Cysteine Proteinase Inhibitors: Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.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.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.Salivary Cystatins: A group of closely-related cystatins found in SALIVA.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.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.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.Protease Inhibitors: Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).Cathepsin H: An ubiquitously-expressed lysosomal cysteine protease that is involved in protein processing. The enzyme has both endopeptidase and aminopeptidase activities.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 L: A ubiquitously-expressed cysteine protease that plays an enzymatic role in POST-TRANSLATIONAL PROTEIN PROCESSING of proteins within SECRETORY GRANULES.Cysteine: A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.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.Serine Proteinase Inhibitors: Exogenous or endogenous compounds which inhibit SERINE ENDOPEPTIDASES.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.Kininogens: Endogenous peptides present in most body fluids. Certain enzymes convert them to active KININS which are involved in inflammation, blood clotting, complement reactions, etc. Kininogens belong to the cystatin superfamily. They are cysteine proteinase inhibitors. HIGH-MOLECULAR-WEIGHT KININOGEN; (HMWK); is split by plasma kallikrein to produce BRADYKININ. LOW-MOLECULAR-WEIGHT KININOGEN; (LMWK); is split by tissue kallikrein to produce KALLIDIN.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.Cystatin M: A cystatin subtype that has a diverse tissue distribution, target specificity, and functions as an endogenous inhibitor of lysosomal cysteine proteases.Endopeptidases: A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.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.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.alpha 1-Antitrypsin: Plasma glycoprotein member of the serpin superfamily which inhibits TRYPSIN; NEUTROPHIL ELASTASE; and other PROTEOLYTIC ENZYMES.Salivary Proteins and Peptides: Proteins and peptides found in SALIVA and the SALIVARY GLANDS. Some salivary proteins such as ALPHA-AMYLASES are enzymes, but their composition varies in different individuals.Helianthus: A genus herbs of the Asteraceae family. The SEEDS yield oil and are used as food and animal feed; the roots of Helianthus tuberosus (Jerusalem artichoke) are edible.Coix: A plant genus of the family POACEAE. The seed is used in folk medicine (DRUGS, CHINESE HERBAL).Cysteine Proteases: A subclass of peptide hydrolases that depend on a CYSTEINE residue for their activity.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.Trypsin Inhibitors: Serine proteinase inhibitors which inhibit trypsin. They may be endogenous or exogenous compounds.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.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.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.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.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.Kinetics: The rate dynamics in chemical or physical systems.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.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.DiazomethaneIsoelectric Focusing: Electrophoresis in which a pH gradient is established in a gel medium and proteins migrate until they reach the site (or focus) at which the pH is equal to their isoelectric point.Serine Endopeptidases: Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.Seeds: The encapsulated embryos of flowering plants. They are used as is or for animal feed because of the high content of concentrated nutrients like starches, proteins, and fats. Rapeseed, cottonseed, and sunflower seed are also produced for the oils (fats) they yield.Molecular Weight: The sum of the weight of all the atoms in a molecule.Recombinant Proteins: Proteins prepared by recombinant DNA technology.alpha-Macroglobulins: Glycoproteins with a molecular weight of approximately 620,000 to 680,000. Precipitation by electrophoresis is in the alpha region. They include alpha 1-macroglobulins and alpha 2-macroglobulins. These proteins exhibit trypsin-, chymotrypsin-, thrombin-, and plasmin-binding activity and function as hormonal transporters.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.Leucine: An essential branched-chain amino acid important for hemoglobin formation.alpha 1-Antichymotrypsin: Glycoprotein found in alpha(1)-globulin region in human serum. It inhibits chymotrypsin-like proteinases in vivo and has cytotoxic killer-cell activity in vitro. The protein also has a role as an acute-phase protein and is active in the control of immunologic and inflammatory processes, and as a tumor marker. It is a member of the serpin superfamily.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.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.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.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.Hemagglutinins: Agents that cause agglutination of red blood cells. They include antibodies, blood group antigens, lectins, autoimmune factors, bacterial, viral, or parasitic blood agglutinins, etc.Saliva: The clear, viscous fluid secreted by the SALIVARY GLANDS and mucous glands of the mouth. It contains MUCINS, water, organic salts, and ptylin.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Chymopapain: A cysteine endopeptidase isolated from papaya latex. Preferential cleavage at glutamic and aspartic acid residues. EC 3.4.22.6.Trypsin Inhibitor, Bowman-Birk Soybean: A low-molecular-weight protein (minimum molecular weight 8000) which has the ability to inhibit trypsin as well as chymotrypsin at independent binding sites. It is characterized by a high cystine content and the absence of glycine.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.Pepstatins: N-acylated oligopeptides isolated from culture filtrates of Actinomycetes, which act specifically to inhibit acid proteases such as pepsin and renin.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.Cathepsin G: A serine protease found in the azurophil granules of NEUTROPHILS. It has an enzyme specificity similar to that of chymotrypsin C.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).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)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.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.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.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.Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.Adhesins, Bacterial: Cell-surface components or appendages of bacteria that facilitate adhesion (BACTERIAL ADHESION) to other cells or to inanimate surfaces. Most fimbriae (FIMBRIAE, BACTERIAL) of gram-negative bacteria function as adhesins, but in many cases it is a minor subunit protein at the tip of the fimbriae that is the actual adhesin. In gram-positive bacteria, a protein or polysaccharide surface layer serves as the specific adhesin. What is sometimes called polymeric adhesin (BIOFILMS) is distinct from protein adhesin.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.Disulfides: Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.Enzyme Precursors: Physiologically inactive substances that can be converted to active enzymes.Chromatography, Gel: Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.Blood Proteins: Proteins that are present in blood serum, including SERUM ALBUMIN; BLOOD COAGULATION FACTORS; and many other types of proteins.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.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).Trypsin Inhibitor, Kunitz Soybean: A high-molecular-weight protein (approximately 22,500) containing 198 amino acid residues. It is a strong inhibitor of trypsin and human plasmin.Dipeptides: Peptides composed of two amino acid units.Aprotinin: A single-chain polypeptide derived from bovine tissues consisting of 58 amino-acid residues. It is an inhibitor of proteolytic enzymes including CHYMOTRYPSIN; KALLIKREIN; PLASMIN; and TRYPSIN. It is used in the treatment of HEMORRHAGE associated with raised plasma concentrations of plasmin. It is also used to reduce blood loss and transfusion requirements in patients at high risk of major blood loss during and following open heart surgery with EXTRACORPOREAL CIRCULATION. (Reynolds JEF(Ed): Martindale: The Extra Pharmacopoeia (electronic version). Micromedex, Inc, Englewood, CO, 1995)Antipain: An oligopeptide produced by various bacteria which acts as a protease inhibitor.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.Phenylmethylsulfonyl Fluoride: An enzyme inhibitor that inactivates IRC-50 arvin, subtilisin, and the fatty acid synthetase complex.Endopeptidase K: An enzyme that catalyzes the hydrolysis of keratin, and of other proteins with subtilisin-like specificity. It hydrolyses peptide amides. Endopeptidase K is from the mold Tritirachium album Limber. (Enzyme Nomenclature, 1992) EC 3.4.21.64.Benzoylarginine Nitroanilide: A chromogenic substrate that permits direct measurement of peptide hydrolase activity, e.g., papain and trypsin, by colorimetry. The substrate liberates p-nitroaniline as a chromogenic product.Ovomucin: A heterogeneous mixture of glycoproteins responsible for the gel structure of egg white. It has trypsin-inhibiting activity.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.Myeloblastin: A polymorphonuclear leukocyte-derived serine protease that degrades proteins such as ELASTIN; FIBRONECTIN; LAMININ; VITRONECTIN; and COLLAGEN. It is named for its ability to control myeloid cell growth and differentiation.Solanum tuberosum: A plant species of the genus SOLANUM, family SOLANACEAE. The starchy roots are used as food. SOLANINE is found in green parts.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.Chromatography, 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.Metalloendopeptidases: ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.Sulfhydryl Compounds: Compounds containing the -SH radical.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.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.Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.Trichomonas vaginalis: A species of TRICHOMONAS that produces a refractory vaginal discharge in females, as well as bladder and urethral infections in males.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.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)Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.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)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.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.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.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.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.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.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.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.Erythrina: A genus of leguminous shrubs or trees, mainly tropical, yielding useful compounds such as ALKALOIDS and PLANT LECTINS.Cerebrospinal Fluid Proteins: Proteins in the cerebrospinal fluid, normally albumin and globulin present in the ratio of 8 to 1. Increases in protein levels are of diagnostic value in neurological diseases. (Brain and Bannister's Clinical Neurology, 7th ed, p221)Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.Coumarins: Synthetic or naturally occurring substances related to coumarin, the delta-lactone of coumarinic acid.Entamoebiasis: Infection with amoebae of the genus ENTAMOEBA. Infection with E. histolytica causes DYSENTERY, AMEBIC and LIVER ABSCESS, AMEBIC.Subtilisins: A family of SERINE ENDOPEPTIDASES isolated from Bacillus subtilis. EC 3.4.21.-Plants: Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.Blotting, Northern: Detection of RNA that has been electrophoretically separated and immobilized by blotting on nitrocellulose or other type of paper or nylon membrane followed by hybridization with labeled NUCLEIC ACID PROBES.Larva: Wormlike or grublike stage, following the egg in the life cycle of insects, worms, and other metamorphosing animals.Plants, Medicinal: Plants whose roots, leaves, seeds, bark, or other constituent parts possess therapeutic, tonic, purgative, curative or other pharmacologic attributes, when administered to man or animals.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.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).Sequence Homology, Nucleic Acid: The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function.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.Bombyx: A genus of silkworm MOTHS in the family Bombycidae of the order LEPIDOPTERA. The family contains a single species, Bombyx mori from the Greek for silkworm + mulberry tree (on which it feeds). A native of Asia, it is sometimes reared in this country. It has long been raised for its SILK and after centuries of domestication it probably does not exist in nature. It is used extensively in experimental GENETICS. (From Borror et al., An Introduction to the Study of Insects, 4th ed, p519)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.Cathepsin F: A lysosomal papain-related cysteine proteinase that is expressed in a broad variety of cell types.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.Trypsin Inhibitor, Kazal Pancreatic: A pancreatic trypsin inhibitor common to all mammals. It is secreted with the zymogens into the pancreatic juice. It is a protein composed of 56 amino acid residues and is different in amino acid composition and physiological activity from the Kunitz bovine pancreatic trypsin inhibitor (APROTININ).Isoelectric Point: The pH in solutions of proteins and related compounds at which the dipolar ions are at a maximum.Oxylipins: Eighteen-carbon cyclopentyl polyunsaturated fatty acids derived from ALPHA-LINOLENIC ACID via an oxidative pathway analogous to the EICOSANOIDS in animals. Biosynthesis is inhibited by SALICYLATES. A key member, jasmonic acid of PLANTS, plays a similar role to ARACHIDONIC ACID in animals.Cyclopentanes: A group of alicyclic hydrocarbons with the general formula R-C5H9.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.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).Protozoan Proteins: Proteins found in any species of protozoan.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.Pandalidae: A family of CRUSTACEA, order DECAPODA, comprising the pandalid shrimp. They are protandric hermaphrodites and can breed in both male and female stages. Many species are commercially harvested in the Pacific Northwest.Sequence Analysis: A multistage process that includes the determination of a sequence (protein, carbohydrate, etc.), its fragmentation and analysis, and the interpretation of the resulting sequence information.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.Tosyllysine Chloromethyl Ketone: An inhibitor of SERINE ENDOPEPTIDASES. Acts as an alkylating agent and is known to interfere with the translation process.Gelatin: A product formed from skin, white connective tissue, or bone COLLAGEN. It is used as a protein food adjuvant, plasma substitute, hemostatic, suspending agent in pharmaceutical preparations, and in the manufacturing of capsules and suppositories.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.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.2,2'-Dipyridyl: A reagent used for the determination of iron.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.Immunodiffusion: Technique involving the diffusion of antigen or antibody through a semisolid medium, usually agar or agarose gel, with the result being a precipitin reaction.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.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.Pepsin A: Formed from pig pepsinogen by cleavage of one peptide bond. The enzyme is a single polypeptide chain and is inhibited by methyl 2-diaazoacetamidohexanoate. It cleaves peptides preferentially at the carbonyl linkages of phenylalanine or leucine and acts as the principal digestive enzyme of gastric juice.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Weevils: BEETLES in the family Curculionidae and the largest family in the order COLEOPTERA. They have a markedly convex shape and many are considered pests.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.Protein PrecursorsManduca: A genus of sphinx or hawk moths of the family Sphingidae. These insects are used in molecular biology studies during all stages of their life cycle.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.Chemistry: A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.Fabaceae: The large family of plants characterized by pods. Some are edible and some cause LATHYRISM or FAVISM and other forms of poisoning. Other species yield useful materials like gums from ACACIA and various LECTINS like PHYTOHEMAGGLUTININS from PHASEOLUS. Many of them harbor NITROGEN FIXATION bacteria on their roots. Many but not all species of "beans" belong to this family.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.Chemical Phenomena: The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.Norleucine: An unnatural amino acid that is used experimentally to study protein structure and function. It is structurally similar to METHIONINE, however it does not contain SULFUR.Autolysis: The spontaneous disintegration of tissues or cells by the action of their own autogenous enzymes.Circular Dichroism: A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Fascioliasis: Liver disease caused by infections with parasitic flukes of the genus FASCIOLA, such as FASCIOLA HEPATICA.Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Neutrophils: Granular leukocytes having a nucleus with three to five lobes connected by slender threads of chromatin, and cytoplasm containing fine inconspicuous granules and stainable by neutral dyes.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.Tobacco: A plant genus of the family SOLANACEAE. Members contain NICOTINE and other biologically active chemicals; its dried leaves are used for SMOKING.Digestive System: A group of organs stretching from the MOUTH to the ANUS, serving to breakdown foods, assimilate nutrients, and eliminate waste. In humans, the digestive system includes the GASTROINTESTINAL TRACT and the accessory glands (LIVER; BILIARY TRACT; PANCREAS).Hemolymph: The blood/lymphlike nutrient fluid of some invertebrates.Kallikreins: Proteolytic enzymes from the serine endopeptidase family found in normal blood and urine. Specifically, Kallikreins are potent vasodilators and hypotensives and increase vascular permeability and affect smooth muscle. They act as infertility agents in men. Three forms are recognized, PLASMA KALLIKREIN (EC 3.4.21.34), TISSUE KALLIKREIN (EC 3.4.21.35), and PROSTATE-SPECIFIC ANTIGEN (EC 3.4.21.77).Chickens: Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA.Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Gene Expression: The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.Fibrinolysin: A product of the lysis of plasminogen (profibrinolysin) by PLASMINOGEN activators. It is composed of two polypeptide chains, light (B) and heavy (A), with a molecular weight of 75,000. It is the major proteolytic enzyme involved in blood clot retraction or the lysis of fibrin and quickly inactivated by antiplasmins.ElastinGranzymes: A family of serine endopeptidases found in the SECRETORY GRANULES of LEUKOCYTES such as CYTOTOXIC T-LYMPHOCYTES and NATURAL KILLER CELLS. When secreted into the intercellular space granzymes act to eliminate transformed and virus-infected host cells.Bacteroidaceae Infections: Infections with bacteria of the family BACTEROIDACEAE.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.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.Genes, Protozoan: The functional hereditary units of protozoa.alpha-2-Antiplasmin: A member of the serpin superfamily found in plasma that inhibits the lysis of fibrin clots which are induced by plasminogen activator. It is a glycoprotein, molecular weight approximately 70,000 that migrates in the alpha 2 region in immunoelectrophoresis. It is the principal plasmin inactivator in blood, rapidly forming a very stable complex with plasmin.Swine: Any of various animals that constitute the family Suidae and comprise stout-bodied, short-legged omnivorous mammals with thick skin, usually covered with coarse bristles, a rather long mobile snout, and small tail. Included are the genera Babyrousa, Phacochoerus (wart hogs), and Sus, the latter containing the domestic pig (see SUS SCROFA).

C/EBPalpha regulates generation of C/EBPbeta isoforms through activation of specific proteolytic cleavage. (1/2872)

C/EBPalpha and C/EBPbeta are intronless genes that can produce several N-terminally truncated isoforms through the process of alternative translation initiation at downstream AUG codons. C/EBPbeta has been reported to produce four isoforms: full-length 38-kDa C/EBPbeta, 35-kDa LAP (liver-enriched transcriptional activator protein), 21-kDa LIP (liver-enriched transcriptional inhibitory protein), and a 14-kDa isoform. In this report, we investigated the mechanisms by which C/EBPbeta isoforms are generated in the liver and in cultured cells. Using an in vitro translation system, we found that LIP can be generated by two mechanisms: alternative translation and a novel mechanism-specific proteolytic cleavage of full-length C/EBPbeta. Studies of mice in which the C/EBPalpha gene had been deleted (C/EBPalpha-/-) showed that the regulation of C/EBPbeta proteolysis is dependent on C/EBPalpha. The induction of C/EBPalpha in cultured cells leads to induced cleavage of C/EBPbeta to generate the LIP isoform. We characterized the cleavage activity in mouse liver extracts and found that the proteolytic cleavage activity is specific to prenatal and newborn livers, is sensitive to chymostatin, and is completely abolished in C/EBPalpha-/- animals. The lack of cleavage activity in the livers of C/EBPalpha-/- mice correlates with the decreased levels of LIP in the livers of these animals. Analysis of LIP production during liver regeneration showed that, in this system, the transient induction of LIP is dependent on the third AUG codon and most likely involves translational control. We propose that there are two mechanisms by which C/EBPbeta isoforms might be generated in the liver and in cultured cells: one that is determined by translation and a second that involves C/EBPalpha-dependent, specific proteolytic cleavage of full-length C/EBPbeta. The latter mechanism implicates C/EBPalpha in the regulation of posttranslational generation of the dominant negative C/EBPbeta isoform, LIP.  (+info)

Herpes virus induced proteasome-dependent degradation of the nuclear bodies-associated PML and Sp100 proteins. (2/2872)

The PML protein is associated to nuclear bodies (NBs) whose functions are as yet unknown. PML and two other NBs-associated proteins, Sp100 And ISG20 are directly induced by interferons (IFN). PML and Sp100 proteins are covalently linked to SUMO-1, and ubiquitin-like peptide. PML NBs are disorganized in acute promyelocytic leukemia and during several DNA virus infections. In particular, the HSV-1 ICP0 protein is known to delocalize PML from NBs. Thus, NBs could play an important role in oncogenesis, IFN response and viral infections. Here, we show that HSV-1 induced PML protein degradation without altering its mRNA level. This degradation was time- and multiplicity of infection-dependent. Sp100 protein was also degraded, while another SUMO-1 conjugated protein, RanGAP1 and the IFN-induced protein kinase PKR were not. The proteasome inhibitor MG132 abrogated the HSV-1-induced PML and Sp100 degradation and partially restored their NB-localization. HSV-1 induced PML and Sp100 degradation constitutes a new example of viral inactivation of IFN target gene products.  (+info)

An antiviral mechanism of nitric oxide: inhibition of a viral protease. (3/2872)

Although nitric oxide (NO) kills or inhibits the replication of a variety of intracellular pathogens, the antimicrobial mechanisms of NO are unknown. Here, we identify a viral protease as a target of NO. The life cycle of many viruses depends upon viral proteases that cleave viral polyproteins into individual polypeptides. NO inactivates the Coxsackievirus protease 3C, an enzyme necessary for the replication of Coxsackievirus. NO S-nitrosylates the cysteine residue in the active site of protease 3C, inhibiting protease activity and interrupting the viral life cycle. Substituting a serine residue for the active site cysteine renders protease 3C resistant to NO inhibition. Since cysteine proteases are critical for virulence or replication of many viruses, bacteria, and parasites, S-nitrosylation of pathogen cysteine proteases may be a general mechanism of antimicrobial host defenses.  (+info)

Activation of stress-activated protein kinase/c-Jun NH2-terminal kinase and p38 kinase in calphostin C-induced apoptosis requires caspase-3-like proteases but is dispensable for cell death. (4/2872)

Apoptosis was induced in human glioma cell lines by exposure to 100 nM calphostin C, a specific inhibitor of protein kinase C. Calphostin C-induced apoptosis was associated with synchronous down-regulation of Bcl-2 and Bcl-xL as well as activation of caspase-3 but not caspase-1. The exposure to calphostin C led to activation of stress-activated protein kinase/c-Jun NH2-terminal kinase (SAPK/JNK) and p38 kinase and concurrent inhibition of extracellular signal-regulated kinase (ERK). Upstream of ERK, Shc was shown to be activated, but its downstream Raf1 and ERK were inhibited. The pretreatment with acetyl-Tyr-Val-Ala-Asp-aldehyde, a relatively selective inhibitor of caspase-3, or benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone (z-VAD.fmk), a broad spectrum caspase inhibitor, similarly inhibited calphostin C-induced activation of SAPK/JNK and p38 kinase as well as apoptotic nuclear damages (chromatin condensation and DNA fragmentation) and cell shrinkage, suggesting that caspase-3 functions upstream of SAPK/JNK and p38 kinase, but did not block calphostin C-induced surface blebbing and cell death. On the other hand, the inhibition of SAPK/JNK by transfection of dominant negative SAPK/JNK and that of p38 kinase by SB203580 induced similar effects on the calphostin C-induced apoptotic phenotypes and cell death as did z-VAD.fmk and acetyl-Tyr-Val-Ala-Asp-aldehyde, but the calphostin C-induced PARP cleavage was not changed, suggesting that SAPK/JNK and p38 kinase are involved in the DNA fragmentation pathway downstream of caspase-3. The present findings suggest, therefore, that the activation of SAPK/JNK and p38 kinase is dispensable for calphostin C-mediated and z-VAD.fmk-resistant cell death.  (+info)

Proteolytic processing of the Alzheimer's disease amyloid precursor protein within its cytoplasmic domain by caspase-like proteases. (5/2872)

Alzheimer's disease is characterized by neurodegeneration and deposition of betaA4, a peptide that is proteolytically released from the amyloid precursor protein (APP). Missense mutations in the genes coding for APP and for the polytopic membrane proteins presenilin (PS) 1 and PS2 have been linked to familial forms of early-onset Alzheimer's disease. Overexpression of presenilins, especially that of PS2, induces increased susceptibility for apoptosis that is even more pronounced in cells expressing presenilin mutants. Additionally, presenilins themselves are targets for activated caspases in apoptotic cells. When we analyzed APP in COS-7 cells overexpressing PS2, we observed proteolytic processing close to the APP carboxyl terminus. Proteolytic conversion was increased in the presence of PS2-I, which encodes one of the known PS2 pathogenic mutations. The same proteolytic processing occurred in cells treated with chemical inducers of apoptosis, suggesting a participation of activated caspases in the carboxyl-terminal truncation of APP. This was confirmed by showing that specific caspase inhibitors blocked the apoptotic conversion of APP. Sequence analysis of the APP cytosolic domain revealed a consensus motif for group III caspases ((IVL)ExD). Mutation of the corresponding Asp664 residue abolished cleavage, thereby identifying APP as a target molecule for caspase-like proteases in the pathways of programmed cellular death.  (+info)

Role of hypoxia-induced Bax translocation and cytochrome c release in reoxygenation injury. (6/2872)

We investigated mechanisms of cell death during hypoxia/reoxygenation of cultured kidney cells. During glucose-free hypoxia, cell ATP levels declined steeply resulting in the translocation of Bax from cytosol to mitochondria. Concurrently, there was cytochrome c release and caspase activation. Cells that leaked cytochrome c underwent apoptosis after reoxygenation. ATP depletion induced by a mitochondrial uncoupler resulted in similar alterations even in the presence of oxygen. Moreover, inclusion of glucose during hypoxia prevented protein translocations and reoxygenation injury by maintaining intracellular ATP. Thus, ATP depletion, rather than hypoxia per se, was the cause of protein translocations. Overexpression of Bcl-2 prevented cytochrome c release and reoxygenation injury without ameliorating ATP depletion or Bax translocation. On the other hand, caspase inhibitors did not prevent protein translocations, but inhibited apoptosis during reoxygenation. Nevertheless, they could not confer long-term viability, since mitochondria had been damaged. Omission of glucose during reoxygenation resulted in continued failure of ATP production, and cell death with necrotic morphology. In contrast, cells expressing Bcl-2 had functional mitochondria and remained viable during reoxygenation even without glucose. Therefore, Bax translocation during hypoxia is a molecular trigger for cell death during reoxygenation. If ATP is available during reoxygenation, apoptosis develops; otherwise, death occurs by necrosis. By preserving mitochondrial integrity, BCL-2 prevents both forms of cell death and ensures cell viability.  (+info)

Mutant p53 can provoke apoptosis in p53-deficient Hep3B cells with delayed kinetics relative to wild-type p53. (7/2872)

Wild-type (wt) p53 frequently induces apoptosis when expressed in tumor cells whereas mutant p53 acts as an oncoprotein and consequently, stimulates cell proliferation. We report here exceptions to that rule. p53 conformational mutant 175H and DNA contact mutant 273H provoke apoptosis in human p53-deficient Hep3B hepatoma cells with delayed kinetics relative to wt p53. Similarly, c-Myc strongly stimulates apoptosis in these cells. In contrast, viral oncoproteins E1A and E7, and the cellular oncoprotein MDM-2, fail to elicit cytocidal responses. Efficient apoptotic cell death by mutant p53 requires oligomerization as 175H and 273H with deletions between amino acid residues 326 and 347 of the oligomerization domain are nontoxic. Apoptosis by mutant or wt p53 was significantly inhibited by the serine protease inhibitor AEBSF but not by the inactive analog AEBSA. Together, these results suggest that a wt p53-independent control mechanism is operational in Hep3B cells that eliminates cells upon sensing illegitimate proliferation signals originating from certain oncoproteins, including mutant p53 and Myc. We suggest that some tumor cell types lack p53 altogether because they tolerate neither wild-type nor mutant forms of the protein.  (+info)

Rubella virus-induced apoptosis varies among cell lines and is modulated by Bcl-XL and caspase inhibitors. (8/2872)

Rubella virus (RV) causes multisystem birth defects in the fetuses of infected women. To investigate the cellular basis of this pathology, we examined the cytopathic effect of RV in three permissive cell lines: Vero 76, RK13, and BHK21. Electron microscopy and the TUNEL assay showed that the cytopathic effect resulted from RV-induced programmed cell death (apoptosis) in all three cell lines, but the extent of apoptosis varied among these cells. At 48 h postinfection, the RK13 cell line showed the greatest number of apoptotic cells, the Vero 76 cell line was approximately 3-fold less, and BHK21 had very few. An increased multiplicity of infection and longer time postinfection were required for the BHK21 cell line to reach the level of apoptotic cells in Vero 76 at 48 h. Purified RV induced apoptosis in a dose-dependent fashion, but not UV-inactivated RV or virus-depleted culture supernatant. Specific inhibitors of the apoptosis-specific proteases caspases reduced RV-induced apoptosis and led to higher levels of RV components in infected cells. To address the role of regulatory proteins in RV-induced apoptosis, the antiapoptotic gene Bcl-2 or Bcl-XL was transfected into RK13 cells. Although a high level of Bcl-2 family proteins was expressed, no protection was observed from apoptosis induced by RV, Sindbis virus, or staurosporine in RK13 cells. In BHK21 cells, however, increased expression of Bcl-XL protected cells from apoptosis. The observed variability in apoptotic response to RV of these cell lines demonstrates that programmed cell death is dependent on the unique properties of each cell and may be indicative of how selective organ damage occurs in a congenital rubella syndrome fetus.  (+info)

Bombyx cysteine proteinase inhibitor: Bombyx cysteine proteinase inhibitor (BCPI) from the hemolymph of Bombyx mori; alpha and beta are two forms differing only in three amino acid residues at N terminal; amino acid sequence in first source
the constitute families differ by insertion into and circular permutation of the common catalytic core made of one alpha-helix and 3-strands of beta- ...
The report generally describes clasto-lactacystin beta-lactone, examines its uses, production methods, patents. CLASTO-LACTACYSTIN BETA-LACTONE market
The cystatin superfamily encompasses proteins that contain multiple cystatin-like sequences. Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory activity. There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins and the kininogens. The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions. The cystatin locus on chromosome 20 contains the majority of the type 2 cystatin genes and pseudogenes. This gene is located in the cystatin locus and encodes a type 2 salivary cysteine peptidase inhibitor. The protein is an S-type cystatin, based on its high level of expression in saliva, tears and seminal plasma. The specific role in these fluids is unclear but antibacterial and antiviral activity is present, consistent with a protective function. [provided by RefSeq, Jul 2008 ...
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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.
Answers to questions you may have can be found in the inhibitor handling instructions. Topics include how to prepare stock solutions, how to store inhibitors, and issues that need special attention for cell-based assays and animal experiments.. Handling Instructions Tel: +1-832-582-8158 Ext:3 If you have any other enquiries, please leave a message.. ...
The Ac-YVAD-cmk and Ac-DEVD-CHO peptide inhibitors block TRAIL-induced DNA fragmentation in mouse and human cells. (A) Soluble DNA was extracted from mouse my
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.
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4) Institute of Chemistry, Slovak Academy of Sciences, Bratislava, Slovakia.. Address for correspondence: O.N. Poteryaeva, Russian Academy of Medical Sciences, Institute of Physiology, Novosibirsk, Russia.. Summary: Cystatin C is the best known extracellular endogenous cysteine proteinase inhibitor and has been studied as a possible index of tumor growth and as a marker of the effectiveness of antitumor therapy. The aim of this study was to evaluate cystatin C concentrations in murine tumor tissues (compared with other organs not directly involved with tumor development, such as the liver and spleen) during treatment with several antitumor drugs (Ukrain and/or cyclophosphane). Cystatin C concentrations in murine tissues and biological fluids was determined by enzyme-linked immunosorbent (ELISA) assay The cystatin C ELISA test is a sandwich immunoassay, which uses immobilized rabbit antihuman cystatin C Pab and mouse antihuman cystatin C Mab-HRP (monoclonal antibodies, conjugated with horseradish ...
The report generally describes calpain inhibitor i, examines its uses, production methods, patterns. CALPAIN INHIBITOR I market situation is overviewed;
Compounds of the formula (I), wherein R.sub.1 is aryl or biaryl; R.sub.2 is aryl-lower alkyl, biaryl-lower alkyl, benzo-fused cycloalkyl, cycloalkyl-lower alkyl, bicycloalkyl-lower alkyl, aryloxy-lower alkyl, or aryl-C.sub.2 -C.sub.7 -alkyl in which C.sub.2 -C.sub.7 -alkyl is interrupted by Y; Y is O, S, SO, SO.sub.2, CO or NR.sub.6 ; R.sub.3 is hydrogen or lower alkyl; or R.sub.2 and R.sub.3 combined are C.sub.2 -C.sub.7 -alkylene or C.sub.2 -C.sub.7 -alkylene interrupted by Y; R.sub.4 is hydrogen or lower alkyl; R.sub.5 is hydrogen, optionally substituted lower alkyl, aryl-lower alkyl, biaryl-lower alkyl, cycloalkyl-lower alkyl, bicycloalkyl-lower alkyl, aryloxy-lower alkyl, or aryl-C.sub.2 -C.sub.7 -alkyl in which C.sub.2 -C.sub.7 -alkyl is interrupted by Y; R.sub.6 is hydrogen, lower alkyl or aryl-lower alkyl; and pharmaceutically acceptable salts thereof, which are useful as cysteine cathepsin inhibitors ##STR1##
Z-FA-FMK is an irreversible cysteine protease inhibitor, and also inhibits effector caspases. Buy Z-FA-FMK from AbMole BioScience.
Calpastatin (CAST) is a calpain inhibitor, a calcium-dependent cysteine protease that is widely distributed in higher order animals. There are different types of calpastatins; examples include the 68 kDa erythrocyte-derived calpastatin and the 107 kDa myocyte-derived calpastatin (as evidenced by SDS-PAGE). Through its inhibition of calpain, calpastatin is believed to play important roles in the regulation of cell proliferation, differentiation and aging. CAST is also involved in the proteolysis of amyloid precursor protein (APP). ...
Calpastatin (CAST) is a calpain inhibitor, a calcium-dependent cysteine protease that is widely distributed in higher order animals. There are different types of calpastatins; examples include the 68 kDa erythrocyte-derived calpastatin and the 107 kDa myocyte-derived calpastatin (as evidenced by SDS-PAGE). Through its inhibition of calpain, calpastatin is believed to play important roles in the regulation of cell proliferation, differentiation and aging. CAST is also involved in the proteolysis of amyloid precursor protein (APP). ...
A new class of polyalkylene oxide vinyl sulfone reagents is described. Also described are a method by which these reagents can be prepared as well as a method for using them in hydrated media for the modification of proteins. The novel polymer-to-protein conjugates made by reacting these reagents with proteins have advantages over similar conjugates prepared with prior art reagents in that they are more stable against hydrolysis and retain the positive charge carrying capacity at amine sites at which the modifying reagents are attached.
77-77-0 - AFOSIXZFDONLBT-UHFFFAOYSA-N - Vinyl sulfone - Similar structures search, synonyms, formulas, resource links, and other chemical information.
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.
Ac-YVAD-CMK | Ac-Tyr-Val-Ala-Asp-CH2Cl Ac-YVAD-Chloromethylketone3180-v 5 mg | 165.00 EUR Acetyl- L-tyrosyl- L-valyl- L-alanyl- ...
Health, ...EDITORS PICK: Calpain inhibitors never forget: improving memory in Al...Overactivation of proteins known as calpains which are involved in me...It is thought that dysfunctional signaling between nerve cells contrib...TITLE: Inhibition of calpains improves memory and synaptic transmissio...,JCI,online,early,table,of,contents:,July,1,,2008,medicine,medical news today,latest medical news,medical newsletters,current medical news,latest medicine news
Welcome! For price inquiries, please feel free to contact us through the form below through the form on the left side. We will get back to you as soon as possible.. ...
Calpain兔多克隆抗体(ab124631)可与小鼠, 大鼠, 人, 曼氏血吸虫样本反应并经WB, IP, ELISA实验严格验证。所有产品均提供质保服务,中国75%以上现货。
|p||strong|CA-074|/strong|, a specific cathepsin B inhibitor, also abolished the neurotoxic effects caused by Abeta42-activated BV2 cell [1]. Co-treatment of cultures with the cathepsin B inhibitors CA-074 or Z-FA-FMK suppressed the cytostatic effects of
Cystatin-SN is a protein that in humans is encoded by the CST1 gene. The cystatin superfamily encompasses proteins that contain multiple cystatin-like sequences. Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory activity. There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins and the kininogens. The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions, where they appear to provide protective functions. The cystatin locus on chromosome 20 contains the majority of the type 2 cystatin genes and pseudogenes. This gene is located in the cystatin locus and encodes a cysteine proteinase inhibitor found in saliva, tears, urine, and seminal fluid. GRCh38: Ensembl release 89: ENSG00000170373 - Ensembl, May 2017 "Human PubMed Reference:". "Entrez Gene: CST1 cystatin SN". The MEROPS online database for ...
SID 26681509 is a reversible and potent human cathepsin L inhibitor. SID 26681509 displays no inhibitory activity of cathepsin G.
Cathepsin B (CtsB) is a lysosomal cysteine proteinase that is specifically translocated to the extracellular milieu during cancer progression. The development of a lipidated CtsB inhibitor incorporated into the envelope of a liposomal nanocarrier (LNC-NS-629) is described. Ex vivo and in vivo studies confirmed selective targeting and internalization of LNC-NS-629 by tumor and stromal cells, thus validating CtsB targeting as a highly promising approach to cancer diagnosis and treatment ...
|p|E-64-c, which is also known as Ep-475, is an analog of E-64 and inhibitor of cysteine proteinases. [1]|br /|The cysteine proteinases, of which Cathepsins B and H and cathepsin L exist in mammals, contain an essential highly reactive thiol group, and th
Z-VAD(OMe)-FMK is a cell permeable peptide which binds irreversibly to the catalytic site of intracellular enzymes known as caspases, which play an important role in the induction of apoptosis. The binding of Z-VAD(OMe)-FMK to caspases inhibits the acti
Oxidized low-density lipoprotein (oxLDL) is known to induce apoptosis in endothelial cells, and this is believed to contribute to the progression of atherosclerosis. In the present study we made the novel observation that oxLDL-induced death of HMEC-1 cells is accompanied by activation of calpain. The μ-calpain inhibitor PD 151746 decreased oxLDL-induced cytotoxicity, whereas the general caspase inhibitor BAF (t-butoxycarbonyl-Asp-methoxyfluoromethylketone) had no effect. Also, oxLDL provoked calpain-dependent proteolysis of cytoskeletal α-fodrin in the HMEC-1 cells. Our observation of an autoproteolytic cleavage of the 80 kDa subunit of μ-calpain provided further evidence for an oxLDL-induced stimulation of calpain activity. The Bcl-2 protein Bid was also cleaved during oxLDL-elicited cell death, and this was prevented by calpain inhibitors, but not by inhibitors of cathepsin B and caspases. Treating the HMEC-1 cells with oxLDL did not result in detectable activation of procaspase 3 or ...
Read "Effects of abscisic acid treatment on the expression of cysteine proteinase gene and enzyme inhibitor during wheat cold adaptation, Russian Journal of Plant Physiology" on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips.
Materials.Benzyloxycarbonyl-Val-Ala-Asp(OMe)-fluoromethylketone (zVAD-fmk), z-Asp-Glu-Val-Asp-fmk (zDEVD-fmk), boc-aspartyl(OMe)-fluoromethylketone (BAF), and the fluorogenic caspase substrate zDEVD-AFC were purchased from Enzyme Systems Products (Livermore, CA). Staurosporine was obtained from ICN Pharmaceuticals (Costa Mesa, CA). A cell lysis buffer for fluorogenic caspase activity assays was obtained from Clontech (ApoAlert CPP32 Assay Kit; Palo Alto, CA).. Cell culture. p53-deficient mice were generated from a 129/Sv × C57BL/6 background as described (Donehower et al., 1992). The genotypes of the mating pairs and all offspring were determined by PCR, using DNA extracted from the tail (Timme and Thompson, 1994). p53−/− mice were generated routinely from (+/−) × (−/−) mating pairs, whereas p53 wild-type mice were obtained by crossing p53+/+ mice. The brains from individual animals were cultured separately and genotyped before treatment.. Neuronal cultures derived from embryonic day ...
... In order to be able to write the value 100 to /proc/acpi/video/.../brightness, we have to allocate 5 bytes: 4 characters will be written (1, 0, 0 plus null byte), and 1 byte should be buffer for a terminating NULL character. http://bugzilla.kernel.org/show_bug.cgi?id=9278 Signed-off-by: Danny Baumann ,[EMAIL PROTECTED], Acked-by: Zhang Rui ,[EMAIL PROTECTED], Signed-off-by: Len Brown ,[EMAIL PROTECTED], --- drivers/acpi/video.c , 2 +- 1 files changed, 1 insertions(+), 1 deletions(-) diff --git a/drivers/acpi/video.c b/drivers/acpi/video.c index dce0a6e..44a0d9b 100644 --- a/drivers/acpi/video.c +++ b/drivers/acpi/video.c @@ -897,7 +897,7 @@ acpi_video_device_write_brightness(struct file *file, { struct seq_file *m = file-,private_data; struct acpi_video_device *dev = m-,private; - char str[4] = { 0 }; + char str[5] = { 0 }; unsigned int level = 0; int i; - To unsubscribe from this list: send the line unsubscribe ...
Buy Z-VAD-FMK, an irreversible general caspase inhibitor. Join researchers using high quality Z-VAD-FMK from Abcam and achieve your mission, faster.
ACPI 3.0 includes UUID-labelled vendor-defined resources (section 6.4.3.2), so move the code that supports this from arch/ia64 into ACPI proper. Len, Tony, this touches both acpi and ia64. Probably easiest if Tony acks it and Len decides whether to apply it. HP owns all the copyrights on the code being moved, and we agree that the code being moved into the ACPI CA may be used under either the GPL or the BSD-style license used by the ACPI CA. (There should be something in Documentation/acpi about how to contribute to the ACPI CA. Its a royal pain in the rear :-)). Signed-off-by: Bjorn Helgaas ,[email protected], ===== arch/ia64/kernel/acpi-ext.c 1.5 vs edited ===== Index: work-vga2/arch/ia64/kernel/acpi-ext.c =================================================================== --- work-vga2.orig/arch/ia64/kernel/acpi-ext.c 2005-09-14 09:28:07.000000000 -0600 +++ work-vga2/arch/ia64/kernel/acpi-ext.c 2005-09-15 14:52:33.000000000 -0600 @@ -1,105 +1,45 @@ /* - * arch/ia64/kernel/acpi-ext.c + * ...
1KYI: Crystal Structure of HslUV Complexed with a Vinyl Sulfone Inhibitor: Corroboration of a Proposed Mechanism of Allosteric Activation of HslV by HslU
Cysteine proteases recognized by the active site-directed probe DCG-04 in macrophage cell lysates. (A) Schematic overview of the approach designed to examine
We are going to change ARM virt ACPI DSDT table, which will cause make check to fail, so temporarily add related golden masters to ignore list. Signed-off-by: Heyi Guo ,[email protected], Reviewed-by: Michael S. Tsirkin ,[email protected], --- Cc: Peter Maydell ,[email protected], Cc: Michael S. Tsirkin ,[email protected], Cc: Igor Mammedov ,[email protected], Cc: Shannon Zhao ,[email protected], Cc: [email protected] Cc: [email protected] --- tests/qtest/bios-tables-test-allowed-diff.h , 3 +++ 1 file changed, 3 insertions(+) diff --git a/tests/qtest/bios-tables-test-allowed-diff.h b/tests/qtest/bios-tables-test-allowed-diff.h index dfb8523c8b..32a401ae35 100644 --- a/tests/qtest/bios-tables-test-allowed-diff.h +++ b/tests/qtest/bios-tables-test-allowed-diff.h @@ -1 +1,4 @@ /* List of comma-separated changed AML files to ignore */ +tests/data/acpi/virt/DSDT, +tests/data/acpi/virt/DSDT.memhp, +tests/data/acpi/virt/DSDT.numamem, -- 2.19.1 ...
Allen339, member , July 11th, 2019 CASP14 caspase 14, apoptosis-related cysteine peptidase BackgroundCaspases are a family of cysteine proteases that are key mediators of programmed cell death or apoptosis.1 The precursor form of all.... view details ...
Caspase-1 Inhibitor I - CAS 143313-51-3 - Calbiochem The Caspase-1 Inhibitor I, also referenced under CAS 143313-51-3, controls the biological activity of Caspase-1. This small molecule/inhibitor is primarily used for Cancer applications. - Find MSDS or SDS, a COA, data sheets and more information.
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hypothetical protein, alpha-2 antiplasmin, Alpha-2-antiplasmin, alpha-2 antiplasmin, pigment epithelium derived factor, AS27_04276, caspin, CB1_000765141, cell proliferation-inducing gene 35 protein, Dmrs91, EPC-1, GW7_05089, H920_13024, I79_024527, M959_13429, MDA_GLEAN10016889, N300_03473, N302_16382, N305_15082, N306_10474, N307_07373, N308_00896, N309_12586, N311_08061, N312_04929, N320_07386, N321_02844, N322_05786, N324_04587, N325_07445, N326_06640, N327_07162, N329_08729, N330_08014, N332_10702, N333_06723, N335_06305, N336_08169, N339_06481, N340_07977, N341_07059, OI12, OI6, PAL_GLEAN10020010, PANDA_006472, PEDF, Pedfl, PIG35, pigment epithelium derived factor, pigment epithelium-derived factor, pigment epithelium-derived factor-like protein, Pigment epithelium-derived factor precursor-like protein, Sdf3, SDF-3, serine (or cysteine) peptidase inhibitor, clade F, member 1, serine (or cysteine) proteinase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member ...
Cysteine proteases, also known as thiol proteases, are enzymes that degrade proteins. These proteases share a common catalytic mechanism that involves a nucleophilic cysteine thiol in a catalytic triad or dyad. Cysteine proteases are commonly encountered in fruits including the papaya, pineapple, fig and kiwifruit. The proportion of protease tends to be higher when the fruit is unripe. In fact, dozens of latices of different plant families are known to contain cysteine proteases. Cysteine proteases are used as an ingredient in meat tenderizers. The MEROPS protease classification system counts 14 superfamilies plus several currently unassigned families (as of 2013) each containing many families. Each superfamily uses the catalytic triad or dyad in a different protein fold and so represent convergent evolution of the catalytic mechanism. For superfamilies, P = superfamily containing a mixture of nucleophile class families, C = purely cysteine proteases. superfamily. Within each superfamily, ...
Glycyl endopeptidase is a cysteine endopeptidase of the papain family, characterized by specificity for cleavage C-terminal to glycyl residues only and by resistance to inhibition by members of the cystatin family of cysteine proteinase inhibitors. Glycyl endopeptidase has been crystallized from high salt with a substrate-like inhibitor covalently bound to the catalytic Cys 25. The structure has been solved by molecular replacement with the structure of papain and refined at 2.1 A to an R factor of 0.196 (Rfree = 0.258) with good geometry. The structure of the S1 substrate binding site of glycyl endopeptidase differs from that of papain by the substitution of glycines at residues 23 and 65 in papain, with glutamic acid and arginine, respectively, in glycyl endopeptidase. The side chains of these residues form a barrier across the binding pocket, effectively excluding substrate residues with large side chains from the S1 subsite. The constriction of this subsite in glycyl endopeptidase explains ...
References for Abcams Human Cystatin C ELISA Kit (ab119589). Please let us know if you have used this product in your publication
Read "An extracellular insoluble inhibitor of cysteine proteinases in cell cultures and seeds of carrot, Plant Molecular Biology" on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips.
The precursor protein in cystatin C amyloidosis (ACys) is cystatin C, which is a cysteine protease inhibitor that contains a point mutation. This condition is clinically termed HCHWA, Icelandic type. ... more
ROZMAN PUNGERČAR, Jerica, KOPITAR-JERALA, Nataša, BOGYO, M., TURK, Dušan, VASILJEVA, Olga, KLEMENČIČ, Ivica, VANDENABEELE, P., BR MME, D., PUIZDAR, Vida, FONOVIĆ, Marko, TRSTENJAK-PREBANDA, Mojca, DOLENC, Iztok, TURK, Vito, TURK, Boris. Inhibition of papain-like cysteine proteases and legumain by caspase-specific inhibitors : when reaction mechanism is more important than specificity. Cell Death Differ, 2003, vol. 10, str. 881-888 ...
BACKGROUND: Cystatin C (cC) is a cysteine protease inhibitor that may influence immune response. Our aim was to test the effect of a high concentration of cC, characteristic for uremic patients, on neutrophil (PMN) apoptosis and respiratory burst, as well as the cC secretion from PMNs stimulated with proinflammatory cytokines. MATERIAL/METHODS: PMNs from 35 healthy volunteers aged 27-61 years were cultured in presence of cC, IL-1beta or TNF-alpha. The percentage of apoptotic cells based on DNA depletion, Fas, FasL and caspase -3 expression were assessed ...
Perforation formation in Aponogeton madagascariensis (Mirb.) H.Bruggen (lace plant) is an excellent model for studying developmentally regulated programmed cell death (PCD). In this study, we isolated and identified two lace plant vacuolar processing enzymes (VPEs) and investigated their involvement in PCD and throughout leaf development. Lace plant VPE transcript levels were determined during sev ...
Sigma-Aldrich offers abstracts and full-text articles by [G Fenteany, R F Standaert, W S Lane, S Choi, E J Corey, S L Schreiber].
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Almost all protease families have been associated with plant development, particularly senescence, which is the final developmental stage of every organ before cell death. Proteolysis remobilizes and recycles nitrogen from senescent organs that is required, for example, seed development. Senescence-associated expression of proteases has recently been characterized using large-scale gene expression analysis seeking to identify and characterize senescence-related genes. Increasing activities of proteolytic enzymes, particularly cysteine proteases, are observed during the senescence of legume nodules, in which a symbiotic relationship between the host plant and bacteria (Rhizobia) facilitate the fixation of atmospheric nitrogen. It is generally considered that cysteine proteases are compartmentalized to prevent uncontrolled proteolysis in nitrogen-fixing nodules. In addition, the activities of cysteine proteases are regulated by endogenous cysteine protease inhibitors called cystatins. These small proteins
Absence of the protease inhibitor cystatin C in inflammatory cells results in larger plaque area in plaque regression of apoE-deficient mice ...
Proteins that have a GPI glycolipid modification are acknowledged to be key in the lifecycle of Plasmodium; for example the involvement of the GPI-anchored MSP1 on merozoites in erythrocyte invasion. The enzyme that transfers the preformed GPI to the proteins such as MSP1 is named GPI:protein transamidase, however, studying this enzyme biochemically has been arduous, due to the following hurdles. Firstly, the GPI:protein transamidase functions as a subunit in multidomain complex, some components of which maybe membrane associated, and there are no reports of functional recombinant reconstitution of this complex. Secondly, there are no convenient and sensitive transamidase assays available that are amenable to medium/high throughput studies, even though large small molecule cysteine peptidase inhibitor libraries exist and can be used to studying this enzyme.. Any input/thoughts on how to overcome the aforementioned obstacles in studying the Plasmodium GPI:protein transamidase would be most ...
Characterization of a second cell-associated Arg-specific cysteine proteinase of Porphyromonas gingivalis and identification of an adhesin-binding motif involved in association of the prtR and prtK proteinases and adhesins into large complexes
BACKGROUND: Human cystatin C is a cysteine protease inhibitor produced by all nucleated cells in the body and the protein is present in all body fluids. The concentration in cerebrospinal fluid (CSF) is considerably higher than in plasma. Cystatin C levels seem to influence the development of Alzheimer disease (AD) and low levels in the brain are associated with an increased risk for AD. The aim of this study was to develop a high throughput assay for the quantification of cystatin C in CSF. METHODS: Antigen excess, imprecision, interference, linearity, recovery, sample stability and reference values were evaluated on Architect ci8200 (Abbott Laboratories, Abbott Park, IL, USA). RESULTS: The assay had an antigen-excess limit at 23 mg/L and was linear over the range of 0.84 to 8.33 mg/L. Results , 8.33 mg/L were automatically rerun in a higher dilution. Within-run coefficient of variation (CV) was 1.71, 1.10 and 0.79%, between day CV was 1.71, 0.39 and 1.45%, between-run CV was 0.58, 0.66 and ...
Cysteine proteases (CPs) are responsible for many biochemical processes occurring in living organisms and they have been implicated in the development and progression of several diseases that involve abnormal protein turnover. The activity of CPs is regulated among others by their specific inhibitors: cystatins. The main aim of this review is to discuss the structure-activity relationships of cysteine proteases and cystatins, as well as of some synthetic inhibitors of cysteine proteases structurally based on the binding fragments of cystatins ...
BioAssay record AID 666968 submitted by ChEMBL: Inhibition of human recombinant caspase-3 catalytic domain using Ac-DEVD-pNA as substrate at 20 ug/ml preincubated for 30 mins before substrate addition measured after 3 mins.
Principal Investigator:KATUNUMA Nobuhiko, Project Period (FY):1989 - 1990, Research Category:Grant-in-Aid for Developmental Scientific Research (B)., Research Field:Pathological medical chemistry
In 1995, scientists at Myogenics Inc. synthesized bortezomib and originally designated it as PS-341, the name used in this 1999 article (1). The drug is an N-protected dipeptide with a boron atom, and subsequent to the 1999 article, it has been characterized as binding with high affinity and specificity to the catalytic site of the 26S proteasome (2). In the 1990s, ubiquitin-oriented proteasomal pathways were considered both unusual and novel targets, and as pointed out by the authors, the results of their structure-activity studies supported the interpretation that selective proteasome inhibitors killed cells by blocking ordered protein degradation. They linked this effect with tumor cell growth inhibition and provided support that the inhibition of the biochemical target, the proteasome, was related directly to the biological effects of PS-341 and related analogues. Their overall conclusions made tangible the now widely held tenets that the proteasome is a novel drug target and that PS-341 ...
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Design and Synthesis of Proteinase Inhibitors Many critical biological processes are initiated, sustained or terminated by the action of a proteinase or peptidase enzyme. Uncontrolled proteolysis is a significant factor in many pathophysiological processes, yet there are almost no drugs with which to address this. Our research has been directed at the design and evaluation of new types of inhibitors for proteinase enzymes.
Click to launch & play an online audio visual presentation by Prof. Guy Salvesen on Natural caspase inhibitors, part of a collection of online lectures.
E7449 is an orally bioavailable, brain penetrable, small molecule dual inhibitor of PARP1/2 that also inhibits PARP5a/5b, otherwise known as tankyrase1 and 2 (TNKS1/2), important regulators of canonical Wnt/β-catenin signaling. It has IC50 values of 1.0 and 1.2 nM for PARP1 and 2, respectively. Buy PARP inhibitor E7449 from AbMole BioScience.
NC_HR7375C.005: HR7375C.005, [U-100% 13C; U-100% 15N], 1.04 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM. NC_HR7375C.006: HR7375C.006, [U-100% 13C; U-100% 15N], 1.04 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM. NC5_HR7375C.007: HR7375C.007, [U-100% 15N] 5% 13C fractionally labeled, 0.33 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM. D2O_NC_HR7375C.005: HR7375C.005, [U-100% 13C; U-100% 15N], 1.04 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O 100%; DSS 50 uM. sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K ...
Z-VAD-FMK is a cell-permeable, irreversible pan-caspase inhibitor, blocks all features of apoptosis in THP.1 and Jurkat T-cells.
Calpains are calcium-dependent cysteine proteases involved in sigl transduction in a variety of cellular processes. A functiol calpain protein…
The proteasome is the main site of protein degradation in human cells, and plays a major role in the regulation of cellular processes including cell cycle progression, DNA repair and the DNA damage response. Proteasome inhibition is emerging as a new anti-cancer strategy, with the development of bortezomib for the treatment of patients with multiple myeloma. Proteasome inhibitors can be used either as single agents or in conjunction with other cancer treatments. Proteasome inhibitors can sensitise cancer cell lines to routinely-used cancer treatments including the platinum-based anti-cancer drug, cisplatin. The aim of this research was to investigate the effect of proteasome inhibition on cisplatininduced DNA damage responses in human cells, including cell viability, cell cycle arrest and the phosphorylation of DNA damage response proteins. The proteasome inhibitor MG132 sensitised the pol n-deficient human fibroblast cell line XP30RO to cisplatin. MG132 treatment induced strong cell cycle ...
Papain-like cysteine proteases are important for the survival of the flagellated protozoa Trypanosoma cruzi, the causative agent of Chagas Disease. the lysosomal cysteine protease designated as cruzipain or cruzain, is the archetype of a multigene family of related isoforms. We investigated the substrate specificity of the cruzipain 2 isoform using internally quenched fluorogenic substrates. We found that cruzipain 2 and cruzain differ substantially regarding the specificity in the S-2, S-1() and S-2() pockets. Our study indicates that cruzipain 2 has a more restricted specificity than cruzain, suggesting that these isoforms might act on distinct natural substrates ...
Anticancer Effect of COX-2 Inhibitor DuP-697 Alone and in Combination with Tyrosine Kinase Inhibitor (E7080) on Colon Cancer Cell Lines Colon cancer;DuP-697;COX-2 inhibition;tyrosine kinase inhibitor; Colorectal cancer remains one of the most common types of cancer and a leading cause of cancer death worldwide. In this study, we aimed to investigate effects of DuP-697, an irreversible selective inhibitor of COX-2 on colorectal cancer cells alone and in combination with a promising new multi-targeted kinase inhibitor E7080. The HT29 colorectal cancer cell line was used. Real time cell analysis (xCELLigence system) was conducted to determine effects on colorectal cell proliferation, angiogenesis was assessed with a chorioallantoic membrane model and apoptosis was determined with annexin V staining. We found that DuP-697 alone exerted antiproliferative, antiangiogenic and apoptotic effects on HT29 colorectal cancer cells. For the antiproliferative effect the half maximum inhibition concentration ($IC_{50
Bortezomib-resistant myeloma cells contain increased proteolytic processing capacity, including upregulation of the β2 proteasome activity not targeted by bortezomib.20 We hypothesized that β2 proteasome activity contributes to bortezomib resistance and may, therefore, represent a rational target for the treatment of proteasome inhibitor-resistant myeloma.. We here describe the effect of LU-102, the first β2/β2i-selective proteasome inhibitor available for pre-clinical studies in myeloma, on bortezomib- and carfilzomib-resistant myeloma cells. Selective elimination of β2 proteasome activity alone was not sufficient to induce a meaningful cytotoxic effect in bortezomib- or carfilzomib-resistant myeloma cells. However, the combination of LU-102 with bortezomib or carfilzomib was highly potent to overcome bortezomib- or carfilzomib-resistance. This was observed not only in a proteasome inhibitor-adapted myeloma cell line model that mirrors several of the biological features of bortezomib ...
Lactacystin is a Streptomyces metabolite that inhibits cell cycle progression and induces neurite outgrowth in a murine neuroblastoma cell line. Tritium-labeled lactacystin was used to identify the 20S proteasome as its specific cellular target. Three distinct peptidase activities of this enzyme complex (trypsin-like, chymotrypsin-like, and peptidylglutamyl-peptide hydrolyzing activities) were inhibited by lactacystin, the first two irreversibly and all at different rates. None of five other proteases were inhibited, and the ability of lactacystin analogs to inhibit cell cycle progression and induce neurite outgrowth correlated with their ability to inhibit the proteasome. Lactacystin appears to modify covalently the highly conserved amino-terminal threonine of the mammalian proteasome subunit X (also called MB1), a close homolog of the LMP7 proteasome subunit encoded by the major histocompatibility complex. This threonine residue may therefore have a catalytic role, and subunit X/MB1 may be a ...
Single agent of proteasome inhibitor resulted in significant responses in leukemic cells and the combination of proteasome inhibitors and other chemotherapeutic drugs enhanced its antitumoral efficacy [3, 33-37]. Initially, the experiments were planned to test whether resveratrol could sensitized K562 cells to the anticancer actions of proteasome inhibitors. To our surprise, resveratrol did not promote, but rather attenuated the apoptotic effects of MG132 in cultured K562 cells. We further extended our investigation using a panel of leukemic cells and found that resveratrol also attenuated the cytotoxic actions of MG132 in NB4, U937, Raji and Daudi cells. Furthermore, resveratrol also compromised the apoptotic effects of other three structurally different proteasome inhibitors, PSI, epoxomicin and lactacystin. This was consistent with the previous study that resveratrol exerted its protective effects against proteasome inhibitor-induced cellular damages in human skeletal myotubes [38]. ...
Apoptosis triggered through the intrinsic pathway by radiation and anti-neoplastic drugs is initiated by the activation of caspase-9. To elucidate control mechanisms in this pathway we used a range of synthetic and natural reagents. The inhibitory potency of acetyl-Asp-Glu-Val-Asp-aldehyde (Ac-DEVD-CHO), benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone (Z-VAD-FMK) and the endogenous caspase inhibitor X-chromosome-linked inhibitor of apoptosis protein (XIAP) against recombinant caspase-9 were predictive of the efficacy of these compounds in a cell-free system. However, the viral proteins CrmA and p35, although potent inhibitors of recombinant caspase-9, had almost no ability to block caspase-9 in this system. These findings were also mirrored in cell expression studies. We hypothesize that the viral inhibitors CrmA and p35 are excluded from reacting productively with the natural form of active caspase-9 in vivo, making the potency of inhibitors highly context-dependent. This is supported by ...
Metacaspases are novel cysteine proteases found in apicomplexan whose function is poorly understood. Our earlier studies on Plasmodium falciparum metacaspase-2 (PfMCA-2) revealed that the caspase inhibitor, Z-FA-FMK efficiently inhibited PfMCA-2 activity and, expression, and significantly blocked in vitro progression of the parasite developmental cycle via apoptosis-like parasite death. Building on these findings, we synthesized a set of novel inhibitors based on structural modification of Z-FA-FMK with the amides of piperic acid and investigated their effect on PfMCA-2. One of these analogues, SS-5, specifically inhibited the activity and expression of PfMCA-2. The activities of some other known malarial proteases (falcipains, plasmepsins, & vivapain), and human cathepsins-B, D and L, and caspase-3 and -7 were not inhibited by SS-5. SS-5 blocked the development of P. falciparumin vitro (IC50 1µM) and caused prominent morphological distortions. Incubation with SS-5 led to persistent parasite ...
Malignant pleural mesothelioma (MPM), caused mainly by occupational or environmental exposure to asbestos, is an aggressive malignancy with a very poor prognosis. The general resistance of MPM to current therapeutic modalities and an ongoing increase in the incidence of MPM demonstrate the need for new treatments for this deadly disease. Proteasome inhibitors have emerged as a category of promisin
Members of the cathepsin family of cysteine proteases are gaining interest as potential imaging biomarkers and drug targets due to their multifunctional roles in a range of diseases such as cancer, asthma and arthritis ...
context: it has been reported that the equilibrium between the erythrocyte protease calpain i and its physiological inhibitor calpastatin is disrupted in patients with essential hypertension. objective: to investigate the activity of non-purified calpain i...
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Caspase 3 (Apopain or Cysteine Protease CPP32 or Protein Yama or SREBP Cleavage Activity 1 or CASP3 or EC 3.4.22.56) - Pipeline Review, H1 2017 Size and Share Published in 2017-05-30 Available for US$ 3500 at Researchmoz.us
Sigma-Aldrich offers Sigma-A6060, Calpain Inhibitor II for your research needs. Find product specific information including CAS, MSDS, protocols and references.
Proteases are one of the largest and best-characterized families of enzymes in the human proteome. Unfortunately, the understanding of protease function in the context of complex proteolytic cascades remains in its infancy. One major reason for this gap in understanding is the lack of technologies t …
A number of studies have now been published describing the effects of PI ingestion on adult worker honeybees in terms of toxicity and changes in bee gut protease activity levels.14-17 There has also been some unpublished work carried out on the effects of PI ingestion on olfactory learning behavior, which is a significant component of foraging behavior in adult bees.18,19 However there have been no published studies of the direct effects of PIs on larvae or reproductive adult bees, or on their.... ...
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FIGURE 4. XPB is essential to maintain proper cellular C1D protein level in hamster cells after UV irradiation in CHO cells. A, 27-1 cells stably expressing Flag-tagged C1D were irradiated at 4, 10, or 40 J/m2 in the absence or presence of 10 μmol/L of the proteasome inhibitor MG132. Cells were collected at the indicated time points after irradiation and prepared for anti-Flag Western blotting. B, 27-1 cells were exposed to 40 J/m2 UV irradiation, which caused a significant decrease in C1D protein level as shown in A. Total RNAs were extracted at the indicated time points for RT-PCR of C1D and GAPDH. C, stable C1D-expressing 27-1 cells were irradiated with 40 J/m2 UV and collected at the indicated time points. In the case of the sample in lane 8, cells were preincubated in cultural medium containing 10 μmol/L MG132 for 2 h. After irradiation, cells were refed with medium supplemented with 10 μmol/L MG132 and cultured for another 30 min. The cell lysates were immunoprecipitated with anti-Flag ...
Cysteine protease is an enzyme for single site digestion of antibodies in the hinge region. Incubation for one hour at 37°C under reducing conditions is enough for cyste
Badari Pulavarty ,[email protected], wrote: , , Andi, , , I noticed these on my AMD64 box earlier. Just a warning or anything , to be concerned about ? What happened with this one? Looks like a bug in the vesafb code. Do we know if it is fixed in 2.6.13-rc4? (Badari is on leave - could one of the fbdev developers please help out?) Thanks. , Thanks, , Badari , , NET: Registered protocol family 16 , PCI: Using configuration type 1 , mtrr: v2.0 (20020519) , ACPI: Subsystem revision 20050309 , ACPI: Interpreter enabled , ACPI: Using IOAPIC for interrupt routing , ACPI: PCI Root Bridge [PCI0] (0000:00) , PCI: Probing PCI hardware (bus 00) , ACPI: PCI Interrupt Link [LNKA] (IRQs 3 *5 10 11) , ACPI: PCI Interrupt Link [LNKB] (IRQs 3 5 *10 11) , ACPI: PCI Interrupt Link [LNKC] (IRQs 3 5 10 *11) , ACPI: PCI Interrupt Link [LNKD] (IRQs 3 5 10 *11) , ACPI: PCI Root Bridge [PCI1] (0000:08) , PCI: Probing PCI hardware (bus 08) , SCSI subsystem initialized , PCI: Using ACPI for IRQ routing , PCI: If a device ...
Old Synopsis: hw.acpi.thermal.tz0.temperature shows strange value New Synopsis: [acpi] hw.acpi.thermal.tz0.temperature shows strange value Responsible-Changed-From-To: freebsd-bugs-,freebsd-acpi Responsible-Changed-By: linimon Responsible-Changed-When: Fri Jan 20 09:00:34 UTC 2012 Responsible-Changed-Why: Over to maintainer(s). http://www.freebsd.org/cgi/query-pr.cgi?pr=164329 ...
BioAssay record AID 750162 submitted by ChEMBL: Inhibition of human 20S proteasome chymotrypsin like activity using Suc-Leu-Leu-Val-Tyr-AMC as substrate measured over 10 mins by fluorescence assay.
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A family of calcium-dependent proteolytic enzymes, that are classified as non-lysosomal cysteine proteases. The enzyme can selectively cleave proteins in response to signaling (calcium signals) thought to be involved in cytoskeletal changes, cell cycle, gene expression and apoptotic cell death. Calpain 1 (micro-calpain) and 2 (m-calpain), are ubiquitously expressed and their activity is inhibited by calpastatin. PMID: 12843408 ...
2A4O: Dual Modes of Modification of Hepatitis A Virus 3C Protease by a Serine-derived beta-Lactone: Selective Crystallization and Formation of a Functional Catalytic Triad in the Active Site
Complexes of gold( I) have long been used to treat rheumatoid arthritis although the precise biological targets of gold are not well understood. One intriguing therapeutic target of Au( I) is the cathepsin family of lysosomal cysteine proteases. Here, we present the inhibition of cathepsin B by a known Au( I)-based drug and a series of derivatives. The complexes investigated were reversible, competitive inhibitors with IC50 values ranging from 0.3 to 250 mu M, depending on the substituents around the Au( I). ...
Calpain II was purified to apparent homogeneity from bovine neural retinas. It was found to be biochemically similar to brain calpain II, purified by the same procedure, with respect to: subunit mobility in SDS-polyacrylamide gel electrophoresis; Ca2+ sensitivity; inhibition by calpeptin and other cysteine protease inhibitors; and optimal pH. Semithin cryosections were immuno-labeled with antibodies specific for the catalytic subunit of calpain II. Calpain II was detected in most layers of the retina, with the most pronounced label present in the plexiform layers (synaptic regions) and the photoreceptor outer segments. In dark-adapted retinas, the label was distributed throughout the outer segments. In light-adapted retinas, outer segment labeling was concentrated in the connecting cilium, and the inner segments were labeled. A partially pure preparation of calpain II from isolated rod outer segments was found to have the same biochemical characteristics as calpain II prepared in the same way ...
TY - JOUR. T1 - Cloning and sequencing of the gene encoding a novel lysine-specific cysteine proteinase (Lys-Gingipain) in porphyromonas gingivalis. T2 - Structural relationship with the arginine-specific cysteine proteinase (Arg-Gingipain). AU - Okamoto, Kuniaki. AU - Kadowaki, Tomoko. AU - Nakayama, Koji. AU - Yamamoto, Kenji. PY - 1996. Y1 - 1996. N2 - Lys-gingipain (KGP), so termed due to its peptide cleavage specificity for lysine residues, is a cysteine proteinase produced by the Gram-negative anaerobic bacterium Porphyromonas gingivalis. Mixed oligonucleotide primers designed from the NH2-terminal sequence of the purified enzyme were used to clone the KGP-encoding gene (kgp) from the organism. The nucleotide sequence of kgp had a 5,169-bp open reading frame encoding 1,723 amino acids with a calculated molecular mass of 218 kDa. As the extracellular mature enzyme had an apparent molecular mass of 51 kDa in gels, the precursor of KGP was found to comprise at least four domains, the signal ...
Lenarcic B, Kos J, Dolenc I, Lucovnik P, Krizaj I, Turk V (July 1988). "Cathepsin D inactivates cysteine proteinase inhibitors ... This proteinase, which is a member of the peptidase A1 family, has a specificity similar to but narrower than that of pepsin A ... Chao J, Miao RQ, Chen V, Chen LM, Chao L (January 2001). "Novel roles of kallistatin, a specific tissue kallikrein inhibitor, ... Umezawa H, Aoyagi T, Morishima H, Matsuzaki M, Hamada M (May 1970). "Pepstatin, a new pepsin inhibitor produced by ...
doi:10.1016/0014-5793(91)80090-p. Turk V. & W. Bode (1991). "The cystatins: protein inhibitors of cysteine proteinases". FEBS ... Derived from the cysteine protease inhibitor family of cystatins, which function in nature as cysteine protease inhibitors, ... Specific cysteine residues were introduced to the protein to allow thiol chemistry to uniformally orient Affimer proteins on a ... Affimer reagents that inhibit protein-protein interactions can also be produced with the potential to express these inhibitors ...
The protein encoded by this gene is a lysosomal cysteine proteinase important in the overall degradation of lysosomal proteins ... Järvinen M, Rinne A (1983). "Human spleen cysteineproteinase inhibitor. Purification, fractionation into isoelectric variants ... Fuchs R, Gassen HG (1990). "Nucleotide sequence of human preprocathepsin H, a lysosomal cysteine proteinase". Nucleic Acids Res ... in the inhibition of cysteine proteinases". Protein Sci. 10 (9): 1729-38. doi:10.1110/ps.11901. PMC 2253190 . PMID 11514663. ...
Turk V, Bode W (1991). "The cystatins: protein inhibitors of cysteine proteinases". FEBS Lett. 285 (2): 213-9. doi:10.1016/0014 ... Ritonja A, Machleidt W, Barrett AJ (1985). "Amino acid sequence of the intracellular cysteine proteinase inhibitor cystatin B ... Kos J, Lah TT (1998). "Cysteine proteinases and their endogenous inhibitors: target proteins for prognosis, diagnosis and ... 1988). "Cathepsin D inactivates cysteine proteinase inhibitors, cystatins". Biochem. Biophys. Res. Commun. 154 (2): 765-72. doi ...
"Protein inhibitors of cysteine proteinases. II. Primary structure of stefin, a cytosolic protein inhibitor of cysteine ... Turk V, Bode W (July 1991). "The cystatins: protein inhibitors of cysteine proteinases". FEBS Letters. 285 (2): 213-9. doi: ... The cystatins are a family of cysteine protease inhibitors which share a sequence homology and a common tertiary structure of ... van Wyk SG, Du Plessis M, Cullis CA, Kunert KJ, Vorster BJ (November 2014). "cysteine protease and cystatin expression and ...
1984). "Protein inhibitors of cysteine proteinases. III. Amino-acid sequence of cystatin from chicken egg white". Hoppe- ... The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions, ... Isemura S, Saitoh E, Sanada K (1988). "Characterization and amino acid sequence of a new acidic cysteine proteinase inhibitor ( ... Saitoh E, Kim HS, Smithies O, Maeda N (1988). "Human cysteine-proteinase inhibitors: nucleotide sequence analysis of three ...
1984). "Protein inhibitors of cysteine proteinases. II. Primary structure of stefin, a cytosolic protein inhibitor of cysteine ... 1991). "Mapping of the gene for human cysteine proteinase inhibitor stefin A, STF1, to chromosome 3cen-q21". Genomics. 9 (1): ... Kos J, Lah TT (1998). "Cysteine proteinases and their endogenous inhibitors: target proteins for prognosis, diagnosis and ... 1995). "Expression of acid cysteine proteinase inhibitor (ACPI) in the normal human prostate, benign prostatic hyperplasia and ...
Mlinarič, A.; Kreft, S.; Umek, A.; Štrukelj, B.; Popovič, T. (2000). "Cysteine proteinase inhibitors screening of fungal ... An extract of Gleophyllum odoratum exhibits high inhibitory activity on thrombin and trypsin as well as cysteine protease. ... "Screening for selective thrombin inhibitors in mushrooms". Blood Coagulation and Fibrinolysis. 12 (2): 123-8. doi:10.1097/ ...
"Novel cysteine proteinase inhibitors homologous to the proregions of cysteine proteinases". Curr Protein Pept Sci. 3 (2): 231- ... Papain, also known as papaya proteinase I, is a cysteine protease (EC 3.4.22.2) enzyme present in papaya (Carica papaya) and ... Papain-like cysteine proteinases are essentially synthesised as inactive proenzymes (zymogens) with N-terminal propeptide ... This cysteine then performs a nucleophilic attack on the carbonyl carbon of a peptide backbone. This forms a covalent acyl- ...
HMWK is a strong inhibitor of cysteine proteinases. Responsible for this activity are domains 2 and 3 on its heavy chain. The ... "Human high molecular weight kininogen as a thiol proteinase inhibitor: presence of the entire inhibition capacity in the native ... The domains contain the following functional sites: Domain 1 - calcium binding Domain 2 - cysteine protease inhibition Domain 3 ... cysteine protease inhibition; platelet and endothelial cell binding Domain 4 - bradykinin generation Domain 5 - heparin and ...
The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions. ... 1991). "Structure and expression of the gene encoding cystatin D, a novel human cysteine proteinase inhibitor". J. Biol. Chem. ... 1985). "Cystatin S: a cysteine proteinase inhibitor of human saliva". J. Biochem. 96 (4): 1311-4. PMID 6394600. Isemura S, ... This gene is located in the cystatin locus and encodes a type 2 salivary cysteine peptidase inhibitor. The protein is an S-type ...
The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions, ... This gene is located in the cystatin locus and encodes a cysteine proteinase inhibitor found in saliva, tears, urine, and ... Isemura S, Saitoh E, Sanada K (1986). "Characterization of a new cysteine proteinase inhibitor of human saliva, cystatin SN, ... Saitoh E, Kim HS, Smithies O, Maeda N (1988). "Human cysteine-proteinase inhibitors: nucleotide sequence analysis of three ...
"The salivary lipocalin von Ebner's gland protein is a cysteine proteinase inhibitor". J. Biol. Chem. 272 (3): 1837-41. doi: ... This protein may bind hydrophobic ligands and inhibit cysteine proteinases. It may also play a role in taste reception. GRCh38 ... 2002). "The N-terminal part of recombinant human tear lipocalin/von Ebner's gland protein confers cysteine proteinase ...
The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions. ... "Cystatin F is a glycosylated human low molecular weight cysteine proteinase inhibitor". J Biol Chem. 273 (38): 24797-804. doi: ... Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory ... This gene encodes a glycosylated cysteine protease inhibitor with a putative role in immune regulation through inhibition of a ...
One such method is the creation of transgene plants using proteins such as cysteine proteinase inhibitors, which would inhibit ... "Transgene Expression of Rice Cysteine Proteinase Inhibitors for the Development of Resistance against Sweetpotato Feathery ... "Structure of the autocatalytic cysteine protease domain of potyvirus helper-component proteinase". Journal of Biological ... The encoded genes are P1, HC-Pro (helper component proteinase), P3, 6K1, CI, 6K2, NIa, NIb, and the coat protein cistron, which ...
Strojan P, Oblak I, Svetic B, Smid L, Kos J (May 2004). "Cysteine proteinase inhibitor cystatin C in squamous cell carcinoma of ... The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions, ... Kos J, Krasovec M, Cimerman N, Nielsen HJ, Christensen IJ, Brünner N (February 2000). "Cysteine proteinase inhibitors stefin A ... a potent inhibitor of cysteine proteinases, is elevated in asthmatic patients". Clin. Chim. Acta. 300 (1-2): 83-95. doi:10.1016 ...
The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions. ... a novel human cysteine proteinase inhibitor". J Biol Chem. 266 (30): 20538-43. PMID 1939105. "Entrez Gene: CST5 cystatin D". ... Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory ... a cysteine peptidase inhibitor with restricted inhibition profile". J. Biol. Chem. 280 (18): 18221-8. doi:10.1074/jbc. ...
The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions, ... a novel cysteine proteinase inhibitor, down-regulated in breast cancer". J. Biol. Chem. 272 (2): 903-10. doi:10.1074/jbc.272.2. ... "Cystatin E is a novel human cysteine proteinase inhibitor with structural resemblance to family 2 cystatins". J Biol Chem. 272 ... "Assignment of a novel cysteine proteinase inhibitor (CST6) to 11q13 by fluorescence in situ hybridization". Cytogenet Cell ...
"Squamous cell carcinoma antigen is a potent inhibitor of cysteine proteinase cathepsin L". FEBS Letters. 359 (1): 78-80. doi: ... Some serpins are both protease inhibitors and perform additional roles. For example, the nuclear cysteine protease inhibitor ... "The serine proteinase inhibitor (serpin) plasminogen activation inhibitor type 2 protects against viral cytopathic effects by ... "The intracellular serpin proteinase inhibitor 6 is expressed in monocytes and granulocytes and is a potent inhibitor of the ...
Cysteine proteinase inhibitors screening of fungal species growing in Slovenia]. Acta Pharmaceutica (in Slovenian). 50 (1): 39- ... Cortinarius violaceus extract demonstrates an inhibitory activity against cysteine protease. Fungi portal List of Cortinarius ...
Tomatoes resistant to a root knot nematode have been created by inserting a cysteine proteinase inhibitor gene from taro. A ... the prosystemin gene in transgenic tomato plants generates a systemic signal that constitutively induces proteinase inhibitor ...
The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions. ... Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory ... The MEROPS online database for peptidases and their inhibitors: I25.027 Brown WM, Dziegielewska KM (1997). "Friends and ...
The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions. ... Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory ...
... which bind to the cysteine active site and block substrate access. The major kiwifruit cysteine proteinase inhibitor KCPI1 has ... As a cysteine protease, peptidase 1 functions by cleaving other mite proteases in a biochemical cascade that results in the ... By the end of the decade, it was suspected that Der p 1 was a cysteine protease when its structure showed similarities to that ... This enzyme exhibits cysteine protease activity with broad endopeptidase specificity. The various forms of peptidase 1 ...
... and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L". J. Biochem. 201 (1): 189-98. doi: ... The low toxic effects of the inhibitor, in addition to its effective mechanism of action, makes E-64 a potential template for ... E-64 is an epoxide which can irreversibly inhibit a wide range of cysteine peptidases. The compound was first isolated and ... The covalent attachment of E-64 to the active site cysteine occurs via nucleophillic attack from the thiol group of the ...
"Simple modifications of the serpin reactive site loop convert SCCA2 into a cysteine proteinase inhibitor: a critical role for ... "Cross-class inhibition of the cysteine proteinases cathepsins K, L, and S by the serpin squamous cell carcinoma antigen 1: a ... "Phylogenetic conservation of cysteine proteinases. Cloning and expression of a cDNA coding for human cathepsin S". The Journal ... "High-molecular-weight kininogen binds two molecules of cysteine proteinases with different rate constants". FEBS Letters. 391 ( ...
Tomatoes resistant to a root knot nematode have been created by inserting a cysteine proteinase inhibitor gene from taro.[26] A ... the prosystemin gene in transgenic tomato plants generates a systemic signal that constitutively induces proteinase inhibitor ...
The cathelicidin family shares primary sequence homology with the cystatin family of cysteine proteinase inhibitors, although ... is cysteine-free and expressed in bone marrow and testis". Proceedings of the National Academy of Sciences of the United States ...
Cysteine proteinase inhibitors decrease articular cartilage and bone destruction in chronic inflammatory arthritis.. Esser RE1 ... These studies suggest that cysteine proteinase inhibitors may limit tissue destruction in diseases such as rheumatoid arthritis ... Oral administration of the fluoroketones reduced tissue cysteine proteinase activity by up to 77%. In addition, fluoroketone ... on tissue cysteine proteinase activity, and on cartilage and bone destruction in experimental arthritis. ...
Bombyx cysteine proteinase inhibitor (BCPI) from the hemolymph of Bombyx mori; alpha and beta are two forms differing only in ... Bombyx cysteine proteinase inhibitor. Subscribe to New Research on Bombyx cysteine proteinase inhibitor ... Bombyx cysteine proteinase inhibitor (BCPI) from the hemolymph of Bombyx mori; alpha and beta are two forms differing only in ... cysteine proteinase inhibitor, Bombyx; BCPI-alpha protein, Bombyx; BCPI-beta protein, Bombyx ...
Cysteine Proteinase Inhibitors in Murine Cysticercosis. Salman Baig, Raymond T. Damian, Jorge Morales-Montor, Rupal Thazhath, ... Cysteine Proteinase Inhibitors in Murine Cysticercosis. Salman Baig, Raymond T. Damian, Jorge Morales-Montor, Rupal Thazhath, ... Cysteine Proteinase Inhibitors in Murine Cysticercosis. Salman Baig, Raymond T. Damian, Jorge Morales-Montor, Rupal Thazhath, ... Cysteine Proteinase Inhibitors in Murine Cysticercosis Message Subject (Your Name) has forwarded a page to you from ...
Cystatin E is a novel human cysteine proteinase inhibitor with structural resemblance to family 2 cystatins.. [J Ni, M ... Cystatin E is thus a functional cysteine proteinase inhibitor despite relatively low amino acid sequence similarities with ... including four cysteine residues and motifs of importance for the inhibitory activity of Family 2 cystatins like cystatin C. ...
Expression of an engineered cysteine proteinase inhibitor (Oryzacystatin-IΔD86) for nematode resistance in transgenic rice ... Expression of an engineered cysteine proteinase inhibitor (Oryzacystatin-IΔD86) for nematode resistance in transgenic rice ... Twenty-five transformed clones containing genes coding for an engineered cysteine proteinase inhibitor (oryzacystatin-IΔD86, OC ... Expression of an engineered cysteine proteinase inhibitor (Oryzacystatin-IΔD86) for nematode resistance in transgenic rice ...
Enzyme inhibitor, Cysteine proteinase, Cerebral hemorrhage, Cystatin C, cDNA cloning, Nucleotide sequence. in FEBS Letters. ... indicating an extracellular function of the inhibitor. The deduced protein sequence confirms the protein sequence of cystatin C ... indicating an extracellular function of the inhibitor. The deduced protein sequence confirms the protein sequence of cystatin C ...
"Effects of abscisic acid treatment on the expression of cysteine proteinase gene and enzyme inhibitor during wheat cold ... Effects of abscisic acid treatment on the expression of cysteine proteinase gene and enzyme inhibitor during wheat cold ... Effects of abscisic acid treatment on the expression of cysteine proteinase gene and enzyme inhibitor during wheat cold ... The effects of exogenous ABA on the expression of the cysteine proteinase (CP) gene and its inhibitor cystatin (WC3) in the ...
"An extracellular insoluble inhibitor of cysteine proteinases in cell cultures and seeds of carrot, Plant Molecular Biology" on ... Protein inhibitors of cysteine proteinases. II. Primary structure of stefin, a cytosolic inhibitor of cysteine proteinases from ... Inhibition of digestive proteinases of stored grain coleoptera by oryzacystatin, a cysteine proteinase inhibitor from rice seed ... An extracellular insoluble inhibitor of cysteine proteinases in cell cultures and seeds of carrot. Ojima, Akiko; Shiota, Hajime ...
... Ayesa, Susana Stockholm ... The second part of the thesis describes the design and synthesis of three classes of protease inhibitors targeting the cysteine ... 1. Design and Synthesis of Amine Building Blocks and Protease Inhibitors. Open this publication in new window or tab ,,Design ... This work resulted in the discovery of highly potent and selective inhibitors of cathepsin S. Two parallel solid-phase ...
Cysteine proteinaseCysteine proteinase inhibitorProteinase activityCoffee. Background. Cysteine proteinases (CP) represent a ... Two cysteine proteinase (CP) and four cysteine proteinase inhibitor (CPI) gene sequences have been identified in coffee with ... Several cysteine proteinase and cysteine proteinase inhibitor genes with strong, relatively specific expression during coffee ... Several cysteine proteinase and cysteine proteinase inhibitor genes with strong, relatively specific expression during coffee ...
The last decade has witnessed enormous progress of protein inhibitors of cysteine proteinases concerning their structures, ... The last decade has witnessed enormous progress of protein inhibitors of cysteine proteinases concerning their structures, ... cysteine proteinases and their inhibitors which is fundamentally different from the standard mechanism for serine proteinases ...
... is an analog of E-64 and inhibitor of cysteine proteinases. [1],br /,The cysteine proteinases, of which Cathepsins B and H and ... is an analog of E-64 and inhibitor of cysteine proteinases. [1]. The cysteine proteinases, of which Cathepsins B and H and ... E-64-c showed promise of acting as class-specific inhibitors for the cysteine proteinases. X-ray diffraction shows that E-64-c ... L-trans-Epoxysuccinyl-leucylamido (4-guanidino) butane (E-64) and its analogues as inhibitors of cysteine proteinases including ...
Summary: Cystatin C is the best known extracellular endogenous cysteine proteinase inhibitor and has been studied as a possible ...
The cysteine proteinase inhibitor (CysPI) and polyphenol oxidase F/B (PPOF/B) were selected as JA-marker genes because they are ... CysPI, cysteine proteinase inhibitor; PPOF/B, polyphenol oxidase F/B; PR-1(P4), pathogenesis-related protein 1 (P4). ... CysPI, cysteine proteinase inhibitor; PPOF/B, polyphenol oxidase F/B; PR-1(P4), pathogenesis-related protein 1 (P4). ... 2005) A hybrid, broad-spectrum inhibitor of Colorado potato beetle aspartate and cysteine digestive proteinases. Arch Insect ...
Caspase Inhibitors. Cysteine Proteinase Inhibitors. Protease Inhibitors. Enzyme Inhibitors. Molecular Mechanisms of ... The primary objective of this protocol is to assess the safety of the IDN-6556 caspase inhibitor in adult Type 1 diabetic ... To assess the safety of the IDN-6556 caspase inhibitor in adult Type 1 diabetic participants receiving their first islet ... 14 day oral treatment of the investigational caspase inhibitor drug IDN-6556 following first islet transplant at 50mg twice ...
Cysteine Proteinase Inhibitors. Protease Inhibitors. Enzyme Inhibitors. Molecular Mechanisms of Pharmacological Action. ...
Cysteine Proteinase Inhibitors. Protease Inhibitors. Enzyme Inhibitors. Molecular Mechanisms of Pharmacological Action. ...
Caspase Inhibitors. Cysteine Proteinase Inhibitors. Protease Inhibitors. Enzyme Inhibitors. Molecular Mechanisms of ... Emricasan, a Caspase Inhibitor, for Treatment of Subjects With Decompensated NASH Cirrhosis (ENCORE-LF). The safety and ... A Multicenter, Randomized, Double-Blind, Placebo-Controlled Trial of Emricasan, an Oral Caspase Inhibitor, in Subjects With ... Current use of medications that are considered inhibitors of organic anion transporting polypeptide OATP1B1 and OATP1B3 ...
Lenarcic B, Kos J, Dolenc I, Lucovnik P, Krizaj I, Turk V (July 1988). "Cathepsin D inactivates cysteine proteinase inhibitors ... cysteine-type endopeptidase activity. • aspartic-type endopeptidase activity. Cellular component. • lysosomal lumen. • ... The MEROPS online database for peptidases and their inhibitors: A01.009. *GeneReviews/NIH/NCBI/UW entry on Neuronal Ceroid- ... Chao J, Miao RQ, Chen V, Chen LM, Chao L (January 2001). "Novel roles of kallistatin, a specific tissue kallikrein inhibitor, ...
Serine (or cysteine) proteinase inhibitor SERPINB2** 0.358 0.428 - 205623_at Aldehyde dehydrogenase 3 family ALDH3A1** 0.325 ... Tissue inhibitor of metalloproteinase 3 TIMP3** 2.419 2.498 - 201601_x_at IFN induced transmembrane protein 1 (9-27) IFITM1**† ...
A Novel Class of Cysteine Protease Inhibitors: Solution Structure of Staphostatin a from Staphylococcus Aureus ... of staphostatin A form Staphylococcus aureus confirms the discovery of a novel class of cysteine proteinase inhibitors.. *DOI: ...
Cysteine proteinase inhibitors from soy seeds]. Biokhimiia 1995;60:118-23. View abstract. ... Potato tuber protein proteinase inhibitors belonging to the Kunitz soybean inhibitor family. Biochemistry (Mosc) 1997;62:1367- ...
The saturation density of NIH3T3 cells was increased by repeated treatment with cysteine proteinase-specific inhibitors such as ... several potent cysteine proteinase inhibitors have been tested for whether they show similar biological activities. ... Taken together, the cysteine proteinase-specific inhibitory activity of p21 may be important for its biological activities. ... inhibits cysteine proteinases. Because p21 transforms NIH3T3 cells and also induces differentiation of PC12 pheochromocytoma ...
Angiotensinogen (serine (or cysteine) proteinase inhibitor,. clade a. patient:. 3. 18ADEE16G02.1625.1625.2.dta. ... gi,125000,sp,P19823,: inter-alpha-trypsin inhibitor heavy chain. h2 precursor (iti heavy chain h2) hyaluronan-associated ...
R) Cystatin and cysteine proteinase inhibitors. See U.S. Pat. No. 7,205,453. ... Some examples of compositions are insecticides, fungicides, pesticides, antimicrobials, germination inhibitors, germination ... ACCase inhibitor-encoding genes). See, for example, U.S. Pat. No. 4,940,835 to Shah et al., which discloses the nucleotide ... germination inhibitors and enhancers, nutrients, plant growth regulators and activators, bactericides, nematicides, avicides ...
  • To determine the effects of peptidyl fluoromethyl ketones on the in vitro activity of purified cathepsins B and L, on tissue cysteine proteinase activity, and on cartilage and bone destruction in experimental arthritis. (nih.gov)
  • The effects of the fluoroketones on cathepsins B and L in vitro and the effects of oral administration of fluoroketones on ex vivo cysteine proteinase activity in tissue homogenates were determined by measuring the inhibition of fluorogenic substrate cleavage. (nih.gov)
  • All of the fluoroketones tested were potent inhibitors of purified cathepsins B and L activity. (nih.gov)
  • The cysteine proteinases, of which Cathepsins B and H and cathepsin L exist in mammals, contain an essential highly reactive thiol group, and therefore are inhibited by thiol-blocking reagents such as iodoacetate and mercuribenzoate. (apexbt.com)
  • 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)
  • This is an Investigator Initiated, Phase I/II study, where Type 1 diabetic participants will receive a 14 day oral treatment of the investigational caspase inhibitor drug IDN-6556 following their first islet transplant. (clinicaltrials.gov)
  • The primary objective of this protocol is to assess the safety of the IDN-6556 caspase inhibitor in adult Type 1 diabetic participants receiving their first islet transplant. (clinicaltrials.gov)
  • 14 day oral treatment of the investigational caspase inhibitor drug IDN-6556 following first islet transplant at 50mg twice daily. (clinicaltrials.gov)
  • However, a broad-spectrum caspase inhibitor (z-VAD.fmk) only partially inhibited cell death although DNA degradation was completely inhibited. (biomedsearch.com)
  • We show here that the caspase inhibitor benzyloxycarbonyl (Cbz)-Val-Ala-Asp(OMe)-fluoromethylketone (zVAD) blocks proliferation, major histocompatibility complex class II expression, and blastic transformation during stimulation of peripheral blood lymphocytes. (nih.gov)
  • We specialize in small molecule inhibitors, agonists, antagonists and screening libraries! (apexbt.com)
  • Twenty-five transformed clones containing genes coding for an engineered cysteine proteinase inhibitor (oryzacystatin-IΔD86, OC-IΔD86), hygromycin resistance (aphIV) and β-glucuronidase (gusA) were recovered from the four varieties. (www.gov.uk)
  • Detailed expression analysis of the cysteine proteinase genes CcCP1 and CcCP4 in Robusta using quantitative RT-PCR showed that these transcripts accumulate primarily during grain maturation and germination/post germination. (biomedcentral.com)
  • QRT-PCR expression analysis of the four cysteine proteinase inhibitor genes in Robusta showed that CcCPI-1 is primarily expressed in developing and germinating grain and CcCPI-4 is very highly expressed during the late post germination period, as well as in mature, but not immature leaves. (biomedcentral.com)
  • Several cysteine proteinase and cysteine proteinase inhibitor genes with strong, relatively specific expression during coffee grain maturation and germination are presented. (biomedcentral.com)
  • EIP18 was found to consist of 133 amino acid residues that included a signal sequence, but it did not contain cysteine, sites for N-linked glycosylation or hydrophobic regions. (deepdyve.com)
  • vWF dimers are assembled from pairs of ˜250 kDa polypeptide subunits in the endoplasmic reticulum via disulfide bridges between cysteine residues located in the carboxy terminal regions. (freepatentsonline.com)
  • Comparative sequence and structural analysis, particularly to penicillin V acylase (MEROPS peptidase family C59) revealed a cysteine as the catalytic nucleophile as well as other conserved residues important for catalysis [ PMID: 12717035 ]. (ebi.ac.uk)
  • Inhibiting either toxopain-1 expression or specific cysteine proteinase activity significantly reduced congenital infection of chicken embryos, as determined by histopathology and by the number of parasites quantified by real-time PCR. (asm.org)
  • Specific cysteine proteinase inhibitors disrupt host cell invasion by toxoplasma tachyzoites in vitro ( 16 ). (asm.org)
  • Finally, Chapter 6 reports peptide-based HCV NS3 protease inhibitors containing a non-electrophilic allylic alcohol moiety as P1 group and also outlines efforts to incorporate this new template into low-molecular-weight drug-like molecules. (diva-portal.org)
  • A publication from the Leeds group described producing a peptide in potato to disrupt cyst nematodes, and compared the mode of action of the peptide to an acetylcholinesterase inhibitor aldicarb . (i-sis.org.uk)
  • However, the additional information document compared the synthetic peptide in the application to the anthelminic levamisole, an inhibitor of the nicotinic acetylcholinesterase receptor . (i-sis.org.uk)
  • These reagents selectively form covalent bonds with the active-site thiol of a cysteine protease, allowing direct biochemical profiling of protease activities in complex proteomes. (nih.gov)
  • Hydrolysis involves usually a catalytic triad consisting of the thiol group of the cysteine, the imidazolium ring of a histidine, and a third residue, usually asparagine or aspartic acid, to orientate and activate the imidazolium ring. (ebi.ac.uk)
  • These cells were tested in an in vitro Matrigel invasion assay with membrane-permeant and impermeant inhibitors of cathepsin B. The results, which provided direct proof for the participation of cathepsin B in matrix penetration, also yielded the unexpected finding that an intracellular form of cathepsin B was required for Matrigel invasion. (aacrjournals.org)
  • It is a non-inflammatory process, mainly mediated by (i) well known defence factors such as lysozyme and lactoferrin, (ii) specific secretory immunoglobulins A (sIgA), appropriate to surface protection, elicited by both local antigen administration and stimulation at related distal sites, and (iii) factors with cysteine proteinase inhibitor activity such as cystatin. (bmj.com)
  • An important cysteine proteinase inhibitor activity is present in tears. (bmj.com)
  • We report here an optimized solid-phase synthesis protocol that allows rapid generation of activity-based probes (ABPs) targeting a range of cysteine protease families. (nih.gov)
  • Since blocking an enzyme's activity can kill a pathogen or correct a metabolic imbalance, many drugs are enzyme inhibitors. (gentaur.com)
  • 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)
  • Serine proteinase inhibitors (serpins) finely regulate serine proteinase activity via a suicide substrate-like inhibitory mechanism. (biomedcentral.com)
  • Administration of these proteinase inhibitors also reduced the ca- and Hyp-level in blood and do not affect the activity of collagenase. (nii.ac.jp)
  • The proteinase had a higher activity with haemoglobin, but was more specific (Vmax. (biochemj.org)
  • Cysteine proteinase inhibitors regulate human and mouse osteoclastogenesis by interfering with RANK signaling. (gu.se)
  • Cysteine peptidases are often active at acidic pH and are therefore confined to acidic environments, such as the animal lysosome or plant vacuole. (ebi.ac.uk)
  • Combined gemcitabine and CHK1 inhibitor treatment induces apoptosis resistance in cancer stem cell-like cells enriched with tumor spheroids from a non-small cell lung cancer cell line. (nih.gov)
  • SSZ-induced cleavage of the U1-70K protein was inhibited by Zn2+ and by specific inhibitors of caspases 3 and 8, but not caspases 1 and 9. (tudelft.nl)