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 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 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 cysteine protease that is highly expressed in OSTEOCLASTS and plays an essential role in BONE RESORPTION as a potent EXTRACELLULAR MATRIX-degrading enzyme.
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.
An ubiquitously-expressed lysosomal cysteine protease that is involved in protein processing. The enzyme has both endopeptidase and aminopeptidase activities.
A serine protease found in the azurophil granules of NEUTROPHILS. It has an enzyme specificity similar to that of chymotrypsin C.
N-acylated oligopeptides isolated from culture filtrates of Actinomycetes, which act specifically to inhibit acid proteases such as pepsin and renin.
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.
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 lysosomal papain-related cysteine proteinase that is expressed in a broad variety of cell types.
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.
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 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 subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
Physiologically inactive substances that can be converted to active enzymes.
Phosphoric acid esters of mannose.
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.
Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).
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.
Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.
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)
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.
A receptor that is specific for IGF-II and mannose-6-phosphate. The receptor is a 250-kDa single chain polypeptide which is unrelated in structure to the type 1 IGF receptor (RECEPTOR, IGF TYPE 1) and does not have a tyrosine kinase domain.
A sub-subclass of endopeptidases that depend on an ASPARTIC ACID residue for their activity.
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.
Peptides composed of two amino acid units.
A hexosaminidase specific for non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. It acts on GLUCOSIDES; GALACTOSIDES; and several OLIGOSACCHARIDES. Two specific mammalian isoenzymes of beta-N-acetylhexoaminidase are referred to as HEXOSAMINIDASE A and HEXOSAMINIDASE B. Deficiency of the type A isoenzyme causes TAY-SACHS DISEASE, while deficiency of both A and B isozymes causes SANDHOFF DISEASE. The enzyme has also been used as a tumor marker to distinguish between malignant and benign disease.
Ubiquitously expressed integral membrane glycoproteins found in the LYSOSOME.
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.
An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.2.
A beta-N-Acetylhexosaminidase that catalyzes the hydrolysis of terminal, non-reducing 2-acetamido-2-deoxy-beta-glucose residues in chitobiose and higher analogs as well as in glycoproteins. Has been used widely in structural studies on bacterial cell walls and in the study of diseases such as MUCOLIPIDOSIS and various inflammatory disorders of muscle and connective tissue.
Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.
A group of inherited metabolic diseases characterized by the accumulation of excessive amounts of acid mucopolysaccharides, sphingolipids, and/or glycolipids in visceral and mesenchymal cells. Abnormal amounts of sphingolipids or glycolipids are present in neural tissue. INTELLECTUAL DISABILITY and skeletal changes, most notably dysostosis multiplex, occur frequently. (From Joynt, Clinical Neurology, 1992, Ch56, pp36-7)
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.
Membrane-bound cytoplasmic vesicles formed by invagination of phagocytized material. They fuse with lysosomes to form phagolysosomes in which the hydrolytic enzymes of the lysosome digest the phagocytized material.
The spontaneous disintegration of tissues or cells by the action of their own autogenous enzymes.
Cytoplasmic vesicles formed when COATED VESICLES shed their CLATHRIN coat. Endosomes internalize macromolecules bound by receptors on the cell surface.
Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.
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 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.
The rate dynamics in chemical or physical systems.
A single-pass type I membrane protein. It is cleaved by AMYLOID PRECURSOR PROTEIN SECRETASES to produce peptides of varying amino acid lengths. A 39-42 amino acid peptide, AMYLOID BETA-PEPTIDES is a principal component of the extracellular amyloid in SENILE PLAQUES.
An extracellular cystatin subtype that is abundantly expressed in bodily fluids. It may play a role in the inhibition of interstitial CYSTEINE PROTEASES.
A degenerative disease of the BRAIN characterized by the insidious onset of DEMENTIA. Impairment of MEMORY, judgment, attention span, and problem solving skills are followed by severe APRAXIAS and a global loss of cognitive abilities. The condition primarily occurs after age 60, and is marked pathologically by severe cortical atrophy and the triad of SENILE PLAQUES; NEUROFIBRILLARY TANGLES; and NEUROPIL THREADS. (From Adams et al., Principles of Neurology, 6th ed, pp1049-57)
Laboratory mice that have been produced from a genetically manipulated EGG or EMBRYO, MAMMALIAN.

Low levels of cathepsin D are associated with a poor prognosis in endometrial cancer. (1/912)

Total cytosolic cathepsin D (Cat D) levels were estimated by an immunoradiometric assay in a series of 156 consecutive patients with surgical stages I-III primary endometrial adenocarcinoma. Simultaneously, the tissue content of both oestrogen (ER) and progesterone (PR) receptors, and p185HER-2/neu, DNA content (ploidy), and the fraction of S-phase cells (S-phase) were also estimated. Tumoral Cat D content ranged from 0 to 243 pmol mg(-1) protein (median 44 pmol mg(-1) protein) and was not associated with any of the established clinicopathological and biological prognostic variables, with the exception of a weak positive correlation with the tumoral p185HER-2/neu levels. Univariable analysis performed on a subset of 97 patients, followed for a minimum of 2 years or until death, showed that patient age at diagnosis, high histological grade, advanced surgical stage, vascular invasion, positive peritoneal cytology, low levels of Cat D, negative ER and PR status, aneuploidy, and high S-phase were predictive of the presence of persistent or recurrent disease. However, multivariable analysis revealed that only histological grade, surgical stage, Cat D and PR were significantly associated with the patient's outcome. From these findings, we conclude that Cat D is an independent prognostic factor in endometrial adenocarcinoma, its low levels being associated with a worse clinical outcome.  (+info)

HaCaT human keratinocytes express IGF-II, IGFBP-6, and an acid-activated protease with activity against IGFBP-6. (2/912)

The insulin-like growth factor (IGF) system plays an important role in skin. HaCaT human keratinocytes proliferate in response to IGFs and synthesize IGF-binding protein-3 (IGFBP-3). Recently, IGFBP-6 was also identified by NH2-terminal sequencing, but it has not been identified by Western ligand blotting. In the present study, IGFBP-6 was detected in HaCaT-conditioned medium by use of immunoblotting and Western ligand blotting with 125I-labeled IGF-II. Proteolytic activity against IGFBPs, an important mechanism for regulation of their activity, was then studied. An acid-activated, cathepsin D-like protease that cleaved both IGFBP-6 and IGFBP-3 was detected. Although proteolysis did not substantially reduce the size of immunoreactive IGFBP-6, it greatly reduced the ability of IGFBP-6 to bind 125I-IGF-II as determined by Western ligand blotting and solution assay. HaCaT keratinocytes do not express IGF-I mRNA, but IGF-II mRNA and protein expression was detected. These observations suggest the possibility of an autocrine IGF-II loop that is regulated by the relative expression of IGF-II, IGFBP-3, and IGFBP-6, and IGFBP proteases in these keratinocytes, although demonstration of this loop requires further study.  (+info)

Time at surgery during menstrual cycle and menopause affects pS2 but not cathepsin D levels in breast cancer. (3/912)

Many studies have addressed the clinical value of pS2 as a marker of hormone responsiveness and of cathepsin D (Cath D) as a prognostic factor in breast cancer. Because pS2 and Cath D are both oestrogen induced in human breast cancer cell lines, we studied the influence of the menstrual cycle phase and menopausal status at the time of surgery on the levels of these proteins in breast cancer. A population of 1750 patients with breast cancer, including 339 women in menstrual cycle, was analysed. Tumoral Cath D and pS2 were measured by radioimmunoassay. Serum oestradiol (E2), progesterone (Pg), follicle-stimulating hormone (FSH) and luteinizing hormone (LH) levels at the day of surgery were used to define the hormonal phase in premenopausal women. There was a trend towards a higher mean pS2 level in the follicular phase compared with the luteal phase (17 ng mg(-1) and 11 ng mg(-1) respectively, P = 0.09). Mean pS2 was lower in menopausal patients than in women with cycle (8 ng mg(-1) and 14 ng mg(-1) respectively, P = 0.0001). No differences in mean Cath D level were observed between the different phases of the menstrual cycle, or between pre- and post-menopausal women. In the overall population, pS2 was slightly positively associated with E2 and Pg levels and negatively associated with FSH and LH, probably reflecting the link between pS2 and menopausal status. In premenopausal women, no association was found between pS2 and E2, Pg, FSH or LH levels. There were no correlations between Cath D level and circulating hormone levels in the overall population. However, in the subgroup of premenopausal women with ER-positive (ER+) tumours, E2 was slightly associated with both pS2 and Cath D, consistent with oestrogen induction of these proteins in ER+ breast cancer cell lines. There are changes in pS2 level in breast cancer throughout the menstrual cycle and menopause. This suggests that the choice of the pS2 cut-off level should take the hormonal status at the time of surgery into account. In contrast, the level of Cath D is unrelated to the menstrual cycle and menopausal status.  (+info)

Selective perturbation of early endosome and/or trans-Golgi network pH but not lysosome pH by dose-dependent expression of influenza M2 protein. (4/912)

Many sorting stations along the biosynthetic and endocytic pathways are acidified, suggesting a role for pH regulation in protein traffic. However, the function of acidification in individual compartments has been difficult to examine because global pH perturbants affect all acidified organelles in the cell and also have numerous side effects. To circumvent this problem, we have developed a method to selectively perturb the pH of a subset of acidified compartments. We infected HeLa cells with a recombinant adenovirus encoding influenza virus M2 protein (an acid-activated ion channel that dissipates proton gradients across membranes) and measured the effects on various steps in protein transport. At low multiplicity of infection (m.o.i.), delivery of influenza hemagglutinin from the trans-Golgi network to the cell surface was blocked, but there was almost no effect on the rate of recycling of internalized transferrin. At higher m.o.i., transferrin recycling was inhibited, suggesting increased accumulation of M2 in endosomes. Interestingly, even at the higher m.o.i., M2 expression had no effect on lysosome morphology or on EGF degradation, suggesting that lysosomal pH was not compromised by M2 expression. However, delivery of newly synthesized cathepsin D to lysosomes was slowed in cells expressing active M2, suggesting that acidification of the TGN and endosomes is important for efficient delivery of lysosomal hydrolases. Fluorescence labeling using a pH-sensitive dye confirmed the reversible effect of M2 on the pH of a subset of acidified compartments in the cell. The ability to dissect the role of acidification in individual steps of a complex pathway should be useful for numerous other studies on protein processing and transport.  (+info)

Acidic pH as a physiological regulator of human cathepsin L activity. (5/912)

Human cysteine protease cathepsin L was inactivated at acid pH by a first-order process. The inactivation rate decreased with increasing concentrations of a small synthetic substrate, suggesting that substrates stabilize the active conformation. The substrate-independent inactivation rate constant increased with organic solvent content of the buffer, consistent with internal hydrophobic interactions, disrupted by the organic solvent, also stabilizing the enzyme. Circular dichroism showed that the inactivation is accompanied by large structural changes, a decrease in alpha-helix content being especially pronounced. The high activation energy of the reaction at pH 3.0 (200 kJ.mol-1) supported such a major conformational change occurring. The acid inactivation of cathepsin L was irreversible, consistent with the propeptide being needed for proper folding of the enzyme. Aspartic protease cathepsin D was shown to cleave denatured, but not active cathepsin L, suggesting a potential mechanism for in-vivo regulation and turnover of cathepsin L inside lysosomes.  (+info)

Analysis of where and which types of proteinases participate in lysosomal proteinase processing using bafilomycin A1 and Helicobacter pylori Vac A toxin. (6/912)

Lysosomal proteinases are translated as preproforms, transported through the Golgi apparatus as proforms, and localized in lysosomes as mature forms. In this study, we analyzed which subclass of proteinases participates in the processing of lysosomal proteinases using Bafilomycin A1, a vacuolar ATPase inhibitor. Bafilomycin A1 raises lysosomal pH resulting in the degradation of lysosomal proteinases such as cathepsins B, D, and L. Twenty-four hours after the withdrawal of Bafilomycin A1, NIH3T3 cells possess these proteinases in amounts and activities similar to those in cells cultured in DMEM and 5% BCS. In the presence of various proteinase inhibitors, procathepsin processing is disturbed by E-64-d, resulting in abnormal processing of cathepsins D and L, but not by APMSF, Pepstatin A, or CA-074. In the presence of Helicobacter pylori Vac A toxin, which prevents vesicular transport from late endosomes to lysosomes, the processing of procathepsins B and D occurs, while that of procathepsin L does not. Thus, procathepsins B and D are converted to their mature forms in late endosomes, while procathepsin L is processed to the mature form after its arrival in lysosomes by some cysteine proteinase other than cathepsin B.  (+info)

Alternative mechanisms for trafficking of lysosomal enzymes in mannose 6-phosphate receptor-deficient mice are cell type-specific. (7/912)

Viable mice nullizygous in genes encoding the 300 kDa and the 46 kDa mannose 6-phosphate receptors (MPR 300 and MPR 46) and the insulin like growth factor II (IGF II) were generated to study the trafficking of lysosomal enzymes in the absence of MPRs. The mice have an I-cell disease-like phenotype, with increase of lysosomal enzymes in serum and normal activities in tissues. Surprisingly, the ability of MPR-deficient cells to transport newly synthesized lysosomal enzymes to lysosomes and the underlying mechanisms were found to depend on the cell type. MPR-deficient thymocytes target newly synthesized cathepsin D to lysosomes via an intracellular route. In contrast, hepatocytes and fibroblasts secrete newly synthesized cathepsin D. In fibroblasts recapture of secreted lysosomal enzymes, including that of cathepsin D, is limited and results in lysosomal storage, both in vivo and in vitro, whereas recapture by hepatocytes is remarkably effective in vivo and can result in lysosomal enzyme levels even above normal.  (+info)

Normal lysosomal morphology and function in LAMP-1-deficient mice. (8/912)

Lysosomal membranes contain two highly glycosylated proteins, designated LAMP-1 and LAMP-2, as major components. LAMP-1 and LAMP-2 are structurally related. To investigate the physiological role of LAMP-1, we have generated mice deficient for this protein. LAMP-1-deficient mice are viable and fertile. In LAMP-1-deficient brain, a mild regional astrogliosis and altered immunoreactivity against cathepsin-D was observed. Histological and ultrastructural analyses of all other tissues did not reveal abnormalities. Lysosomal properties, such as enzyme activities, lysosomal pH, osmotic stability, density, shape, and subcellular distribution were not changed in comparison with controls. Western blot analyses of LAMP-1-deficient and heterozygote tissues revealed an up-regulation of the LAMP-2 protein pointing to a compensatory effect of LAMP-2 in response to the LAMP-1 deficiency. The increase of LAMP-2 was neither correlated with an increase in the level of lamp-2 mRNAs nor with increased half-life time of LAMP-2. This findings suggest a translational regulation of LAMP-2 expression.  (+info)

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.

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 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.

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 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 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 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.

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.

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.

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 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.

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 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 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.

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.

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.

I'm sorry for any confusion, but "Mannosephosphates" is not a widely recognized or established term in medicine or biochemistry. It seems that this term may be a combination of "mannose," which is a type of sugar (monosaccharide), and "phosphates," which are compounds containing phosphorus. However, without more context, it's difficult to provide an accurate medical definition for this term.

In biochemistry, mannose can be linked to phosphate groups in various ways, such as in the context of mannose-1-phosphate or mannose-6-phosphate, which are involved in different metabolic pathways. If you could provide more information about where you encountered this term, I might be able to give a more precise definition or explanation.

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.

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).

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.

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.

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.

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.

IGF-2 (Insulin-like Growth Factor 2) receptor is a type of transmembrane protein that plays a role in cell growth, differentiation, and survival. Unlike other receptors in the insulin and IGF family, IGF-2 receptor does not mediate the activation of intracellular signaling pathways upon binding to its ligand (IGF-2). Instead, it acts as a clearance receptor that facilitates the removal of IGF-2 from circulation by transporting it to lysosomes for degradation.

The IGF-2 receptor is also known as cation-independent mannose-6-phosphate receptor (CI-M6PR) because it can also bind and transport mannose-6-phosphate-containing enzymes to lysosomes for degradation.

Mutations in the IGF-2 receptor gene have been associated with certain types of cancer, as well as developmental disorders such as Beckwith-Wiedemann syndrome.

Aspartic acid endopeptidases are a type of enzyme that cleave peptide bonds within proteins. They are also known as aspartyl proteases or aspartic proteinases. These enzymes contain two catalytic aspartic acid residues in their active site, which work together to hydrolyze the peptide bond.

Aspartic acid endopeptidases play important roles in various biological processes, including protein degradation, processing, and activation. They are found in many organisms, including viruses, bacteria, fungi, plants, and animals. Some well-known examples of aspartic acid endopeptidases include pepsin, cathepsin D, and HIV protease.

Pepsin is a digestive enzyme found in the stomach that helps break down proteins in food. Cathepsin D is a lysosomal enzyme that plays a role in protein turnover and degradation within cells. HIV protease is an essential enzyme for the replication of the human immunodeficiency virus (HIV), which causes AIDS. Inhibitors of HIV protease are used as antiretroviral drugs to treat HIV infection.

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.

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.

Beta-N-Acetylhexosaminidases are a group of enzymes that play a role in the breakdown and recycling of complex carbohydrates in the body. Specifically, they help to break down gangliosides, which are a type of molecule found in cell membranes.

There are several different isoforms of beta-N-Acetylhexosaminidases, including A, B, and S. These isoforms are formed by different combinations of subunits, which can affect their activity and substrate specificity.

Mutations in the genes that encode for these enzymes can lead to a variety of genetic disorders, including Tay-Sachs disease and Sandhoff disease. These conditions are characterized by an accumulation of gangliosides in the brain, which can cause progressive neurological deterioration and death.

Treatment for these conditions typically involves managing symptoms and providing supportive care, as there is currently no cure. Enzyme replacement therapy has been explored as a potential treatment option, but its effectiveness varies depending on the specific disorder and the age of the patient.

Lysosome-Associated Membrane Glycoproteins (LAMPs) are a group of proteins found in the membrane of lysosomes, which are cellular organelles responsible for breaking down and recycling various biomolecules. LAMPs play a crucial role in maintaining the integrity and function of the lysosomal membrane.

There are two major types of LAMPs: LAMP-1 and LAMP-2. Both proteins share structural similarities, including a large heavily glycosylated domain that faces the lumen of the lysosome and a short hydrophobic region that anchors them to the membrane.

The primary function of LAMPs is to protect the lysosomal membrane from degradation by hydrolytic enzymes present inside the lysosome. They also participate in the process of autophagy, a cellular recycling mechanism, by fusing with autophagosomes (double-membraned vesicles formed during autophagy) to form autolysosomes, where the contents are degraded.

Moreover, LAMPs have been implicated in several cellular processes, such as antigen presentation, cholesterol homeostasis, and intracellular signaling. Mutations in LAMP-2 have been associated with certain genetic disorders, including Danon disease, a rare X-linked dominant disorder characterized by heart problems, muscle weakness, and intellectual disability.

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.

Acid phosphatase is a type of enzyme that is found in various tissues and organs throughout the body, including the prostate gland, red blood cells, bone, liver, spleen, and kidneys. This enzyme plays a role in several biological processes, such as bone metabolism and the breakdown of molecules like nucleotides and proteins.

Acid phosphatase is classified based on its optimum pH level for activity. Acid phosphatases have an optimal activity at acidic pH levels (below 7.0), while alkaline phosphatases have an optimal activity at basic or alkaline pH levels (above 7.0).

In clinical settings, measuring the level of acid phosphatase in the blood can be useful as a tumor marker for prostate cancer. Elevated acid phosphatase levels may indicate the presence of metastatic prostate cancer or disease progression. However, it is important to note that acid phosphatase is not specific to prostate cancer and can also be elevated in other conditions, such as bone diseases, liver disorders, and some benign conditions. Therefore, acid phosphatase should be interpreted in conjunction with other diagnostic tests and clinical findings for a more accurate diagnosis.

Acetylglucosaminidase (ACG) is an enzyme that catalyzes the hydrolysis of N-acetyl-beta-D-glucosaminides, which are found in glycoproteins and glycolipids. This enzyme plays a crucial role in the degradation and recycling of these complex carbohydrates within the body.

Deficiency or malfunction of Acetylglucosaminidase can lead to various genetic disorders, such as mucolipidosis II (I-cell disease) and mucolipidosis III (pseudo-Hurler polydystrophy), which are characterized by the accumulation of glycoproteins and glycolipids in lysosomes, resulting in cellular dysfunction and progressive damage to multiple organs.

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.

Mucolipidoses are a group of inherited metabolic disorders characterized by the accumulation of complex carbohydrates (muco-) and fatty substances (lipids) in various tissues and cells (-oses). This is due to deficiency in enzymes that help break down these substances within lysosomes, which are organelles responsible for recycling and breaking down waste materials inside the cell.

There are four main types of mucolipidoses (I, II, III, and IV), each resulting from specific genetic mutations affecting different enzymes or proteins involved in the lysosomal degradation pathway. The symptoms, severity, and age of onset can vary widely among these types, ranging from mild to severe and including developmental delays, bone abnormalities, vision and hearing loss, heart problems, and coarse facial features.

Mucolipidoses are typically inherited in an autosomal recessive manner, meaning that an individual must inherit two copies of the mutated gene (one from each parent) to develop the condition. However, mucolipidosis II is caused by X-linked inheritance, where a single copy of the mutated gene on the X chromosome is enough to cause the disorder.

Early diagnosis and management of mucolipidoses can help improve quality of life and slow disease progression. Treatment options include physical therapy, occupational therapy, speech therapy, medications for symptom management, and in some cases, enzyme replacement therapy or bone marrow transplantation.

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.

Post-translational protein processing refers to the modifications and changes that proteins undergo after their synthesis on ribosomes, which are complex molecular machines responsible for protein synthesis. These modifications occur through various biochemical processes and play a crucial role in determining the final structure, function, and stability of the protein.

The process begins with the translation of messenger RNA (mRNA) into a linear polypeptide chain, which is then subjected to several post-translational modifications. These modifications can include:

1. Proteolytic cleavage: The removal of specific segments or domains from the polypeptide chain by proteases, resulting in the formation of mature, functional protein subunits.
2. Chemical modifications: Addition or modification of chemical groups to the side chains of amino acids, such as phosphorylation (addition of a phosphate group), glycosylation (addition of sugar moieties), methylation (addition of a methyl group), acetylation (addition of an acetyl group), and ubiquitination (addition of a ubiquitin protein).
3. Disulfide bond formation: The oxidation of specific cysteine residues within the polypeptide chain, leading to the formation of disulfide bonds between them. This process helps stabilize the three-dimensional structure of proteins, particularly in extracellular environments.
4. Folding and assembly: The acquisition of a specific three-dimensional conformation by the polypeptide chain, which is essential for its function. Chaperone proteins assist in this process to ensure proper folding and prevent aggregation.
5. Protein targeting: The directed transport of proteins to their appropriate cellular locations, such as the nucleus, mitochondria, endoplasmic reticulum, or plasma membrane. This is often facilitated by specific signal sequences within the protein that are recognized and bound by transport machinery.

Collectively, these post-translational modifications contribute to the functional diversity of proteins in living organisms, allowing them to perform a wide range of cellular processes, including signaling, catalysis, regulation, and structural support.

A phagosome is a type of membrane-bound organelle that forms around a particle or microorganism following its engulfment by a cell, through the process of phagocytosis. This results in the formation of a vesicle containing the ingested material, which then fuses with another organelle called a lysosome to form a phago-lysosome. The lysosome contains enzymes that digest and break down the contents of the phagosome, allowing the cell to neutralize and dispose of potentially harmful substances or pathogens.

In summary, phagosomes are important organelles involved in the immune response, helping to protect the body against infection and disease.

Autolysis is the process of self-digestion that occurs when living cells are broken down and destroyed through the action of their own enzymes. This term is often used in the context of biological or medical research, particularly in studies involving cell death and tissue breakdown. Autolysis can occur as a result of injury, disease, or programmed cell death (apoptosis). It's important to note that autolysis is different from necrosis, which is the premature death of cells due to external factors such as infection, toxins, or trauma.

Endosomes are membrane-bound compartments within eukaryotic cells that play a critical role in intracellular trafficking and sorting of various cargoes, including proteins and lipids. They are formed by the invagination of the plasma membrane during endocytosis, resulting in the internalization of extracellular material and cell surface receptors.

Endosomes can be classified into early endosomes, late endosomes, and recycling endosomes based on their morphology, molecular markers, and functional properties. Early endosomes are the initial sorting stations for internalized cargoes, where they undergo sorting and processing before being directed to their final destinations. Late endosomes are more acidic compartments that mature from early endosomes and are responsible for the transport of cargoes to lysosomes for degradation.

Recycling endosomes, on the other hand, are involved in the recycling of internalized cargoes back to the plasma membrane or to other cellular compartments. Endosomal sorting and trafficking are regulated by a complex network of molecular interactions involving various proteins, lipids, and intracellular signaling pathways.

Defects in endosomal function have been implicated in various human diseases, including neurodegenerative disorders, developmental abnormalities, and cancer. Therefore, understanding the mechanisms underlying endosomal trafficking and sorting is of great importance for developing therapeutic strategies to treat these conditions.

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.

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.

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.

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.

The Amyloid Beta-Protein Precursor (AβPP) is a type of transmembrane protein that is widely expressed in various tissues and organs, including the brain. It plays a crucial role in normal physiological processes, such as neuronal development, synaptic plasticity, and repair.

AβPP undergoes proteolytic processing by enzymes called secretases, resulting in the production of several protein fragments, including the amyloid-beta (Aβ) peptide. Aβ is a small peptide that can aggregate and form insoluble fibrils, which are the main component of amyloid plaques found in the brains of patients with Alzheimer's disease (AD).

The accumulation of Aβ plaques is believed to contribute to the neurodegeneration and cognitive decline observed in AD. Therefore, AβPP and its proteolytic processing have been the focus of extensive research aimed at understanding the pathogenesis of AD and developing potential therapies.

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.

Alzheimer's disease is a progressive disorder that causes brain cells to waste away (degenerate) and die. It's the most common cause of dementia — a continuous decline in thinking, behavioral and social skills that disrupts a person's ability to function independently.

The early signs of the disease include forgetting recent events or conversations. As the disease progresses, a person with Alzheimer's disease will develop severe memory impairment and lose the ability to carry out everyday tasks.

Currently, there's no cure for Alzheimer's disease. However, treatments can temporarily slow the worsening of dementia symptoms and improve quality of life.

Transgenic mice are genetically modified rodents that have incorporated foreign DNA (exogenous DNA) into their own genome. This is typically done through the use of recombinant DNA technology, where a specific gene or genetic sequence of interest is isolated and then introduced into the mouse embryo. The resulting transgenic mice can then express the protein encoded by the foreign gene, allowing researchers to study its function in a living organism.

The process of creating transgenic mice usually involves microinjecting the exogenous DNA into the pronucleus of a fertilized egg, which is then implanted into a surrogate mother. The offspring that result from this procedure are screened for the presence of the foreign DNA, and those that carry the desired genetic modification are used to establish a transgenic mouse line.

Transgenic mice have been widely used in biomedical research to model human diseases, study gene function, and test new therapies. They provide a valuable tool for understanding complex biological processes and developing new treatments for a variety of medical conditions.

... 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 ...
... 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: ...
... 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. ...
Miv-711 Cathepsin K inhibitor for osteoarthritis. Fast track (FDA) MALT1 "Swedish pharma firm Medivir partners Aragen Life ...
"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 ...
The protein is able to form a dimer stabilized by noncovalent forces, inhibiting papain and cathepsins L, H and B. The protein ... 1994). "Cathepsin B activity in human lung tumor cell lines: ultrastructural localization, pH sensitivity, and inhibitor status ... 1988). "Cathepsin D inactivates cysteine proteinase inhibitors, cystatins". Biochem. Biophys. Res. Commun. 154 (2): 765-72. doi ... Cystatin B has been shown to interact with Cathepsin B. GRCh38: Ensembl release 89: ENSG00000160213 - Ensembl, May 2017 GRCm38 ...
These cysteine proteases include calpain, caspase, and cathepsin. These three proteins are examples of detectable signs of ...
It is an inhibitor of cathepsin K, an enzyme involved in bone resorption. The drug was developed by Merck & Co. The phase III ... Le Gall, C. L.; Bonnelye, E.; Clézardin, P. (2008). "Cathepsin K inhibitors as treatment of bone metastasis". Current Opinion ... February 2008). "The discovery of odanacatib (MK-0822), a selective inhibitor of cathepsin K". Bioorg. Med. Chem. Lett. 18 (3 ...
Shimizu, K.; Cha, J.; Stucky, G. D.; Morse, D. E. (1998). "Silicatein : Cathepsin L-like protein in sponge biosilica". ...
... α: cathepsin L-like protein in sponge biosilica. Proceedings of the National Academy of Sciences, 95(11), pp.6234- ... Silicateins are homologous to the cysteine protease cathepsin. In sponges, the silicatein enzymes reside in the axial filaments ...
2000). "Secreted cathepsin L generates endostatin from collagen XVIII". EMBO J. 19 (6): 1187-94. doi:10.1093/emboj/19.6.1187. ... 2000). "Secreted cathepsin L generates endostatin from collagen XVIII". EMBO J. 19 (6): 1187-94. doi:10.1093/emboj/19.6.1187. ... by proteases such as cathepsins. Collagen is a component of epithelial and endothelial basement membranes. Endostatin, as a ...
Mediation by cathepsin G has been suggested. The treatment of RAS usually involves administering dexamethasone IV, with the ...
... 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 ...
"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 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 is involved in CLN10. DNA analysis can be used to help confirm the diagnosis of Batten disease. When the mutation ...
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 ...
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 ...
Directed screening of nitrile compounds revealed 3 as a highly potent cathepsin K inhibitor but with cathepsin S activity and ... Directed screening of nitrile compounds revealed 3 as a highly potent cathepsin K inhibitor but with cathepsin S activity and ... a potent and highly selective cathepsin K inhibitor for the treatment of osteoarthritis.. Dossetter, A.G., Beeley, H., Bowyer, ...
This procedure applies to all products that have a specification for Cathepsin B activity determined by the liberation of 7- ... Cathepsin B Enzyme Solution (Enzyme). Immediately before use, prepare a solution containing 5-10 units/mL of Cathepsin B in ... Lysosomal Cathepsin B has also been shown to degrade soluble monomeric collagen and insoluble polymeric collagen in vitro. ... Cathepsin B is a lysosomal cysteine proteinase that will hydrolyze proteins with a broad specificity for peptide bonds, but ...
CATHEPSIN D (human). Find diseases associated with this biological target and compounds tested against it in bioassay ...
Ausgesuchte Qualitäts-Hersteller für Cathepsin G Antikörper. Hier bestellen. ... Monoklonale und polyklonale Cathepsin G Antikörper für viele Methoden. ... Aliase für Cathepsin G Antikörper. cathepsin G (CTSG) Antikörper. cathepsin G (Ctsg) Antikörper. cathepsin G (LOC505658) ... cathepsin G (LOC509956) Antikörper. cathepsin G (ctsg) Antikörper. cathepsin G (LOC100053921) Antikörper. cathepsin G ( ...
The worlds first wiki where authorship really matters. Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts.
Cathepsin E mRNA was detected in enalapril-treated aorta and kidney, and cathepsin D mRNA was detected in all tissues examined ... Cathepsin E and cathepsin S, endosomal/lysosomal proteases, have been shown to play important roles in the major ... While significant amounts of cathepsin D were found in both the hippocampus and the neostriatum of normal rats, cathepsin E was ... Cathepsin E in follicle associated epithelium of intestine and tonsils: localization to M cells and possible role in antigen ...
"If cathepsin Bs activity is to chew back at the C-terminus of Aβ, particularly Aβ42, then a mouse with increased Aβ42 ... The enzyme, cathepsin B (CatB), caught the attention of Li Gan at the Gladstone Institute of Neurological Disease in San ... Cystatin Cs Naughty Side-Slowing Aβ Degradation by Cathepsin B. Quick Links. *Article ... production (the APP-J20 mouse) will show the greatest effects when cathepsin B activity is increased," he said. "I think that ...
One of the less explored is the milk enzyme cathepsin D, proteolytic enzyme located in the lysosomes, which are an integral ... Detection of cathepsin D in ewes milk by Western Blotting method. Iva Dolenčić Špehar orcid.org/0000-0002-8036-583X ; ... 2013). Detection of cathepsin D in ewes milk by Western Blotting method, Mljekarstvo, 63(1), str. 36-41. Preuzeto s: https ... Dolenčić Špehar I, Martinković F, Havranek J, Marinculić A, Tudor Kalit M, Kalit S. Detection of cathepsin D in ewes milk by ...
The cysteinal lysosomal proteases, cathepsin L (CL) and cathepsin S (CS), have been shown to process invariant chain, thereby ... A role for cathepsin L and cathepsin S in peptide generation for MHC class II presentation J Immunol. 2002 Mar 15;168(6):2618- ... The cysteinal lysosomal proteases, cathepsin L (CL) and cathepsin S (CS), have been shown to process invariant chain, thereby ...
Cathepsin B, also known as CTSB, is a lysosomal cysteine protease. ... Cathepsin B Activity Protocol: 1. Dilute the recombinant mouse Cathepsin B to 10 μg/ml in activation buffer (25 mM MES, 1 mM ... Cathepsin B, also known as CTSB, is a lysosomal cysteine protease. While most cathepsins are exclusively endopeptidases, CTSB ... CTSB, CPSB, APP secretase, APPS, Cathepsin B1, CB Ave. Rating Submit a Review Product Citations publications Mouse CTSB enzyme ...
Cathepsin B activity was selectively elevated early in the course of illness. Luepeptin, a cathepsin B inhibitor, and ... Inhibitors of prostaglandin synthesis or cathepsin B prevent muscle wasting due to sepsis in the rat.. ... Inhibitors of prostaglandin synthesis or cathepsin B prevent muscle wasting due to sepsis in the rat.. ... Muscle wasting and impaired contractility associated with sepsis may involve selective prostaglandin stimulation of cathepsin B ...
Pharmacological inhibition of cathepsin activity with CA074-Me resulted in a substantial reduction of both mature IL-1β ... Pharmacological inhibition of cathepsin activity with CA074-Me resulted in a substantial reduction of both mature IL-1β ... Moreover, cathepsin inhibition abolished the interaction between NLRP3 and ASC, measured by co-immunoprecipitation and by ... Moreover, cathepsin inhibition abolished the interaction between NLRP3 and ASC, measured by immunofluorescence imaging in H37Rv ...
Cathepsins are a class of globular lysosomal proteases, playing a vital role in mammalian cellular turnover. They degrade ... The cathepsin family consists of 12 cysteine proteases with broad exo- and endopeptidase activity, of which Cathepsin B is a ... Cathepsin B enzyme, human liver: 5 µL Component D: Assay Buffer: 20 mL Component E: Cathepsin B inhibitor Ac-LVK-CHO: 100 µM, ... Component A: Cathepsin B substrate, Ex/Em=354 nm/442 nm upon cleavage: 1 mM, 50 µL Component B: AMC, Fluorescence Reference ...
Verschiedene Studien weisen auf eine Beteiligung von Cathepsin D an Apoptose hin. In manchen Systemen ist die durch Cathepsin D ... Proteinolyse-unabhaengige proapoptotische Wirkung von Cathepsin D und Procathepsin D ... Übergangszustandsmimetika zur selektiven Inhibition der HIV-1 Protease und Cathepsin D by: Specker, Edgar Published: (2004) ... mediierte Apoptose durch seinen Inhibitor Pepstatin A hemmbar, in anderen ist die enzymatische Aktivität des Cathepsin D für ...
Western blot analysis of PARP-1 cleavage patterns in mutant lysates suggests that increases in pH dependent cathepsin activity ... Consistently, treatment with ALLM and Bafilomycin A1 (cathepsin/calpain and vacuolar-type H+-ATPase inhibitors, respectively), ... Taken together, these data suggest that vps11 promotes normal melanophore morphology and survival by inhibiting cathepsin ...
Tatò, Maia Lucia (2019): Untersuchungen zur Rolle von Cathepsin S beim experimentellen und humanen Systemischen Lupus ... Untersuchungen zur Rolle von Cathepsin S beim experimentellen und humanen Systemischen Lupus Erythematodes ... Untersuchungen zur Rolle von Cathepsin S beim experimentellen und humanen Systemischen Lupus Erythematodes ...
Cathepsin D was assayed with a Dako set. Keratin was measured by the Kreyberg method. Normal skin from behind the ear was taken ... There were trace amounts of cathepsin D within the dermis. In the control group (the skin samples), there were trace amounts of ... The aim of the present study was to evaluate the activity of cathepsin D in the structures of cholesteatoma.Material/Methods: ... cathepsin D within the corneous layer of the epithelium.Conclusions: Cathepsin D places a major role in bone tissue destruction ...
Serum cathepsin B activity was significantly higher in both the BRT-treated group (27.8±4.1 U/I,p<0.01) and the tumor- ... Serum cathepsin B activity was determined, tumor volumes were measured, and histological examinations of the tumor tissues were ... The aim of this study was to assess serum cathepsin activity during tumor progression and regression.Material/Methods: Of 60 ... bearing group (19.9±2.5 U/l, p<0.05), as compared to the controls (13.3±3.4U/l).Conclusions:Cathepsin B may play an ...
Recombinant Autographa californica nuclear polyhedrosis virus Viral cathepsin (VCATH) from Cusabio. Cat Number: CSB-EP340730ARA ... Recombinant Autographa californica nuclear polyhedrosis virus Viral cathepsin (VCATH) , CSB-EP340730ARA. (No reviews yet) Write ... Recombinant Autographa californica nuclear polyhedrosis virus Viral cathepsin (VCATH) , CSB-EP340730ARA Cusabio Other Organism ... Recombinant Autographa californica nuclear polyhedrosis virus Viral cathepsin (VCATH) , CSB-EP340730ARA. Rating Required Select ...
Mutations of the cathepsin C gene are responsible for Papillon-Lefèvre syndrome ... Mutations of the cathepsin C gene are responsible for Papillon-Lefèvre syndrome ...
Cathepsin L might be an efficient way to reduce the spread & severity of COVID-19 - Learn how. ... In addition, a broad range of other Cathepsin Assays, Cathepsin Inhibitors as well as recombinant Cathepsins, Cathepsin ... Furin Inhibitor Screening Kit as well as Cathepsin L Activity Assay Kit & Cathepsin L Inhibitor Screening Kit as tools to ... Cathepsin Inhibitors. Product Info Related Resources Cell Analysis Brochure. For cutting-edge research, you need the best cell- ...
Haim-Munk syndrome and Papillon-Lefèvre syndrome are allelic mutations in cathepsin C ... Haim-Munk syndrome and Papillon-Lefèvre syndrome are allelic mutations in cathepsin C ...
Submit a product review for Human Cathepsin L Biotinylated Antibody BAF952 ...
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 ...
Synthetic peptide surrounding aa 140 of mouse cathepsins D.. Activity cross reaction. Reacts with mouse CTSD / Cathepsin D. ... CTSD / Cathepsin D antibody CTSD, CPSD, CLN10, Lysosomal aspartyl peptidase, Lysosomal aspartyl protease, ProCathepsin D, CatD ...
cathepsin L - C1: Papain. Detailed annotation on the structure, function, physiology, pharmacology and clinical relevance of ... Cathepsins B, H and L have become important therapeutic targets as their proteolytic activity has been implicated in several ... cathepsin L1 , fs , furless , MEP , nackt , nkt , Cat L , p39 cysteine proteinase ... 2010) Identification and pre-clinical testing of a reversible cathepsin protease inhibitor reveals anti-tumor efficacy in a ...
The encoded protein is also known as cathepsin X and cathepsin P. This gene is ubiquitously expressed in cancer cell lines and ... Ortholog to human CTSZ (cathepsin Z); INTERACTS WITH 1-naphthyl isothiocyanate; 2,3,7,8-tetrachlorodibenzodioxin; 3,3,5,5- ...
Assessment of cathepsin D and L-like proteinases of poultry red mite, Dermanyssus gallinae (De Geer), as potential vaccine ... Assessment of cathepsin D and L-like proteinases of poultry red mite, Dermanyssus gallinae (De Geer), as potential vaccine ... Printed from /publications/assessment-cathepsin-d-and-l-proteinases-poultry-red-mite-dermanyssus-gallinae-de-geer on 07/12/23 ... assessment-cathepsin-d-and-l-proteinases-poultry-red-mite-dermanyssus-gallinae-de-geer ...
The Role of Cathepsin B in Pathophysiologies of Non-tumor and Tumor tissues: A Systematic Review. J Cancer. 14(12):2344-2358. ... The Role of Cathepsin B in Pathophysiologies of Non-tumor and Tumor tissues: A Systematic Review Jiangping Wang1#, Minying ... Wang J, Zheng M, Yang X, Zhou X, Zhang S. The Role of Cathepsin B in Pathophysiologies of Non-tumor and Tumor tissues: A ... Wang J, Zheng M, Yang X, Zhou X, Zhang S. The Role of Cathepsin B in Pathophysiologies of Non-tumor and Tumor tissues: A ...
  • 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)
  • Directed screening of nitrile compounds revealed 3 as a highly potent cathepsin K inhibitor but with cathepsin S activity and very poor stability to microsomes. (rcsb.org)
  • In manchen Systemen ist die durch Cathepsin D mediierte Apoptose durch seinen Inhibitor Pepstatin A hemmbar, in anderen ist die enzymatische Aktivität des Cathepsin D für seine apoptotische Involvierung entbehrlich. (uni-marburg.de)
  • In addition to our assays for studying binding of SARS-CoV-2 to the ACE2 receptor and screening for respective inhibitors/drugs (see below), we offer the Furin Activity Assay Kit & Furin Inhibitor Screening Kit as well as Cathepsin L Activity Assay Kit & Cathepsin L Inhibitor Screening Kit as tools to develop new targeted therapeutics for Covid-19. (promocell.com)
  • 2010) Identification and pre-clinical testing of a reversible cathepsin protease inhibitor reveals anti-tumor efficacy in a pancreatic cancer model. (guidetopharmacology.org)
  • 4. Méthot N, Rubin J, Guay D, Beaulieu C, Ethier D, Reddy TJ, Riendeau D, Percival MD. (2007) Inhibition of the activation of multiple serine proteases with a cathepsin C inhibitor requires sustained exposure to prevent pro-enzyme processing. (guidetopharmacology.org)
  • 5. Takahashi K, Ueno T, Tanida I, Minematsu-Ikeguchi N, Murata M, Kominami E. (2009) Characterization of CAA0225, a novel inhibitor specific for cathepsin L, as a probe for autophagic proteolysis. (guidetopharmacology.org)
  • Roche's cathepsin S inhibitor petesicatib (RO5459072 or RG7625) completed Phase 2 clinical evaluation in Sjögren's syndrome ( NCT02701985 ) and Phase 1 in celiac disease ( NCT02679014 ), but there are no active clinical trials registered with ClinicalTrials.gov . (guidetoimmunopharmacology.org)
  • 2008) The discovery of odanacatib (MK-0822), a selective inhibitor of cathepsin K. Bioorg Med Chem Lett , 18 (3): 923-8. (guidetoimmunopharmacology.org)
  • Pharmacological inhibition of cathepsin activity with CA074-Me resulted in a substantial reduction of both mature IL-1β production and caspase-1 activation in infected macrophages. (frontiersin.org)
  • Moreover, cathepsin inhibition abolished the interaction between NLRP3 and ASC, measured by immunofluorescence imaging in H37Rv-infected macrophages, demonstrating a critical role of the enzyme in NLRP3-inflammasome activation. (frontiersin.org)
  • Inhibition of the Furin protease and Cathepsin L might therefore be an efficient way to attenuate the infection process and reduce the spread and severity of COVID-19. (promocell.com)
  • 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)
  • SerpinB1 is critical for neutrophil survival through cell-autonomous inhibition of cathepsin G." Blood 121, no. 19 (2013): 3900-3907 van den Berg, Carmen W., et al. (athensresearch.com)
  • By screening a combinatorial pentapeptide amide collection in an inhibition assay, we systematically evaluated the potential of 19 proteinogenic amino acids and seven nonproteinogenic amino acids to serve as building blocks for inhibitors of human cathepsin L. Particularly efficient were aromatic, bulky, hydrophobic amino-acid residues, especially leucine, and positively charged residues, especially arginine. (uni-bielefeld.de)
  • RNAi mediated depletion of CD44 and MT1-MMP expression and pharmacological inhibition of cathepsin K attenuated CD44 promoted invasion through a collagen I matrix. (biomedcentral.com)
  • 2017) Cathepsin S inhibition combines control of systemic and peripheral pathomechanisms of autoimmune tissue injury. (guidetoimmunopharmacology.org)
  • 2010) Functionalized benzophenone, thiophene, pyridine, and fluorene thiosemicarbazone derivatives as inhibitors of cathepsin L. Bioorg Med Chem Lett , 20 (22): 6610-5. (guidetopharmacology.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)
  • The enzyme, cathepsin B (CatB), caught the attention of Li Gan at the Gladstone Institute of Neurological Disease in San Francisco several years ago when it appeared to prevent buildup of amyloid plaques in the brains of AD mice overexpressing mutant human amyloid precursor protein (APP). (alzforum.org)
  • 1. Dilute the recombinant mouse Cathepsin B to 10 μg/ml in activation buffer (25 mM MES, 1 mM DTT, pH 5.0) and incubate the protein at 25°C for 3 min. (biolegend.com)
  • This protein mediates either fusion of the virus membrane with the host cell membrane (TMPRSS2 activated mediation) or endocytosis of the virus particle (Cathepsin-activated mediation) and its entry into the cell. (promocell.com)
  • A further host protease required for activation of the S Protein is Cathepsin L which also facilitates SARS-CoV-2 entry into target cells through an alternative route. (promocell.com)
  • The S Protein is then processed/activated by the lysosomal Cathepsin L in the late endosomes (endo-lysosomes) following endocytosis of the virus. (promocell.com)
  • Specific Furin and Cathepsin L inhibitors which block proteolytic activation of the S Protein , and thus SARS-CoV-2 virus entry and replication, are potential antiviral agents to counteract SARS-CoV-2 infection and pathogenesis. (promocell.com)
  • Reacts with mouse CTSD / Cathepsin D. Cross reacts with human and rat protein. (covalab.com)
  • The encoded protein is also known as cathepsin X and cathepsin P. This gene is ubiquitously expressed in cancer cell lines and primary tumors and, like other members of this family, may be involved in tumorigenesis. (enigmadiagnostics.com)
  • The deduced amino acid sequence between the primers was identical to that reported for neutrophil cathepsin G, indicating that the protein of cutaneous mast cells previously shown to be immunologically cross-reactive with neutrophil cathepsin G has a comparable amino acid sequence. (duke.edu)
  • Quantitative real-time PCR, immuno-blotting and ELISA-based experiments have demonstrated that the transcript and protein expression of cathepsin K and MT1MMP increase in response to CD44/HA signalling in a panel of CD44-expressing breast cancer cell lines (MDA231, MDA157 and MCF7F). (biomedcentral.com)
  • Furthermore, CD44/HA signalling was shown to increase cathepsin K and MT1MMP mRNA and protein expression in the MDAMB231BO cells. (biomedcentral.com)
  • Cathepsin E Protein, Human (HEK293, His) is an approximately 46.0 kDa mouse cathepsin Dwith a His tag. (medchemexpress.com)
  • Human Cathepsin E is synthesized as a precursor protein, consisting of a signal peptide (residues 1 17), a propeptide (residues 18 53), and a mature chain (residues 54 396) [3] . (medchemexpress.com)
  • Furthermore, the discovery of Cathepsin B secretion and function as an extracellular matrix protein has broadened our appreciation for the impact of Cathepsin B on cancer progression. (edu.rs)
  • Cathepsin S is expressed in the lysosome of antigen presenting cells (dendritic cells, B-cells and macrophages) where it processes the invariant chain-MHC-II complex (a chaperone protein that prevents premature peptide loading) inside antigen presenting cells and in this way controls antigen presentation. (guidetoimmunopharmacology.org)
  • This invention relates to a compound of formula I and their use as inhibitors of Cathepsin C, pharmaceutical compositions containing the same, and methods of using the same as agents for treatment and/or prevention of diseases connected with dipeptidyl peptidase I activity, e.g. respiratory diseases. (justia.com)
  • Thus, inhibitors of Cathepsin C could potentially be useful therapeutics for the treatment of neutrophil-dominated inflammatory diseases such as chronic obstructive pulmonary disease (COPD), pulmonary emphysema, asthma, multiple sclerosis, and cystic fibrosis (Guay et al. (justia.com)
  • The cysteinal lysosomal proteases, cathepsin L (CL) and cathepsin S (CS), have been shown to process invariant chain, thereby facilitating MHC class II maturation. (nih.gov)
  • Cathepsins are a class of globular lysosomal proteases playing a vital role in mammalian cellular turnover. (eurogentec.com)
  • The cathepsin family consists of 12 cysteine proteases with broad exo- and endopeptidase activity, of which Cathepsin B is a member. (eurogentec.com)
  • Neutrophils are recruited to the site of joint inflammation and release Cathepsin G, elastase and proteinase 3, proteases which are believed to be responsible for cartilage destruction associated with rheumatoid arthritis. (justia.com)
  • Cathepsin E is an aspartic protease and a member of the peptidase A1 family of proteases. (medchemexpress.com)
  • Cathepsins represent a group of such proteases aimed at maintenance of cellular homeostasis. (edu.rs)
  • Cathepsin K is the most potent mammalian collagenase. (wikipedia.org)
  • It has been surprisingly found that the bicyclic compounds of the present invention possess potent Cathepsin C activity, high selectivity against other Cathepsins, e.g. (justia.com)
  • Among the most potent novel inhibitors, one peptide, RKLLW-NH2, shares the amphiphilic character of the nonamer fragment VMNGLQNRK of the autoinhibitory, substrate-like, but reverse-binding prosegment of human cathepsin L which blocks the active center of the enzyme. (uni-bielefeld.de)
  • Highly potent inhibitors of human cathepsin L identified by screening combinatorial pentapeptide amide collections", EUROPEAN JOURNAL OF BIOCHEMISTRY , vol. 267, 2000, pp. 5085-5092. (uni-bielefeld.de)
  • Cathepsins have a vital role in mammalian cellular turnover. (wikipedia.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)
  • Cathepsin B is a lysosomal cysteine proteinase that will hydrolyze proteins with a broad specificity for peptide bonds, but will preferentially cleave at the carboxyl side of Arg-Arg bonds in small molecule substrates. (sigmaaldrich.com)
  • The activity of Cathepsin B is determined by its ability to cleave the fluorogenic peptide substrate, Z-Leu-Arg-AMC (Z=Benzyloxycarbonyl, and AMC=7-amino-4-methylcoumarin) after activation. (biolegend.com)
  • The SensoLyte® 440 Cathepsin B Assay Kit provides a fluorogenic peptide for measurement of enzyme activity. (eurogentec.com)
  • This peptide releases the AMC (7-amino-4-methylcoumarin) fluorophore upon cathepsin B cleavage and can be detected with excitation at 354 nm and emission at 442 nm. (eurogentec.com)
  • Synthetic peptide surrounding aa 140 of mouse cathepsins D. (covalab.com)
  • Cathepsin E functions by breaking down proteins through the hydrolysis of peptide bonds at a specific peptide sequence site. (medchemexpress.com)
  • One of the less explored is the milk enzyme cathepsin D, proteolytic enzyme located in the lysosomes, which are an integral part of the somatic cells whose number varies depending on the animal's health. (srce.hr)
  • Cathepsins B, H and L have become important therapeutic targets as their proteolytic activity has been implicated in several pathological inflammatory conditions, such as arthritis and periodontitis. (guidetopharmacology.org)
  • 2. Frizler M, Schmitz J, Schulz-Fincke AC, Gütschow M. (2012) Selective nitrile inhibitors to modulate the proteolytic synergism of cathepsins S and F. J Med Chem , 55 (12): 5982-6. (guidetoimmunopharmacology.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)
  • The substrate Nα-CBZ-Arg-Arg-7-amido-4-methylcoumarin is used for the fluorometric detection of Cathepsin B activity. (sigmaaldrich.com)
  • Add 50 μl of the diluted, activated Cathepsin B (0.0025 µg/well) to a black well and start the reaction by adding 50 μl of 40 μM substrate. (biolegend.com)
  • Sensitive fluorogenic substrate for the quantitative determination of cathepsin B activity. (emdmillipore.com)
  • There are, however, exceptions such as cathepsin K, which works extracellularly after secretion by osteoclasts in bone resorption. (wikipedia.org)
  • Objectives: To investigate serum biomarkers, tartrate resistant acid phosphatase 5b (TRAcP5b) and cathepsin K, indicative of osteoclastic bone resorption, and their relationship to pain and pain change in knee osteoarthritis (OA). (nottingham.ac.uk)
  • Unlike some of the other cathepsins, cathepsin D has some protease activity at neutral pH. (wikipedia.org)
  • CTS protease activity also measured by zymograph electrophoresis of Cathepsins. (histoready.com)
  • Cathepsin B, also known as CTSB, is a lysosomal cysteine protease. (biolegend.com)
  • While most cathepsins are exclusively endopeptidases, CTSB exhibits both carboxypeptidase and endopeptidase activities. (biolegend.com)
  • Lysosomal cathepsin B (CTSB) has been proposed to play a role in the induction of acute inflammation. (frontiersin.org)
  • These observations suggest that during Mtb infection, lysosomal release of activated CTSB and possibly other cathepsins inhibitable by CA07-Me is critical for the induction of inflammasome-mediated IL-1β processing by regulating NLRP3-inflammasome assembly in the cytosol. (frontiersin.org)
  • Cathepsin B (CTSB), a lysosomal cysteine protease, plays an important role in human physiology and pathology. (jcancer.org)
  • This study establishes the primary structure of human skin chymase and provides further evidence for the presence of a cathepsin G-like proteinase within human mast cells. (duke.edu)
  • 2. Dilute the recombinant mouse Cathepsin B to 0.05 μg/ml in assay buffer (25 mM MES, pH 5.0). (biolegend.com)
  • In addition, a broad range of other Cathepsin Assays , Cathepsin Inhibitors as well as recombinant Cathepsins , Cathepsin antibodies & ELISAs also useful to study SARS-CoV infections (e.g. (promocell.com)
  • Cathepsin D (an aspartyl protease) appears to cleave a variety of substrates such as fibronectin and laminin. (wikipedia.org)
  • Cathepsin K, among other cathepsins, plays a role in cancer metastasis through the degradation of the extracellular matrix. (wikipedia.org)
  • Background:Serum cathepsin B activity has been considered a potential marker of tumor progression. (medscimonit.com)
  • The aim of this study was to assess serum cathepsin activity during tumor progression and regression.Material/Methods: Of 60 female rats inoculated with Morris hepatoma cells, 45 were treated with BRT, and the remaining 15 were left without treatment. (medscimonit.com)
  • Serum cathepsin B activity was determined, tumor volumes were measured, and histological examinations of the tumor tissues were performed.Results: Of the 45 BRT-treated rats, tumor regression was observed in 31 rats, and serum cathepsin activity was analyzed in these rats. (medscimonit.com)
  • Conclusions: Cathepsin B may play an important role, not only in tumor expansion, but also during the processes of cancer cell death and resorption. (medscimonit.com)
  • Wang J, Zheng M, Yang X, Zhou X, Zhang S. The Role of Cathepsin B in Pathophysiologies of Non-tumor and Tumor tissues: A Systematic Review. (jcancer.org)
  • Nevertheless, recent reports suggest that Cathepsin B executes other cellular programs such as controlling tumor growth, migration, invasion, angiogenesis, and metastases development. (edu.rs)
  • Underneath a façade of an intracellular protease with limited therapeutic potential hides a central role of cathepsins in extracellular functions. (edu.rs)
  • Here we discuss the role of Cathepsin B in the oncogenic process and perspective the use of Cathepsin B for diagnostic and therapeutic applications. (edu.rs)
  • In particular, cathepsin D is often overexpressed and hypersecreted in cancer cells , implying it may constitute a therapeutic target. (bvsalud.org)
  • The cathepsin A activity in lysates of metastatic lesions of malignant melanoma is significantly higher than in primary focus lysates. (wikipedia.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)
  • This procedure applies to all products that have a specification for Cathepsin B activity, such as product numbers C0150 and C8571 , determined by the liberation of 7-amino-4-methylcoumarin from Z-Arg-Arg 7-amido-4-methylcoumarin. (sigmaaldrich.com)
  • Cathepsin B activity was selectively elevated early in the course of illness. (jci.org)
  • Muscle wasting and impaired contractility associated with sepsis may involve selective prostaglandin stimulation of cathepsin B activity. (jci.org)
  • Immunohistochemical investigations on cathepsin D activity in structures of cholesteatoma. (medscimonit.com)
  • Results: Serum TRAcP5b activity, but not cathepsin K-immunoreactivity, was associated with density of TRAcP-positive osteoclasts in the subchondral bone of medial tibia plateaux. (nottingham.ac.uk)
  • Cathepsin G Protease Assay for compound screening and profiling via fluorescence-based quantification of enzyme activity. (reactionbiology.com)
  • Cathepsins B and L are involved in matrix degradation and cell invasion. (wikipedia.org)
  • And Cathepsin E plays an important role in the degradation of proteins, the generation of bioactive proteins, and antigen processing [2] . (medchemexpress.com)
  • Cathepsin L-deficient mice were shown to have less adipose tissue, lower serum glucose and insulin levels, more insulin receptor subunits, more glucose transporter (GLUT4) and more fibronectin than wild type controls. (wikipedia.org)
  • To compare the levels of Dynamin and Cathepsin L in serum and urine of participants with proteinuric kidney disease to those of normal controls. (wits.ac.za)
  • Methods A prospective study of 37 patients with proteinuric kidney disease versus a healthy control group of 40 individuals, where the serum and urine levels of Cathepsin L and Dynamin were determined using an Enzyme Linked immunosorbent assay and the levels compared between the two groups. (wits.ac.za)
  • An independent sample t-test was used to assess whether the mean serum Dynamin, urine Dynamin, serum Cathepsin L and urine Cathepsin L differed for the control group compared with kidney disease group. (wits.ac.za)
  • There was no difference in the levels of serum Cathepsin L between the renal disease and the control groups (p= 0.23). (wits.ac.za)
  • Intracellular electrolyte changes may involve prostaglandin synthesis but do not require cathepsin B activation. (jci.org)
  • As an intracellular, hydrolytic aspartic protease, Cathepsin E is mainly expressed in cells of the immune and gastrointestinal systems, lymphoid tissues, erythrocytes, and cancer cells [1] . (medchemexpress.com)
  • UP-cDNA demonstrating amplification products for cathepsin G did not demonstrate amplification products for human neutrophil elastase, suggesting that the cathepsin G PCR amplification product was not derived from neutrophils or monocytes possibly contaminating the lesion. (duke.edu)
  • 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)
  • Hier sind Cathepsin G Antikörper für eine Vielzahl von Species wie anti-Human Cathepsin G, anti-Rat Cathepsin G, anti-Mouse Cathepsin G zu finden. (antikoerper-online.de)
  • Buy Purified Native Human Cathepsin G (CatG), Human Neutrophil. (athensresearch.com)
  • This random approach for the design of inhibitors was introduced to compensate for the inaccuracy induced by shifted docking of combinatorial compound collections at the active center of cathepsin L. Thereby, we obtained structurally defined pentapeptide amides which inhibited human cathepsin L at nanomolar concentrations. (uni-bielefeld.de)
  • Scholars@Duke publication: Determination of the primary structures of human skin chymase and cathepsin G from cutaneous mast cells of urticaria pigmentosa lesions. (duke.edu)
  • Amplification of the same UP-cDNA with primers coding for the NH2- and COOH-terminal sequences of human neutrophil cathepsin G also produced a specific amplification product which was sequenced. (duke.edu)
  • Cathepsin D has garnered increased attention in recent years, mainly since it has been associated with several human pathologies . (bvsalud.org)
  • Cathepsin L levels were elevated in the urine of the renal disease group, in keeping with the notion that Cathepsin L proteolysis plays a critical role in the various forms of proteinuria. (wits.ac.za)
  • In this review , we provide an overview of the role of cathepsin D in physiological and pathological scenarios. (bvsalud.org)
  • Mouse Cathepsin B, amino acids (His18-Phe339) (Accession# P10605), with C-terminal 10x His tag, was expressed in CHO cells. (biolegend.com)
  • Cathepsin K has also been shown to play a role in arthritis. (wikipedia.org)
  • 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)
  • The cysteine cathepsins have attracted significant research effort as drug targets. (wikipedia.org)
  • Hier sind Cathepsin G Antikörper zu finden, welche für eine bestimmte Anwendung wie WB, FACS, ELISA, IHC validiert wurde. (antikoerper-online.de)
  • In fact, elevated levels of Cathepsins are found under different pathological conditions including inflammation, infection, neurodegenerative disease, and cancer. (edu.rs)
  • Therefore, a more detailed understanding of cathepsin D regulation and how to modulate its apoptotic functions is clearly needed. (bvsalud.org)
  • Elevated levels of cathepsin B were detected in metastases and neurological disorders including Alzheimer's disease (AD). (eurogentec.com)
  • 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)
  • 1) You stated that there is a lack of information on other SNPs of cathepsin, after a few minutes in Clarivate's Web of Science a paper was found (10.1016/j.jpeds.2017.08.063) describing an extra cathepsin mutation (Q334P) possibly involved in pancreatitis, though not tropical calcific pancreatitis. (peerj.com)
  • A New Analytical Method for Determination of Cathepsin L Based on the Surface Plasmon Resonance Imaging Biosensor. (uni-bielefeld.de)
  • The expression of cathepsin K in cultured endothelial cells is regulated by shear stress. (wikipedia.org)
  • Further experiments conducted using a parental and bone-homing subclone of the MDAMB231 cell line (MDAMB213BO) have shown that the expression of CD44, cathepsin K and MT1MMP is elevated in the MDAMB231BO cells relative to their parental counterparts. (biomedcentral.com)
  • CpG DNA inhibits the proliferation of pro-B, but not pre-B, cells by inducing caspase-independent cell death through a pathway that requires the expression of cathepsin B. This pathway is operative in Rag-deficient mice carrying an SP6 transgene, in which B lymphopoiesis is compromised, to reduce the size of the B lymphocyte precursor compartments in the bone marrow. (pasteur.fr)
  • The genetic knockout for cathepsin S and K in mice with atherosclerosis was shown to reduce the size of atherosclerotic lesions. (wikipedia.org)
  • Tatò, Maia Lucia (2019): Untersuchungen zur Rolle von Cathepsin S beim experimentellen und humanen Systemischen Lupus Erythematodes. (uni-muenchen.de)

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