TGF-beta signaling in atherosclerosis and restenosis
| Autor: | Kitamoto Y, Zheng Xl, Sadler Je |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Serine protease
Enteropeptidase Protease General Immunology and Microbiology biology Trypsinogen medicine.medical_treatment Chymotrypsinogen Trypsin digestive system Carboxypeptidase General Biochemistry Genetics and Molecular Biology chemistry.chemical_compound Biochemistry chemistry Zymogen medicine biology.protein medicine.drug |
| Zdroj: | Frontiers in Bioscience. 1:236 |
| ISSN: | 1945-0508 1945-0516 |
| DOI: | 10.2741/e23 |
| Popis: | Enteropeptidase, a type II transmembrane serine protease, is localized to the brush border of the duodenal and jejunal mucosa. It is synthesized as a zymogen (proenteropeptidase) that requires activation by another protease, either trypsin or possibly duodenase. Active enteropeptidase then converts the pancreatic precursor, trypsinogen, to trypsin by cleavage of the specific trypsinogen activation peptide, Asp-Asp-Asp-Asp-Lys- Ile that is highly conserved in vertebrates. Trypsin, in turn, activates other digestive zymogens such as chymotrypsinogen, proelastase, procarboxypeptidase and prolipase in the lumen of the gut. The important biological function of enteropeptidase is highlighted by the manifestation of severe diarrhea, failure to thrive, hypoproteinemia and edema as a result of congenital deficiency of enteropeptidase activity in the gut. Conversely, duodenopancreatic reflux of proteolytically active enteropeptidase may cause acute and chronic pancreatitis. |
| Databáze: | OpenAIRE |
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