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The hormone gastrin and the vagus nerve trigger the release of both pepsinogen and HCl from the stomach lining when food is ingested. Hydrochloric acid creates an acidic environment, which allows pepsinogen to unfold and cleave itself in an autocatalytic fashion, thereby generating pepsin (the active form). Pepsin cleaves the 44 amino acids ...
n/a Ensembl ENSG00000229859 n/a UniProt P0DJD8 n/a RefSeq (mRNA) NM_001079807 n/a RefSeq (protein) NP_001073275 n/a Location (UCSC) Chr 11: 61.2 – 61.21 Mb n/a PubMed search n/a Wikidata View/Edit Human Pepsinogen 3, group I (pepsinogen A) is a protein that in humans is encoded by the PGA3 gene. Function This gene encodes a protein precursor of the digestive enzyme pepsin, a member of the ...
A gastric chief cell, peptic cell, or gastric zymogenic cell is a type of gastric gland cell that releases pepsinogen and gastric lipase.It is the cell responsible for secretion of chymosin (rennin) in ruminant animals and some other animals. [1]
It is produced in the stomach by gastric chief cells in its inactive form pepsinogen, which is a zymogen. Pepsinogen is then activated by the stomach acid into its active form, pepsin. Pepsin breaks down the protein in the food into smaller particles, such as peptide fragments and amino acids.
Gastric chief cells produce pepsinogen, which is activated by the acid to form pepsin. Pepsin is a protease that can digest and damage stomach cells. To prevent these disastrous effects, mucus and bicarbonate ions (HCO 3 −) are secreted by the foveolar cells.
In biochemistry, a zymogen (/ ˈ z aɪ m ə dʒ ən,-m oʊ-/ [1] [2]), also called a proenzyme (/ ˌ p r oʊ ˈ ɛ n z aɪ m / [3] [4]), is an inactive precursor of an enzyme.A zymogen requires a biochemical change (such as a hydrolysis reaction revealing the active site, or changing the configuration to reveal the active site) for it to become an active enzyme.
The precursor of pepsin, pepsinogen, is secreted by the stomach, and is activated only in the acidic environment found in stomach. The pancreas secretes the precursors of a number of proteases such as trypsin and chymotrypsin .
In pepsinogen A, the first 11 residues of the mature pepsin sequence are displaced by residues of the propeptide. The propeptide contains two helices that block the active site cleft, in particular the conserved Asp11 residue, in pepsin, hydrogen bonds to a conserved Arg residue in the propeptide.