Interaction of protein C inhibitor with the type II transmembrane serine protease enteropeptidase.

The serine protease inhibitor protein C inhibitor (PCI) is expressed in many human tissues and exhibits broad protease reactivity. PCI binds glycosaminoglycans and certain phospholipids, which modulate its inhibitory activity. Enteropeptidase (EP) is a type II transmembrane serine protease mainly fo...

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Autores principales:	Thomas A Prohaska, Felix C Wahlmüller, Margareta Furtmüller, Margarethe Geiger
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/01db5cba2b884f7697cefbec69a98b54
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spelling	oai:doaj.org-article:01db5cba2b884f7697cefbec69a98b542021-11-18T07:14:58ZInteraction of protein C inhibitor with the type II transmembrane serine protease enteropeptidase.1932-620310.1371/journal.pone.0039262https://doaj.org/article/01db5cba2b884f7697cefbec69a98b542012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22723979/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203The serine protease inhibitor protein C inhibitor (PCI) is expressed in many human tissues and exhibits broad protease reactivity. PCI binds glycosaminoglycans and certain phospholipids, which modulate its inhibitory activity. Enteropeptidase (EP) is a type II transmembrane serine protease mainly found on the brush border membrane of epithelial cells in the duodenum, where it activates trypsinogen to initiate the digestion of food proteins. Some active EP is also present in duodenal fluid and has been made responsible for causing pancreatitis in case of duodeno-pancreatic reflux. Together with its substrate trypsinogen, EP is furthermore present in the epidermis and in some cancer cells. In this report, we show that PCI inhibited EP with an apparent 2nd order rate constant of 4.48 × 10(4) M(-1) s(-1). Low molecular weight (LMWH) and unfractionated heparin (UFH) slightly reduced the inhibitory effect of PCI. The SI (stoichiometry of inhibition) value for the inhibition of EP by PCI was 10.8 in the absence and 17.9 in the presence of UFH (10 U/ml). By inhibiting trypsin, chymotrypsin, and additionally EP, PCI might play a role in the protection of the pancreas from autodigestion. Furthermore the interaction of PCI with EP may influence the regulation of epithelial differentiation.Thomas A ProhaskaFelix C WahlmüllerMargareta FurtmüllerMargarethe GeigerPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 6, p e39262 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Thomas A Prohaska Felix C Wahlmüller Margareta Furtmüller Margarethe Geiger Interaction of protein C inhibitor with the type II transmembrane serine protease enteropeptidase.
description	The serine protease inhibitor protein C inhibitor (PCI) is expressed in many human tissues and exhibits broad protease reactivity. PCI binds glycosaminoglycans and certain phospholipids, which modulate its inhibitory activity. Enteropeptidase (EP) is a type II transmembrane serine protease mainly found on the brush border membrane of epithelial cells in the duodenum, where it activates trypsinogen to initiate the digestion of food proteins. Some active EP is also present in duodenal fluid and has been made responsible for causing pancreatitis in case of duodeno-pancreatic reflux. Together with its substrate trypsinogen, EP is furthermore present in the epidermis and in some cancer cells. In this report, we show that PCI inhibited EP with an apparent 2nd order rate constant of 4.48 × 10(4) M(-1) s(-1). Low molecular weight (LMWH) and unfractionated heparin (UFH) slightly reduced the inhibitory effect of PCI. The SI (stoichiometry of inhibition) value for the inhibition of EP by PCI was 10.8 in the absence and 17.9 in the presence of UFH (10 U/ml). By inhibiting trypsin, chymotrypsin, and additionally EP, PCI might play a role in the protection of the pancreas from autodigestion. Furthermore the interaction of PCI with EP may influence the regulation of epithelial differentiation.
format	article
author	Thomas A Prohaska Felix C Wahlmüller Margareta Furtmüller Margarethe Geiger
author_facet	Thomas A Prohaska Felix C Wahlmüller Margareta Furtmüller Margarethe Geiger
author_sort	Thomas A Prohaska
title	Interaction of protein C inhibitor with the type II transmembrane serine protease enteropeptidase.
title_short	Interaction of protein C inhibitor with the type II transmembrane serine protease enteropeptidase.
title_full	Interaction of protein C inhibitor with the type II transmembrane serine protease enteropeptidase.
title_fullStr	Interaction of protein C inhibitor with the type II transmembrane serine protease enteropeptidase.
title_full_unstemmed	Interaction of protein C inhibitor with the type II transmembrane serine protease enteropeptidase.
title_sort	interaction of protein c inhibitor with the type ii transmembrane serine protease enteropeptidase.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/01db5cba2b884f7697cefbec69a98b54
work_keys_str_mv	AT thomasaprohaska interactionofproteincinhibitorwiththetypeiitransmembraneserineproteaseenteropeptidase AT felixcwahlmuller interactionofproteincinhibitorwiththetypeiitransmembraneserineproteaseenteropeptidase AT margaretafurtmuller interactionofproteincinhibitorwiththetypeiitransmembraneserineproteaseenteropeptidase AT margarethegeiger interactionofproteincinhibitorwiththetypeiitransmembraneserineproteaseenteropeptidase
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Interaction of protein C inhibitor with the type II transmembrane serine protease enteropeptidase.

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