of the body such as blood, a high hydrogen-ion concentration can be harmful and lead to acidosis. Conversely, a low hydrogen-ion concentration (high pH) in the blood can lead to alkalosis. Both acidosis and alkalosis can have serious consequences on various organ systems if not corrected.

Exopeptidases are a type of enzyme that break down peptides or proteins by cleaving off one amino acid at a time from the end of the protein or peptide chain. There are two main types of exopeptidases: aminopeptidases, which remove amino acids from the N-terminus (the end of the chain with a free amino group), and carboxypeptidases, which remove amino acids from the C-terminus (the end of the chain with a free carboxyl group).

Exopeptidases play important roles in various biological processes, including protein degradation and turnover, digestion, and processing of peptide hormones and neuropeptides. They are also involved in the pathogenesis of certain diseases, such as cancer and neurodegenerative disorders, where they can contribute to the accumulation of abnormal proteins and toxic protein fragments.

Exopeptidases are found in various organisms, including bacteria, fungi, plants, and animals. They are also used in biotechnology and research, for example, in the production of pharmaceuticals, food ingredients, and diagnostic tools.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Serine endopeptidases are a type of enzymes that cleave peptide bonds within proteins (endopeptidases) and utilize serine as the nucleophilic amino acid in their active site for catalysis. These enzymes play crucial roles in various biological processes, including digestion, blood coagulation, and programmed cell death (apoptosis). Examples of serine endopeptidases include trypsin, chymotrypsin, thrombin, and elastase.

Trypsinogen is a precursor protein that is converted into the enzyme trypsin in the small intestine. It is produced by the pancreas and released into the duodenum, where it is activated by enterokinase, an enzyme produced by the intestinal mucosa. Trypsinogen plays a crucial role in digestion by helping to break down proteins into smaller peptides and individual amino acids.

In medical terms, an elevated level of trypsinogen in the blood may indicate pancreatic disease or injury, such as pancreatitis or pancreatic cancer. Therefore, measuring trypsinogen levels in the blood is sometimes used as a diagnostic tool to help identify these conditions.

Pancreatic elastase is a type of elastase that is specifically produced by the pancreas. It is an enzyme that helps in digesting proteins found in the food we eat. Pancreatic elastase breaks down elastin, a protein that provides elasticity to tissues and organs in the body.

In clinical practice, pancreatic elastase is often measured in stool samples as a diagnostic tool to assess exocrine pancreatic function. Low levels of pancreatic elastase in stool may indicate malabsorption or exocrine pancreatic insufficiency, which can be caused by various conditions such as chronic pancreatitis, cystic fibrosis, or pancreatic cancer.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

Hydrolysis is a chemical process, not a medical one. However, it is relevant to medicine and biology.

Hydrolysis is the breakdown of a chemical compound due to its reaction with water, often resulting in the formation of two or more simpler compounds. In the context of physiology and medicine, hydrolysis is a crucial process in various biological reactions, such as the digestion of food molecules like proteins, carbohydrates, and fats. Enzymes called hydrolases catalyze these hydrolysis reactions to speed up the breakdown process in the body.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Leucine is an essential amino acid, meaning it cannot be produced by the human body and must be obtained through the diet. It is one of the three branched-chain amino acids (BCAAs), along with isoleucine and valine. Leucine is critical for protein synthesis and muscle growth, and it helps to regulate blood sugar levels, promote wound healing, and produce growth hormones.

Leucine is found in various food sources such as meat, dairy products, eggs, and certain plant-based proteins like soy and beans. It is also available as a dietary supplement for those looking to increase their intake for athletic performance or muscle recovery purposes. However, it's important to consult with a healthcare professional before starting any new supplement regimen.

Leukocyte elastase is a type of enzyme that is released by white blood cells (leukocytes), specifically neutrophils, during inflammation. Its primary function is to help fight infection by breaking down the proteins in bacteria and viruses. However, if not properly regulated, leukocyte elastase can also damage surrounding tissues, contributing to the progression of various diseases such as chronic obstructive pulmonary disease (COPD), acute respiratory distress syndrome (ARDS), and cystic fibrosis.

Leukocyte elastase is often measured in clinical settings as a marker of inflammation and neutrophil activation, particularly in patients with lung diseases. Inhibitors of leukocyte elastase have been developed as potential therapeutic agents for these conditions.

Urokinase Plasminogen Activator Receptors (uPAR) are a type of cell surface receptor that play a role in several biological processes including cell migration, tissue remodeling, and angiogenesis. They bind to urokinase plasminogen activator (uPA), a serine protease that converts plasminogen to plasmin, leading to the degradation of extracellular matrix components.

The interaction between uPAR and uPA plays a crucial role in various physiological processes such as wound healing and tissue repair, but it has also been implicated in several pathological conditions, including cancer, where it contributes to tumor cell invasion and metastasis. The regulation of uPAR expression and activity is therefore an important area of research for the development of new therapeutic strategies.

Electrophoresis, polyacrylamide gel (EPG) is a laboratory technique used to separate and analyze complex mixtures of proteins or nucleic acids (DNA or RNA) based on their size and electrical charge. This technique utilizes a matrix made of cross-linked polyacrylamide, a type of gel, which provides a stable and uniform environment for the separation of molecules.

In this process:

1. The polyacrylamide gel is prepared by mixing acrylamide monomers with a cross-linking agent (bis-acrylamide) and a catalyst (ammonium persulfate) in the presence of a buffer solution.
2. The gel is then poured into a mold and allowed to polymerize, forming a solid matrix with uniform pore sizes that depend on the concentration of acrylamide used. Higher concentrations result in smaller pores, providing better resolution for separating smaller molecules.
3. Once the gel has set, it is placed in an electrophoresis apparatus containing a buffer solution. Samples containing the mixture of proteins or nucleic acids are loaded into wells on the top of the gel.
4. An electric field is applied across the gel, causing the negatively charged molecules to migrate towards the positive electrode (anode) while positively charged molecules move toward the negative electrode (cathode). The rate of migration depends on the size, charge, and shape of the molecules.
5. Smaller molecules move faster through the gel matrix and will migrate farther from the origin compared to larger molecules, resulting in separation based on size. Proteins and nucleic acids can be selectively stained after electrophoresis to visualize the separated bands.

EPG is widely used in various research fields, including molecular biology, genetics, proteomics, and forensic science, for applications such as protein characterization, DNA fragment analysis, cloning, mutation detection, and quality control of nucleic acid or protein samples.

Peptide hydrolases, also known as proteases or peptidases, are a group of enzymes that catalyze the hydrolysis of peptide bonds in proteins and peptides. They play a crucial role in various biological processes such as protein degradation, digestion, cell signaling, and regulation of various physiological functions. Based on their catalytic mechanism and the specificity for the peptide bond, they are classified into several types, including serine proteases, cysteine proteases, aspartic proteases, and metalloproteases. These enzymes have important clinical applications in the diagnosis and treatment of various diseases, such as cancer, viral infections, and inflammatory disorders.

Oligopeptides are defined in medicine and biochemistry as short chains of amino acids, typically containing fewer than 20 amino acid residues. These small peptides are important components in various biological processes, such as serving as signaling molecules, enzyme inhibitors, or structural elements in some proteins. They can be found naturally in foods and may also be synthesized for use in medical research and therapeutic applications.

'2,2'-Dipyridyl is an organic compound with the formula (C5H4N)2. It is a bidentate chelating ligand, which means that it can form stable coordination complexes with many metal ions by donating both of its nitrogen atoms to the metal. This ability to form complexes makes '2,2'-Dipyridyl useful in various applications, including as a catalyst in chemical reactions and as a reagent in the analysis of metal ions.

The compound is a solid at room temperature and has a molecular weight of 108.13 g/mol. It is soluble in organic solvents such as ethanol, acetone, and dichloromethane, but is insoluble in water. '2,2'-Dipyridyl is synthesized by the reaction of pyridine with formaldehyde and hydrochloric acid.

In medical contexts, '2,2'-Dipyridyl may be used as a reagent in diagnostic tests to detect the presence of certain metal ions in biological samples. However, it is not itself a drug or therapeutic agent.

'Fasciola hepatica' is a medical term that refers to a type of flatworm, specifically a liver fluke, which is a parasitic flatworm that infects the livers of various animals, including sheep, cattle, and humans. The parasite has a complex life cycle involving aquatic snails as an intermediate host and can cause significant damage to the liver and bile ducts in its definitive host. Infection with Fasciola hepatica is known as fascioliasis, which can lead to symptoms such as abdominal pain, fever, and jaundice.

The liver is a large, solid organ located in the upper right portion of the abdomen, beneath the diaphragm and above the stomach. It plays a vital role in several bodily functions, including:

1. Metabolism: The liver helps to metabolize carbohydrates, fats, and proteins from the food we eat into energy and nutrients that our bodies can use.
2. Detoxification: The liver detoxifies harmful substances in the body by breaking them down into less toxic forms or excreting them through bile.
3. Synthesis: The liver synthesizes important proteins, such as albumin and clotting factors, that are necessary for proper bodily function.
4. Storage: The liver stores glucose, vitamins, and minerals that can be released when the body needs them.
5. Bile production: The liver produces bile, a digestive juice that helps to break down fats in the small intestine.
6. Immune function: The liver plays a role in the immune system by filtering out bacteria and other harmful substances from the blood.

Overall, the liver is an essential organ that plays a critical role in maintaining overall health and well-being.

... A (serine protease) Cathepsin B (cysteine protease) Cathepsin C (cysteine protease) Cathepsin D (aspartyl protease) ... Cathepsin H (cysteine protease) Cathepsin K (cysteine protease) Cathepsin L1 (cysteine protease) Cathepsin L2 (or V) (cysteine ... Cathepsin S (cysteine protease) Cathepsin W (cysteine proteinase) Cathepsin Z (or X) (cysteine protease) Cathepsins are ... Cathepsin K has also been shown to play a role in arthritis. Mouse cathepsin L is homologous to human cathepsin V. Mouse ...
Cathepsin+T at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.22). ... Cathepsin T (EC 3.4.22.24) is an enzyme. This enzyme catalyses the following chemical reaction: Interconversion of the three ... Cathepsin Gohda E, Pitot HC (May 1981). "Purification and characterization of a new thiol proteinase from rat kidney". ... Pitot HC, Gohda E (1987). Cathepsin T. Methods in Enzymology. Vol. 142. pp. 279-89. doi:10.1016/s0076-6879(87)42038-7. PMID ...
... is a protein that in humans is encoded by the CTSF gene. Cysteine cathepsins are a family of cysteine proteases ... The cathepsin F gene is ubiquitously expressed, and it maps to chromosome 11q13, close to the gene encoding cathepsin W. ... Wex T, Levy B, Wex H, Brömme D (1999). "Human cathepsins F and W: A new subgroup of cathepsins". Biochem. Biophys. Res. Commun ... Wex T, Wex H, Brömme D (2000). "The human cathepsin F gene--a fusion product between an ancestral cathepsin and cystatin gene ...
... may refer to: Cathepsin L1, a human protease enzyme encoded by the CTSL gene and known for its role in viral entry ... Cathepsin L2, a human protease enzyme encoded by the CTSV gene and also known as cathepsin V This disambiguation page lists ... articles associated with the title Cathepsin L. If an internal link led you here, you may wish to change the link to point ...
"Human cathepsins W and F form a new subgroup of cathepsins that is evolutionary separated from the cathepsin B- and L-like ... Wex T, Levy B, Wex H, Brömme D (1999). "Human cathepsins F and W: A new subgroup of cathepsins". Biochem. Biophys. Res. Commun ... The protein encoded by this gene, a member of the peptidase C1 family of cysteine cathepsins, is a cysteine protease cathepsin ... 2003). "Characterization of novel anti-cathepsin W antibodies and cellular distribution of cathepsin W in the gastrointestinal ...
... cathepsin S can be replaced by cathepsin F. Secreted cathepsin S cleaves some extracellular matrix (ECM) proteins. Cathepsin S ... 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 ... Cathepsin S is a member of the peptidase C1 family of cysteine cathepsins, a lysosomal cysteine protease that may participate ...
... (EC 3.4.18.1, cathepsin B2, cysteine-type carboxypeptidase, cathepsin IV, cathepsin Z, acid carboxypeptidase, ... Shows weak endopeptidase activity Cathepsin X is a cysteine cathepsin, a lysosomal cysteine peptidase of family C1 (papain ... Otto K, Riesenkönig H (February 1975). "Improved purification of cathepsin B1 and cathepsin B2". Biochimica et Biophysica Acta ... "On the substrate specificity of cathepsins B1 and B2 including a new fluorogenic substrate for cathepsin B1". Life Sciences. 17 ...
... can also be found in the extracellular space and it is one of the few cathepsins, that shows some activity at ... Cathepsin D is an aspartic endo-protease that is ubiquitously distributed in lysosomes. The main function of cathepsin D is to ... "Entrez Gene: CTSD cathepsin D". Barrett AJ (April 1970). "Cathepsin D. Purification of isoenzymes from human and chicken liver ... The optimum pH for cathepsin D in vitro is 4.5-5.0. Cathepsin-D is an aspartic protease that depends critically on protonation ...
... is degraded by Cathepsin S, in a process referred to as Controlled Cathepsin Cannibalism. Cathepsin K expression is ... Cathepsin K has also been found to be over-expressed in glioblastoma. That the expression of cathepsin K is characteristic for ... Cathepsin K antibodies are marketed for research into expression of this enzyme by various cells. Merck had a cathepsin K ... Other cathepsin K inhibitors are in various stages of development. Medivir has a cathepsin K inhibitor, MIV-711 (L-006235), in ...
... cathepsin C, cathepsin F, cathepsin H, cathepsin K, cathepsin L, cathepsin L2 or V, cathepsin O, cathepsin S, cathepsin Z, and ... Cathepsin Z, also called cathepsin X or cathepsin P, is a protein that in humans is encoded by the CTSZ gene. It is a member of ... As one of the 11 cathepsins, cathepsin Z contains distinctive features from others. Cathepsin Z has been reported involved in ... Cathepsin Z has an exposed integrin-binding Arg-Gly-Asp motif within the propeptide of the enzyme, through which cathepsin Z ...
"Entrez Gene: CTSL1 cathepsin L1". Barrett AJ, Kirschke H (1981). Cathepsin B, Cathepsin H, and cathepsin L. Methods in ... or by cathepsins (primarily cathepsin L) in endolysosomes. Hydroxychloroquine inhibits the action of cathepsin L in ... Cathepsin L1 is a protein that in humans is encoded by the CTSL1 gene. The protein is a cysteine cathepsin, a lysosomal ... Cathepsin L1 is a member of the Peptidase C1 (cathepsin) MEROPS family, which plays an important role in diverse processes ...
... is a protein that in humans is encoded by the CTSH gene. The protein encoded by this gene is a cysteine cathepsin, ... "Entrez Gene: CTSH cathepsin H". Sawicki G, Warwas M (1990). "Cathepsin H from human placenta". Acta Biochim. Pol. 36 (3-4): 343 ... 2003). "Expression of cathepsins B, H, K, L, and S during human fetal lung development". Dev. Dyn. 225 (1): 14-21. doi:10.1002/ ... 2001). "Expression of cathepsins B, H, K, L, and S and matrix metalloproteinases 9 and 13 during chondrocyte hypertrophy and ...
... is one of those homologous protease that evolved from a common ancestor by gene duplication. Cathepsin G is a 255- ... An upregulation of cathepsin G was reported in studies of keratoconus. Cathepsin G has been found to interact with: SERPINB1 ... "Entrez Gene: CTSG cathepsin G". Shafer WM, Pohl J, Onunka VC, Bangalore N, Travis J (January 1991). "Human lysosomal cathepsin ... "Generation of the neutrophil-activating peptide-2 by cathepsin G and cathepsin G-treated human platelets". The American Journal ...
... prepro-cathepsin C) comprising signal peptides of 24 residues, pro-regions of 205 (rat cathepsin C) or 206 (human cathepsin C) ... Cathepsin C appears to be a central coordinator for activation of many serine proteases in immune/inflammatory cells. Cathepsin ... identical to the mature amino acid sequences of papain and a number of other cathepsins including cathepsins, B, H, K, L, and S ... "Entrez Gene: CTSC cathepsin C". Paris A, Strukelj B, Pungercar J, Renko M, Dolenc I, Turk V (Aug 1995). "Molecular cloning and ...
Cathepsin K detection by zymography Zymographic techniques for detection of cathepsins K, L, S, and V Zymography for detection ... Cathepsin zymography is a technique for quantifying enzymatic activity of the cathepsin family of cysteine proteases. It is ... While the proform of cathepsins are generally stable, once activated, proteases such as cathepsin K are vulnerable to ... After the renaturing period, the gel is then incubated in assay buffer to allow the now active cathepsins to proteolyze the ...
... (EC 3.4.22.43, also known as cathepsin V or cathepsin U) is a protein encoded in humans by the CTSV gene. The ... "Entrez Gene: CTSL2 cathepsin L2". Brömme D, Li Z, Barnes M, Mehler E (February 1999). "Human cathepsin V functional expression ... 2006). "Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the ... 2007). "Inhibition of cathepsin L-like proteases by cathepsin V propeptide". Biol. Chem. 388 (5): 541-5. doi:10.1515/BC. ...
... is an enzyme that is classified both as a cathepsin and a carboxypeptidase. In humans, it is encoded by the CTSA ... Cathepsin+A at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology v t e (Genes on human ... "Entrez Gene: CTSA cathepsin A". Mitchell, Richard Sheppard; Kumar, Vinay; Robbins, Stanley L.; Abbas, Abul K.; Fausto, Nelson ( ... Cathepsin A has been shown to interact with NEU1. GRCh38: Ensembl release 89: ENSG00000064601 - Ensembl, May 2017 GRCm38: ...
... is an enzyme that in humans is encoded by the CTSO gene. Cathepsin O is a cysteine cathepsin, a cysteine protease ... "Entrez Gene: cathepsin O". Shi GP, Chapman HA, Bhairi SM, et al. (1995). "Molecular cloning of human cathepsin O, a novel ... 1994). "Human cathepsin O. Molecular cloning from a breast carcinoma, production of the active enzyme in Escherichia coli, and ... "Genomic structure and chromosomal localization of the human cathepsin O gene (CTSO)". Genomics. 53 (2): 231-4. doi:10.1006/geno ...
... cathepsin D-like acid proteinase, cathepsin E-like acid proteinase, cathepsin D-type proteinase) is an enzyme. Cathepsin E is a ... The structure of Cathepsin E is very similar to those of Cathepsin D and BACE1, and all 3 have almost identical active site ... Along with renin and Cathepsin D, Cathepsin E is one of the only few aspartic proteases known to be made in human tissues other ... A distinguishing factor of Cathepsin E in comparison with the structure of Cathepsin D and BACE1 can be seen at the formation ...
In humans, cathepsin B is encoded by the CTSB gene. Cathepsin B is upregulated in certain cancers, in pre-malignant lesions, ... Cathepsin B belongs to a family of lysosomal cysteine proteases known as the cysteine cathepsins and plays an important role in ... Cathepsin B has been shown to interact with: CTSD CSTA, CSTB, and S100A10. Cathepsin B is inhibited by: Nitroxoline CA-074 ... Cathepsin B has been proposed as a potentially effective biomarker for a variety of cancers. Overexpression of cathepsin B is ...
... , Histones & Cathepsin; PMAP The Proteolysis Map-animation Nature journal: recent chromatin publications and news ...
... collagenases such as cathepsin B1; and hyaluronidase. PSGAG inhibits the synthesis of prostaglandin E2, which is released upon ...
Cathepsin A Breddam, K. (1986). "Serine carboxypeptidases. A review". Carlsberg Res. Commun. 51: 83-128. doi:10.1007/bf02907561 ... Miller JJ, Changaris DG, Levy RS (December 1992). "Purification, subunit structure and inhibitor profile of cathepsin A". ... Carboxypeptidase C (EC 3.4.16.5, carboxypeptidase Y, serine carboxypeptidase I, cathepsin A, lysosomal protective protein, ...
Cathepsin E. TALE homeodomain transcription factors. Hydrocortisone. Since keratinocyte differentiation inhibits keratinocyte ... "The role of cathepsin E in terminal differentiation of keratinocytes". Biological Chemistry. 392 (6): 571-85. doi:10.1515/BC. ...
Cathepsin D is involved in CLN10. DNA analysis can be used to help confirm the diagnosis of Batten disease. When the mutation ...
Miv-711 Cathepsin K inhibitor for osteoarthritis. Fast track (FDA) MALT1 "Swedish pharma firm Medivir partners Aragen Life ...
Her research has examined cathepsins and proteases associated with cancer. She has also used imaging with fluorescent probes to ... Sloane, Bonnie F.; Dunn, John R.; Honn, Kenneth V. (1981-06-05). "Lysosomal Cathepsin B: Correlation with Metastatic Potential ... Sloane, Bonnie F.; Dunn, John R.; Honn, Kenneth V. (1981-06-05). "Lysosomal Cathepsin B: Correlation with Metastatic Potential ... Mohamed, Mona Mostafa; Sloane, Bonnie F. (2006). "Cysteine cathepsins: multifunctional enzymes in cancer". Nature Reviews ...
... these include cathepsin L, papain, and procaricain. It forms an alpha-helical domain that runs through the substrate-binding ...
"Cathepsins as transcriptional activators? Developmental Cell 2004, 6(5):610-1. Goulet B, and Nepveu A. "Complete and Limited ...
Lushbaugh WB, Hofbauer AF, Pittman FE (June 1985). "Entamoeba histolytica: purification of cathepsin B". Experimental ...
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 are ... Cathepsin K has also been shown to play a role in arthritis. Mouse cathepsin L is homologous to human cathepsin V. Mouse ...
Final Theses freely available via Open Access
Aspartic proteinase, Cathepsin D, Endopeptidase, Hordeum (proteinase). in Planta. volume. 186. issue. 3. pages. 7 pages. ... Aspartic proteinase from barley grains is related to mammalian lysosomal cathepsin D. *Mark ... Cathepsin D; Endopeptidase; Hordeum (proteinase)}}, language = {{eng}}, number = {{3}}, pages = {{317--323}}, publisher = {{ ... sequence alignment and inhibition studies showed that the barley aspartic proteinase resembles mammalian lysosomal cathepsin D ...
cysteine protease inhibitors, cathepsin K, azapeptide, cathepsin B, peptidomimetic. in Journal of Peptide Research. volume. 66 ... We have designed and synthesized a new series of azapeptides which act as potential inhibitors of cathepsin B and/or cathepsin ... We have designed and synthesized a new series of azapeptides which act as potential inhibitors of cathepsin B and/or cathepsin ... Novel azapeptide inhibitors of cathepsins B and K. Structural background to increased specificity for cathepsin B. *Mark ...
Neutrophils discharge proteases such as for example elastase and cathepsin G, which exert a plasmin-independent fibrinolytic ... Neutrophils discharge proteases such as for example elastase and cathepsin G, which exert a plasmin-independent fibrinolytic ...
Residual active granzyme B in cathepsin C-null lymphocytes is sufficient for perforin-dependent target cell apoptosis. Request ... Cathepsin C activates serine proteases expressed in hematopoietic cells by cleaving an N-terminal dipeptide from the proenzyme ... The lymphocytes of cathepsin C-null mice are therefore proposed to totally lack granzyme B activity and ... Home » ANU Research » ANU Scholarly Output » ANU Research Publications » Residual active granzyme B in cathepsin C-null ...
It has been suggested that the C-→ (224Ala→Val) transition within exon 2 of the cathepsin D gene (CTSD) might represent a risk ... It has been suggested that the C-→ (224Ala→Val) transition within exon 2 of the cathepsin D gene (CTSD) might represent a risk ... It has been suggested that the C-→ (224Ala→Val) transition within exon 2 of the cathepsin D gene (CTSD) might represent a risk ... It has been suggested that the C-→ (224Ala→Val) transition within exon 2 of the cathepsin D gene (CTSD) might represent a risk ...
Animals Antibodies, Helminth Antigens, Helminth Cathepsin L Clinical Laboratory Techniques Enzyme-Linked Immunosorbent Assay ... The Diagnosis of Human Fascioliasis by Enzyme-Linked Immunosorbent Assay (ELISA) Using Recombinant Cathepsin L Protease. ... The Diagnosis of Human Fascioliasis by Enzyme-Linked Immunosorbent Assay (ELISA) Using Recombinant Cathepsin L Protease ... "The Diagnosis of Human Fascioliasis by Enzyme-Linked Immunosorbent Assay (ELISA) Using Recombinant Cathepsin L Protease" 7, no ...
Cathepsin K. Cathepsin K is a cysteine protease expressed predominantly in osteoclasts. Search. Main menu. Skip to primary ...
Et al. Pavlov et al. Johansson et al,and proline has been linked with slow ...
Human CTSK(Cathepsin K) ELISA Kit. Human CTSK(Cathepsin K) ELISA Kit. To Order: [email protected] ... Description: A sandwich ELISA kit for detection of Cathepsin K from Human in samples from blood, serum, plasma, cell culture ... Description: A sandwich quantitative ELISA assay kit for detection of Human Cathepsin K (CTSK) in samples from serum, plasma, ... Description: A sandwich quantitative ELISA assay kit for detection of Human Cathepsin K (CTSK) in samples from serum, plasma, ...
... is a potent and selective inhibitor of cathepsin K and has the potential for osteoporosis research. ... Cathepsin K is a cysteine protease member of the lysosomal protease family of cathepsin. Besides, cathepsin K is the only ... Odanacatib is a Selective Cathepsin K Inhibitor for Osteoporosis Research By Edward Jenner 2024-03-04. #cathepsin K, #lysosomal ... First of all, Odanacatib (MK-0822) is a selective inhibitor of cathepsin K, with an IC50 of 0.2 nM for human cathepsin K. ...
In this study, we demonstrated that targeting cathepsin S by either specific small molecular inhibitors or cathepsin S siRNA ... In this study, we demonstrated that targeting cathepsin S by either specific small molecular inhibitors or cathepsin S siRNA ... In this study, we demonstrated that targeting cathepsin S by either specific small molecular inhibitors or cathepsin S siRNA ... In this study, we demonstrated that targeting cathepsin S by either specific small molecular inhibitors or cathepsin S siRNA ...
Cathepsin activity-based probes and inhibitor for preclinical atherosclerosis imaging and macrophage depletion. In: PLoS ONE. ... Abd-Elrahman, I, Kosuge, H, Sadan, TW, Ben-Nun, Y, Meir, K, Rubinstein, C, Bogyo, M, McConnell, MV & Blum, G 2016, Cathepsin ... Cathepsin activity-based probes and inhibitor for preclinical atherosclerosis imaging and macrophage depletion. PLoS ONE. 2016 ... In addition, our cathepsin inhibitor selectively induced cell apoptosis of 55%±10% of the macrophage within excised human ...
CTSA: cathepsin A. *CTSD: cathepsin D. *CUBN: cubilin. *CUL3: cullin 3. *CUL7: cullin 7 ...
Cathepsin G (CTSG)]Product Name Synonyme: N/AOther Names: [cathepsin G preproprotein; Cathepsin G; cathepsin G;... ... Human Cathepsin G (CTSG) ELISA Kit , MBS167220 , MybiosourceProduct Short Name: [ ...
Cathepsin D as a marker for breast cancer. Present data are insufficient to recommend the use of cathepsin D measurements for ... Cathepsin D as a marker for breast cancer. Present data are insufficient to recommend the use of cathepsin D measurements for ...
Yeast as a tool to explore cathepsin D function. Pereira, H; Oliveira, C S F; Castro, L; Preto, A; Chaves, S R; Côrte-Real, M. ... Emphasis is given to the role of the yeast protease Pep4p, the vacuolar counterpart of cathepsin D, in life and death. Finally ... In particular, cathepsin D is often overexpressed and hypersecreted in cancer cells, implying it may constitute a therapeutic ... Cathepsin D has garnered increased attention in recent years, mainly since it has been associated with several human ...
Enzymatic Assay of Cathepsin B. Cathepsin B is a lysosomal cysteine proteinase with broad specificity. This protocol uses Nα- ... CBZ-Arg-Arg-7-amido-4-methylcoumarin as the substrate for fluorometric detection of Cathepsin B activity. ...
Strain Detail Sheet for C57BL/6J-MtgxR4483Btlr/Mmmh
Title: Cathepsin B p.Gly284Val Variant in Parkinsons Disease Pathogenesis Author(s): Łukasz Milanowski, Xu Hou, Jenny M. ...
Synthesis and structure activity relationships of novel small molecule cathepsin D inhibitors. Dumas J Brittelli D Chen J Dixon ... Inhibition of human recombinant His-tagged cathepsin K using Cbz-Phe-Arg-AMC as substrate ...
Role of cathepsin B in intracellular trypsinogen activation and the onset of acute pancreatitis. J Clin Invest 2000. 106:773- ... These organelles contain cathepsin B and other proteases that can activate trypsin, and a number of cell fractionation studies ... Within the lysosomes proteolytic enzymes, including the cathepsins, degrade and inactivate trypsin and the other digestive ... Thus, there is strong evidence that trypsin can be activated within lysosomes by cathepsins. ...
Cathepsin), Cell And Gene Therapies (Allogenic Products, Autologous Products, Acellular Products), Synthetic Immunomodulators ( ...
Open the PDF for Biochemical Membrane Constituents and Activities of Alkaline and Acid Phosphatase and Cathepsin in Cortical ... View article titled, Biochemical Membrane Constituents and Activities of Alkaline and Acid Phosphatase and Cathepsin in ... Biochemical Membrane Constituents and Activities of Alkaline and Acid Phosphatase and Cathepsin in Cortical and Subcortical ... alkaline and acid phosphatases and cathepsin activity were determined in homogenates from frontal, temporal, and occipital ...
Cathepsin-K immunoreactivity distinguishes MiTF/TFE family renal translocation carcinomas from other renal carcinomas. Mod ... It has been shown that translocation-association carcinomas of the MiTF/TFE family also immunologically express cathepsin-K, ...
Fasciola gigantica Cathepsin L1H: High Sensitivity and Specificity of Immunochromatographic Strip Test for Antibody Detection ...
Cathepsin B is a member of cysteine protease family, which is normally found in lysosome. The normal function of cathepsin B ... J. S. Mort and D. J. Buttle, "Cathepsin B," The International Journal of Biochemistry & Cell Biology, vol. 29, no. 5, pp. 715- ... L. Cao, R. T. Taggart, I. M. Berquin, K. Moin, D. Fong, and B. F. Sloane, "Human gastric adenocarcinoma cathepsin B: isolation ... In several cancers, cathepsin B involves degradation of ECM and promotes angiogenesis and metastatic capability inversely ...
  • We have designed and synthesized a new series of azapeptides which act as potential inhibitors of cathepsin B and/or cathepsin K. Their structures are based upon the inhibitory sites of natural cysteine protease inhibitors, cystatins. (lu.se)
  • Cathepsin K is a cysteine protease member of the lysosomal protease family of cathepsin. (immune-system-research.com)
  • Cathepsin K is a cysteine protease similar to papain, with high matrix degradation activity. (immune-system-research.com)
  • Cathepsin S is a cellular cysteine protease, which is frequently over-expressed in human cancer cells and plays important role in tumor metastasis. (tmu.edu.tw)
  • SAR114137, a Cathepsin S inhibitor, did not progress past phase I for chronic pain. (wikipedia.org)
  • In 2022, STI-1558, a Cathepsin L inhibitor, received FDA clearance to begin phase I studies to treat COVID-19. (wikipedia.org)
  • Here, we will introduce a selective inhibitor of cathepsin K, Odanacatib . (immune-system-research.com)
  • First of all, Odanacatib (MK-0822) is a selective inhibitor of cathepsin K, with an IC 50 of 0.2 nM for human cathepsin K. Importantly, Odanacatib is a weak inhibitor of antigen presentation, measured in a mouse B cell line (IC 50 =1.5±0.4 μM). (immune-system-research.com)
  • All in all, Odanacatib (MK-0822) is a potent and selective inhibitor of cathepsin K and has the potential for osteoporosis research. (immune-system-research.com)
  • Additionally, freshly dissected human carotid plaques were treated with our potent cathepsin inhibitor and macrophage apoptosis was evaluated by fluorescent microscopy. (huji.ac.il)
  • In addition, our cathepsin inhibitor selectively induced cell apoptosis of 55%±10% of the macrophage within excised human atherosclerotic plaques. (huji.ac.il)
  • Our inhibitor confirms cathepsin-targeting as a promising approach to treat atherosclerotic plaque inflammation. (huji.ac.il)
  • Unlike some of the other cathepsins, cathepsin D has some protease activity at neutral pH. (wikipedia.org)
  • cathepsin protease activity is highly elevated in macrophages of vulnerable plaques and contributes to plaque instability. (huji.ac.il)
  • Cathepsin K is the most potent mammalian collagenase. (wikipedia.org)
  • Amino-acid sequence alignment and inhibition studies showed that the barley aspartic proteinase resembles mammalian lysosomal cathepsin D (EC 3.4.23.5). (lu.se)
  • The aim of this study was to determine whether targeting cathepsin S could induce autophagy/apoptosis in cancer cells. (tmu.edu.tw)
  • In this study, we demonstrated that targeting cathepsin S by either specific small molecular inhibitors or cathepsin S siRNA induced autophagy and subsequent apoptosis in human cancer cells, and the induction of autophagy was dependent on the phosphorylation of EGFR and activation of the EGFR-related ERK/MAPK-signaling pathway. (tmu.edu.tw)
  • We then focus on the opposing functions of cathepsin D in apoptosis , particularly relevant in cancer research . (bvsalud.org)
  • Finally, we discuss how insights from yeast cathepsin D and its role in regulated cell death can unveil novel functions of mammalian cathepsin D in apoptosis and cancer . (bvsalud.org)
  • Five cyclic peptides show inhibitory activity towards human cathepsins L, B, H, and K. Several inhibitors have reached clinical trials, targeting cathepsins K and S as promising therapeutics for osteoporosis, osteoarthritis, and chronic pain. (wikipedia.org)
  • We also determined the structure of the most potent and selective cathepsin B azainhibitor by means of NMR studies and theoretical calculations. (lu.se)
  • Cathepsin C (CTSC) is a lysosomal protease known to activate enzymes that are vital to the body's defenses. (lu.se)
  • There are, however, exceptions such as cathepsin K, which works extracellularly after secretion by osteoclasts in bone resorption. (wikipedia.org)
  • Osteoclasts are the bone resorbing cells of the body, and they secrete cathepsin K in order to break down collagen, the major component of the non-mineral protein matrix of the bone. (wikipedia.org)
  • Besides, cathepsin K is the only tissue protease that is highly expressed in osteoclasts. (immune-system-research.com)
  • Furthermore, cathepsin K secretes from osteoclasts to the sealed osteoclast bone cell interface, leading to effective degradation of type I collagen. (immune-system-research.com)
  • Meanwhile, cathepsin K is a recognized component in osteoclasts and plays an important role in the function of osteoclasts and the degradation of protein components in cells. (immune-system-research.com)
  • Results: We demonstrate that our ABPs accurately detect murine atherosclerotic plaques non-invasively, identifying cathepsin activity within plaque macrophages. (huji.ac.il)
  • In this review , we provide an overview of the role of cathepsin D in physiological and pathological scenarios. (bvsalud.org)
  • Para la elaboración de este artículo de revisión narrativa se consultaron las publicaciones disponibles a neutrófilos en el través de una búsqueda automatizada en las bases de datos de PubMed, Scopus y Embase. (bvsalud.org)
  • Cathepsin K, among other cathepsins, plays a role in cancer metastasis through the degradation of the extracellular matrix. (wikipedia.org)
  • Stroke Traumatic brain injury Alzheimer's disease Arthritis Ebola, Cathepsin B and to a lesser extent cathepsin L have been found to be necessary for the virus to enter host cells. (wikipedia.org)
  • The genetic knockout for cathepsin S and K in mice with atherosclerosis was shown to reduce the size of atherosclerotic lesions. (wikipedia.org)
  • Conclusions: Cathepsin ABPs present a rapid diagnostic tool for macrophage detection in atherosclerotic plaque. (huji.ac.il)
  • Cathepsin K is involved in osteoporosis, a disease in which a decrease in bone density causes an increased risk for fracture. (wikipedia.org)
  • Methods: We have applied quenched fluorescent cathepsin activity-based probes (ABPs) to a murine atherosclerosis model and evaluated their use for in vivo imaging using fluorescent molecular tomography (FMT), as well as ex vivo fluorescence imaging and fluorescent microscopy. (huji.ac.il)
  • Cathepsin B has also been implicated in the progression of various human tumors including ovarian cancer. (wikipedia.org)
  • Mouse cathepsin L is homologous to human cathepsin V. Mouse cathepsin L has been shown to play a role in adipogenesis and glucose intolerance in mice. (wikipedia.org)
  • Description: A sandwich quantitative ELISA assay kit for detection of Human Cathepsin K (CTSK) in samples from serum, plasma, tissue homogenates or other biological fluids. (elisastrip.com)
  • Cathepsin D has garnered increased attention in recent years, mainly since it has been associated with several human pathologies . (bvsalud.org)
  • Cathepsins have a vital role in mammalian cellular turnover. (wikipedia.org)
  • However, cathepsin D can have both anti- and pro- survival functions depending on its proteolytic activity, cellular context and stress stimulus. (bvsalud.org)
  • Cathepsin zymography separates different cathepsins based on their migration through a polyacrylamide gel co-polymerized with a gelatin substrate. (wikipedia.org)
  • Comparison of these values indicated that all of the azainhibitors act much stronger toward cathepsin B. Z-Arg-Leu-His-Agly-Ile-Val-OMe (7) proved to be approximately 500 times more potent for cathepsin B than for cathepsin K. To be able to explain the obtained experimental values we used the molecular dynamics procedures to analyze the interactions between cathepsin B and compound 7. (lu.se)
  • In conclusion, the current study reveals that cathepsin S plays an important role in the regulation of cell autophagy through interference with the EGFR-ERK/MAPK-signaling pathway. (tmu.edu.tw)
  • Therefore, a more detailed understanding of cathepsin D regulation and how to modulate its apoptotic functions is clearly needed. (bvsalud.org)
  • The expression of cathepsin K in cultured endothelial cells is regulated by shear stress. (wikipedia.org)
  • The cathepsin A activity in lysates of metastatic lesions of malignant melanoma is significantly higher than in primary focus lysates. (wikipedia.org)
  • Cathepsin K has also been shown to play a role in arthritis. (wikipedia.org)
  • However, the role of cathepsin S in regulating cancer cell survival and death remains undefined. (tmu.edu.tw)
  • Emphasis is given to the role of the yeast protease Pep4p, the vacuolar counterpart of cathepsin D , in life and death . (bvsalud.org)
  • Role of engineered metal oxide nanoparticle agglomeration in reactive oxygen species generation and cathepsin B release in NLRP3 inflammasome activation and pulmonary toxicity. (cdc.gov)
  • Therefore, specific particle parameters, i.e. preexposure dispersion status and particle surface area, of two ENM (NiO and CeO2) were used to evaluate the role of ROS generation and cathepsin B release during ENM-induced toxicity. (cdc.gov)
  • Role of neutrophil extracellular la NETosis en las enfermedades infecciosas pulmonares. (bvsalud.org)
  • Cathepsin B may function as a beta-secretase 1, cleaving amyloid precursor protein to produce amyloid beta. (wikipedia.org)
  • Yeast as a tool to explore cathepsin D function. (bvsalud.org)
  • Cathepsins B and L are involved in matrix degradation and cell invasion. (wikipedia.org)
  • In particular, cathepsin D is often overexpressed and hypersecreted in cancer cells , implying it may constitute a therapeutic target. (bvsalud.org)
  • The cysteine cathepsins have attracted significant research effort as drug targets. (wikipedia.org)