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Pepsin / ˈ p ɛ p s ɪ n / is an endopeptidase that breaks down proteins into smaller peptides and amino acids. It is one of the main digestive enzymes in the digestive systems of humans and many other animals, where it helps digest the proteins in food. Pepsin is an aspartic protease, using a catalytic aspartate in its active site. [2]
Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and is involved in digestion in humans and other animals. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes.
A1AT is a glycoprotein mainly produced in the liver by hepatocytes, [9] and, in some quantity, by enterocytes, monocytes, and macrophages. [12] In a healthy lung, it functions as an inhibitor against neutrophil elastase , [ 13 ] a neutral serine protease that controls lung elastolytic activity which stimulates mucus secretion and CXCL8 release ...
Tissue plasminogen activator (TPA) is a serine protease occurring in animals including humans. Human-identical TPA (produced industrially by genetically recombinant microorganisms) has an established medical use in the treatment of ischemic stroke: by its proteolytic activity it enables the action of another enzyme (plasmin), which breaks down the protein (fibrin) of blood clots.
Aminopeptidases are a diverse group of enzymes that play crucial roles in various biological processes, including protein digestion, cell growth, and immune response.They are classified based on their substrate specificity (strength of binding) and catalytic mechanism (means of catalyzing their reaction) into two main categories: metalloaminopeptidases and cysteine aminopeptidases.
Trypsinogen is an inactive form of trypsin, its inactive form ensures protein aspects of the body, such as the pancreas and muscles, are not broken down. It is formed in the pancreas and activated to trypsin with enteropeptidase [ 6 ] Chymotrypsinogen is the inactive form of chymotrypsin and has similar functions as trypsin.
As of 2012, there are 50 lysosomal storage diseases, and more are still being discovered. [8] [7] These disorders arise because of genetic mutations that prevent the production of certain enzymes used in the lysosomes. [7] The missing enzyme often leads to a build-up of the substrate within the body.
Liver regeneration is the process by which the liver is able to replace damaged or lost liver tissue. The liver is the only visceral organ with the capacity to regenerate. [ 1 ] [ 2 ] The liver can regenerate after partial hepatectomy or injury due to hepatotoxic agents such as certain medications, toxins, or chemicals. [ 3 ]