Pepsinogen a

From WikiMD's Food, Medicine & Wellness Encyclopedia

Pepsinogen is a zymogen form of the digestive enzyme pepsin. It is secreted by the chief cells located in the stomach lining and is activated into pepsin upon exposure to hydrochloric acid.

Production and Activation[edit | edit source]

Pepsinogen is produced in the gastric chief cells of the stomach lining. The production of pepsinogen is stimulated by the hormone gastrin, which is released when food enters the stomach.

Upon release into the stomach, pepsinogen is inactive. It is activated into pepsin when it comes into contact with hydrochloric acid, which is secreted by the parietal cells in the stomach. The acid changes the structure of the pepsinogen molecule, revealing its active site and transforming it into pepsin.

Function[edit | edit source]

The primary function of pepsin is to break down proteins in the food we eat. It does this by cleaving the peptide bonds that hold the amino acids together in the protein chain. This process is known as proteolysis.

Pepsin is most effective at a low pH, which is provided by the acidic environment of the stomach. It begins the process of protein digestion, which is then continued by other enzymes in the small intestine.

Clinical Significance[edit | edit source]

Abnormal levels of pepsinogen in the blood can be indicative of certain medical conditions. High levels may suggest a peptic ulcer, while low levels can be a sign of atrophic gastritis or pernicious anemia.

Pepsinogen testing is often used in combination with other tests to diagnose these conditions. It can also be used to monitor the effectiveness of treatment for peptic ulcers.

See Also[edit | edit source]



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Contributors: Prab R. Tumpati, MD