Cysteine Proteases: A subclass of peptide hydrolases that depend on a CYSTEINE residue for their activity.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.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Protease Inhibitors: Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).Cysteine: A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.HIV Protease: Enzyme of the human immunodeficiency virus that is required for post-translational cleavage of gag and gag-pol precursor polyproteins into functional products needed for viral assembly. HIV protease is an aspartic protease encoded by the amino terminus of the pol gene.Endopeptidases: A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.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.Serine Endopeptidases: Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.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.Cysteine Proteinase Inhibitors: Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.Proteomics: The systematic study of the complete complement of proteins (PROTEOME) of organisms.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.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.Cathepsin L: A ubiquitously-expressed cysteine protease that plays an enzymatic role in POST-TRANSLATIONAL PROTEIN PROCESSING of proteins within SECRETORY GRANULES.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.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.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.Calpain: Cysteine proteinase found in many tissues. Hydrolyzes a variety of endogenous proteins including NEUROPEPTIDES; CYTOSKELETAL PROTEINS; proteins from SMOOTH MUSCLE; CARDIAC MUSCLE; liver; platelets; and erythrocytes. Two subclasses having high and low calcium sensitivity are known. Removes Z-discs and M-lines from myofibrils. Activates phosphorylase kinase and cyclic nucleotide-independent protein kinase. This enzyme was formerly listed as EC 3.4.22.4.Protease La: A prokaryotic ATP-dependent protease that plays a role in the degradation of many abnormal proteins. It is a tetramer of 87-kDa subunits, each of which contains a proteolytic site and a ATP-binding site.Kinetics: The rate dynamics in chemical or physical systems.ATP-Dependent Proteases: Proteases that contain proteolytic core domains and ATPase-containing regulatory domains. They are usually comprised of large multi-subunit assemblies. The domains can occur within a single peptide chain or on distinct subunits.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Serine Proteinase Inhibitors: Exogenous or endogenous compounds which inhibit SERINE ENDOPEPTIDASES.Recombinant Proteins: Proteins prepared by recombinant DNA technology.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.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Cathepsin F: A lysosomal papain-related cysteine proteinase that is expressed in a broad variety of cell types.Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Protease Nexins: Extracellular protease inhibitors that are secreted from FIBROBLASTS. They form a covalent complex with SERINE PROTEASES and can mediate their cellular internalization and degradation.Protein Structure, Tertiary: The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.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)Escherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.Catalytic Domain: The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.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.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Dipeptides: Peptides composed of two amino acid units.Enzyme Precursors: Physiologically inactive substances that can be converted to active enzymes.Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Bacterial Proteins: Proteins found in any species of bacterium.Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Caspase 1: A long pro-domain caspase that has specificity for the precursor form of INTERLEUKIN-1BETA. It plays a role in INFLAMMATION by catalytically converting the inactive forms of CYTOKINES such as interleukin-1beta to their active, secreted form. Caspase 1 is referred as interleukin-1beta converting enzyme and is frequently abbreviated ICE.Caspases: A family of intracellular CYSTEINE ENDOPEPTIDASES that play a role in regulating INFLAMMATION and APOPTOSIS. They specifically cleave peptides at a CYSTEINE amino acid that follows an ASPARTIC ACID residue. Caspases are activated by proteolytic cleavage of a precursor form to yield large and small subunits that form the enzyme. Since the cleavage site within precursors matches the specificity of caspases, sequential activation of precursors by activated caspases can occur.Sequence Alignment: The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.Enzyme Activation: Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.Oligopeptides: Peptides composed of between two and twelve amino acids.Protein Processing, Post-Translational: Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Proteolysis: Cleavage of proteins into smaller peptides or amino acids either by PROTEASES or non-enzymatically (e.g., Hydrolysis). It does not include Protein Processing, Post-Translational.Molecular Weight: The sum of the weight of all the atoms in a molecule.Structure-Activity Relationship: The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.Spirometra: A genus of tapeworms of the family Diphyllobothriidae, which are parasites of fish-eating cats, dogs, and birds. Infection in man is caused by eating undercooked fish. The larval form is called SPARGANUM.Ubiquitin-Specific Proteases: Members of the peptidase C19 family which regulate signal transduction by removing UBIQUITIN from specific protein substrates via a process known as deubiquitination or deubiquitylation.Cysteine Dioxygenase: An enzyme that catalyzes the conversion of L-CYSTEINE to 3-sulfinoalanine (3-sulfino-L-alanine) in the CYSTEINE metabolism and TAURINE and hypotaurine metabolic pathways.Trypsin: A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.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.Leucine: An essential branched-chain amino acid important for hemoglobin formation.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)Serpins: A family of serine proteinase inhibitors which are similar in amino acid sequence and mechanism of inhibition, but differ in their specificity toward proteolytic enzymes. This family includes alpha 1-antitrypsin, angiotensinogen, ovalbumin, antiplasmin, alpha 1-antichymotrypsin, thyroxine-binding protein, complement 1 inactivators, antithrombin III, heparin cofactor II, plasminogen inactivators, gene Y protein, placental plasminogen activator inhibitor, and barley Z protein. Some members of the serpin family may be substrates rather than inhibitors of SERINE ENDOPEPTIDASES, and some serpins occur in plants where their function is not known.Apoptosis: One of the mechanisms by which CELL DEATH occurs (compare with NECROSIS and AUTOPHAGOCYTOSIS). Apoptosis is the mechanism responsible for the physiological deletion of cells and appears to be intrinsically programmed. It is characterized by distinctive morphologic changes in the nucleus and cytoplasm, chromatin cleavage at regularly spaced sites, and the endonucleolytic cleavage of genomic DNA; (DNA FRAGMENTATION); at internucleosomal sites. This mode of cell death serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth.Pepstatins: N-acylated oligopeptides isolated from culture filtrates of Actinomycetes, which act specifically to inhibit acid proteases such as pepsin and renin.Disulfides: Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.Metalloendopeptidases: ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.Cysteine Synthase: An enzyme that catalyzes the biosynthesis of cysteine in microorganisms and plants from O-acetyl-L-serine and hydrogen sulfide. This enzyme was formerly listed as EC 4.2.99.8.Peptides: 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.Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.Leupeptins: A group of acylated oligopeptides produced by Actinomycetes that function as protease inhibitors. They have been known to inhibit to varying degrees trypsin, plasmin, KALLIKREINS, papain and the cathepsins.Helminth Proteins: Proteins found in any species of helminth.Caspase 3: A short pro-domain caspase that plays an effector role in APOPTOSIS. It is activated by INITIATOR CASPASES such as CASPASE 9. Isoforms of this protein exist due to multiple alternative splicing of its MESSENGER RNA.Paragonimus: A genus of lung flukes of the family Troglotrematidae infecting humans and animals. This genus consists of several species one of which is PARAGONIMUS WESTERMANI, a common lung fluke in humans.Coumarins: Synthetic or naturally occurring substances related to coumarin, the delta-lactone of coumarinic acid.Aspartic Acid Endopeptidases: A sub-subclass of endopeptidases that depend on an ASPARTIC ACID residue for their activity.Enzyme Stability: The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.Streptococcus pyogenes: A species of gram-positive, coccoid bacteria isolated from skin lesions, blood, inflammatory exudates, and the upper respiratory tract of humans. It is a group A hemolytic Streptococcus that can cause SCARLET FEVER and RHEUMATIC FEVER.Protein Conformation: The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).Sulfhydryl Compounds: Compounds containing the -SH radical.Cells, Cultured: Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.Bromelains: Protein-digesting and milk-clotting enzymes found in PINEAPPLE fruit juice and stem tissue. Enzymes from the two sources are distinguished as fruit bromelain and stem bromelain. This enzyme was formerly listed as EC 3.4.22.4.Protozoan Proteins: Proteins found in any species of protozoan.Endopeptidase Clp: An ATP-dependent protease found in prokaryotes, CHLOROPLASTS, and MITOCHONDRIA. It is a soluble multisubunit complex that plays a role in the degradation of many abnormal proteins.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.Amino Acid Chloromethyl Ketones: Inhibitors of SERINE ENDOPEPTIDASES and sulfhydryl group-containing enzymes. They act as alkylating agents and are known to interfere in the translation process.Amino Acid Substitution: The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.Chymotrypsin: A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side.DNA, Complementary: Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.Subtilisins: A family of SERINE ENDOPEPTIDASES isolated from Bacillus subtilis. EC 3.4.21.-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.Protein Structure, Secondary: The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.Membrane Proteins: Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.Oxidation-Reduction: A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).Caspase 6: A short pro-domain caspase that plays an effector role in APOPTOSIS. It is activated by INITIATOR CASPASES such as CASPASE 7; CASPASE 8; and CASPASE 10. Isoforms of this protein exist due to multiple alternative splicing of its MESSENGER RNA.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.Amino Acids: Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.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.DNA Primers: Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.Cattle: Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.Recombinant Fusion Proteins: Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.Chromatography, Gel: Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.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.Blotting, Western: Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.Protein PrecursorsTemperature: The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.Proteins: Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.Molecular Structure: The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds.Mass Spectrometry: An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.Gene Expression Regulation, Enzymologic: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.Time Factors: Elements of limited time intervals, contributing to particular results or situations.Plant Proteins: Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.Metalloproteases: Proteases which use a metal, normally ZINC, in the catalytic mechanism. This group of enzymes is inactivated by metal CHELATORS.RNA, Messenger: RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.Viral Proteins: Proteins found in any species of virus.Plasmids: Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.Vinyl CompoundsCystine: A covalently linked dimeric nonessential amino acid formed by the oxidation of CYSTEINE. Two molecules of cysteine are joined together by a disulfide bridge to form cystine.Immunoblotting: Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.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.Escherichia coli Proteins: Proteins obtained from ESCHERICHIA COLI.Transfection: The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.Trypsin Inhibitors: Serine proteinase inhibitors which inhibit trypsin. They may be endogenous or exogenous compounds.Conserved Sequence: A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences.Models, Biological: Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.Enzyme Inhibitors: Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.SulfonesCaseins: A mixture of related phosphoproteins occurring in milk and cheese. The group is characterized as one of the most nutritive milk proteins, containing all of the common amino acids and rich in the essential ones.Caspase Inhibitors: Endogenous and exogenous compounds and that either inhibit CASPASES or prevent their activation.Signal Transduction: The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.Phylogeny: The relationships of groups of organisms as reflected by their genetic makeup.Cystatin M: A cystatin subtype that has a diverse tissue distribution, target specificity, and functions as an endogenous inhibitor of lysosomal cysteine proteases.Cricetinae: A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.Viral Nonstructural Proteins: Proteins encoded by a VIRAL GENOME that are produced in the organisms they infect, but not packaged into the VIRUS PARTICLES. Some of these proteins may play roles within the infected cell during VIRUS REPLICATION or act in regulation of virus replication or VIRUS ASSEMBLY.Rabbits: The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.HeLa Cells: The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for VIRUS CULTIVATION and antitumor drug screening assays.Paragonimiasis: Infection with TREMATODA of the genus PARAGONIMUS.Caspase 2: A long pro-domain caspase that contains a caspase recruitment domain in its pro-domain region. Activation of this enzyme can occur via the interaction of its caspase recruitment domain with CARD SIGNALING ADAPTOR PROTEINS. Caspase 2 plays a role in APOPTOSIS by cleaving and activating effector pro-caspases. Several isoforms of this protein exist due to multiple alternative splicing of its MESSENGER RNA.Haemonchus: A genus of parasitic nematode worms which infest the duodenum and stomach of domestic and wild herbivores, which ingest it with the grasses (POACEAE) they eat. Infestation of man is accidental.Models, Chemical: Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.Leishmania mexicana: A parasitic hemoflagellate of the subgenus Leishmania leishmania that infects man and animals including rodents. The Leishmania mexicana complex causes both cutaneous (LEISHMANIASIS, CUTANEOUS) and diffuse cutaneous leishmaniasis (LEISHMANIASIS, DIFFUSE CUTANEOUS) and includes the subspecies amazonensis, garnhami, mexicana, pifanoi, and venezuelensis. L. m. mexicana causes chiclero ulcer, a form of cutaneous leishmaniasis (LEISHMANIASIS, CUTANEOUS) in the New World. The sandfly, Lutzomyia, appears to be the vector.Iodoacetamide: An alkylating sulfhydryl reagent. Its actions are similar to those of iodoacetate.Dithiothreitol: A reagent commonly used in biochemical studies as a protective agent to prevent the oxidation of SH (thiol) groups and for reducing disulphides to dithiols.Dose-Response Relationship, Drug: The relationship between the dose of an administered drug and the response of the organism to the drug.Arthropod Proteins: Proteins synthesized by organisms belonging to the phylum ARTHROPODA. Included in this heading are proteins from the subdivisions ARACHNIDA; CRUSTACEA; and HORSESHOE CRABS. Note that a separate heading for INSECT PROTEINS is listed under this heading.Dimerization: The process by which two molecules of the same chemical composition form a condensation product or polymer.Chymases: A family of neutral serine proteases with CHYMOTRYPSIN-like activity. Chymases are primarily found in the SECRETORY GRANULES of MAST CELLS and are released during mast cell degranulation.Proteasome Endopeptidase Complex: A large multisubunit complex that plays an important role in the degradation of most of the cytosolic and nuclear proteins in eukaryotic cells. It contains a 700-kDa catalytic sub-complex and two 700-kDa regulatory sub-complexes. The complex digests ubiquitinated proteins and protein activated via ornithine decarboxylase antizyme.Adenosine Triphosphate: An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Phosphorylation: The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.Trypanosoma cruzi: The agent of South American trypanosomiasis or CHAGAS DISEASE. Its vertebrate hosts are man and various domestic and wild animals. Insects of several species are vectors.Gene Expression: The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.Entamoeba histolytica: A species of parasitic protozoa causing ENTAMOEBIASIS and amebic dysentery (DYSENTERY, AMEBIC). Characteristics include a single nucleus containing a small central karyosome and peripheral chromatin that is finely and regularly beaded.HIV-1: The type species of LENTIVIRUS and the etiologic agent of AIDS. It is characterized by its cytopathic effect and affinity for the T4-lymphocyte.Subtilisin: A serine endopeptidase isolated from Bacillus subtilis. It hydrolyzes proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. It also hydrolyzes peptide amides. (From Enzyme Nomenclature, 1992) EC 3.4.21.62.Saccharomyces cerevisiae: A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.Ficain: A sulfhydryl proteinase with cysteine at the active site from ficus latex. Preferential cleavage is at tyrosine and phenylalanine residues. EC 3.4.22.3.Phenylmethylsulfonyl Fluoride: An enzyme inhibitor that inactivates IRC-50 arvin, subtilisin, and the fatty acid synthetase complex.Saquinavir: An HIV protease inhibitor which acts as an analog of an HIV protease cleavage site. It is a highly specific inhibitor of HIV-1 and HIV-2 proteases, and also inhibits CYTOCHROME P-450 CYP3A.Porphyromonas gingivalis: A species of gram-negative, anaerobic, rod-shaped bacteria originally classified within the BACTEROIDES genus. This bacterium produces a cell-bound, oxygen-sensitive collagenase and is isolated from the human mouth.Virulence: The degree of pathogenicity within a group or species of microorganisms or viruses as indicated by case fatality rates and/or the ability of the organism to invade the tissues of the host. The pathogenic capacity of an organism is determined by its VIRULENCE FACTORS.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).Haemonchiasis: Infection with nematodes of the genus HAEMONCHUS, characterized by digestive abnormalities and anemia similar to that from hookworm infestation.Protein Folding: Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.Chromatography, Affinity: A chromatographic technique that utilizes the ability of biological molecules to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Mutagenesis: Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.Histidine: An essential amino acid that is required for the production of HISTAMINE.Ubiquitin: A highly conserved 76-amino acid peptide universally found in eukaryotic cells that functions as a marker for intracellular PROTEIN TRANSPORT and degradation. Ubiquitin becomes activated through a series of complicated steps and forms an isopeptide bond to lysine residues of specific proteins within the cell. These "ubiquitinated" proteins can be recognized and degraded by proteosomes or be transported to specific compartments within the cell.DiazomethaneChromatography, Ion Exchange: Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins.Calcium: A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.Indinavir: A potent and specific HIV protease inhibitor that appears to have good oral bioavailability.Isoenzymes: Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.Ubiquitins: A family of proteins that are structurally-related to Ubiquitin. Ubiquitins and ubiquitin-like proteins participate in diverse cellular functions, such as protein degradation and HEAT-SHOCK RESPONSE, by conjugation to other proteins.Vacuoles: Any spaces or cavities within a cell. They may function in digestion, storage, secretion, or excretion.Iodoacetic Acid: A derivative of ACETIC ACID that contains one IODINE atom attached to its methyl group.DNA: A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).Protein Transport: The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.Exotoxins: Toxins produced, especially by bacterial or fungal cells, and released into the culture medium or environment.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.Plasmodium falciparum: A species of protozoa that is the causal agent of falciparum malaria (MALARIA, FALCIPARUM). It is most prevalent in the tropics and subtropics.Periplasmic Proteins: Proteins found in the PERIPLASM of organisms with cell walls.Sequence Analysis, DNA: A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.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.Caspase 7: A short pro-domain caspase that plays an effector role in APOPTOSIS. It is activated by INITIATOR CASPASES such as CASPASE 3 and CASPASE 10. Several isoforms of this protein exist due to multiple alternative splicing of its MESSENGER RNA.Antigens, Dermatophagoides: Antigens from the house dust mites (DERMATOPHAGOIDES), mainly D. farinae and D. pteronyssinus. They are proteins, found in mite feces or mite extracts, that can cause ASTHMA and other allergic diseases such as perennial rhinitis (RHINITIS, ALLERGIC, PERENNIAL) and atopic dermatitis (DERMATITIS, ATOPIC). More than 11 groups of Dermatophagoides ALLERGENS have been defined. Group I allergens, such as Der f I and Der p I from the above two species, are among the strongest mite immunogens in humans.Proteinase Inhibitory Proteins, Secretory: Peptides and proteins found in BODILY SECRETIONS and BODY FLUIDS that are PROTEASE INHIBITORS. They play a role in INFLAMMATION, tissue repair and innate immunity (IMMUNITY, INNATE) by inhibiting endogenous proteinases such as those produced by LEUKOCYTES and exogenous proteases such as those produced by invading microorganisms.Sulfhydryl Reagents: Chemical agents that react with SH groups. This is a chemically diverse group that is used for a variety of purposes. Among these are enzyme inhibition, enzyme reactivation or protection, and labelling.Cathepsin H: An ubiquitously-expressed lysosomal cysteine protease that is involved in protein processing. The enzyme has both endopeptidase and aminopeptidase activities.Zinc: A metallic element of atomic number 30 and atomic weight 65.38. It is a necessary trace element in the diet, forming an essential part of many enzymes, and playing an important role in protein synthesis and in cell division. Zinc deficiency is associated with ANEMIA, short stature, HYPOGONADISM, impaired WOUND HEALING, and geophagia. It is known by the symbol Zn.Caspase 10: A long pro-domain caspase that contains a death effector domain in its pro-domain region. Activation of this enzyme can occur via the interaction of its N-terminal death effector domain with DEATH DOMAIN RECEPTOR SIGNALING ADAPTOR PROTEINS. Caspase 10 plays a role in APOPTOSIS by cleaving and activating EFFECTOR CASPASES. Several isoforms of this protein exist due to multiple alternative splicing of its MESSENGER RNA.Secretory Leukocyte Peptidase Inhibitor: A proteinase inhibitor found in various BODILY SECRETIONS that coat mucosal surfaces such as SEMINAL PLASMA; CERVICAL MUCUS; and bronchial secretions. It plays a role in protecting epithelial tissues from LEUKOCYTE-derived serine proteases such as NEUTROPHIL ELASTASE.Mitochondria: Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)Tumor Cells, Cultured: Cells grown in vitro from neoplastic tissue. If they can be established as a TUMOR CELL LINE, they can be propagated in cell culture indefinitely.Cytosol: Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.Carbamates: Derivatives of carbamic acid, H2NC(=O)OH. Included under this heading are N-substituted and O-substituted carbamic acids. In general carbamate esters are referred to as urethanes, and polymers that include repeating units of carbamate are referred to as POLYURETHANES. Note however that polyurethanes are derived from the polymerization of ISOCYANATES and the singular term URETHANE refers to the ethyl ester of carbamic acid.
USP10
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JCI -
Caspases: pharmacological manipulation
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What is Caspase Activity? (with pictures)CathepsinCathepsinsInhibitor cystatinProteinasesProteolyticRegulationSpecificActivitySpecificityCaspasesProteinsCleavage siteCathepsinsInhibitionSuperfamilyHomologousDegradationMetalloproteasesPeptidaseIntracellularSpecific cysteine proteaseLysosomal cysteine proteaseAmino acidFluorescently quenched activity-based probesThiol proteasesEndopeptidaseNucleophileApoptotic protease activaProteolysisCalpainsMajor cysteineResidueActive site cysteineCathepsin protease familyAssaysDifferent proteasesPrecursorPlasmodiumInhibitor E-64Serine protease activityAspartyl1999Ubiquitin ProteaseActivationBiologicalTherapeuticCruzainCystatins
Cathepsin1
- Legumain, cathepsin B and L were analyzed in cell lysates by immunoblotting and their enzymatic activities were analyzed by peptide substrates. (uio.no)
Cathepsins1
- High activity of cysteine proteases such as legumain and the cathepsins have been shown to facilitate growth and invasion of a variety of tumor types. (uio.no)
Inhibitor cystatin1
- In breast cancer, several recent studies have indicated that loss of the cysteine protease inhibitor cystatin E/M leads to increased growth and metastasis. (uio.no)
Proteinases4
- The aim of this study was to characterize the specific interactions occurring between E. histolytica secreted cysteine proteinases and colonic mucin as a model to examine the initial events of invasive amebiasis. (asm.org)
- Cysteine proteinases degraded mucin in a time- and dose-dependent manner. (asm.org)
- These results are the first to show that E. histolytica cysteine proteinases alter the protective function of the mucous barrier by disrupting the structure of the MUC2 polymer. (asm.org)
- This phenomenon may be a result of the concerted actions of a battery of cysteine proteinases (CPs) released by the parasite into its microenvironment ( 17 ). (asm.org)
Proteolytic1
- Mechanistically, the parasite achieves this via proteolytic degradation of the terminal cysteine-rich domains. (asm.org)
Regulation1
- Although cystatin E/M is normally expressed in the skin, its role in cysteine protease regulation and progression of malignant melanoma has not been studied. (uio.no)
Specific1
- Mucinase activity was eliminated by the specific cysteine protease inhibitor trans -epoxysuccinyl- l -leucylamido-(4-guanidino)butane and was independent of glycosidase activity. (asm.org)
Activity1
Specificity29
- The specificity of staphopain A, B and C substrate-binding subsites was mapped using different synthetic substrate libraries, inhibitor libraries and a protein substrate combinatorial library. (uni-bielefeld.de)
- However, we show that at the same time the overall specificity of staphopains is relaxed, insofar as multiple substrates that diverge from the sequences described above are also efficiently hydrolyzed. (uni-bielefeld.de)
- 2012). Substrate specificity of Staphylococcus aureus cysteine proteases - Staphopains A, B and C. Biochimie , 94 (2), 318-327. (uni-bielefeld.de)
- Substrate specificity of Staphylococcus aureus cysteine proteases - Staphopains A, B and C". Biochimie 94.2 (2012): 318-327. (uni-bielefeld.de)
- We investigated the substrate specificity of the cruzipain 2 isoform using internally quenched fluorogenic substrates. (unifesp.br)
- Our study indicates that cruzipain 2 has a more restricted specificity than cruzain, suggesting that these isoforms might act on distinct natural substrates. (unifesp.br)
- Positional scanning substrate combinatorial library (PS-SCL) approach to define caspase substrate specificity. (semanticscholar.org)
- Knowledge of the substrate specificity of a protease can dramatically improve our ability to predict its target protein substrates, but this information must be utilized in an effective manner in order to efficiently identify protein substrates by in silico approaches. (plos.org)
- PROSPER utilizes established specificity information for these proteases (derived from the MEROPS database) with a machine learning approach to predict protease cleavage sites by using different, but complementary sequence and structure characteristics. (plos.org)
- Thus, for proteases with known amino acid specificity, PROSPER provides a convenient, pre-prepared tool for use in identifying protein substrates for the enzymes. (plos.org)
- The substrate specificity of clan CA enzymes is primarily controlled by the S2 subsite. (creativebiomart.net)
- Papain has a very broad specificity compared to other clan CA proteases. (creativebiomart.net)
- The substrate specificity of cathepsin B is similar to papain family and the primary determinant of specificity is the S2 subsite. (creativebiomart.net)
- While known DUBs can be grouped into six families, the authors here present biochemical and structural evidence for a seventh DUB family, defining determinants of substrate specificity for two representative enzymes. (nature.com)
- This Review gives an overview of caspases and their classification, structure, and substrate specificity. (jci.org)
- Molecular model of the specificity pocket of the hepatitis C virus protease: implications for substrate recognition. (pnas.org)
- We have built a model of the specificity pocket of the protease of hepatitis C virus on the basis of the known structures of trypsin-like serine proteases and of the conservation pattern of the protease sequences among various hepatitis C strains. (pnas.org)
- Proteases regulate numerous biological processes with a degree of specificity often dictated by the amino acid sequence of the substrate cleavage site. (upenn.edu)
- This is the first comprehensive study to report the substrate specificity of rhodesain, a papain-like cysteine protease expressed by Trypanasoma brucei rhodesiense , a parasitic protozoa responsible for causing sleeping sickness. (upenn.edu)
- Solution phase microarrays facilitate protease/substrate specificity profiling in a rapid manner with minimal peptide library or enzyme usage. (upenn.edu)
- Thus, the specificity of RPS5 can be changed simply by altering the protease cleavage sequence within PBS1. (apsnet.org)
- A large number of E2 enzymes provide substrate specificity either alone or along with the E3 enzymes ( H ochstrasser 1996 ). (genetics.org)
- Lima CA, Watanabe, ROM, Barros NMT , Carmona AK, Masuda A, Vaz Junior IS, Tanaka A. Boophilus microplus cathepsin L-like (BmCL1) cysteine protease: specificity study using a peptide phage display library (2011) Veterinary Parasitology . (mcgill.ca)
- Identification and Characterization of IgdE, a Novel IgG-degrading Protease of Streptococcus suis with Unique Specificity for Porcine IgG. (diva-portal.org)
- This enzyme, designated IgdE for immunoglobulin G-degrading enzyme of S. suis, is a cysteine protease distinct from previous characterized streptococcal immunoglobulin degrading proteases of the IdeS family and mediates efficient cleavage of the hinge region of porcine IgG with a high degree of specificity. (diva-portal.org)
- The current study investigated the specificity of IV-2 by examining its interaction with tubulin, a protein in which cysteine oxidation causes loss of polymerization competence. (aacrjournals.org)
- Independent amino acid residues in the S2 pocket of falcipain-3 determine its specificity for P2 residues in substrates. (ccmb.res.in)
- Critical role of amino acid 23 in mediating activity and specificity of vinckepain-2, a papain-family cysteine protease of rodent malaria parasites. (ccmb.res.in)
- Their equilibrium is shifted towards the monomer upon Ca 2+ -removal and towards the dimer upon Ca 2+ -addition, which is accompanied by a change in substrate specificity from a general protease (monomer) to the specific cleavage of the PTS2 (dimer). (springer.com)
Caspases15
- Like caspases, cathepsins have a wide range of cellular substrates. (hindawi.com)
- Caspases, a family of cysteine proteases, play a central role in apoptosis. (jci.org)
- Subsequently, active caspases specifically process various substrates that are implicated in apoptosis and inflammation. (jci.org)
- Among cysteine proteases, caspase-3, caspases-8 and caspase-9 play an important role in controlling apoptosis. (frontiersin.org)
- Caspases belong to a particular class of proteases, known as cysteine proteases. (wisegeek.com)
- Caspases are members of the cysteine-aspartic acid protease (caspase) family. (abcam.com)
- Caspases are cysteine proteases, expressed as inactive precursors, that mediate apoptosis by proteolysis of specific substrates. (fishersci.com)
- The proteins that execute the apoptotic programme are a group of proteases termed caspases (cysteine‐dependent aspartate‐specific protease). (els.net)
- Caspases proteolytically cleave a host of cellular substrates at aspartate residues, which may render them either functionally inactive or confer novel activities that help to promote cellular demise. (els.net)
- Substrates targeted by caspases during the apoptotic programme include proteins involved in maintaining various aspects of cytoskeletal and organelle architecture as well as proteins that function in signalling networks critical for cell function. (els.net)
- Apoptotic caspases are cysteine proteases that become activated in response to diverse extracellular and intracellular stimuli and subsequently carry out the cell death programme by systematically cleaving intracellular proteins. (els.net)
- In all cases, apoptosis is mediated by caspases, although it is unclear how these diverse apoptotic stimuli cause protease activation. (rupress.org)
- Caspases lead to the proteolysis of a number of cellular substrates, a process which finally results in the apoptotic collapse of the cell. (rupress.org)
- Further downstream, caspase-8 triggers the proteolytic activation of other caspases and cleavage of cellular substrates. (rupress.org)
- FITC-VAD-FMK is a mammalian caspase reporter that mimics the required Asp cleavage site found in natural substrates of mammalian caspases. (sciencemag.org)
Proteins10
- Based on these results, we suggest that CM and TCEs of N. fowleri degrade iron-binding proteins by employing cysteine proteases, which enables the parasite to obtain iron to survive while invading the central nervous system. (hindawi.com)
- However, it is known that, during invasion, N. fowleri is able to release proteolytic proteins including naegleriapores A and B, phospholipases, glycosidases, neuraminidase, elastase, and other proteases, such as cathepsin B and mucinases [ 8 - 14 ]. (hindawi.com)
- Proteases cleave proteins into smaller fragments by catalyzing peptide bonds hydrolysis. (frontiersin.org)
- Proteases are usually synthesized as large precursor proteins called zymogens , such as the serine protease precursors trypsinogen and chymotrypsinogen , and the aspartic protease precursor pepsinogen . (wikipedia.org)
- Using fractionation experiments followed by immunoblot detection, the protease was found to be associated with the S-layer proteins, mostly as a nonmature species. (asm.org)
- Proteases thus have central roles in "life and death" processes, such as neural, endocrine and cardiovascular signaling, digestion, degradation of misfolded or unwanted proteins, immunity, cell division and apoptosis. (plos.org)
- The preservation of proteins from protease and phosphatase activities after cell or tissue lysis is essential for many research applications. (thermofisher.com)
- Our formulations protected proteins from protease and phosphatase degradation and performed favorably compared to other commercial preparations. (thermofisher.com)
- Previous work has shown that, just prior to egress, an essential, subtilisin-like parasite protease called PfSUB1 is discharged into the PV lumen, where it directly cleaves a number of important merozoite surface and PV proteins. (asm.org)
- Giardia orthologues of mammalian lysosomal proteases function within an ER-like tubulovesicular compartment, which itself can dynamically communicate with clathrin-containing vacuoles at the periphery of the cell to receive endocytosed proteins. (pubmedcentralcanada.ca)
Cleavage site2
- Proteases are divided into two broad categories based on cleavage site and then subdivided based on the active site and pH preferences. (thermofisher.com)
- We hypothesize that we will be able to engineer resistance to SMV by introducing a cleavage site recognized by the SMV protease into a soybean PBS1 ortholog. (apsnet.org)
Cathepsins7
- Papain and cathepsins belong to the most abundant family of the cysteine proteases. (frontiersin.org)
- In mammals, a main group of cysteine proteases is known as lysosomal cathepsins ( McGrath, 1999 ). (frontiersin.org)
- Cathepsins A and G are serine proteases, meaning that their active site contains a vital serine. (hindawi.com)
- Cathepsins D and E are aspartic proteases. (hindawi.com)
- Cysteine cathepsins are the most stable and active at an acidic pH. (hindawi.com)
- Prior reports have shown that several proteases (e.g., cathepsins and matrix metalloproteinases) are up-regulated in many cancer types ( 6 - 8 ), and potentially, these tumor-associated proteases could act as activators of the proposed PM-PDT agent. (aacrjournals.org)
- Arampatzidou M, Rehders M, Dauth S, Yu DMT, Tedelind S, Brix K. Imaging of protease functions-current guide to spotting cysteine cathepsins in classical and novel scenes of action in mammalian epithelial cells and tissues. (springer.com)
Inhibition7
- Inhibition assays revealed that cysteine proteases were involved in this process. (hindawi.com)
- We compared protease inhibition by the Pierce Tablet formulations (Table 1) to other commercial formulations. (thermofisher.com)
- Cysteine protease inhibition was assayed with carbobenzyloxy-PHE-ARG-7-aminomethylcoumarin substrate. (ovid.com)
- Finally, my experience as a biochemist and enzymologist allows me to investigate the role of proteases in bone biology and in tumor-associated processes to understand their specificities and inhibition mechanisms. (mcgill.ca)
- Inhibition of the IgG cleaving activity by iodoacetamide and Z-LVG-CHN2 indicated that a cysteine protease is involved. (diva-portal.org)
- We also demonstrate that cysteine proteases are involved in the infectious process, and that cathepsin B treatment of viral particles was shown to overcome the block of infection observed in the presence of furin inhibition. (biomedcentral.com)
- Independent intramolecular mediators of folding, activity, and inhibition for the Plasmodium falciparum cysteine protease falcipain-2. (ccmb.res.in)
Superfamily5
- For superfamilies , P = superfamily containing a mixture of nucleophile class families, C = purely cysteine proteases. (wikipedia.org)
- Within each superfamily, families are designated by their catalytic nucleophile (C = cysteine proteases). (wikipedia.org)
- In this database, proteases are classified firstly by 'clan' ( superfamily ) based on structure, mechanism and catalytic residue order (e.g. the PA clan where P indicates a mixture of nucleophile families). (wikipedia.org)
- Sequence analysis of the BamHI F fragment of the genome of Bombyx mori nuclear polyhedrosis virus (BmNPV) revealed an open reading frame whose deduced amino acid sequence had homology to those of cysteine proteases of the papain superfamily. (nih.gov)
- The product of this gene is a member of the OTU superfamily of predicted cysteine proteases. (thermofisher.com)
Homologous4
- In order to determine the activity and function of the putative cysteine protease, a BmNPV mutant (BmCysPD) was constructed by homologous recombination of the protease gene with a beta-galactosidase gene cassette. (nih.gov)
- 15 16 Caspase 3 is a cysteine protease homologous with ICE. (bloodjournal.org)
- As more protease structures were solved by X-ray crystallography in the 1970s and 80s, homologous (such as TEV protease ) and analogous (such as papain) triads were found. (wikipedia.org)
- However, the technologies they used do not provide reliable evidence that fungal cells die via a protease signaling cascade thwarted by a fungal caspase inhibitor homologous to human survivin. (sciencemag.org)
Degradation9
- The ability of macrophages and other cells to mobilize elastolytic cysteine proteases to their surfaces under specialized conditions may also lead to accelerated collagen and elastin degradation at sites of inflammation in diseases such as atherosclerosis and emphysema . (wikipedia.org)
- These hydrolases, which include the cathepsin family of proteases, are responsible for degradation, recycling, and disposal of cellular macromolecules [ 1 ]. (hindawi.com)
- Endocytic proteases play a key role in two different steps of MHC class II-restricted antigen presentation: invariant chain cleavage and antigen degradation. (rupress.org)
- Mechanistically, the parasite achieves this via proteolytic degradation of the terminal cysteine-rich domains. (asm.org)
- This is the first report of (i) a virus-encoded protease with activity on general substrates and (ii) evidence that a virus-encoded protease may play a role in degradation of infected larvae to facilitate horizontal transmission of the virus. (nih.gov)
- Positive regulation occurs when polyubiquitin chains are cleaved to produce free ubiquitin groups that are then available for attachment to new substrates targeted for degradation. (genetics.org)
- A negative effect on proteolysis could occur if substrates were diverted from proteasomal degradation by the reversal of ubiquitination. (genetics.org)
- Proteases of multiple catalytic classes appear to contribute to hemoglobin degradation. (asmscience.org)
- Proteases and Hemoglobin Degradation, p 311-326. (asmscience.org)
Metalloproteases1
- Proteases are classified according to their catalytic site, and distributed into four major classes: cysteine proteases, serine proteases, aspartic proteases, and metalloproteases. (frontiersin.org)
Peptidase2
- Crystal structure of the cysteine peptidase papain in complex with its covalent inhibitor E-64. (wikipedia.org)
- Caspase 9 (ICE-like apoptotic protease 6, ICE LAP6, apoptotic protease Mch6, apoptotic protease activating factor 3, Apaf3) is a member of the peptidase family C14 that contains a CARD domain. (fishersci.com)
Intracellular9
- Activation occurs once the protease is delivered to a specific intracellular compartment (e.g. lysosome ) or extracellular environment (e.g. stomach ). (wikipedia.org)
- Following each round of intracellular growth, the PV membrane (PVM) and host cell membrane rupture to release infectious merozoites in a protease-dependent process called egress. (asm.org)
- However, comprehensive studies in changes of TM intracellular proteases have not been performed. (molvis.org)
- The changes in the intracellular protease proteome can be identified using high-throughput proteomic mass spectrometric approaches. (molvis.org)
- Here, we present a simple and efficient method that allows better capturing of TM intracellular proteases. (molvis.org)
- This method will enhance our understanding of TM intracellular protease changes that occur as part of glaucoma pathophysiology. (molvis.org)
- Here we report the subcellular localization of an intracellular serine protease of 68 kDa in axenic promastigotes of Leishmania (Leishmania) amazonensis , using subcellular fractionation, enzymatic assays, immunoblotting, and immunocytochemistry. (scielo.br)
- Our findings indicate that the internal location of this serine protease in L. amazonensis is mainly restricted to the membranes of intracellular compartments resembling endocytic/exocytic elements. (scielo.br)
- We present data that suggest HPV16 infection is in part mediated by cysteine proteases, and that NH 4 Cl blocks the intracellular trafficking of infectious viral particles. (biomedcentral.com)
Specific cysteine protease1
- Mucinase activity was eliminated by the specific cysteine protease inhibitor trans -epoxysuccinyl- l -leucylamido-(4-guanidino)butane and was independent of glycosidase activity. (asm.org)
Lysosomal cysteine protease2
- the lysosomal cysteine protease designated as cruzipain or cruzain, is the archetype of a multigene family of related isoforms. (unifesp.br)
- Cathepsin B is a lysosomal cysteine protease with both endopeptidase and dipeptidyl carboxypeptidase activities. (creativebiomart.net)
Amino acid3
- Some of the cysteine proteases use an extra amino acid to provide additional stabilization via hydrogen bonds, thus forming a catalytic triad. (creativebiomart.net)
- Cysteine proteases are defined by the latter grouping and all have the amino acid cysteine in their active site. (wisegeek.com)
- The nucleophile is most commonly a serine or cysteine amino acid, but occasionally threonine or even selenocysteine . (wikipedia.org)
Fluorescently quenched activity-based probes2
- Dynamic imaging of protease activity with fluorescently quenched activity-based probes. (nih.gov)
- Blum G, von Degenfeld G, Merchant MJ, Blau HM, Bogyo M. Noninvasive optical imaging of cysteine protease activity using fluorescently quenched activity-based probes. (springer.com)
Thiol proteases1
- Therefore, they are also sometimes referred to as thiol proteases. (wikipedia.org)
Endopeptidase1
- Moreover, an anti-IdeS antibody directed against the IgG endopeptidase IdeS of S. pyogenes showed cross reactivity with the putative IgG protease of S. phocae subsp. (diva-portal.org)
Nucleophile2
- One way to make a nucleophile is by a catalytic triad , where a histidine residue is used to activate serine , cysteine , or threonine as a nucleophile. (wikipedia.org)
- Cysteine proteases have a cysteine residue in their active side and therefore employ the sulfhydryl group of the side chain of a cysteine residue as the catalytic nucleophile. (creativebiomart.net)
Apoptotic protease activa1
- The other pathway is controlled by the release of cytochrome c from mitochondria and the subsequent ATP-dependent activation of the death regulator apoptotic protease-activating factor 1 (Apaf-1). (rupress.org)
Proteolysis1
- Calpain-9 (CAPN9) belongs to the calpain family, which consists of a group of Ca2+ dependent cysteine proteases that regulate functions of substrates by proteolysis [ PMID: 12843408 , PMID: 24085852 ]. (ebi.ac.uk)
Calpains2
- Calpains are a unique family of cysteine proteases since they require calcium to become activated. (creativebiomart.net)
- A BODIPY Fluorescent Microplate Assay for Measuring Activity of Calpains and Other Proteases," Analytical Biochemistry, 279, (2000), pp. 170-178. (patentgenius.com)
Major cysteine1
- Rhodesain is the major cysteine protease of T. brucei rhodesiense, the causative agent of African sleeping sickness. (creativebiomart.net)
Residue3
- In this step, a fragment of the substrate is released with an amine terminus, the histidine residue in the protease is restored to its deprotonated form, and a thioester intermediate linking the new carboxy-terminus of the substrate to the cysteine thiol is formed. (wikipedia.org)
- A catalytic dyad is formed with the imidazole side chain of histidine residue and the sulfhydryl group of the active site cysteine. (creativebiomart.net)
- The model allowed us to predict that the substrate of this protease should have a cysteine residue in position P1. (pnas.org)
Active site cysteine1
- The FMK moiety results in tight binding to the caspase active-site cysteine, potently inhibiting caspase activity. (sciencemag.org)
Cathepsin protease family1
- Combined deletion of cathepsin protease family members reveals compensatory mechanisms in cancer. (springer.com)
Assays3
- Zymography assays were performed for each substrate under physiological conditions (pH 7 at 37°C) employing conditioned medium (CM) and total crude extracts (TCEs) of N. fowleri . (hindawi.com)
- Protease assays are somewhat confounding in that general protease substrates are not a true assessment of the contribution of each individual inhibitor activity. (thermofisher.com)
- Biochemical assays indicated that the oxidative properties of IV-2 are not limited to thioredoxin and tubulin, as cysteine-dependent proteases were also inhibited. (aacrjournals.org)
Different proteases1
- To address this problem, we present PROSPER, an integrated feature-based server for in silico identification of protease substrates and their cleavage sites for twenty-four different proteases. (plos.org)
Precursor1
- The putative cysteine protease sequence (BmNPV-CP) was 323 amino acids long and showed 35% identity to a cysteine proteinase precursor from Trypanosoma brucei. (nih.gov)
Plasmodium9
- The most notorious serine proteases are found in species of Plasmodium . (scielo.br)
- The Ionic and Hydrophobic Interactions Are Required for the Auto Activation of Cysteine Proteases of Plasmodium falciparum. (ccmb.res.in)
- A chimeric cysteine protease of Plasmodium berghei engineered to resemble the Plasmodium falciparum protease falcipain-2. (ccmb.res.in)
- Falcipain cysteine proteases require bipartite motifs for trafficking to the Plasmodium falciparum food vacuole. (ccmb.res.in)
- Gene disruptions demonstrate independent roles for the four falcipain cysteine proteases of Plasmodium falciparum. (ccmb.res.in)
- The Plasmodium falciparum cysteine protease falcipain-2 captures its substrate, hemoglobin, via a unique motif. (ccmb.res.in)
- Plasmodium falciparum cysteine protease falcipain-1 is not essential in erythrocytic stage malaria parasites. (ccmb.res.in)
- Folding of the Plasmodium falciparum cysteine protease falcipain-2 is mediated by a chaperone-like peptide and not the prodomain. (ccmb.res.in)
- Systematic optimization of expression and refolding of the Plasmodium falciparum cysteine protease falcipain-2. (ccmb.res.in)
Inhibitor E-641
- The cysteine protease inhibitor E-64 [trans-epoxysuccinylleucylamido-(4-guanidino)butane] inhibited wild-type virus-expressed protease activity. (nih.gov)
Serine protease activity1
- 80% of serine protease activity. (thermofisher.com)
Aspartyl1
- In contrast, an aspartyl protease inhibitor suppressed the presentation of OVA, an effect attributed to the blockade of cathepsin E ( 10 ). (jimmunol.org)
19992
- Dieter Bromme, "Cysteine Proteases as Therapeutic Targets," Drug News Perspect 12(2) Mar. 1999, pp. 73-82. (patentgenius.com)
- Synthesis of Two Novel Cyclic Biphenyl Ether Analogs of an Inhibitor of HCV NS3 Protease," Synlett (1999), pp. 1000-1002. (patentgenius.com)
Ubiquitin Protease1
- It interacts with another ubiquitin protease and an E3 ubiquitin ligase that inhibits cytokine gene transcription in the immune system. (thermofisher.com)
Activation2
- Furthermore, the delivery of active proteases to the phagosome is significantly reduced after the activation of DCs with lipopolysaccharide. (rupress.org)
- In a feline right ventricular (RV) PO (RVPO) model, calpeptin (0.6 mg/kg, i.v.) blocks the activation of calpain and caspase-3, cleavage of their substrates, and cardiomyocyte programmed cell death. (selleckchem.com)
Biological3
- Proteases represent ∼2% of all gene products in humans (about 500-600 proteases), reflecting their diverse functional roles in many biological processes. (plos.org)
- Cysteine cathepsin S processes leptin, inactivating its biological activity. (mcgill.ca)
- Proteases are directly or indirectly involved in virtually every biological function or dysfunction. (ucsf.edu)
Therapeutic1
- Expansion of these inhibitor concepts can be envisioned for the many other cysteine proteases implicated for therapeutic intervention. (rcsb.org)
Cruzain1
- Cruzain is the only parasitic cysteine protease with a crystal structure. (creativebiomart.net)
Cystatins1
- The mode of chagasin binding is generally similar, albeit distinctly different in detail, when compared to those displayed by cystatins and the cysteine protease inhibitory p41 fragment of the invariant chain. (lu.se)
