Trypsinogen

Trypsinogen [ trypsin gene. ] ( Physiol. ) is secreted ( secreted ) precursor ( proenzyme ) of the pancreatic enzyme trypsin. It is secreted as well as chymotrypsinogen, proelastase and other enzymes in an inactive form.

Importance

The inactive proenzyme trypsinogen is the precursor of the digestive proteolytic enzyme trypsin. Trypsinogen in the pancreas is secreted and activated in the duodenum by a membrane-bound enteropeptidase. This occurs by proteolytic cleavage by the enteropeptidase the hexapeptide (Val -Asp- Asp-Asp -Asp- Lys) cleaving the inactive enzyme precursor trypsinogen. The proteolytic enzyme trypsin is now in turn involved in digestive processes by the proteolytic cleavage of trypsinogen into trypsin catalyzes itself, and is responsible for the proteolytic cleavage of chymotrypsin and procarboxypeptidase.

Diseases

Mutations of the cationic trypsinogen are with chronic non-alcoholic pancreatitis found in patients with a clear autosomal dominant inheritance could not be documented. Other point mutations that could be found from the index patient in the screening of relatives, are L104P, R116C, and C139F. However, the significance of these trypsinogen mutants should not be overestimated, since 69.4 percent of the index patients of families with hereditary pancreatitis no mutation could be detected. As before, a careful clinical examination and a survey of the family history is displayed of suspicion and not the search for genetic variants.