title: Biochemistry and biology of SPINK-PSTI and monitor peptide.
abstract: This article summarizes structural and functional properties of pancreatic secretory trypsin inhibitor (PSTI), which has been identified in many species. Its prominent role is to protect the pancreas from prematurely activated trypsinogen before entry into the duodenum. In the rat there are two isoforms, one of which is PSTI-I, a 61-amino acid peptide involved in the feedback regulation of pancreatic enzymes. Independent investigations in neoplastic diseases led to the discovery of tumor-associated trypsin inhibitor,which is identical to PSTI.
authors.affiliation: Pancreatitis Research Laboratory, Department of Visceral and Transplantation Surgery, University Hospital Zürich, DL 34, Rämistrasse 100, Zürich 8091, Switzerland. rolf.graf@usz.ch
authors.forename: Rolf
authors.initials: R
authors.lastname: Graf
authors.forename: Daniel
authors.initials: D
authors.lastname: Bimmler
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism*; D004789:Enzyme Activation; D004791:Enzyme Inhibitors / Q000378:metabolism; D006801:Humans; D036341:Intercellular Signaling Peptides and Proteins / Q000378:metabolism; D008969:Molecular Sequence Data; D010179:Pancreas / Q000378:metabolism*; D051381:Rats; D017386:Sequence Homology, Amino Acid; D014359:Trypsin Inhibitor, Kazal Pancreatic
chemical_list: D002352:Carrier Proteins; D004791:Enzyme Inhibitors; D036341:Intercellular Signaling Peptides and Proteins; C486642:SPINK1 protein, human; C504705:Spink1 protein, rat; D014359:Trypsin Inhibitor, Kazal Pancreatic