Cathepsins: A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.Cathepsin B: A lysosomal cysteine proteinase with a specificity similar to that of PAPAIN. The enzyme is present in a variety of tissues and is important in many physiological and pathological processes. In pathology, cathepsin B has been found to be involved in DEMYELINATION; EMPHYSEMA; RHEUMATOID ARTHRITIS, and NEOPLASM INVASIVENESS.Cathepsin L: A ubiquitously-expressed cysteine protease that plays an enzymatic role in POST-TRANSLATIONAL PROTEIN PROCESSING of proteins within SECRETORY GRANULES.Cathepsin D: An intracellular proteinase found in a variety of tissue. It has specificity similar to but narrower than that of pepsin A. The enzyme is involved in catabolism of cartilage and connective tissue. EC 3.4.23.5. (Formerly EC 3.4.4.23).Cathepsin K: A cysteine protease that is highly expressed in OSTEOCLASTS and plays an essential role in BONE RESORPTION as a potent EXTRACELLULAR MATRIX-degrading enzyme.Cathepsin G: A serine protease found in the azurophil granules of NEUTROPHILS. It has an enzyme specificity similar to that of chymotrypsin C.Cathepsin H: An ubiquitously-expressed lysosomal cysteine protease that is involved in protein processing. The enzyme has both endopeptidase and aminopeptidase activities.Cathepsin E: An aspartic endopeptidase that is similar in structure to CATHEPSIN D. It is found primarily in the cells of the immune system where it may play a role in processing of CELL SURFACE ANTIGENS.Cathepsin C: A papain-like cysteine protease that has specificity for amino terminal dipeptides. The enzyme plays a role in the activation of several pro-inflammatory serine proteases by removal of their aminoterminal inhibitory dipeptides. Genetic mutations that cause loss of cathepsin C activity in humans are associated with PAPILLON-LEFEVRE DISEASE.Cathepsin F: A lysosomal papain-related cysteine proteinase that is expressed in a broad variety of cell types.Cathepsin Z: A ubiquitously-expressed cysteine peptidase that exhibits carboxypeptidase activity. It is highly expressed in a variety of immune cell types and may play a role in inflammatory processes and immune responses.Cysteine Endopeptidases: ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.Cathepsin W: A cysteine endopeptidase found in NATURAL KILLER CELLS and CYTOTOXIC T-LYMPHOCYTES. It may have a specific function in the mechanism or regulation of cytolytic activity of immune cells.Lysosomes: A class of morphologically heterogeneous cytoplasmic particles in animal and plant tissues characterized by their content of hydrolytic enzymes and the structure-linked latency of these enzymes. The intracellular functions of lysosomes depend on their lytic potential. The single unit membrane of the lysosome acts as a barrier between the enzymes enclosed in the lysosome and the external substrate. The activity of the enzymes contained in lysosomes is limited or nil unless the vesicle in which they are enclosed is ruptured. Such rupture is supposed to be under metabolic (hormonal) control. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)Cathepsin A: 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.Pepstatins: N-acylated oligopeptides isolated from culture filtrates of Actinomycetes, which act specifically to inhibit acid proteases such as pepsin and renin.Cystatins: A homologous group of endogenous CYSTEINE PROTEINASE INHIBITORS. The cystatins inhibit most CYSTEINE ENDOPEPTIDASES such as PAPAIN, and other peptidases which have a sulfhydryl group at the active site.Endopeptidases: A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.Cysteine Proteinase Inhibitors: Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.DiazomethaneDipeptides: Peptides composed of two amino acid units.Serine Endopeptidases: Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.Protease Inhibitors: Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).Papain: 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.Cystatin B: 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.Cysteine Proteases: A subclass of peptide hydrolases that depend on a CYSTEINE residue for their activity.Enzyme Precursors: Physiologically inactive substances that can be converted to active enzymes.Cystatin A: A cytastin subtype found at high levels in the SKIN and in BLOOD CELLS. Cystatin A incorporates into the cornified cell envelope of stratified squamous epithelial cells and may play a role in bacteriostatic properties of skin.Pancreatic Elastase: A protease of broad specificity, obtained from dried pancreas. Molecular weight is approximately 25,000. The enzyme breaks down elastin, the specific protein of elastic fibers, and digests other proteins such as fibrin, hemoglobin, and albumin. EC 3.4.21.36.Leukocyte Elastase: An enzyme that catalyzes the hydrolysis of proteins, including elastin. It cleaves preferentially bonds at the carboxyl side of Ala and Val, with greater specificity for Ala. EC 3.4.21.37.Amino Acid Sequence: 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.Molecular Sequence Data: 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.Hydrogen-Ion Concentration: 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)Papillon-Lefevre Disease: Rare, autosomal recessive disorder occurring between the first and fifth years of life. It is characterized by palmoplantar keratoderma with periodontitis followed by the premature shedding of both deciduous and permanent teeth. Mutations in the gene for CATHEPSIN C have been associated with this disease.Cystatin C: An extracellular cystatin subtype that is abundantly expressed in bodily fluids. It may play a role in the inhibition of interstitial CYSTEINE PROTEASES.Fasciola hepatica: A species of helminth commonly called the sheep liver fluke. It occurs in the biliary passages, liver, and gallbladder during various stages of development. Snails and aquatic vegetation are the intermediate hosts. Occasionally seen in man, it is most common in sheep and cattle.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Benzoylarginine-2-Naphthylamide: An enzyme substrate which permits the measurement of peptide hydrolase activity, e.g. trypsin and thrombin. The enzymes liberate 2-naphthylamine, which is measured by colorimetric procedures.Kinetics: The rate dynamics in chemical or physical systems.Peptide Hydrolases: Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.Dipeptidyl-Peptidases and Tripeptidyl-Peptidases: A subclass of exopeptidases that includes enzymes which cleave either two or three AMINO ACIDS from the end of a peptide chain.Leucine: An essential branched-chain amino acid important for hemoglobin formation.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Mannosephosphates: Phosphoric acid esters of mannose.Oligopeptides: Peptides composed of between two and twelve amino acids.Awards and PrizesPeptides: Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.Drug Design: The molecular designing of drugs for specific purposes (such as DNA-binding, enzyme inhibition, anti-cancer efficacy, etc.) based on knowledge of molecular properties such as activity of functional groups, molecular geometry, and electronic structure, and also on information cataloged on analogous molecules. Drug design is generally computer-assisted molecular modeling and does not include pharmacokinetics, dosage analysis, or drug administration analysis.Amyloid beta-Protein Precursor: A single-pass type I membrane protein. It is cleaved by AMYLOID PRECURSOR PROTEIN SECRETASES to produce peptides of varying amino acid lengths. A 39-42 amino acid peptide, AMYLOID BETA-PEPTIDES is a principal component of the extracellular amyloid in SENILE PLAQUES.Alzheimer Disease: A degenerative disease of the BRAIN characterized by the insidious onset of DEMENTIA. Impairment of MEMORY, judgment, attention span, and problem solving skills are followed by severe APRAXIAS and a global loss of cognitive abilities. The condition primarily occurs after age 60, and is marked pathologically by severe cortical atrophy and the triad of SENILE PLAQUES; NEUROFIBRILLARY TANGLES; and NEUROPIL THREADS. (From Adams et al., Principles of Neurology, 6th ed, pp1049-57)Myocardial Ischemia: A disorder of cardiac function caused by insufficient blood flow to the muscle tissue of the heart. The decreased blood flow may be due to narrowing of the coronary arteries (CORONARY ARTERY DISEASE), to obstruction by a thrombus (CORONARY THROMBOSIS), or less commonly, to diffuse narrowing of arterioles and other small vessels within the heart. Severe interruption of the blood supply to the myocardial tissue may result in necrosis of cardiac muscle (MYOCARDIAL INFARCTION).Myocardium: The muscle tissue of the HEART. It is composed of striated, involuntary muscle cells (MYOCYTES, CARDIAC) connected to form the contractile pump to generate blood flow.Myocardial Infarction: NECROSIS of the MYOCARDIUM caused by an obstruction of the blood supply to the heart (CORONARY CIRCULATION).Fibrosis: Any pathological condition where fibrous connective tissue invades any organ, usually as a consequence of inflammation or other injury.Ramipril: A long-acting angiotensin-converting enzyme inhibitor. It is a prodrug that is transformed in the liver to its active metabolite ramiprilat.Angioscopy: Endoscopic examination, therapy or surgery performed on the interior of blood vessels.Transplantation, Heterologous: Transplantation between animals of different species.Mice, SCID: Mice homozygous for the mutant autosomal recessive gene "scid" which is located on the centromeric end of chromosome 16. These mice lack mature, functional lymphocytes and are thus highly susceptible to lethal opportunistic infections if not chronically treated with antibiotics. The lack of B- and T-cell immunity resembles severe combined immunodeficiency (SCID) syndrome in human infants. SCID mice are useful as animal models since they are receptive to implantation of a human immune system producing SCID-human (SCID-hu) hematochimeric mice.Proteomics: The systematic study of the complete complement of proteins (PROTEOME) of organisms.Coronary Restenosis: Recurrent narrowing or constriction of a coronary artery following surgical procedures performed to alleviate a prior obstruction.Caenorhabditis elegans: A species of nematode that is widely used in biological, biochemical, and genetic studies.Caenorhabditis elegans Proteins: Proteins from the nematode species CAENORHABDITIS ELEGANS. The proteins from this species are the subject of scientific interest in the area of multicellular organism MORPHOGENESIS.Antifungal Agents: Substances that destroy fungi by suppressing their ability to grow or reproduce. They differ from FUNGICIDES, INDUSTRIAL because they defend against fungi present in human or animal tissues.Aspergillosis: Infections with fungi of the genus ASPERGILLUS.Search Engine: Software used to locate data or information stored in machine-readable form locally or at a distance such as an INTERNET site.Translational Medical Research: The application of discoveries generated by laboratory research and preclinical studies to the development of clinical trials and studies in humans. A second area of translational research concerns enhancing the adoption of best practices.Databases, Genetic: Databases devoted to knowledge about specific genes and gene products.BerlinAdenocarcinoma: A malignant epithelial tumor with a glandular organization.Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.Taenia solium: Species of tapeworm in the genus TAENIA, that infects swine. It is acquired by humans through the ingestion of cured or undercooked pork.Neurocysticercosis: Infection of the brain, spinal cord, or perimeningeal structures with the larval forms of the genus TAENIA (primarily T. solium in humans). Lesions formed by the organism are referred to as cysticerci. The infection may be subacute or chronic, and the severity of symptoms depends on the severity of the host immune response and the location and number of lesions. SEIZURES represent the most common clinical manifestation although focal neurologic deficits may occur. (From Joynt, Clinical Neurology, 1998, Ch27, pp46-50)Fascioliasis: Liver disease caused by infections with parasitic flukes of the genus FASCIOLA, such as FASCIOLA HEPATICA.Fasciola: A genus of trematode liver flukes of the family Fasciolidae. Two species of this genus are F. hepatica and F. gigantica. The parasites are found in the liver and gallbladder and associated ducts in mammals and occasionally man. F. gigantica occurs rarely in man.Contrast Media: Substances used to allow enhanced visualization of tissues.Fluorescent Dyes: Agents that emit light after excitation by light. The wave length of the emitted light is usually longer than that of the incident light. Fluorochromes are substances that cause fluorescence in other substances, i.e., dyes used to mark or label other compounds with fluorescent tags.Magnetic Resonance Imaging: Non-invasive method of demonstrating internal anatomy based on the principle that atomic nuclei in a strong magnetic field absorb pulses of radiofrequency energy and emit them as radiowaves which can be reconstructed into computerized images. The concept includes proton spin tomographic techniques.Gadolinium: Gadolinium. An element of the rare earth family of metals. It has the atomic symbol Gd, atomic number 64, and atomic weight 157.25. Its oxide is used in the control rods of some nuclear reactors.Liver Cirrhosis: Liver disease in which the normal microcirculation, the gross vascular anatomy, and the hepatic architecture have been variably destroyed and altered with fibrous septa surrounding regenerated or regenerating parenchymal nodules.Ribavirin: A nucleoside antimetabolite antiviral agent that blocks nucleic acid synthesis and is used against both RNA and DNA viruses.Body Mass Index: An indicator of body density as determined by the relationship of BODY WEIGHT to BODY HEIGHT. BMI=weight (kg)/height squared (m2). BMI correlates with body fat (ADIPOSE TISSUE). Their relationship varies with age and gender. For adults, BMI falls into these categories: below 18.5 (underweight); 18.5-24.9 (normal); 25.0-29.9 (overweight); 30.0 and above (obese). (National Center for Health Statistics, Centers for Disease Control and Prevention)Tablets: Solid dosage forms, of varying weight, size, and shape, which may be molded or compressed, and which contain a medicinal substance in pure or diluted form. (Dorland, 28th ed)Hepacivirus: A genus of FLAVIVIRIDAE causing parenterally-transmitted HEPATITIS C which is associated with transfusions and drug abuse. Hepatitis C virus is the type species.Atlases as Topic: Collections of illustrative plates, charts, etc., usually with explanatory captions.Cervical Atlas: The first cervical vertebra.Tears: The fluid secreted by the lacrimal glands. This fluid moistens the CONJUNCTIVA and CORNEA.Lupus Erythematosus, Systemic: A chronic, relapsing, inflammatory, and often febrile multisystemic disorder of connective tissue, characterized principally by involvement of the skin, joints, kidneys, and serosal membranes. It is of unknown etiology, but is thought to represent a failure of the regulatory mechanisms of the autoimmune system. The disease is marked by a wide range of system dysfunctions, an elevated erythrocyte sedimentation rate, and the formation of LE cells in the blood or bone marrow.Dry Eye Syndromes: Corneal and conjunctival dryness due to deficient tear production, predominantly in menopausal and post-menopausal women. Filamentary keratitis or erosion of the conjunctival and corneal epithelium may be caused by these disorders. Sensation of the presence of a foreign body in the eye and burning of the eyes may occur.Organophosphonates: Carbon-containing phosphonic acid compounds. Included under this heading are compounds that have carbon bound to either OXYGEN atom or the PHOSPHOROUS atom of the (P=O)O2 structure.Adenine: A purine base and a fundamental unit of ADENINE NUCLEOTIDES.Drug Interactions: The action of a drug that may affect the activity, metabolism, or toxicity of another drug.Product Labeling: Use of written, printed, or graphic materials upon or accompanying a product or its container or wrapper. It includes purpose, effect, description, directions, hazards, warnings, and other relevant information.Glycogen Synthase Kinase 3: A glycogen synthase kinase that was originally described as a key enzyme involved in glycogen metabolism. It regulates a diverse array of functions such as CELL DIVISION, microtubule function and APOPTOSIS.Stem Cells: Relatively undifferentiated cells that retain the ability to divide and proliferate throughout postnatal life to provide progenitor cells that can differentiate into specialized cells.Glycogen Synthase Kinases: A class of protein-serine-threonine kinases that was originally found as one of the three types of kinases that phosphorylate GLYCOGEN SYNTHASE. Glycogen synthase kinases along with CA(2+)-CALMODULIN DEPENDENT PROTEIN KINASES and CYCLIC AMP-DEPENDENT PROTEIN KINASES regulate glycogen synthase activity.Glycogen Synthase: An enzyme that catalyzes the transfer of D-glucose from UDPglucose into 1,4-alpha-D-glucosyl chains. EC 2.4.1.11.MedlinePlus: NATIONAL LIBRARY OF MEDICINE service for health professionals and consumers. It links extensive information from the National Institutes of Health and other reviewed sources of information on specific diseases and conditions.Health Records, Personal: Longitudinal patient-maintained records of individual health history and tools that allow individual control of access.Health Status: The level of health of the individual, group, or population as subjectively assessed by the individual or by more objective measures.

Re-entering the translocon from the lumenal side of the endoplasmic reticulum. Studies on mutated carboxypeptidase yscY species. (1/315)

Misfolded or unassembled secretory proteins are retained in the endoplasmic reticulum (ER) and subsequently degraded by the cytosolic ubiquitin-proteasome system. This requires their retrograde transport from the ER lumen into the cytosol, which is mediated by the Sec61 translocon. It had remained a mystery whether ER-localised soluble proteins are at all capable of re-entering the Sec61 channel de novo or whether a permanent contact of the imported protein with the translocon is a prerequisite for retrograde transport. In this study we analysed two new variants of the mutated yeast carboxypeptidase yscY, CPY*: a carboxy-terminal fusion protein of CPY* and pig liver esterase and a CPY* species carrying an additional glycosylation site at its carboxy-terminus. With these constructs it can be demonstrated that the newly synthesised CPY* chain is not retained in the translocation channel but reaches its ER lumenal side completely. Our data indicate that the Sec61 channel provides the essential pore for protein transport through the ER membrane in either direction; persistent contact with the translocon after import seems not to be required for retrograde transport.  (+info)

The protein disulphide-isomerase family: unravelling a string of folds. (2/315)

The mammalian protein disulphide-isomerase (PDI) family encompasses several highly divergent proteins that are involved in the processing and maturation of secretory proteins in the endoplasmic reticulum. These proteins are characterized by the presence of one or more domains of roughly 95-110 amino acids related to the cytoplasmic protein thioredoxin. All but the PDI-D subfamily are composed entirely of repeats of such domains, with at least one domain containing and one domain lacking a redox-active -Cys-Xaa-Xaa-Cys- tetrapeptide. In addition to their known roles as redox catalysts and isomerases, the last few years have revealed additional functions of the PDI proteins, including peptide binding, cell adhesion and perhaps chaperone activities. Attention is now turning to the non-redox-active domains of the PDIs, which may play an important role in all of the known activities of these proteins. Thus the presence of both redox-active and -inactive domains within these proteins portends a complexity of functions differentially accommodated by the various family members.  (+info)

Ligand recognition and domain structure of Vps10p, a vacuolar protein sorting receptor in Saccharomyces cerevisiae. (3/315)

Vp10p is a receptor that sorts several different vacuolar proteins by cycling between a late Golgi compartment and the endosome. The cytoplasmic tail of Vps10p is necessary for the recycling, whereas the lumenal domain is predicted to interact with the soluble ligands. We have studied ligand binding to Vps10p by introducing deletions in the lumenal region. This region contains two domains with homology to each other. Domain 2 binds carboxypeptidase Y (CPY), proteinase A (PrA) and hybrids of these proteases with invertase. Moreover, we show that aminopeptidase Y (APY) is a ligand of Vps10p. The native proteases compete for binding to domain 2. Binding of CPY(156)-invertase or PrA(137)-invertase, on the other hand, do not interfere with binding of CPY to Vps10p. Furthermore, the Q24RPL27 sequence known to be important for vacuolar sorting of CPY, is of little importance in the Vps10p-dependent sorting of CPY-invertase. Apparently, domain 2 contains two different binding sites; one for APY, CPY and PrA, and one for CPY-invertase and PrA-invertase. The latter interaction seems not to be sequence specific, and we suggest that an unfolded structure in these ligands is recognized by Vps10p.  (+info)

Effect of prolonged administration of a urinary kinase inhibitor, ebelactone B on the development of deoxycorticosterone acetate-salt hypertension in rats. (4/315)

The effect of prolonged administration of a carboxypeptidase Y-like kininase inhibitor, ebelactone B (EB) (2-ethyl-3, 11-dihydroxy-4, 6, 8, 10, 12-pentamethyl-9-oxo-6-tetradecenoic 1, 3-lactone), on the development of deoxycorticosterone acetate (DOCA)-salt hypertension was tested. The systolic blood pressure (SBP) of non-treated 6-week-old Sprague-Dawley strain rats was gradually increased by DOCA-salt treatment from 137+/-2 mmHg (n=11) to 195+/-7 mmHg at 10 weeks of age. With daily oral administration of lisinopril (5 mg kg(-1), twice a day), which is an inhibitor of angiotensin converting enzyme, a major kininase in plasma, the development of hypertension was not suppressed. By contrast, administration of EB (5 mg kg(-1), twice a day), completely inhibited the development of hypertension (SBP: 146+/-1 mmHg, n=5, 10 weeks old). The reduced SBP at 10 weeks of age was equal to the SBP before any treatment (142+/-1 mmHg, n=5). Direct determination of mean blood pressure (MBP) in conscious, unrestrained rats confirmed that MBP elevation was completely inhibited by EB. Continuous subcutaneous infusion (5 mg kg(-1) day(-1)) of HOE140, a bradykinin B2 receptor antagonist, restored the elevation of SBP, which was suppressed by EB. The weights of left ventricle of DOCA-salt treated rats 10-weeks-old (0.36+/-0.02 g 100 g body weight(-1), n=11) was significantly reduced by EB (0.27+/-0.01, n=5), as were the sodium levels in serum, cerebrospinal fluid and erythrocyte. These findings suggested that EB is effective in preventing salt-related hypertension presumably by eliminating sodium retention.  (+info)

Stable expression of protective protein/cathepsin A-green fluorescent protein fusion genes in a fibroblastic cell line from a galactosialidosis patient. Model system for revealing the intracellular transport of normal and mutated lysosomal enzymes. (5/315)

Fibroblastic cell lines derived from a galactosialidosis patient, stably expressing the chimaeric green fluorescent protein variant (EGFP) gene fused to the wild-type and mutant human lysosomal protective protein/cathepsin A (PPCA) cDNA, were first established as a model system for revealing the sorting and processing of lysosomal enzymes and for investigating the molecular bases of their deficiencies. In the cell line expressing the wild-type PPCA-EGFP chimaera gene (EGFP-PPwild), an 81 kDa form (27 kDa EGFP fused to the C-terminus of the 54 kDa PPCA precursor) was produced, then processed into the mature 32/20 kDa two-chain form free of the EGFP domain. The intracellular cathepsin A, alpha-N-acetylneuraminidase and beta-galactosidase activities, which are deficient in the parent fibroblastic cells, could also be significantly restored in the cells. In contrast with the uniform and strong fluorescence throughout the cytoplasm and nucleus in the mock-cell line expressing only EGFP cDNA, weak reticular and punctate fluorescence was distributed throughout the EGFP-PPwild cell line. Bafilomycin A1, a potent inhibitor of vacuolar ATPase and intracellular acidification, induced the distribution of Golgi-like perinuclear fluorescence throughout the living and fixed cells, in which only the 81 kDa product was detected. After removal of the agent, time-dependent transport of the chimaeric protein from the Golgi apparatus to the prelysosomal structure in living cells was monitored with a confocal laser scanning microscope system. Leupeptin caused the distribution of lysosome-like granular fluorescence throughout the cytoplasm in the fixed cells, although it was hardly observed in living cells. The latter agent also dose-dependently induced an increase in the intracellular amount of the 81 kDa product containing the EGFP domain and inhibited the restoration of cathepsin A activity in the EGFP-PPwild cells after the removal of bafilomycin A1. In parallel, both the mature two-chain form and PPCA function disappeared. These results suggested that the chimaera gene product was transported to acidic compartments (endosomes/lysosomes), where proteolytic processing of the PPCA precursor/zymogen, quenching of the fluorescence, and random degradation of the EGFP portion occurred. A cell line stably expressing a chimaeric gene with a mutant PPCA cDNA containing an A1184-->G (Y395C) mutation, commonly detected in Japanese severe early-infantile type of galactosialidosis patients, showed an endoplasmic reticulum (ER)-like reticular fluorescence pattern. The PPCA-immunoreactive gene product was hardly detected in this cell line. The mutant chimaeric product was suggested to be degraded rapidly in the ER before transport to post-ER compartments. A cell line expressing the chimaeric gene with a T746-->A (Y249N) PPCA mutation exhibited both ER-like reticular and granular fluorescence on the reticular structure that was stronger than that in the EGFP-PPwild cells. Some of them contained large fluorescent inclusion-body-like structures. The ineffectiveness of transport inhibitors in the distribution changes in the two mutant chimaeric proteins suggested that they were not delivered to acidic compartments. Therefore this expression system can possibly be applied to the direct analysis of the sorting defects of mutant gene products in living cells and will be useful for the molecular investigation of lysosomal diseases, including galactosialidosis.  (+info)

Contribution of the carbohydrate moiety to conformational stability of the carboxypeptidase Y high pressure study. (6/315)

The process of pressure-induced denaturation of carboxypeptidase Y and the role of the carbohydrate moiety in its response to pressure and low temperature were investigated by measuring in situ the catalytic activity and, the intrinsic and 8-anilino-1-naphthalene sulfonic acid binding fluorescences. Pressure-induced denaturation of carboxypeptidase Y is a process involving at least three transitions. Low pressures (below 150 MPa) induced slight conformational changes characterized by a slight decrease in the center of the spectral mass of intrinsic fluorescence, whereas no changes in 8-anilino-1-naphthalene sulfonic acid binding fluorescence were observed and 80% of the catalytic activity remained. Higher pressure (150-500 MPa) induced further conformational changes, characterized by a large decrease in the center of the spectral mass of intrinsic fluorescence, a large increase in the 8-anilino-1-naphthalene sulfonic acid binding fluorescence and the loss of all catalytic activity. Thus, this intermediate exhibited characteristics of molten globule-like state. A further increase, in pressure (above 550 MPa) induced transition from this first molten globule-like state to a second molten globule-like state. This two-stage denaturation process can be explained by assuming the existence of two independent structural domains in the carboxypeptidase molecule. A similar three-transition process was found for unglycosylated carboxypeptidase Y, but, the first two transitions clearly occurred at lower pressures than those for glycosylated carboxypeptidase Y. These findings indicate that the carbohydrate moiety protects carboxypeptidase Y against pressure-induced denaturation. The origin of the protective effects is discussed based on the known crystallographic structure of CPY.  (+info)

Crystal structure of human gastric lipase and model of lysosomal acid lipase, two lipolytic enzymes of medical interest. (7/315)

Fat digestion in humans requires not only the classical pancreatic lipase but also gastric lipase, which is stable and active despite the highly acidic stomach environment. We report here the structure of recombinant human gastric lipase at 3.0-A resolution, the first structure to be described within the mammalian acid lipase family. This globular enzyme (379 residues) consists of a core domain belonging to the alpha/beta hydrolase-fold family and a "cap" domain, which is analogous to that present in serine carboxypeptidases. It possesses a classical catalytic triad (Ser-153, His-353, Asp-324) and an oxyanion hole (NH groups of Gln-154 and Leu-67). Four N-glycosylation sites were identified on the electron density maps. The catalytic serine is deeply buried under a segment consisting of 30 residues, which can be defined as a lid and belonging to the cap domain. The displacement of the lid is necessary for the substrates to have access to Ser-153. A phosphonate inhibitor was positioned in the active site that clearly suggests the location of the hydrophobic substrate binding site. The lysosomal acid lipase was modeled by homology, and possible explanations for some previously reported mutations leading to the cholesterol ester storage disease are given based on the present model.  (+info)

The phosphatidylinositol 3-phosphate binding protein Vac1p interacts with a Rab GTPase and a Sec1p homologue to facilitate vesicle-mediated vacuolar protein sorting. (8/315)

Activated GTP-bound Rab proteins are thought to interact with effectors to elicit vesicle targeting and fusion events. Vesicle-associated v-SNARE and target membrane t-SNARE proteins are also involved in vesicular transport. Little is known about the functional relationship between Rabs and SNARE protein complexes. We have constructed an activated allele of VPS21, a yeast Rab protein involved in vacuolar protein sorting, and demonstrated an allele-specific interaction between Vps21p and Vac1p. Vac1p was found to bind the Sec1p homologue Vps45p. Although no association between Vps21p and Vps45p was seen, a genetic interaction between VPS21 and VPS45 was observed. Vac1p contains a zinc-binding FYVE finger that may bind phosphatidylinositol 3-phosphate [PtdIns(3)P]. In other FYVE domain proteins, this motif and PtdIns(3)P are necessary for membrane association. Vac1 proteins with mutant FYVE fingers still associated with membranes but showed vacuolar protein sorting defects and reduced interactions with Vps45p and activated Vps21p. Vac1p membrane association was not dependent on PtdIns(3)P, Pep12p, Vps21p, Vps45p, or the PtdIns 3-kinase, Vps34p. Vac1p FYVE finger mutant missorting phenotypes were suppressed by a defective allele of VPS34. These data indicate that PtdIns(3)P may perform a regulatory role, possibly involved in mediating Vac1p protein-protein interactions. We propose that activated-Vps21p interacts with its effector, Vac1p, which interacts with Vps45p to regulate the Golgi to endosome SNARE complex.  (+info)

*Cathepsin

... A (serine protease) Cathepsin B (cysteine protease) Cathepsin C (cysteine protease) Cathepsin D (aspartyl protease) ... Cathepsin H (cysteine protease) Cathepsin K (cysteine protease) Cathepsin L1 (cysteine protease) Cathepsin L2 (or V) (cysteine ... Cathepsin S (cysteine protease) Cathepsin W (cysteine proteinase) Cathepsin Z (or X) (cysteine protease) Cathepsins have been ... Cathepsin K has also been shown to play a role in arthritis. Mouse cathepsin L is homologous to human cathepsin V. Mouse ...

*Cathepsin T

Cathepsin Cathepsin T at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... Cathepsin T (EC 3.4.22.24) is an enzyme. This enzyme catalyses the following chemical reaction Interconversion of the three ... Pitot, H.C.; Gohda, E. (1987). "Cathepsin T". Methods Enzymol. 142: 279-289. doi:10.1016/s0076-6879(87)42038-7. PMID 2885716. ...

*Cathepsin H

"Entrez Gene: CTSH cathepsin H". Sawicki G, Warwas M (1990). "Cathepsin H from human placenta". Acta Biochim. Pol. 36 (3-4): 343 ... Cathepsin H is a protein that in humans is encoded by the CTSH gene. The protein encoded by this gene is a lysosomal cysteine ... 2003). "Expression of cathepsins B, H, K, L, and S during human fetal lung development". Dev. Dyn. 225 (1): 14-21. doi:10.1002/ ... 2001). "Expression of cathepsins B, H, K, L, and S and matrix metalloproteinases 9 and 13 during chondrocyte hypertrophy and ...

*Cathepsin S

... cathepsin S can be replaced by cathepsin F. Secreted cathepsin S cleaves some extracellular matrix (ECM) proteins. Cathepsin S ... In vitro, cathepsin S retains some enzyme activity in the presence of 3M urea. Cathepsin S is produced as a zymogen and is ... Cathepsin S can function as an elastase over a broad pH range in alveolar macrophages. Cathepsin S is a lysosomal enzyme that ... In tumorogenesis, cathepsin S promotes a tumor growth. Cathepsin S expression and activity has also been shown to be ...

*Cathepsin A

... is an enzyme that is classified both as a cathepsin and a carboxypeptidase. In humans, it is encoded by the CTSA ... Cathepsin A at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology portal. ... Cathepsin A has been shown to interact with NEU1. GRCh38: Ensembl release 89: ENSG00000064601 - Ensembl, May 2017 GRCm38: ... 1991). "Human lysosomal protective protein has cathepsin A-like activity distinct from its protective function". J. Biol. Chem ...

*Cathepsin B

... has been shown to interact with: CTSD CSTA, CSTB, and S100A10. Cathepsin B is inhibited by: Nitroxoline Cathepsins ... Cathepsin B is in humans encoded by the CTSB gene. Cathepsin B belongs to a family of lysosomal cysteine proteases and plays an ... Cathepsin B has been proposed as a potentially effective biomarker for a variety of cancers. Overexpression of cathepsin B is ... Similarly, cathepsin B gene knockout and cathepsin B inhibitor treatment studies in traumatic brain injury mouse models have ...

*Cathepsin zymography

Cathepsin K detection by zymography Zymographic techniques for detection of cathepsins K, L, S, and V Zymography for detection ... Cathepsin zymography is a technique for quantifying enzymatic activity of the cathepsin family of cysteine proteases. It is ... While the proform of cathepsins are generally stable, once activated, proteases such as cathepsin K are vulnerable to ... After the renaturing period, the gel is then incubated in assay buffer to allow the now active cathepsins to proteolyze the ...

*Cathepsin V

... (EC 3.4.22.43, Cathepsin L2, cathepsin U) is an enzyme. This enzyme catalyses the following chemical reaction The ... Cathepsin L2 Brömme, D.; Li, Z.; Barnes, M.; Mehler, E. (1999). "Human cathepsin V functional expression, tissue distribution, ... Cathepsin V at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology portal. ... Santamaría, I.; Velasco, G.; Cazorla, M.; Fueyo, A.; Campo, E.; López-Otín, C. (1998). "Cathepsin L2, a novel human cysteine ...

*Cathepsin F

... is a protein that in humans is encoded by the CTSF gene. Cathepsins are papain family cysteine proteinases that ... The cathepsin F gene is ubiquitously expressed, and it maps to chromosome 11q13, close to the gene encoding cathepsin W. GRCh38 ... "Entrez Gene: CTSF cathepsin F". Nägler DK, Sulea T, Ménard R (1999). "Full-length cDNA of human cathepsin F predicts the ... Wex T, Levy B, Wex H, Brömme D (1999). "Human cathepsins F and W: A new subgroup of cathepsins". Biochem. Biophys. Res. Commun ...

*Cathepsin W

"Human cathepsins W and F form a new subgroup of cathepsins that is evolutionary separated from the cathepsin B- and L-like ... Wex T, Levy B, Wex H, Brömme D (1999). "Human cathepsins F and W: A new subgroup of cathepsins". Biochem. Biophys. Res. Commun ... 2003). "Characterization of novel anti-cathepsin W antibodies and cellular distribution of cathepsin W in the gastrointestinal ... Cathepsin W is a protein that in humans is encoded by the CTSW gene. The protein encoded by this gene, a member of the ...

*Cathepsin D

... is an aspartic endo-protease that is ubiquitously distributed in lysosomes. The main function of cathepsin D is to ... "Entrez Gene: CTSD cathepsin D". Barrett AJ (April 1970). "Cathepsin D. Purification of isoenzymes from human and chicken liver ... The optimum pH for cathepsin D in vitro is 4.5-5.0. Cathepsin-D is an aspartic protease that depends critically on protonation ... Cathepsin D is a protein that in humans is encoded by the CTSD gene. This gene encodes a lysosomal aspartyl protease composed ...

*Cathepsin L1

... is a protein that in humans is encoded by the CTSL1 gene. The protein encoded by this gene is a lysosomal cysteine ... Major sites of cleavage by cathepsins B, D, and L". J. Biol. Chem. 266 (30): 20198-204. PMID 1939080. Stearns NA, Dong JM, Pan ... 1991). "Comparison of cathepsin L synthesized by normal and transformed cells at the gene, message, protein, and ... Joseph L, Lapid S, Sukhatme V (1987). "The major ras induced protein in NIH3T3 cells is cathepsin L". Nucleic Acids Res. 15 (7 ...

*Cathepsin Z

... cathepsin G, cathepsin H, cathepsin K, cathepsin L, cathepsin L2, cathepsin O, cathepsin S, cathepsin Z, and cathepsin W. These ... Cathepsin Z, also called cathepsin X or cathepsin P, is a protein that in humans is encoded by the CTSZ gene. It is a member of ... As one of the 11 cathepsins, cathepsin Z contains distinctive features from others. Cathepsin Z has been reported involved in ... Cathepsin Z has an exposed integrin-bindign Arg-Gly-Asp motif within the propeptide of the enzyme, through which cathepsin Z ...

*Cathepsin L2

... , also known as cathepsin V and encoded by the CTSL2 gene, is a human gene. The protein encoded by this gene, a ... 2006). "Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the ... 2007). "Inhibition of cathepsin L-like proteases by cathepsin V propeptide". Biol. Chem. 388 (5): 541-5. doi:10.1515/BC. ... 2005). "The human cysteine protease cathepsin V can compensate for murine cathepsin L in mouse epidermis and hair follicles". ...

*Cathepsin L

... 1, previously called cathepsin L Cathepsin L2 or cathepsin V Barrett, A.J.; Kirschke, H. (1981). "Cathepsin B, ... cathepsin H and cathepsin L". Methods Enzymol. 80: 535-561. doi:10.1016/s0076-6879(81)80043-2. PMID 7043200. Barrett, A.J.; ... Reinheckel T.Human cathepsin L rescues the neurodegeneration and lethality in cathepsin B/L double-deficient mice. Biol Chem. ... Cathepsin L at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology portal. ...

*Cathepsin G

... is one of those homologous protease that evolved from a common ancestor by gene duplication. Cathepsin G is a 255- ... An upregulation of cathepsin G was reported in studies of keratoconus. Cathepsin G has been found to interact with: SERPINB1 ... "Entrez Gene: CTSG cathepsin G". Shafer WM, Pohl J, Onunka VC, Bangalore N, Travis J (January 1991). "Human lysosomal cathepsin ... "Generation of the neutrophil-activating peptide-2 by cathepsin G and cathepsin G-treated human platelets". The American Journal ...

*Cathepsin O

... is an enzyme that in humans is encoded by the CTSO gene. Cathepsin O is a cysteine protease and a member of the ... "Entrez Gene: cathepsin O". Shi GP, Chapman HA, Bhairi SM, et al. (1995). "Molecular cloning of human cathepsin O, a novel ... 1994). "Human cathepsin O. Molecular cloning from a breast carcinoma, production of the active enzyme in Escherichia coli, and ... "Genomic structure and chromosomal localization of the human cathepsin O gene (CTSO)". Genomics. 53 (2): 231-4. doi:10.1006/geno ...

*Cathepsin E

... is an enzyme that in humans is encoded by the CTSE gene. Cathepsin E is a protease found in animals, as well as ... The structure of Cathepsin E is very similar to those of Cathepsin D and BACE1, and all 3 have almost identical active site ... "Entrez Gene: CTSE cathepsin E". "CTSE cathepsin E [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2016- ... Along with renin and Cathepsin D, Cathepsin E is one of the only few aspartic proteases known to be made in human tissues other ...

*Cathepsin K

... is degraded by Cathepsin S, called Controlled Cathepsin Cannibalism. Cathepsin K expression is stimulated by ... Cathepsin K has also been found to be over-expressed in glioblastoma. That the expression of cathepsin K is characteristic for ... Cathepsin K antibodies are marketed for research into expression of this enyzme by various cells. Merck had a cathepsin K ... Other cathepsin K inhbitors are in various stages of development. Medivir has a cathepsin K inhibitor, MIV-711 (L-006235), in ...

*Cathepsin X

... (EC 3.4.18.1, cathepsin B2, cysteine-type carboxypeptidase, cathepsin IV, cathepsin Z, acid carboxypeptidase, ... Cathepsin Z Cathepsin X at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... Otto, K.; Riesenkönig, H. (1975). "Improved purification of cathepsin B1 and cathepsin B2". Biochim. Biophys. Acta. 379 (2): ... "On the substrate specificity of cathepsins B1 and B2 including a new fluorogenic substrate for cathepsin B1". Life Sci. 17 (8 ...

*Cathepsin C

... prepro-cathepsin C) comprising signal peptides of 24 residues, pro-regions of 205 (rat cathepsin C) or 206 (human cathepsin C) ... Cathepsin C appears to be a central coordinator for activation of many serine proteases in immune/inflammatory cells. Cathepsin ... identical to the mature amino acid sequences of papain and a number of other cathepsins including cathepsins, B, H, K, L, and S ... Cathepsin C (CTSC) also known as dipeptidyl peptidase I (DPP-I) is a lysosomal exo-cysteine protease belonging to the peptidase ...

*Chromatin

... , Histones & Cathepsin; PMAP The Proteolysis Map-animation [ Recent chromatin publications and news] Protocol for in ...

*Polysulfated glycosaminoglycan

... collagenases such as cathepsin B1; and hyaluronidase. PSGAG inhibits the synthesis of prostaglandin E2, which is released upon ...

*Carboxypeptidase C

Cathepsin A Breddam, K. (1986). "Serine carboxypeptidases. A review". Carlsberg Res. Commun. 51: 83-128. doi:10.1007/bf02907561 ... Miller, J.J.; Changaris, D.G.; Levy, R.S. (1992). "Purification, subunit structure and inhibitor profile of cathepsin-A". J. ... Carboxypeptidase C (EC 3.4.16.5, carboxypeptidase Y, serine carboxypeptidase I, cathepsin A, lysosomal protective protein, ...
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
Lysosomal Storage Disorders are a class of inherited metabolic conditions that result from alterations in the function of lysosomal enzymes. One example is GM1 Gangliosidosis (GM1), a disorder in which the activity of β-galactosidase is deficient resulting in neurodegeneration and early death. The enzyme, β-gal, is a member of the Lysosomal Multienzyme Complex (LMC), which transports proteins to the lysosome and enables various functions. LMC members include β-gal, α-neuraminidase and the Protective Protein Cathepsin A (PPCA). In a unique ovine model of GM1, there is a primary deficiency in the activity of β- galactosidase and a secondary deficiency in α-neuraminidase activity. The cause of the secondary deficiency in α-neuraminidase activity, which is not seen in any other animal model of GM1, is currently unknown. The α-neuraminidase protein is coded for by the NEU1 gene and is, a glycohydrolitic enzyme that is active in the lysosome. The secondary deficiency of α- neuraminidase seen in our
Lysosomal serine carboxypeptidase Cathepsin A (CTSA) is a multifunctional enzyme with distinct protective and catalytic function. CTSA that is present in the lysosomal multienzyme complex facilitates correct lysosomal routing, stability and activation of betagalactosidase and alpha-neuraminidase. In addition, CTSA plays a role in the inactivation of bioactive peptides including bradykinin, substances P, oxytocin, angiotensin I and endothelin-I by cleavage of one or two amino acid(s) from the C-terminal ends. In this study, we aimed to elucidate the regulatory role of CTSA on bioactive peptides in a knock-in mouse model of CTSAS190A. We evaluated the levels of bradykinin, substances P, oxytocin, angiotensin I and endothelin-I in the kidney, liver, lung, brain and serum of the CTSAS190A mouse model at three- and six-months of age. Our results suggest that CTSA selectively contributes to the processing of bioactive peptides in different tissues of CTSAS190A mice compared to those of age-matched wild
Galactosialidosis (MIM 256540) is an autosomal recessive lysosomal storage disease caused by a defect of the protective protein/cathepsin A. Increased amounts of urinary sialic acid-rich oligosaccharides are considered to be an essential diagnostic marker of the disease. We here report a patient with atypical clinical features who consistently has excreted normal amounts of sialyloligosaccharides in the urine. The boy started to have attacks of neuropathic pain associated with hyperesthesia around 1(1/2) years of age. From 4 years of age when his vision was first tested, the patient developed progressive visual loss and at the age of 10 years, macular cherry-red spots were found. At this age, he also had a mild learning disability and clinical examination showed mild facial coarsening, increased lumbar lordosis and pyramidal signs in the legs. In conclusion, the clinical and laboratory features of this patient show that galactosialidosis may be considered in patients even in the absence of ...
(Medical Xpress) -- A protein produced by the central nervous system’s support cells seems to play two opposing roles in protecting nerve cells from damage, an animal study by Johns Hopkins researchers suggests: Decreasing ...
To gain further insight into the mechanisms underlying miRNA-induced protection, we probed several target protective proteins that are implicated in IPC, including eNOS, iNOS, HSP70, and the HSP70 transcription factor HSF-1. As shown in Figure 3A, induction of eNOS mRNA (61±6.7%) was detected in the IPC-miRNA group 2 hours following treatment. However, no changes in iNOS mRNA were observed. Western blot analysis confirmed a significant upregulation in eNOS protein (62.0±6.7%) and HSF-1 (42.7±3.0%) 4 hours after IPC-miRNA treatment. HSP70 was also significantly increased (102.3±8.9%) 48 hours after IPC-miRNA treatment. Again, similar to mRNA, iNOS protein was not significantly changed (Figure 3C and 3D).. Despite potential species differences in cardioprotection,7 it is widely known that the protective effects of IPC occur in an early phase that develops rapidly after the initial stimulus but dissipates within 2 to 3 hours and a late phase that becomes apparent 12 to 24 hours later and ...
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May be involved in the digestion of phagocytosed particles in the lysosome, participation in an inflammatory protease cascade, and trimming of peptides for antigen presentation.
A first-time capable integration in a PCB inner layer a high-voltage human protective component up to 200.000 Volt by polymer thick film technology was produced by German PCB manufacturer Wuerth Elektronik.
Sorting nexin required to maintain late-Golgi resident enzymes in their proper location by recycling molecules from the prevacuolar ...
Page contains details about [email protected] . It has composition images, properties, Characterization methods, synthesis, applications and reference articles : nano.nature.com
18 Des 2017 - Sewa Apartemen di Santa Eugènia, Spanyol mulai dari Rp271950/malam. Temukan tempat menginap unik dengan tuan rumah setempat di 191 negara. Serasa di rumah di mana saja bersama Airbnb.
did you cpy and paste it to the ticker writing then copied it all together into the signiture ????? I am not to clever in that department ...
Galactosialidosis is a condition that affects many areas of the body. The three forms of galactosialidosis are distinguished by the age at which symptoms develop and the pattern of features.. The early infantile form of galactosialidosis is associated with extensive swelling caused by fluid accumulation before birth (hydrops fetalis), a soft out-pouching in the lower abdomen (an inguinal hernia), and an enlarged liver and spleen (hepatosplenomegaly). Additional features of this form include abnormal bone development (dysostosis multiplex) and distinctive facial features that are often described as "coarse." Some infants have an enlarged heart (cardiomegaly); an eye abnormality called a cherry-red spot, which can be identified with an eye examination; and kidney disease that can progress to kidney failure. Infants with this form usually are diagnosed between birth and 3 months; they typically live into late infancy.. The late infantile form of galactosialidosis shares some features with the early ...
TY - JOUR. T1 - Transforming growth factor-beta protection of cancer cells against tumor necrosis factor cytotoxicity is counteracted by hyaluronidase (review).. AU - Chang, N. S.. PY - 1998/12. Y1 - 1998/12. N2 - Numerous cancer cells, when exposed to transforming growth factor beta (TGF-beta), become resistant to tumor necrosis factor (TNF) cytotoxicity. Pretreatment of L929 fibroblasts, for example, with TGF-beta isoforms (beta 1, beta 2 and beta 3) for at least 0.5-1 h results in resistance to TNF killing. TGF-beta 1 mediates the following sequential events in L929 cells: i) rapid induction of protein tyrosine-phosphorylation (, 30 min), ii) stimulation of protective protein synthesis and acquisition of TNF resistance (approximately 0.5-1 h), and iii) suppression of I kappa B-alpha expression (1-2 h). Two protective proteins induced by TGF-beta 1 are a 46 kDa extracellular matrix TNF-resistance triggering (TRT) protein and a putative transmembrane anti-apoptotic adhesion protein TIF2 ...
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
BPC-157 2mg/5mg Healing Peptides BPC-157 is a long peptide have 15 amino acids, it is derived from a protective protein found in the stomach. It is a signalling peptide; it signals for certain processes to take place in the body. BPC-157 protects...
View mouse Vps37d Chr5:135072900-135078266 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
Worth mentioning because the same themes kept coming up. Specifically, there was quite a bit about everyone developing their own list of false positive variants/genes and how to filter SNPs adequately. Generally, its agreed that (1) there is a subset of variants and genes that show up in nearly every sequencing experiment and therefore are more likely false positives than anything else (they dont tend to validate, either) and (2) that dbSNP is too inclusive of disease samples and lacking adequate phenomic info to be used as a blind filter. Ive personally always told people to use dbSNP as a guide. Never dismiss a variant just because its in dbSNP. You can look at the non-dbSNP variants first if you want, since those might be the "jackpot" spots, but if you find nothing there, try looking in those in dbSNP ...
Functions as a sorting receptor in the Golgi compartment required for the intracellular sorting and delivery of soluble vacuolar proteins, like carboxypeptidase Y (CPY) and proteinase A.
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Several sRNA on the same phagemid : Although our silencing small RNAs were assembled in phagemids with Gibson assembly, the Biobricks cutting sites included in our BBG adapter method provide full modularity. In our case a direct application is the assembly of multiple silencing modules (promotor+sRNA+terminator) on a single phagemid vector. As the main clinical problem with bacteria is multi or even pan-resistance this modularity provide an interesting strategy to explore as it allows simultaneous downregulation of multiple target genes. Building a library of sRNA : As our silencing strategy rely on base pair complementarity, a main concern from the clinical point of view would be the fast emergence of resistances to silencing through single point mutations. Indeed even if the majority of mutations that would decrease the efficiency of the silencing would also lead to an impaired or non functionnal protective protein, some neutral mutations will still be made possible by the redundancy of the ...
Mathematicians and scientists from two UK universities have collaborated to shed new light on the process of viral replication during an infection.. Experimentalists from the University of Leeds and mathematicians from the University of York devised a mathematical model that gives new insights into the molecular mechanisms behind virus assembly, helping to explain the efficiency of their operation.. Researchers from the Departments of Mathematics and Biology at the University of York have developed a theoretical basis for the speed and efficiency with which viruses assemble the protective proteins for their genetic information - in this case an RNA molecule - during an infection.. The team incorporated multiple specific contacts between the genomic RNA and the proteins in the containers, along with other details of real virus infections, into a mathematical model that demonstrates how these contacts act collectively to reduce the complexity of virus formation.. They thus solved a longstanding ...
Mitch Leslie http://sageke.sciencemag.org/cgi/content/full/sageke;2003/42/nw144 Key Words: cardiac fibrosis cardiomyocytes apoptosis. Abstract: Like a flame slowly burning through a piece of wood, inflammation gnaws at the heart, sapping its pumping power. A new study suggests that a protective protein fashioned by the heart works by quashing an inflammation-sparking molecule. The finding could guide researchers to treatments that prevent heart failure, the number one cardiac killer among the elderly.. Citation: M. Leslie, Quench a Burning Heart. Sci. SAGE KE 2003 (42), nw144 (2003). ...
Artist: Eugène Atget (French, Libourne 1857-1927 Paris) Date: 1910 Medium: Albumen silver print from glass negative Accession: 1990.1026.1 On view in:Not on view ...
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Khat Khat (pronounced COT) is known by over 40 different street names including, kat, qat, chat, gat, graba, tohai, tschat, and mirraa. Khat is a stimulant derived from Catha Edulis, a 6-12-foot flowering evergreen shrub. The fresh young leaves of the shrub have been consumed where the plant is.... Read More ...
It has been suggested that the Golgi localization of GRIP-golgin in mammalian cells is dependent on the homo-dimerization of the GRIP domain, the interaction of the GRIP domain with activated Arl1, and the interaction of the GRIP domain with membrane phospholipids (Lu et al., 2006; Panic et al., 2003; Setty et al., 2003; Wu et al., 2004). In the current study, we found that the C-terminal region of Imh1p (Imh1-C177) is sufficient to maintain Arl1p at the trans-Golgi (Fig. 1E). To investigate whether the dimerization of Imh1p is required for its Golgi targeting as well as stabilizing of Arl1p on the Golgi, we generated Imh1p mutants with increasing large truncations of the coiled-coil region. The GRIP domain comprises the C-terminal 62 residues of Imh1p (Kjer-Nielsen et al., 1999). We therefore constructed Imh1-GRIP, Imh1-C89, Imh1-C177, and Imh1-C213, each of which possess an intact GRIP domain without or with part of the coiled-coil region (Fig. 5A). First, we performed two different yeast ...
Individuals with deficiencies of these factors or platelets exhibit to bleed; they do not bleed more very likely than people without these conditions, but it is justifiable more difficult allowing for regarding the clot to form, and bleeding cannot be stopped easily. J Biol Chem 282:12377В-12387 Schurigt U, Schad C, Glowa C, Baum U, Thomale K, Schnitzer JK, Schultheis M, Schaschke N, Schirmeister T, Moll H (2010) Aziridine-2,3-dicarboxylate-based cysteine cathepsin inhibitors bring about apartment death in Leishmania crucial associated with accumulation of debris in autophagy- kindred lysosome-like vacuoles. What if benzol levels are really uttermost greater discount pilex 60 caps with mastercard prostate cancer oncologist. In physiological terms, interactions between natural networks result in changes chief to another form of equilibrium that okay better coping with the unfamiliar condition. Morbidity statistics are revised less frequently because of the formidableness in defining or obtaining ...
carboxypeptidase L: Cathepsin A (also named protective protein and carboxypeptidase L) stabilizes beta-galactosidase and activates neuraminidase by forming with them a high-molecular-weight lysosomal complex
During the process of sporulation, a/α diploids degrade about 50% of their vegetative proteins. This degradation is not sporulation specific, for asporogenous diploids of a/a mating type degrade their vegetative proteins in a fashion similar to that of their a/α counterparts. Diploids lacking carboxypeptidase Y activity, prc1/prc1, show about 80% of wild-type levels of protein degradation, but are unimpaired in the production of normal asci. Diploids lacking proteinase B activity, prb1/prb1, show about 50% of wild-type levels of protein degradation. The effect on degradation of the proteinase B deficiency is epistatic to the degradation deficit attributable to the carboxypeptidase Y deficiency. The prb1 homozygotes undergo meiosis and produce spores, but the asci and, possibly, the spores are abnormal. Diploids homozygous for the pleiotropic pep4-3 mutation show only 30% of the wild-type levels of degradation when exposed to a sporulation regimen, and do not undergo meiosis or sporulation. ...
Journal of Pediatric Ophthalmology and Strabismus | The authors report a 5-year follow-up examination of two sisters diagnosed as having a juvenile form of type II sialidosis. Diagnosis occurred during a routine ophthalmic examination when the girls were 5 and 3 years old after bilateral macular cherry-red spots were revealed. Main clinical findings were hypotonia, hepatosplenomegaly, hearing loss, dysostosis, and respiratory distress. Ophthalmic
Introduction. Are Viruses Alive? What is a Virus? Viruses are very small microorganisms, much smaller than bacteria. They are among the smallest organisms known and consist of a fragment of genetic material inside a protective protein coat. Viruses can only reproduce inside host cells and as a result, they damage the cell when they do this. Once a virus has invaded a cell, it then takes over and makes copies of itself. Eventually the copies of the virus fill the whole host cell, causing it to burst open. The viruses are then passed out in the bloodstream, the airways, or by other routes. ...read more. Middle. They are arranged in a precise and highly repetitive pattern around the nucleic acid. A single type of capsomere or several chemically distinct types may make up the capsid. 3. Some viruses contain an envelope. An envelope is a membrane-like structure that encloses the nucleocapsid and is obtained from a host cell during the replication process. The envelope contains viral-specified ...
When reoviruses infect a cell, they induce that cell to secrete chemicals that both cause its own death and initiate the bodys immune response against that cell. Normal cells can protect themselves from this onslaught by secreting their own protective protein called PKR. However, many types of cancer cells inactivate PKR, leaving them vulnerable to reovirus attack.. In this study, the researchers took the growth media from dying reovirus-infected human melanoma cells and administered that extract to new tumor cells. Even in the absence of live virus, immune cells were recruited to attack the cancer cells.. Although this line of attack is only in the preliminary stages, I wonder if eventually doctors will be able to brew up great vats of cancer-fighting reovirus media. ...
Lysosomal Pro-X Carboxypeptidase/PRCP Overexpression Lysate (Denatured). Tested Reactivity: Hu. Validated: WB. Backed by our 100% Guarantee.
Artist: Eugène Atget (French, Libourne 1857-1927 Paris) Date: ca. 1910 Medium: Albumen silver print from glass negative Accession: 1990.1026.2 On view in:Not on view ...
thats a common mechanism in enzymes, not only in carboxypeptidase. However, the point is, there are several of these weak bonds and their sum is strong enough to stretch the peptide causing to be better to hydrolyse ...
1HYT: Redetermination and refinement of the complex of benzylsuccinic acid with thermolysin and its relation to the complex with carboxypeptidase A.
VPS45A山羊多克隆抗体(ab40853)可与人样本反应并经WB, ELISA实验严格验证,被1篇文献引用。所有产品均提供质保服务,中国75%以上现货。
Looking for online definition of Carboxypeptidases a in the Medical Dictionary? Carboxypeptidases a explanation free. What is Carboxypeptidases a? Meaning of Carboxypeptidases a medical term. What does Carboxypeptidases a mean?
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High-energy X-ray diffraction was used to pinpoint some 5 million atoms in the protective protein coat used by hundreds of viruses. Credit: J. Pan & Y.J. Tao/Rice University (PhysOrg.com) -- If a picture is worth a thousand words, then Rice Universitys precise new image of a virus protective coat is seriously undervalued. More than three years in the making, the image contains some 5 million atoms -- each in precisely the right place -- and it could help scientists find better ways to both fight viral infections and design new gene therapies. The stunning image, which appears online this week in the Proceedings of the National Academy of Sciences, reveals the structure of a type of protein coat shared by hundreds of known viruses containing double-stranded RNA genomes. The image was painstakingly created from hundreds of high-energy X-ray diffraction images and paints the clearest picture yet of the viruses genome-encasing shell called a "capsid." "When these viruses invade cells, the capsids ...
The results showed that retinal function was significantly protected in the mice consuming the grape-enriched diet. The grape-consuming group had three-fold higher rod and cone photoreceptor responses compared with those on the control diets. They also exhibited thicker retinas. Grape consumption also protected retinal function in an oxidative stress model of macular degeneration. Further analysis revealed that the grape diet resulted in lower levels of inflammatory proteins and higher amounts of protective proteins in the retinas ...
Catha edulis Forssk belongs to the Celastraceae family and, a neighbouring species of the Evonymus, it is the sole representative of the genus Catha. The Swedish botanist Forsskal, the explorer of lower Egypt and Arabia, was the first to mention this plant, which he called gat or khat. His description of it was published posthumously in 1775 in his Flora aegyptico-arabica 8
Nasal Cavity Sections (/Rhythmyx/assembler/render?sys_contentid=34273&sys_revision=1&sys_variantid=639&sys_context=0&sys_authtype=0&sys_siteid=&sys_folderid= sys_dependentvariantid=639 sys_dependentid=34273 inlinetype=rxhyperlink rxinlineslot=103 sys_dependentid=34273 sys_siteid= sys_folderid=), Infusion (/Rhythmyx/assembler/render?sys_contentid=34273&sys_revision=1&sys_variantid=639&sys_context=0&sys_authtype=0&sys_siteid=&sys_folderid= sys_dependentvariantid=639 sys_dependentid=34273 inlinetype=rxhyperlink rxinlineslot=103 sys_dependentid=34273 sys_siteid= sys_folderid=) ...
Define carboxypeptidase. carboxypeptidase synonyms, carboxypeptidase pronunciation, carboxypeptidase translation, English dictionary definition of carboxypeptidase. n. Any of several enzymes that catalyze the hydrolysis of the terminal amino acid of a polypeptide from the end that contains a free carboxyl group
Carboxypeptidases are enzymes that hydrolyze C-terminal peptide bonds. The carboxypeptidase family includes metallo-, serine, and cysteine carboxypeptidases. According to their substrate specificity, these enzymes are referred to as carboxypeptidase A (cleaving aliphatic residues) or carboxypeptidase B (cleaving basic amino residues). The protein encoded by this gene is activated by trypsin and acts on carboxypeptidase B substrates. After thrombin activation, the mature protein downregulates fibrinolysis. Polymorphisms have been described for this gene and its promoter region. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Jun 2013 ...
21.10.2019 - Patients who survive a cerebral hemorrhage may suffer delayed severe brain damage caused by free hemoglobin, which comes from red blood cells and damages neurons. Researchers at the University of Zurich and the UniversityHospital Zurich have now discovered a protective protein in the body called haptoglobin, which prevents this effect.
Contact Us. Tel:732-484-9848. Fax:888-484-5008. Email:[email protected]. Add:1 Deer Park Dr, Suite Q,. Monmouth Junction, NJ 08852, USA. ...
Projekt Ni nam vseeno je naše darilo vam. Ustvarjamo ga s srcem, v želji, da najdete koristne informacije, ki bi vam lahko pomagale, da (p)ostanete zdravi. Vsak doniran znesek bo porabljen za dober namen. ...
The neuronal ceroid lipofuscinoses (NCLs) are a group of inherited neurodegenerative disorders with pathological phenotypes that auto fluorescent lipopigments present in neurons and other cell types. Over the past two decades, accumulating evidences indicates that NCLs are caused by mutations in eight different genes, including genes encoding several soluble proteins (cathepsin D, PPT1, and TPP1).[7] Mutations of gene TPP1 result in late-infantile neuronal ceroid lipofuscinosis which is associated with the failure to degrade specific neuropeptides and a subunit of ATP synthase in the lysosome.[8] Mutations in the TPP1 gene lead to late infantile neuronal ceroid lipofuscinosis, a fatal neurodegenerative disease of childhood.[6] It has been demonstrated that a single injection of intravitreal implantation of autologous bone marrow derived stem cells transduced with a TPP1 expression construct at an early stage in the disease progression could substantially inhibit the development of ...
Tight repression of yeast endoplasmic reticulum stress sensor Ire1 by its N-terminal intrinsically disordered subdomainTight repression of yeast endoplasmic reticulum stress sensor Ire1 by its N-terminal intrinsically disordered subdomain ...
We have cloned the cDNA for human carboxypeptidase D (CPD), a new B-type metallocarboxypeptidase that is membrane bound and has an acidic pH optimum. The 5.8 kb of cDNA sequenced contains an open reading frame of 4131 bp encoding 1377 amino acid residues. The sequence is similar (75% identity) to duck gp180, a protein that was isolated, cloned and sequenced as a hepatitis B virus-binding protein but not characterized as a carboxypeptidase. Hydropathic analysis revealed a hydrophobic region at the N-terminus, representing the signal peptide, and one near the C-terminus that probably represents the transmembrane anchor. The most striking feature is the presence of three tandem carboxypeptidase homology domains that have sequence similarity to the regulatory B-type carboxypeptidase family, typified by carboxypeptidases M, E and N. Because of the three repeats, CPD is about three times larger (175-180 kDa) than other members of this family (approx. 50-62 kDa). Domain 2 is most closely related to ...
Gangliosides play key roles in cell differentiation, cell-cell interactions, and transmembrane signaling. Sialidases hydrolyze sialic acids to produce asialo compounds, which is the first step of degradation processes of glycoproteins and gangliosides. Sialidase involvement has been implicated in some lysosomal storage disorders such as sialidosis and galactosialidosis. Neu2 is a recently identified human cytosolic sialidase. Here we report the first high resolution x-ray structures of mammalian sialidase, human Neu2, in its apo form and in complex with an inhibitor, 2-deoxy-2,3-dehydro-N-acetylneuraminic acid (DANA). The structure shows the canonical six-blade beta-propeller observed in viral and bacterial sialidases with its active site in a shallow crevice. In the complex structure, the inhibitor lies in the catalytic crevice surrounded by ten amino acids. In particular, the arginine triad, conserved among sialidases, aids in the proper positioning of the carboxylate group of DANA within the ...
In the yeast Saccharomyces cerevisiae, mutations in vacuolar protein sorting (VPS) genes result in secretion of proteins normally localized to the vacuole. Characterization of the VPS pathway has provided considerable insight into mechanisms of protein sorting and vesicle-mediated intracellular transport. We have cloned VPS9 by complementation of the vacuolar protein sorting defect of vps9 cells, characterized its gene product, and investigated its role in vacuolar protein sorting. Cells with a vps9 disruption exhibit severe vacuolar protein sorting defects and a temperature-sensitive growth defect at 38 degrees C. Electron microscopic examination of delta vps9 cells revealed the appearance of novel reticular membrane structures as well as an accumulation of 40- to 50-nm-diameter vesicles, suggesting that Vps9p may be required for the consumption of transport vesicles containing vacuolar protein precursors. A temperature-conditional allele of vps9 was constructed and used to investigate the ...
carboxypeptidase M: from human placental microvilli; MW 62kDa; cleaves Arg or Lys from the COOH terminus of synthetic peptides as well as several biologically active substrates; membrane-bound; structurally, catalytically & immunologically distinct from carboxypeptidase A,B,N & H
Results Overall the HIV-1 Quant Assay performed on the GeneXpert® Instrument Systems correlated with the routine analytical platform (r2 = 0.9333). Samples ranged undetectable (16, 8.8%), below the benchmark test lower limit of detection (,20 cpy/ml) (10, 7.9%), low range (20-5,000) (43, 33.1%), medium (5,000-50,000) (24, 18.5%) and high range (,50,000 cpy/ml) (29, 22.3%). Thirteen samples (10%) were invalid as a result of insufficient sample. Samples in the lower analytical range ,1,000 cpy/ml showed little variance when compared with the Roche (CAP/CTM) assay using Bland-Altman correlation analysis. Reproducibility was assessed in the high, medium and low range within 1-2SD of mean. Sixteen replicates of a commercial external control showed very good reproducibility. ...
Gentaur molecular products has all kinds of products like :search , Abfron \ anti-Carboxypeptidase N subunit 2 precusor , Mouse monoclonal to Carboxypeptidase N subunit 2 precusor , Isotype IgG1, Host Mouse \ LF-MA0203 for more molecular products just contact us
Free Online Library: Assay of procarboxypeptidase U, a novel determinant of the fibrinolytic cascade, in human plasma.(Enzymes and Protein Markers) by Clinical Chemistry; Fibrin Lysine
Spletna knjigarna in založba Cangura vam nudi knjige in ostale artikle za zdravje. Izbirate lahko med knjigami za samopomoč in ostalimi koristnimi dodatki.
Spletna knjigarna in založba Cangura vam nudi knjige in ostale artikle za zdravje. Izbirate lahko med knjigami za samopomoč in ostalimi koristnimi dodatki.

D - Health Conditions - Genetics Home Reference - NIHD - Health Conditions - Genetics Home Reference - NIH

deficiency of cathepsin A, see Galactosialidosis. *deficiency of cytochrome-b5 reductase, see Autosomal recessive congenital ...
more infohttps://ghr.nlm.nih.gov/condition?initial=d

Comparative proteomics of excretory-secretory proteins released by the liver fluke Fasciola hepatica in sheep host bile and...Comparative proteomics of excretory-secretory proteins released by the liver fluke Fasciola hepatica in sheep host bile and...

Only cathepsin L proteases from F. hepatica were identified in our ovine host bile preparations. Several host proteins were ... Western blotting of in vitro and in vivo ES proteins showed only cathepsin L proteases were recognized by serum pooled from F. ... Time course in vitro analysis confirmed cathepsin L proteases as the major constituents of the in vitro ES proteome. In ... and further confirms the potential of the cathepsin L proteases as therapy candidates. ...
more infohttp://cadair.aber.ac.uk/dspace/handle/2160/1608

Transcriptome profiling of gene expression during immunisation trial against Fasciola hepatica: identification of genes and...Transcriptome profiling of gene expression during immunisation trial against Fasciola hepatica: identification of genes and...

... hepatica cathepsin B and amoebapore proteins, as novel vaccine candidates against F. hepatica formulated in an adjuvant ... F. hepatica cathepsin B is mainly expressed in metacercariae and newly excysted juveniles whilst cathepsin L is mainly ... Cathepsin B proteases of flukes: the key to facilitating parasite control? Trends Parasitol. 2010;26(10):506-14.View Article ... F. hepatica cathepsin B and amoebapore-like proteins were selected as vaccine candidates in the present study. According to the ...
more infohttps://bmcinfectdis.biomedcentral.com/articles/10.1186/s12879-017-2205-3

Human CTSZ ELISA Kit | biobool.comHuman CTSZ ELISA Kit | biobool.com

Human cathepsin B2 ELISA Kit;Human cathepsin IV ELISA Kit;Human cathepsin Y ELISA Kit;Human cathepsin Z1 ELISA Kit;Human ... Human cathepsin P ELISA Kit;Human cathepsin X ELISA Kit;Human CTSX ELISA Kit;Human cathepsin Z ELISA Kit;Human carboxypeptidase ... The concentration of Cathepsin Z (CTSZ) in the samples is then determined by comparing the O.D. of the samples to the standard ... The microtiter plate provided in this kit has been pre-coated with an antibody specific to Cathepsin Z (CTSZ). Standards or ...
more infohttps://www.biobool.com/elisa_kit/7091.html

Cathepsins (CTS) Gene Family | HUGO Gene Nomenclature CommitteeCathepsins (CTS) Gene Family | HUGO Gene Nomenclature Committee

Cathepsin: Cathepsins ( Ancient Greek kata- "down" and hepsein "boil"; abbreviated CTS ) are proteases ( enzymes that degrades ... Cathepsins have a vital role in mammalian cellular turnover, e.g. bone resorption. They degrade polypeptides and are ... There are, however, exceptions such as cathepsin K, which works extracellularly after secretion by osteoclasts in bone ...
more infohttps://www.genenames.org/cgi-bin/genefamilies/set/470

Cathepsin W - WikipediaCathepsin W - Wikipedia

"Human cathepsins W and F form a new subgroup of cathepsins that is evolutionary separated from the cathepsin B- and L-like ... Wex T, Levy B, Wex H, Brömme D (1999). "Human cathepsins F and W: A new subgroup of cathepsins". Biochem. Biophys. Res. Commun ... 2003). "Characterization of novel anti-cathepsin W antibodies and cellular distribution of cathepsin W in the gastrointestinal ... Cathepsin W is a protein that in humans is encoded by the CTSW gene.[5][6][7] ...
more infohttps://en.wikipedia.org/wiki/Cathepsin_W

Cathepsin D - WikipediaCathepsin D - Wikipedia

"Entrez Gene: CTSD cathepsin D".. *^ Barrett AJ (April 1970). "Cathepsin D. Purification of isoenzymes from human and chicken ... Cathepsin D is an aspartic endo-protease that is ubiquitously distributed in lysosomes.[7] The main function of cathepsin D is ... The optimum pH for cathepsin D in vitro is 4.5-5.0.[13] Cathepsin-D is an aspartic protease that depends critically on ... Cathepsin D is a protein that in humans is encoded by the CTSD gene.[5][6] This gene encodes a lysosomal aspartyl protease ...
more infohttps://en.wikipedia.org/wiki/Cathepsin_D

Cathepsin K (O35186) | InterPro | EMBL-EBICathepsin K (O35186) | InterPro | EMBL-EBI

InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
more infohttp://www.ebi.ac.uk/interpro/protein/O35186

Cathepsin - WikipediaCathepsin - Wikipedia

Cathepsin A (serine protease) Cathepsin B (cysteine protease) Cathepsin C (cysteine protease) Cathepsin D (aspartyl protease) ... Cathepsin H (cysteine protease) Cathepsin K (cysteine protease) Cathepsin L1 (cysteine protease) Cathepsin L2 (or V) (cysteine ... Cathepsin S (cysteine protease) Cathepsin W (cysteine proteinase) Cathepsin Z (or X) (cysteine protease) Cathepsins have been ... Cathepsin K has also been shown to play a role in arthritis. Mouse cathepsin L is homologous to human cathepsin V. Mouse ...
more infohttps://en.wikipedia.org/wiki/Cathepsin

CathePsin L family (O45734) | InterPro | EMBL-EBICathePsin L family (O45734) | InterPro | EMBL-EBI

InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
more infohttps://www.ebi.ac.uk/interpro/protein/O45734

Cathepsin T - WikipediaCathepsin T - Wikipedia

Cathepsin Cathepsin T at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... Cathepsin T (EC 3.4.22.24) is an enzyme. This enzyme catalyses the following chemical reaction Interconversion of the three ... Pitot, H.C.; Gohda, E. (1987). "Cathepsin T". Methods Enzymol. 142: 279-289. doi:10.1016/s0076-6879(87)42038-7. PMID 2885716. ...
more infohttps://en.wikipedia.org/wiki/Cathepsin_T

RCSB PDB - Gene View 









 - CTSK - cathepsin KRCSB PDB - Gene View - CTSK - cathepsin K

The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
more infohttps://www.rcsb.org/pdb/gene/CTSK

Cathepsin Protease Inhibition Reduces Endometriosis Lesion Establishment.  - PubMed - NCBICathepsin Protease Inhibition Reduces Endometriosis Lesion Establishment. - PubMed - NCBI

Incubation with the cathepsin L specific inhibitor, Z-FY-DMK, blocked cathepsin L signals, confirming the cathepsin L bands in ... Z-FY-DMK cathepsin L inhibitor does not inhibit all cathepsin activity of murine endometriotic lesions. Incubation with Z-FY- ... DMK, a selective inhibitor of cathepsin L, inhibited many of the cathepsin active bands but did not block all active cathepsin ... E-64 blocks all cathepsin proteolytic activity in murine endometriotic lesions. Incubation with the broad cathepsin inhibitor, ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/26482207

CTSV cathepsin V [Homo sapiens (human)] - Gene - NCBICTSV cathepsin V [Homo sapiens (human)] - Gene - NCBI

cathepsin L2. Names. cathepsin L2, preproprotein. cathepsin U. NP_001188504.1. *EC 3.4.22.43 ... using cathepsin V and cathepsin L as model enzymes, a series of chimeras were generated to identify noncatalytic regions that ... functions of cathepsin V are controlled by N-glycosylation Title: Determination of cathepsin V activity and intracellular ... CTSV cathepsin V [Homo sapiens] CTSV cathepsin V [Homo sapiens]. Gene ID:1515 ...
more infohttps://www.ncbi.nlm.nih.gov/gene/1515

Enzymes Attack One Another In Cathepsin CannibalismEnzymes Attack One Another In 'Cathepsin Cannibalism'

Cathepsin K degrades both collagen and elastin, and is one of the most powerful proteases. Cathepsin S degrades elastin, and ... "We saw that the cathepsin K was going away much faster when there was cathepsin S present than when it was by itself," said ... "We kept increasing the amount of cathepsin S until the collagen was not affected at all because all of the cathepsin K was ... Barrys modeling suggested that effects observed could occur if cathepsin S were degrading cathepsin K instead of attacking the ...
more infohttp://www.innovations-report.com/html/reports/life-sciences/enzymes-attack-quot-cathepsin-cannibalism-quot-200491.html

Cathepsin K Antibody
		        
	Cathepsin K Antibody

Cathepsin K Polyclonal Antibody from Invitrogen for Western Blot, Immunohistochemistry (Paraffin) and Flow Cytometry ... Protein Aliases: Cathepsin K; Cathepsin O; cathepsin O1; Cathepsin O2; Cathepsin X; CTSK; CTSO; CTSO2 ... Cite Cathepsin K Polyclonal Antibody. The following antibody was used in this experiment: Cathepsin K Polyclonal Antibody from ...
more infohttps://www.thermofisher.com/antibody/product/CTSK-Antibody-Polyclonal/PA5-14270

Anti-Cathepsin G antibody (ab231149) | AbcamAnti-Cathepsin G antibody (ab231149) | Abcam

Rabbit polyclonal Cathepsin G antibody. Validated in WB, IHC and tested in Rat, Human. Immunogen corresponding to recombinant ... Anti-Cathepsin G antibody (ab231149) at 3 µg/ml + Recombinant rat Cathepsin G protein. Secondary. HRP-Linked Guinea pig anti- ... This product Rabbit Anti-Cathepsin G antibody (ab231149) WB, IHC-P Goat Anti-Rabbit IgG H&L (HRP) (ab205718) IHC-P, WB, ELISA, ... All lanes : Anti-Cathepsin G antibody (ab231149) at 3 µg/ml. Lane 1 : Rat serum. Lane 2 : Rat heart lysate. Lane 3 : MCF7 ( ...
more infohttps://www.abcam.com/cathepsin-g-antibody-ab231149.html

Anti-Cathepsin D antibody (ab19555) | AbcamAnti-Cathepsin D antibody (ab19555) | Abcam

Rabbit polyclonal Cathepsin D antibody validated for WB, ELISA, IHC, ICC/IF and tested in Human. Referenced in 1 publication ... This antibody reacts with human liver cathepsin D, and does not react with cathepsins B, H and L. ... IHC image of Cathepsin D staining in Human Lung formalin fixed paraffin embedded tissue section, performed on a Leica Bond™ ... Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Cathepsin D antibody (ab19555) ...
more infohttp://www.abcam.com/cathepsin-d-antibody-ab19555.html

Cathepsin A (CTSA) AntikörperCathepsin A (CTSA) Antikörper

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

Cathepsin Detection Kits - MP BiomedicalsCathepsin Detection Kits - MP Biomedicals

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

WikiGenes - Ctsl - cathepsin LWikiGenes - Ctsl - cathepsin L

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

WikiGenes - CTSC - cathepsin CWikiGenes - CTSC - cathepsin C

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

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

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

Cathepsin Assay KitsCathepsin Assay Kits

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

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

Cathepsin B. Cathepsin B, EC 3.4.22.1 (APP secretase, APPS) (Cathepsin B1) [Cleaved into: Cathepsin B light chain; Cathepsin B ... Cathepsin BImported. ,p>Information which has been imported from another database using automatic procedures.,/p> ,p>,a href="/ ... tr,E9PL32,E9PL32_HUMAN Cathepsin B (Fragment) OS=Homo sapiens OX=9606 GN=CTSB PE=1 SV=2 ...
more infohttps://www.uniprot.org/uniprot/E9PL32
  • These results suggest that the ecdysone response elements are vital for activation of the promoter by 20-hydroxyecdysone (20E) in the larval fat body and further support the crucial role of ecdysone signaling to control cathepsin D gene transcription. (antibodies-online.com)
  • Schwartz-Roberts, Shajahan, Cook, Wärri, Abu-Asab, Clarke: GX15-070 (obatoclax) induces apoptosis and inhibits cathepsin D- and L-mediated autophagosomal lysis in antiestrogen-resistant breast cancer cells. (antibodies-online.com)
  • The requirement for cathepsin L proteolysis identifies a previously uncharacterized class of inhibitor for SARS-CoV infection. (pnas.org)
  • Our results are consistent with a model in which SARS-CoV employs a unique three-step method for membrane fusion, involving receptor-binding and induced conformational changes in S glycoprotein followed by cathepsin L (CTSL) proteolysis and activation of membrane fusion within endosomes. (pnas.org)
  • Determination of cathepsin V activity and intracellular trafficking by N-glycosylation. (nih.gov)
  • E-64 blocks all cathepsin proteolytic activity in murine endometriotic lesions. (nih.gov)
  • Mouse endometriotic lesions exhibit elevated cathepsin proteolytic activity. (nih.gov)
  • Cathepsin-D is an aspartic protease that depends critically on protonation of its active site Asp residue. (wikipedia.org)
  • A significantly elevated cathepsin S expression in gingival biopsies from rats with experimental periodontitis was found in vivo , as compared to that from control. (hindawi.com)
  • Gingival biopsies from periodontitis patients showed a significantly higher cathepsin S expression than those from healthy gingiva. (hindawi.com)
  • Cathepsin D enzymatic activity induces hydrolytic modification of apolipoprotein B-100-containing lipoproteins, including LDL, which means it may be involved in atherosclerosis as well. (wikipedia.org)
  • Cathepsin D (an aspartyl protease) appears to cleave a variety of substrates such as fibronectin and laminin. (wikipedia.org)
  • Along with Asp-protonation, lower pH also leads to conformational switch in cathepsin-D : the N-terminal segment of the protease moves out of the active site as pH drops. (wikipedia.org)