Trypsinogen and Trypsin; Definition, Secretion, Differences, Activation, Function скачать в хорошем качестве

Trypsinogen and Trypsin; Definition, Secretion, Differences, Activation, Function

Trypsinogen and trypsin are two related enzymes involved in the digestion of proteins. Here’s a breakdown of their roles and functions: Trypsinogen Definition: Trypsinogen is an inactive precursor (zymogen) of the enzyme trypsin. Production: It is produced in the pancreas. Activation: Trypsinogen is secreted into the small intestine, where it is activated to form trypsin by the enzyme enterokinase (also known as enteropeptidase), which is found on the surface of the intestinal lining. Trypsin Definition: Trypsin is an active enzyme that breaks down proteins into smaller peptides. Function: Once activated, trypsin helps digest proteins by cleaving peptide bonds. It is crucial for the digestion of dietary proteins. Regulation: Trypsin can activate other digestive enzymes from their inactive forms, such as chymotrypsinogen to chymotrypsin. Clinical Significance Pancreatitis: In conditions like pancreatitis, the premature activation of trypsinogen within the pancreas can lead to self-digestion of pancreatic tissue, causing inflammation and damage. Hereditary Pancreatitis: Mutations in the gene coding for trypsinogen (PRSS1) can lead to hereditary pancreatitis due to the increased likelihood of premature activation. Exocrine Pancreatic Insufficiency (EPI): Reduced production or secretion of trypsinogen can lead to EPI, where the body cannot properly digest proteins, resulting in malnutrition. #Trypsinogen #Trypsin