A lysosomal papain-related cysteine proteinase that is expressed in a broad variety of cell types.
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 cysteine endopeptidase found in NATURAL KILLER CELLS and CYTOTOXIC T-LYMPHOCYTES. It may have a specific function in the mechanism or regulation of cytolytic activity of immune cells.
A lysosomal cysteine proteinase with a specificity similar to that of PAPAIN. The enzyme is present in a variety of tissues and is important in many physiological and pathological processes. In pathology, cathepsin B has been found to be involved in DEMYELINATION; EMPHYSEMA; RHEUMATOID ARTHRITIS, and NEOPLASM INVASIVENESS.
A ubiquitously-expressed cysteine protease that plays an enzymatic role in POST-TRANSLATIONAL PROTEIN PROCESSING of proteins within SECRETORY GRANULES.
A genus of trematode liver flukes of the family Opisthorchidae. It consists of the following species: O. felineus, O. noverca (Amphimerus noverca), and O. viverrini. The intermediate hosts are snails, fish, and AMPHIBIANS.
An intracellular proteinase found in a variety of tissue. It has specificity similar to but narrower than that of pepsin A. The enzyme is involved in catabolism of cartilage and connective tissue. EC 3.4.23.5. (Formerly EC 3.4.4.23).
A cysteine protease that is highly expressed in OSTEOCLASTS and plays an essential role in BONE RESORPTION as a potent EXTRACELLULAR MATRIX-degrading enzyme.
Infection with flukes of the genus Opisthorchis.
A serine protease found in the azurophil granules of NEUTROPHILS. It has an enzyme specificity similar to that of chymotrypsin C.
An ubiquitously-expressed lysosomal cysteine protease that is involved in protein processing. The enzyme has both endopeptidase and aminopeptidase activities.
An aspartic endopeptidase that is similar in structure to CATHEPSIN D. It is found primarily in the cells of the immune system where it may play a role in processing of CELL SURFACE ANTIGENS.
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 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.

Molecular cloning and structural and functional characterization of human cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain. (1/18)

A cDNA encoding a new cysteine proteinase belonging to the papain family and called cathepsin F has been cloned from a human prostate cDNA library. This cDNA encodes a polypeptide of 484 amino acids, with the same domain organization as other cysteine proteinases, including a hydrophobic signal sequence, a prodomain, and a catalytic region. However, this propeptide domain is unusually long and distinguishes cathepsin F from other proteinases of the papain family. Cathepsin F also shows all structural motifs characteristic of these proteinases, including the essential cysteine residue of the active site. Consistent with these structural features, cathepsin F produced in Escherichia coli as a fusion protein with glutathione S-transferase degrades the synthetic peptide benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin, a substrate commonly used for functional characterization of cysteine proteinases. Furthermore, this proteolytic activity is blocked by trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane, an inhibitor of cysteine proteinases. The gene encoding cathepsin F maps to chromosome 11q13, close to that encoding cathepsin W. Cathepsin F is widely expressed in human tissues, suggesting a role in normal protein catabolism. Northern blot analysis also revealed a significant level of expression in some cancer cell lines opening the possibility that this enzyme could be involved in degradative processes occurring during tumor progression.  (+info)

Role of N-glycosylation in cathepsin E. A comparative study of cathepsin E with distinct N-linked oligosaccharides and its nonglycosylated mutant. (2/18)

Cathepsin E (CE), a nonlysosomal, intracellular aspartic proteinase, exists in several molecular forms that are N-glycosylated with high-mannose and/or complex-type oligosaccharides. To investigate the role of N-glycosylation on the catalytic properties and molecular stability of CE, both natural and recombinant enzymes with distinct oligosaccharides were purified from different sources. An N-glycosylation minus mutant, that was constructed by site-directed mutagenesis (by changing asparagine residues to glutamine and aspartic acid residues at positions 73 and 305 in potential N-glycosylation sites of rat CE) and expressed in normal rat kidney cells, was also purified to homogeneity from the cell extracts. The kinetic parameters of the nonglycosylated mutant were found to be essentially equivalent to those of natural enzymes N-glycosylated with either high-mannose or complex-type oligosaccharides. In contrast, the nonglycosylated mutant showed lower pH and thermal stabilities than the glycosylated enzymes. The nonglycosylated mutant exhibited particular sensitivity to conversion to a monomeric form by 2-mercaptoethanol, as compared with those of the glycosylated enzymes. Further, the high-mannose-type enzymes were more sensitive to this agent than the complex-type proteins. A striking difference was found between the high-mannose and complex-type enzymes in terms of activation by ATP at a weakly acidic pH. At pH 5.5, the complex-type enzymes were stabilized by ATP to be restored to the virtual activity, whereas the high-mannose-type enzymes as well as the nonglycosylated mutant were not affected by ATP. These results suggest that N-glycosylation in CE is important for the maintenance of its proper folding upon changes in temperature, pH and redox state, and that the complex-type oligosaccharides contribute to the completion of the tertiary structure to maintain its active conformation in the weakly acidic pH environments.  (+info)

Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages. (3/18)

The major histocompatibility complex (MHC) class II-associated invariant chain (Ii) regulates intracellular trafficking and peptide loading of MHC class II molecules. Such loading occurs after endosomal degradation of the invariant chain to a approximately 3-kD peptide termed CLIP (class II-associated invariant chain peptide). Cathepsins L and S have both been implicated in degradation of Ii to CLIP in thymus and peripheral lymphoid organs, respectively. However, macrophages from mice deficient in both cathepsins S and L can process Ii and load peptides onto MHC class II dimers normally. Both processes are blocked by a cysteine protease inhibitor, indicating the involvement of an additional Ii-processing enzyme(s). Comparison of cysteine proteases expressed by macrophages with those found in splenocytes and dendritic cells revealed two enzymes expressed exclusively in macrophages, cathepsins Z and F. Recombinant cathepsin Z did not generate CLIP from Ii-MHC class II complexes, whereas cathepsin F was as efficient as cathepsin S in CLIP generation. Inhibition of cathepsin F activity and MHC class II peptide loading by macrophages exhibited similar specificity and activity profiles. These experiments show that cathepsin F, in a subset of antigen presenting cells (APCs), can efficiently degrade Ii. Different APCs can thus use distinct proteases to mediate MHC class II maturation and peptide loading.  (+info)

Cathepsin L antisense oligonucleotides in a human osteosarcoma cell line: effects on the invasive phenotype. (4/18)

Alterations in cathepsin L expression and trafficking have been associated with the progression and metastasis of several tumor entities. In the present study, we examined the effects of various cathepsin L antisense (as) phosphorothioate oligonucleotides on both the expression of cathepsin L and the invasive potential of the human osteosarcoma cell line MNNG/HOS. Seven oligonucleotides of 20-bp length each and one random control oligonucleotide were chosen to block cathepsin L expression. Northern blot analysis demonstrated a significant reduction in cathepsin L mRNA expression by the six antisense oligonucleotides at a concentration of 10 microM. Cathepsin L protein expression was reduced significantly (50-85%) by the antisense oligonucleotides, as compared with the controls. Adhesion to matrices of collagen I and matrigel was not affected. In in vitro motility and invasion assays performed in uncoated and precoated transwell chambers, the ability of cells to migrate through the filters was inhibited by 35-75% using antisense oligonucleotides. The random control did not show any inhibitory effect. These data demonstrate that in MNNG/HOS cells cathepsin L influences cellular malignancy by promoting migration and basement membrane degradation.  (+info)

Cysteine protease cathepsin F is expressed in human atherosclerotic lesions, is secreted by cultured macrophages, and modifies low density lipoprotein particles in vitro. (5/18)

During atherogenesis, low density lipoprotein (LDL) particles in the arterial intima become modified and fuse to form extracellular lipid droplets. Proteolytic modification of apolipoprotein (apo) B-100 may be one mechanism of droplet formation from LDL. Here we studied whether the newly described acid protease cathepsin F can generate LDL-derived lipid droplets in vitro. Treatment of LDL particles with human recombinant cathepsin F led to extensive degradation of apoB-100, which, as determined by rate zonal flotation, electron microscopy, and NMR spectroscopy, triggered both aggregation and fusion of the LDL particles. Two other acid cysteine proteases, cathepsins S and K, which have been shown to be present in the arterial intima, were also capable of degrading apoB-100, albeit less efficiently. Cathepsin F treatment resulted also in enhanced retention of LDL to human arterial proteoglycans in vitro. Cultured monocyte-derived macrophages were found to secrete active cathepsin F. In addition, similarly with cathepsins S and K, cathepsin F was found to be localized mainly within the macrophage-rich areas of the human coronary atherosclerotic plaques. These results suggest that proteolytic modification of LDL by cathepsin F may be one mechanism leading to the extracellular accumulation of LDL-derived lipid droplets within the proteoglycan-rich extracellular matrix of the arterial intima during atherogenesis.  (+info)

Overexpression of cathepsin F, matrix metalloproteinases 11 and 12 in cervical cancer. (6/18)

BACKGROUND: Cervical carcinoma (CC) is one of the most common cancers among women worldwide and the first cause of death among the Mexican female population. CC progression shows a continuum of neoplastic transitions until invasion. Matrix metalloproteinases (MMPs) and cathepsins play a central role on the enhancement of tumor-induced angiogenesis, cell migration, proliferation, apoptosis and connective tissue degradation. MMPs -2 and -9 expression has been widely studied in cervical cancer. Nevertheless, no other metalloproteinases or cathepsins have been yet related with the progression and/or invasion of this type of cancer. METHODS: Three HPV18 CC cell lines, two HPV16 CC cell lines and three HPV16 tumor CC tissues were compared with three morphologically normal, HPV negative, cervical specimens by cDNA arrays. Overexpression of selected genes was confirmed by end point semiquantitative reverse transcription-PCR with densitometry. In situ hybridization and protein expression of selected genes was further studied by means of two tissue microarrays, one consisting of 10 HSIL and 15 CC and the other one of 15 normal cervical and 10 LSIL tissues. RESULTS: TIMP1, Integrins alpha 1 and 4, cadherin 2 and 11, Cathepsins F, B L2, MMP 9, 10 11 and 12 were upregulated and Cathepsin S, L, H and C, Cadherins 3 and 4, TIMP3, MMP 13, Elastase 2 and Integrin beta 8 were found to be downregulated by cDNA arrays. Endpoint RT-PCR with densitometry gave consistent results with the cDNA array findings for all three genes selected for study (CTSF, MMP11 and MMP12). In situ hybridization of all three genes confirmed overexpression in all the HSIL and CC. Two of the selected proteins were detected in LSIL, HSIL and CC by immunohistochemistry. CONCLUSION: Novel undetected CC promoting genes have been identified. Increased transcription of these genes may result in overexpression of proteins, such as CTSF, MMP11 and MMP12 which could contribute to the pathogenesis of CC.  (+info)

Murine cathepsin F deficiency causes neuronal lipofuscinosis and late-onset neurological disease. (7/18)

Cathepsin F (cat F) is a widely expressed lysosomal cysteine protease whose in vivo role is unknown. To address this issue, mice deficient in cat F were generated via homologous recombination. Although cat F-/- mice appeared healthy and reproduced normally, they developed progressive hind leg weakness and decline in motor coordination at 12 to 16 months of age, followed by significant weight loss and death within 6 months. cat F was found to be expressed throughout the central nervous system (CNS). cat F-/- neurons accumulated eosinophilic granules that had features typical of lysosomal lipofuscin by electron microscopy. Large amounts of autofluorescent lipofuscin, characteristic of the neurodegenerative disease neuronal ceroid lipofuscinosis (NCL), accumulated throughout the CNS but not in visceral organs, beginning as early as 6 weeks of age. Pronounced gliosis, an indicator of neuronal stress and neurodegeneration, was also apparent in older cat F-/- mice. cat F is the only cysteine cathepsin whose inactivation alone causes a lysosomal storage defect and progressive neurological features in mice. The late onset suggests that this gene may be a candidate for adult-onset NCL.  (+info)

Cloning and expression of the cathepsin F-like cysteine protease gene in Escherichia coli and its characterization. (8/18)

In this study, we have cloned a novel cDNA encoding for a papain-family cysteine protease from the Uni-ZAP XR cDNA library of the polychaete, Periserrula leucophryna. This gene was expressed in Escherichia coli using the T7 promoter system, and the protease was characterized after partial purification. First, the partial DNA fragment (498 bp) was amplified from the total RNA via RT-PCR using degenerated primers derived from the conserved region of cysteine protease. The full-length cDNA of cysteine protease (PLCP) was prepared via the screening of the Uni-ZAP XR cDNA library using the 32P-labeled partial DNA fragment. As a result, the PLCP gene was determined to consist of a 2591 bp nucleotide sequence (CDS: 173-1024 bp) which encodes for a 283-amino acid polypeptide, which is itself composed of an 59-residue signal sequence, a 6-residue propeptide, a 218-residue mature protein, and a long 3'-noncoding region encompassing 1564 bp. The predicted molecular weights of the preproprotein and the mature protein were calculated as 31.8 kDa and 25 kDa, respectively. The results of sequence analysis and alignment revealed a significant degree of sequence similarity with other eukaryotic cysteine proteases, including the conserved catalytic triad of the Cys90, His226, and Asn250 residues which characterize the C1 family of papain-like cysteine protease. The nucleotide and amino acid sequences of the novel gene were deposited into the GenBank database under the accession numbers, AY390282 and AAR27011, respectively. The results of Northern blot analysis revealed the 2.5 kb size of the transcript and ubiquitous expression throughout the entirety of the body, head, gut, and skin, which suggested that the PLCP may be grouped within the cathepsin F-like proteases. The region encoding for the mature form of the protease was then subcloned into the pT7-7 expression vector following PCR amplification using the designed primers, including the initiation and termination codons. The recombinant cysteine proteases were generated in a range of 6.3% to 12.5% of the total cell proteins in the E. coli BL21(DE3) strain for 8 transformants. The results of SDS-PAGE and Western blot analysis indicated that a cysteine protease of approximately 25 kDa (mature form) was generated. The optimal pH and temperature of the enzyme were determined to be approximately 9.5 and 35 degrees, respectively, thereby indicating that the cysteine protease is a member of the alkaline protease group. The evaluation of substrate specificity indicated that the purified protease was more active towards Arg-X or Lys-X and did not efficiently cleave the substrates with non-polar amino acids at the P1 site. The PLCP evidenced fibrinolytic activity on the plasminogen-free fibrin plate test.  (+info)

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.

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 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.

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.

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.

Opisthorchis is a genus of trematode flatworms that are commonly known as liver flukes. These parasites primarily infect the bile ducts and liver of various mammals, including humans. The most common species that infect humans are Opisthorchis viverrini and Opisthorchis felineus.

Humans become infected with these parasites by consuming raw or undercooked fish that contain the larval stage of the fluke (metacercariae). Once ingested, the metacercariae excyst in the small intestine and migrate to the bile ducts, where they mature into adults. Adult Opisthorchis worms are thin and elongated, with a length of 7-15 mm and a width of 1-3 mm. They have a characteristic brownish color due to their diet, which consists mainly of blood and bile.

Infection with Opisthorchis can lead to chronic inflammation of the bile ducts and liver, which may result in symptoms such as abdominal pain, diarrhea, weight loss, and fatigue. Long-term infection has been linked to an increased risk of cholangiocarcinoma, a rare but aggressive form of liver cancer.

Prevention of Opisthorchis infection involves avoiding the consumption of raw or undercooked fish, particularly in areas where the parasite is endemic. Infection can also be treated with anti-parasitic drugs such as praziquantel.

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 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.

Opisthorchiasis is a parasitic infection caused by the trematode flatworms of the genus Opisthorchiidae, specifically Opisthorchis viverrini and Opisthorchis felineus. These flatworms are transmitted to humans through the consumption of raw or undercooked fish that contain the infective larval stage (metacercariae) of the parasite.

Once ingested, the metacercariae excyst in the small intestine and migrate to the bile ducts of the liver, where they mature into adult worms and reside. The adults can live for several years in the host's body, producing eggs that are released into the bile and then passed through the stool.

The infection can cause a range of symptoms, including abdominal pain, diarrhea, liver enlargement, and bile duct inflammation. Chronic opisthorchiasis can lead to more severe complications such as cholangitis, cholecystitis, gallstones, and liver cirrhosis. In some cases, it may also increase the risk of developing cholangiocarcinoma, a rare but aggressive form of bile duct cancer.

Preventive measures include avoiding the consumption of raw or undercooked fish, particularly in areas where the infection is endemic, and practicing good personal hygiene to prevent fecal-oral transmission. Treatment typically involves the use of anti-parasitic drugs such as praziquantel or albendazole to kill the adult worms and prevent further complications.

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 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 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.

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 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.

... 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 ...
... J Biol Chem. 2016 May 6;291(19):9920-8. doi: 10.1074/ ... Cathepsin S (Ctss) is a cysteine protease that is actively secreted in areas of tissue injury and ongoing inflammation, where ...
Highly specific and rigorously validated in-house, Cathepsin H (E6L4W) Rabbit Monoclonal Antibody (CST #54007) is ready to ship ... Monoclonal Antibody for studying Cathepsin H mouse. Validated for Western Blotting. ... Cathepsin H (E6L4W) Rabbit mAb recognizes endogenous levels of mature cathepsin H protein. ... using Cathepsin H (E6L4W) Rabbit mAb (upper) or β-Actin (D6A8) Rabbit mAb #8457 (lower). Negative expression of cathepsin H ...
Final Theses freely available via Open Access
CTSL / Cathepsin L. Cathepsin L. CTSL / Cathepsin L is a lysosomal cysteine proteinase that plays a major role in intracellular ... Modulation of Cathepsin L Expression in the Coronary Arteries of Atherosclerotic Swine. Palanikumar Gunasekar, Mohan Satish, ... Human CTSL / Cathepsin L Protein (Recombinant 6His, C-terminus) (Thr18-Val333) - LS-G38921 ... Human CTSL / Cathepsin L Protein (Recombinant His, N-Terminal) (aa114-288) - LS-G11978 ...
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 ...
Effects of -1.5 degrees C Super-chilling on quality of Atlantic salmon (Salmo salar) pre-rigor Fillets: Cathepsin activity, ... Effects of -1.5 degrees C Super-chilling on quality of Atlantic salmon (Salmo salar) pre-rigor Fillets: Cathepsin activity, ... Effects of -1.5 degrees C Super-chilling on quality of Atlantic salmon (Salmo salar) pre-rigor Fillets: Cathepsin activity, ... Lysosome breakages followed by release of cathepsin B and L during storage and myofibre-myofibre detachments were accelerated ...
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 ...
Murine β-galactosidase stability is not dependent on temperature or protective protein/cathepsin A Journal Articles ... and that human GLB1 activity is temperature and protective-dependent on protein cathepsin A, while that of mouse GLB1 is not. ...
CTSS cathepsin S, url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene Cmd=ShowDetailView TermToSearch=1520, accessdate = ] ... Cathepsin S, also known as CTSS, is a human gene.cite web , title = Entrez Gene: ... Cathepsin S. Cathepsin S, also known as CTSS, is a human gene. .. cite web , title = Entrez Gene: CTSS cathepsin S, url = http ... Cathepsin K - Cathepsin K, also known as CTSK, is a human enzyme controlled by a gene.cite web , title = Entrez Gene: CTSK ...
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 ...
"Cathepsin G" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical Subject ... This graph shows the total number of publications written about "Cathepsin G" by people in this website by year, and whether " ... Below are the most recent publications written about "Cathepsin G" by people in Profiles. ... Below are MeSH descriptors whose meaning is more general than "Cathepsin G". ...
Onsolidation with two cycles of high-dose ara-C. The studys principal objective was to examine ...
Our research is focused on cathepsin proteases and proteolytic systems controlled by these enzymes. They play a critical role ... Cathepsin-like proteases are also essential for viability or virulence of important human pathogens, parasites and pests. In ... Our research is focused on cathepsin proteases and proteolytic systems controlled by these enzymes. They play a critical role ... Structural Basis for Inhibition of Cathepsin B Drug Target from the Human Blood Fluke, Schistosoma mansoni ...
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, ...
The MSDS of Human for cathepsin is available from Karlan upon request. ... Human cathepsin G (GTSG) Sandwich ELISA Kit - 96 wells plate - 1 kit is backordered and will ship as soon as it is back in ... The MSDS of Human for cathepsin is available from Karlan upon request. ... The MSDS of Human for cathepsin is available from Karlan upon request. ...
Cathepsin D (CTSD) is a gene involved in amyloid precursor protein processing and is considered a candidate for Alzheimers ... Cathepsin D gene and the risk of Alzheimers disease: a population-based study and meta-analysis. ... Cathepsin D (CTSD) is a gene involved in amyloid precursor protein processing and is considered a candidate for Alzheimers ... Cathepsin D gene and the risk of Alzheimers disease: a population-based study and meta-analysis. ...
Cathepsin D of rat spleen. Affinity purification and properties of two types of cathepsin D ... Early events in the biosynthesis of the lysosomal enzyme cathepsin D. scientific article published on December 10, 1979 ... Early events in the biosynthesis of the lysosomal enzyme cathepsin D (English) ...
... 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 ...
CTSA: cathepsin A. *CTSD: cathepsin D. *CUBN: cubilin. *CUL3: cullin 3. *CUL7: cullin 7 ...
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 ...
Broadly acting cathepsins inhibitors against COVID-19 and emerging infectious diseases. Ted Daley, Chief Executive Officer, ... Ted Daley / Broadly acting cathepsins inhibitors against COVID-19 and emerging infectious diseases. ...
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 ...
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 S (Ctss) is a cysteine protease that is actively secreted in areas of tissue injury and ongoing inflammation, where it participates in extracellular matrix remodeling and healing. (nih.gov)
  • 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)
  • title=Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease. (en-academic.com)
  • title=The lysosomal cysteine protease, cathepsin S, is increased in Alzheimer's disease and Down syndrome brain. (en-academic.com)
  • 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)
  • 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)
  • Armed with this knowledge, we develop cathepsin inhibitors as a molecular tool for new therapeutic strategies. (uochb.cz)
  • 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)
  • Cathepsin C activates serine proteases expressed in hematopoietic cells by cleaving an N-terminal dipeptide from the proenzyme upon granule packaging. (edu.au)
  • Our research is focused on cathepsin proteases and proteolytic systems controlled by these enzymes. (uochb.cz)
  • Cathepsin-like proteases are also essential for viability or virulence of important human pathogens, parasites and pests. (uochb.cz)
  • In our work, we employ methods of biochemistry, molecular biology and structural biology to reveal mechanisms of function and natural regulation of cathepsins and related proteases. (uochb.cz)
  • 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)
  • Lysosome breakages followed by release of cathepsin B and L during storage and myofibre-myofibre detachments were accelerated in the super-chilled fillets. (nofima.no)
  • The differences in bioactivity of NiO-NP and CeO2-NP are likely due to NiO-NP facilitating the release of cathepsin B and in turn inflammasome activation generating proinflammatory cytokines. (cdc.gov)
  • 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)
  • The aim of this study was to determine whether targeting cathepsin S could induce autophagy/apoptosis in cancer cells. (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)
  • 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)
  • Cathepsin D gene and the risk of Alzheimer's disease: a population-based study and meta-analysis. (ox.ac.uk)
  • Cathepsin D (CTSD) is a gene involved in amyloid precursor protein processing and is considered a candidate for Alzheimer's disease (AD). (ox.ac.uk)
  • 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)
  • Cathepsin L in COVID-19: From Pharmacological Evidences to Genetics. (cdc.gov)
  • Cathepsin A increased in muscles moderately affected by muscular dystrophy and denervating diseases. (wikipedia.org)
  • Cathepsin B may function as a beta-secretase 1, cleaving amyloid precursor protein to produce amyloid beta. (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)
  • Negative expression of cathepsin H protein in mouse brain tissue is consistent with the predicted expression pattern. (cellsignal.com)
  • CTSL / Cathepsin L is a lysosomal cysteine proteinase that plays a major role in intracellular protein catabolism. (lsbio.com)
  • We show here that mouse GLB1 has greater stability when compared to human GLB1, and that human GLB1 activity is temperature and protective-dependent on protein cathepsin A, while that of mouse GLB1 is not. (mcmaster.ca)
  • 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)
  • There are, however, exceptions such as cathepsin K, which works extracellularly after secretion by osteoclasts in bone resorption. (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)
  • It has been suggested that the C-→ (224Ala→Val) transition within exon 2 of the cathepsin D gene (CTSD) might represent a risk factor for late onset AD. (manchester.ac.uk)
  • 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 expression of cathepsin K in cultured endothelial cells is regulated by shear stress. (wikipedia.org)
  • Modulation of Cathepsin L Expression in the Coronary Arteries of Atherosclerotic Swine. (lsbio.com)
  • title=Immunohistochemical and clinical evaluation of cathepsin expression in soft tissue sarcomas. (en-academic.com)
  • Cathepsin G" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (childrensmercy.org)
  • In particular, cathepsin D is often overexpressed and hypersecreted in cancer cells , implying it may constitute a therapeutic target. (bvsalud.org)
  • Cathepsin K is involved in osteoporosis, a disease in which a decrease in bone density causes an increased risk for fracture. (wikipedia.org)
  • Cathepsin D has garnered increased attention in recent years, mainly since it has been associated with several human pathologies . (bvsalud.org)
  • 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)
  • 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)
  • 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)
  • 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)
  • Human cathepsin G (GTSG) Sandwich ELISA Kit - 96 wells plate - 1 kit is backordered and will ship as soon as it is back in stock. (phantome.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)
  • 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)
  • 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)
  • 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)
  • title=Human cathepsin S: chromosomal localization, gene structure, and tissue distribution. (en-academic.com)
  • title=Structure and chromosomal assignment of the human cathepsin K gene. (en-academic.com)
  • The MSDS of Human for cathepsin is available from Karlan upon request. (phantome.org)
  • Cathepsin L-deficient mice were shown to have less adipose tissue, lower serum glucose and insulin levels, more insulin receptor subunits, more glucose transporter (GLUT4) and more fibronectin than wild type controls. (wikipedia.org)
  • 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)
  • 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)
  • Yeast as a tool to explore cathepsin D function. (bvsalud.org)
  • This graph shows the total number of publications written about "Cathepsin G" by people in this website by year, and whether "Cathepsin G" was a major or minor topic of these publications. (childrensmercy.org)
  • Below are the most recent publications written about "Cathepsin G" by people in Profiles. (childrensmercy.org)
  • Cathepsins B and L are involved in matrix degradation and cell invasion. (wikipedia.org)
  • Western blot analysis of extracts from various tissues and cell lines using Cathepsin H (E6L4W) Rabbit mAb (upper) or β-Actin (D6A8) Rabbit mAb #8457 (lower). (cellsignal.com)
  • The cysteine cathepsins have attracted significant research effort as drug targets. (wikipedia.org)