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Trypsinogen isoforms in the ferret pancreas
Eszter Hegyi1, Miklós Sahin-Tóth2
1Center for Exocrine Disorders, Department of Molecular and Cell Biology, Boston University Henry M. Goldman School of Dental Medicine, Boston, MA, 02118, USA.
Scientific Reports
|October 12, 2018
Summary
Ferret trypsinogens do not autoactivate like human ones, making them unsuitable for studying hereditary pancreatitis linked to this process. However, cathepsin B activation of ferret trypsinogen may still play a role in ferret pancreatitis.
Area of Science:
- Biochemistry
- Comparative physiology
- Gastroenterology
Background:
- The domestic ferret (Mustela putorius furo) is a new model for human pancreatic diseases.
- Hereditary pancreatitis is often linked to abnormal trypsinogen autoactivation.
Purpose of the Study:
- To assess the suitability of ferrets for studying hereditary pancreatitis.
- To investigate ferret trypsinogen autoactivation properties and compare them to human trypsinogen.
Main Methods:
- Purification and cloning of ferret trypsinogen isoforms.
- Functional analysis of ferret trypsinogen autoactivation.
- Comparison with human cationic trypsinogen (PRSS1).
Main Results:
- Two main ferret trypsinogen isoforms were identified: anionic and cationic.
- Ferret anionic trypsinogen showed limited autoactivation only at high calcium levels.
- Ferret cationic trypsinogen exhibited no autoactivation under tested conditions.
- Both isoforms were activated by enteropeptidase and cathepsin B.
Conclusions:
- Ferret trypsinogens do not autoactivate similarly to human paralogs, limiting their use for modeling hereditary pancreatitis.
- Cathepsin B-mediated intra-pancreatic trypsinogen activation in ferrets could potentially trigger pancreatitis independently of trypsinogen autoactivation.
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