Protease in the context of "Calpain"

Proteins are essential nutrients for the human body. They are one of the constituents of body tissue and also serve as a fuel source. As fuel, proteins have the same energy density as carbohydrates: 17 kJ (4 kcal) per gram. The defining characteristic of protein from a nutritional standpoint is its amino acid composition.

Proteins are polymer chains made of amino acids linked by peptide bonds. During human digestion, proteins are broken down in the stomach into smaller polypeptide chains via hydrochloric acid and protease actions. This is crucial for the absorption of the essential amino acids that cannot be biosynthesized by the body.

A chordate (/ˈkɔːrdeɪt/ KOR-dayt) is a bilaterian animal belonging to the phylum Chordata (/kɔːrˈdeɪtə/ kor-DAY-tə). All chordates possess, at some point during their larval or adult stages, five distinctive physical characteristics (synapomorphies) that distinguish them from other taxa. These five synapomorphies are a notochord, a hollow dorsal nerve cord, an endostyle or thyroid, pharyngeal slits, and a post-anal tail.

In addition to the morphological characteristics used to define chordates, analysis of genome sequences has identified two conserved signature indels (CSIs) in their proteins: cyclophilin-like protein and inner mitochondrial membrane protease ATP23, which are exclusively shared by all vertebrates, tunicates and cephalochordates. These CSIs provide molecular means to reliably distinguish chordates from all other animals.

Proteasomes are essential protein complexes responsible for the degradation of proteins by proteolysis, a chemical reaction that breaks peptide bonds. Enzymes that help such reactions are called proteases. Proteasomes are found inside all eukaryotes and archaea, and in some bacteria.In eukaryotes, proteasomes are located both in the nucleus and in the cytoplasm. The proteasomal degradation pathway is essential for many cellular processes, including the cell cycle, the regulation of gene expression, and responses to oxidative stress. The importance of proteolytic degradation inside cells and the role of ubiquitin in proteolytic pathways was acknowledged in the award of the 2004 Nobel Prize in Chemistry to Aaron Ciechanover, Avram Hershko and Irwin Rose.

The core 20S proteasome (blue in the adjacent figure) is a cylindrical, compartmental protein complex of four stacked rings forming a central pore. Each ring is composed of seven individual proteins. The inner two rings are made of seven β subunits that contain three to seven protease active sites, within the central chamber of the complex. Access to these proteases is gated on the top of the 20S, and access is regulated by several large protein complexes, including the 19S Regulatory Particle forming the 26S Proteasome. In eukaryotes, proteins that are tagged with Ubiquitin are targeted to the 26S proteasome and is the penultimate step of the Ubiquitin Proteasome System (UPS). Proteasomes are part of a major mechanism by which cells regulate the concentration of particular proteins and degrade misfolded proteins.

Proteolysis is the breakdown of proteins into smaller polypeptides or amino acids. Protein degradation is a major regulatory mechanism of gene expression and contributes substantially to shaping mammalian proteomes. Uncatalysed, the hydrolysis of peptide bonds is extremely slow, taking hundreds of years. Proteolysis is typically catalysed by cellular enzymes called proteases, but may also occur by intra-molecular digestion.

Proteolysis in organisms serves many purposes; for example, digestive enzymes break down proteins in food to provide amino acids for the organism, while proteolytic processing of a polypeptide chain after its synthesis may be necessary for the production of an active protein. It is also important in the regulation of some physiological and cellular processes including apoptosis, as well as preventing the accumulation of unwanted or misfolded proteins in cells. Consequently, abnormality in the regulation of proteolysis can cause diseases.

Fibrin (also called Factor Ia) is a fibrous, non-globular protein involved in the clotting of blood. It is formed by the action of the protease thrombin on fibrinogen, which causes it to polymerize. The polymerized fibrin, together with platelets, forms a hemostatic plug or clot over a wound site.

When the lining of a blood vessel is broken, platelets are attracted, forming a platelet plug. These platelets have thrombin receptors on their surfaces that bind serum thrombin molecules, which in turn convert soluble fibrinogen in the serum into fibrin at the wound site. Fibrin forms long strands of tough insoluble protein that are bound to the platelets. Factor XIII completes the cross-linking of fibrin so that it hardens and contracts. The cross-linked fibrin forms a mesh atop the platelet plug that completes the clot. Fibrin was discovered by Marcello Malpighi in 1666.

Malt is any cereal grain that has been made to germinate by soaking in water and then stopped from germinating further by drying with hot air, a process known as "malting".Malted grain is used to make beer, whisky, malted milk, malt vinegar, confections such as Maltesers and Whoppers, flavored drinks such as Horlicks, Ovaltine, and Milo, and some baked goods, such as malt loaf, bagels, and Rich Tea biscuits. Malted grain that has been ground into a coarse meal is known as "sweet meal".

Malting grain develops the enzymes (α-amylase, β-amylase) required for modifying the grains' starches into various types of sugar, including monosaccharide glucose, disaccharide maltose, trisaccharide maltotriose, and higher sugars called maltodextrines. It also develops other enzymes, such as proteases, that break down the proteins in the grain into forms that can be used by yeast. The point at which the malting process is stopped affects the starch-to-enzyme ratio, and partly converted starch becomes fermentable sugars.

The complement system, also known as complement cascade, is a part of the humoral, innate immune system and enhances (complements) the ability of antibodies and phagocytic cells to clear microbes and damaged cells from an organism, promote inflammation, and attack the pathogen's cell membrane. Despite being part of the innate immune system, the complement system can be recruited and brought into action by antibodies generated by the adaptive immune system.

The complement system consists of a number of small, inactive, liver synthesized protein precursors circulating in the blood. When stimulated by one of several triggers, proteases in the system cleave specific proteins to release cytokines and initiate an amplifying cascade of further cleavages. The end result of this complement activation or complement fixation cascade is stimulation of phagocytes to clear foreign and damaged material, inflammation to attract additional phagocytes, and activation of the cell-killing membrane attack complex. About 50 proteins and protein fragments make up the complement system, including plasma proteins, and cell membrane receptors. They account for about 10% of the globulin fraction of blood serum.

Rennet (/ˈrɛnɪt/) is a complex set of enzymes produced in the stomachs of ruminant mammals. Chymosin, its key component, is a protease enzyme that curdles the casein in milk. In addition to chymosin, rennet contains other enzymes, such as pepsin and a lipase.

Rennet has traditionally been used to separate milk into solid curds and liquid whey, used in the production of cheeses. Rennet from calves has become less common for this use, to the point that less than 5% of cheese in the United States is made using animal rennet today. Most cheese is now made using chymosin derived from bacterial sources.

An aortic aneurysm is an enlargement (dilatation) of the aorta to greater than 1.5 times normal size. Typically, there are no symptoms except when the aneurysm dissects or ruptures, which causes sudden, severe pain in the abdomen and lower back.

The cause remains an area of active research. Known causes include trauma, infection, and inflammatory disorders. Risk factors include cigarette smoking, heavy alcohol consumption, advanced age, harmful patterns of high cholesterol in the blood, high blood pressure, and coronary artery disease. The pathophysiology of the disease is related to an initial arterial insult causing a cascade of inflammation and extracellular matrix protein breakdown by proteinases leading to arterial wall weakening. They are most commonly located in the abdominal aorta, but can also be located in the thoracic aorta.

Prostate-specific antigen (PSA), also known as gamma-seminoprotein or kallikrein-3 (KLK3), P-30 antigen, is a glycoprotein enzyme encoded in humans by the KLK3 gene. PSA is a member of the kallikrein-related peptidase family and is secreted by the epithelial cells of the prostate gland in men and the paraurethral glands in women.

PSA is produced for the ejaculate, where it liquefies semen in the seminal coagulum and allows sperm to swim freely. It is also believed to be instrumental in dissolving cervical mucus, allowing the entry of sperm into the uterus.

Adherent cell cultures are a type of cell culture that requires cells to be attached to a surface in order for growth to occur. Most vertebrate-derived cells (with the exception of hematopoietic cells) are anchorage dependent and require a two-dimensional monolayer to facilitate cell adhesion, spreading and replication. Cell samples can be taken from tissue explants or cell suspension cultures. Adherent cell cultures with an excess of nutrient-containing growth medium will continue to grow until they cover the available surface area. Proteases like trypsin are most commonly used to break the adhesion from the cells to the flask. Alternatively, cell scrapers can be used to mechanically break the adhesion if introducing proteases could damage the cell cultures. Unlike suspension cultures, the other main type of cell culture, adherent cultures require regular passaging performed using mechanical or enzymatic dissociation. The culture can be visualized using an inverted microscope, however the growth of adherent cultures is dependent on the available surface area. For this reason, adherent cell cultures are not commonly used to obtain a high yield of cells, instead the use of suspension cultures is preferred.

Chymosin /ˈkaɪməsɪn/ or rennin /ˈrɛnɪn/ is a protease found in rennet. It is an aspartic endopeptidase belonging to MEROPS A1 family. It is produced by newborn ruminant animals in the lining of the abomasum to curdle the milk they ingest, allowing a longer residence in the bowels and better absorption. It is widely used in the production of cheese.

Historically, chymosin was obtained by extracting it from the stomachs of slaughtered calves. Today, most commercial chymosin used in cheese production is produced recombinantly in Escherichia coli, Aspergillus niger var. awamori, and Kluyveromyces lactis.

A proteose is any of various water-soluble compounds that are produced during in-vitro or in-vivo hydrolytic breakdown of proteins a little before producing amino acids. It forms after breaking down of polypeptides by proteases such as gastric pepsin. In addition to proteoses, peptones are also formed at this stage. The difference between peptones and proteoses is that proteoses are precipitated from solution by half saturation with ammonium sulfate, while peptones don't react even with fully saturated ammonium sulfate.

The major prion protein (PrP) is encoded in the human body by the PRNP gene also known as CD230 (cluster of differentiation 230). Expression of the protein is most prominent in the nervous system but occurs in many other tissues throughout the body.

The protein can exist in multiple isoforms: the normal PrP form, and the protease-resistant form designated PrP such as the disease-causing PrP (scrapie) and an isoform located in mitochondria. The misfolded version PrP is associated with a variety of uniformly fatal neurodegenerative diseases in humans and nonhuman species. In nonhuman species these include ovine scrapie, bovine spongiform encephalopathy (BSE, mad cow disease), feline spongiform encephalopathy, transmissible mink encephalopathy (TME), exotic ungulate encephalopathy, chronic wasting disease (CWD) which affects deer; human prion diseases include Creutzfeldt–Jakob disease (CJD), fatal familial insomnia (FFI), Gerstmann–Sträussler–Scheinker syndrome (GSS), kuru, and variant Creutzfeldt–Jakob disease (vCJD). Similarities exist between kuru, thought to be due to human ingestion of diseased individuals, and vCJD, thought to be due to human ingestion of BSE-tainted cattle products.

Anaphase (from Ancient Greek ἀνα- (ana-) 'back, backward' and φάσις (phásis) 'appearance') is the stage of mitosis after the process of metaphase, when replicated chromosomes are split and the newly-copied chromosomes (daughter chromatids) are moved to opposite poles of the cell. Chromosomes also reach their overall maximum condensation in late anaphase, to help chromosome segregation and the re-formation of the nucleus.

Anaphase starts when the anaphase promoting complex marks an inhibitory chaperone called securin for destruction by ubiquitylating it. Securin is a protein which inhibits a protease known as separase. The destruction of securin unleashes separase which then breaks down cohesin, a protein responsible for holding sister chromatids together.

Broad-spectrum antivirals (BSAs) are a class of molecules or compounds, which inhibit the infection of multiple viruses from the same (intra-family BSAs) or different (inter-family BSAs) virus families. BSAs could be divided into experimental and investigational agents, and approved drugs. BSAs work by inhibiting viral proteins (such as polymerases and proteases) or by targeting host cell factors and processes exploited by different viruses during infection. As of 2021, there are 150 known BSAs in varying stages of development, effective against 78 human viruses. BSAs are potential candidates for treatment of emerging and re-emerging viruses, such as ebola, marburg, and SARS-CoV-2. Many BSAs show antiviral activity against other viruses than originally investigated (such as remdesivir and interferon alfa). Efforts in drug repurposing for SARS-CoV-2 is currently underway. A database of BSAs and viruses they inhibit could be found here (https://drugvirus.info/).