Forskning ved Københavns Universitet - Københavns Universitet

Forside

The protease inhibitor HAI-2, but not HAI-1, regulates matriptase activation and shedding through prostasin

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Standard

The protease inhibitor HAI-2, but not HAI-1, regulates matriptase activation and shedding through prostasin. / Friis, Stine; Sales, Katiuchia Uzzun; Schafer, Jeffrey Martin; Vogel, Lotte K; Kataoka, Hiroaki; Bugge, Thomas H.

I: The Journal of Biological Chemistry, Bind 289, Nr. 32, 08.08.2014, s. 22319-22332.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Friis, S, Sales, KU, Schafer, JM, Vogel, LK, Kataoka, H & Bugge, TH 2014, 'The protease inhibitor HAI-2, but not HAI-1, regulates matriptase activation and shedding through prostasin', The Journal of Biological Chemistry, bind 289, nr. 32, s. 22319-22332. https://doi.org/10.1074/jbc.M114.574400

APA

Friis, S., Sales, K. U., Schafer, J. M., Vogel, L. K., Kataoka, H., & Bugge, T. H. (2014). The protease inhibitor HAI-2, but not HAI-1, regulates matriptase activation and shedding through prostasin. The Journal of Biological Chemistry, 289(32), 22319-22332. https://doi.org/10.1074/jbc.M114.574400

Vancouver

Friis S, Sales KU, Schafer JM, Vogel LK, Kataoka H, Bugge TH. The protease inhibitor HAI-2, but not HAI-1, regulates matriptase activation and shedding through prostasin. The Journal of Biological Chemistry. 2014 aug 8;289(32):22319-22332. https://doi.org/10.1074/jbc.M114.574400

Author

Friis, Stine ; Sales, Katiuchia Uzzun ; Schafer, Jeffrey Martin ; Vogel, Lotte K ; Kataoka, Hiroaki ; Bugge, Thomas H. / The protease inhibitor HAI-2, but not HAI-1, regulates matriptase activation and shedding through prostasin. I: The Journal of Biological Chemistry. 2014 ; Bind 289, Nr. 32. s. 22319-22332.

Bibtex

@article{875bb2e6aeca40bf91e1c89687a69cbe,
title = "The protease inhibitor HAI-2, but not HAI-1, regulates matriptase activation and shedding through prostasin",
abstract = "The membrane-anchored serine proteases, matriptase and prostasin, and the membrane-anchored serine protease inhibitors, hepatocyte growth factor activator inhibitor (HAI)-1 and HAI-2, are critical effectors of epithelial development and postnatal epithelial homeostasis. Matriptase and prostasin form a reciprocal zymogen activation complex that results in the formation of active matriptase and prostasin that are targets for inhibition by HAI-1 and HAI-2. Conflicting data, however, have accumulated as to the existence of auxiliary functions for both HAI-1 and HAI-2 in regulating the intracellular trafficking and activation of matriptase. In this study, we, therefore, used genetically-engineered mice to determine the effect of ablation of endogenous HAI-1 and endogenous HAI-2 on endogenous matriptase expression, subcellular localization, and activation in polarized intestinal epithelial cells. Whereas ablation of HAI-1 did not affect matriptase in epithelial cells of the small or large intestine, ablation of HAI-2 resulted in the loss of matriptase from both tissues. Gene silencing studies in intestinal Caco-2 cell monolayers revealed that this loss of cell-associated matriptase was mechanistically linked to accelerated activation and shedding of the protease caused by loss of prostasin regulation by HAI-2. Taken together, these data indicate that HAI-1 regulates the activity of activated matriptase, whereas HAI-2 has an essential role in regulating prostasin-dependent matriptase zymogen activation.",
author = "Stine Friis and Sales, {Katiuchia Uzzun} and Schafer, {Jeffrey Martin} and Vogel, {Lotte K} and Hiroaki Kataoka and Bugge, {Thomas H}",
note = "Copyright {\circledC} 2014, The American Society for Biochemistry and Molecular Biology.",
year = "2014",
month = "8",
day = "8",
doi = "10.1074/jbc.M114.574400",
language = "English",
volume = "289",
pages = "22319--22332",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "32",

}

RIS

TY - JOUR

T1 - The protease inhibitor HAI-2, but not HAI-1, regulates matriptase activation and shedding through prostasin

AU - Friis, Stine

AU - Sales, Katiuchia Uzzun

AU - Schafer, Jeffrey Martin

AU - Vogel, Lotte K

AU - Kataoka, Hiroaki

AU - Bugge, Thomas H

N1 - Copyright © 2014, The American Society for Biochemistry and Molecular Biology.

PY - 2014/8/8

Y1 - 2014/8/8

N2 - The membrane-anchored serine proteases, matriptase and prostasin, and the membrane-anchored serine protease inhibitors, hepatocyte growth factor activator inhibitor (HAI)-1 and HAI-2, are critical effectors of epithelial development and postnatal epithelial homeostasis. Matriptase and prostasin form a reciprocal zymogen activation complex that results in the formation of active matriptase and prostasin that are targets for inhibition by HAI-1 and HAI-2. Conflicting data, however, have accumulated as to the existence of auxiliary functions for both HAI-1 and HAI-2 in regulating the intracellular trafficking and activation of matriptase. In this study, we, therefore, used genetically-engineered mice to determine the effect of ablation of endogenous HAI-1 and endogenous HAI-2 on endogenous matriptase expression, subcellular localization, and activation in polarized intestinal epithelial cells. Whereas ablation of HAI-1 did not affect matriptase in epithelial cells of the small or large intestine, ablation of HAI-2 resulted in the loss of matriptase from both tissues. Gene silencing studies in intestinal Caco-2 cell monolayers revealed that this loss of cell-associated matriptase was mechanistically linked to accelerated activation and shedding of the protease caused by loss of prostasin regulation by HAI-2. Taken together, these data indicate that HAI-1 regulates the activity of activated matriptase, whereas HAI-2 has an essential role in regulating prostasin-dependent matriptase zymogen activation.

AB - The membrane-anchored serine proteases, matriptase and prostasin, and the membrane-anchored serine protease inhibitors, hepatocyte growth factor activator inhibitor (HAI)-1 and HAI-2, are critical effectors of epithelial development and postnatal epithelial homeostasis. Matriptase and prostasin form a reciprocal zymogen activation complex that results in the formation of active matriptase and prostasin that are targets for inhibition by HAI-1 and HAI-2. Conflicting data, however, have accumulated as to the existence of auxiliary functions for both HAI-1 and HAI-2 in regulating the intracellular trafficking and activation of matriptase. In this study, we, therefore, used genetically-engineered mice to determine the effect of ablation of endogenous HAI-1 and endogenous HAI-2 on endogenous matriptase expression, subcellular localization, and activation in polarized intestinal epithelial cells. Whereas ablation of HAI-1 did not affect matriptase in epithelial cells of the small or large intestine, ablation of HAI-2 resulted in the loss of matriptase from both tissues. Gene silencing studies in intestinal Caco-2 cell monolayers revealed that this loss of cell-associated matriptase was mechanistically linked to accelerated activation and shedding of the protease caused by loss of prostasin regulation by HAI-2. Taken together, these data indicate that HAI-1 regulates the activity of activated matriptase, whereas HAI-2 has an essential role in regulating prostasin-dependent matriptase zymogen activation.

U2 - 10.1074/jbc.M114.574400

DO - 10.1074/jbc.M114.574400

M3 - Journal article

C2 - 24962579

VL - 289

SP - 22319

EP - 22332

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 32

ER -

ID: 119583353