The membrane-anchored serine protease Prostasin (CAP1/PRSS8) supports epidermal development and postnatal homeostasis independent of its enzymatic activity

Diane E. Peters; Roman Szabo; Stine Friis; Natalia A. Shylo; Katiuchia Uzzun Sales; Kenn Holmbeck; Thomas H. Bugge

doi:10.1074/jbc.M113.541318

The membrane-anchored serine protease Prostasin (CAP1/PRSS8) supports epidermal development and postnatal homeostasis independent of its enzymatic activity

Diane E. Peters, Roman Szabo, Stine Friis, Natalia A. Shylo, Katiuchia Uzzun Sales, Kenn Holmbeck, Thomas H. Bugge

Research output: Contribution to journal › Article › peer-review

22 Scopus citations

Abstract

Background: Prostasin is a membrane-anchored serine protease with essential functions in epithelial development and homeostasis. Results: Mice expressing enzymatically inactive endogenous prostasin, unlike prostasin null mice, display normal tissue development and homeostasis. Conclusion: Essential in vivo functions of prostasin are independent of the catalytic activity of prostasin. Significance: Prostasin may have a unique role as an allosteric regulator of other membrane-anchored proteases.

Original language	English (US)
Pages (from-to)	14740-14749
Number of pages	10
Journal	Journal of Biological Chemistry
Volume	289
Issue number	21
DOIs	https://doi.org/10.1074/jbc.M113.541318
State	Published - 2014
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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10.1074/jbc.M113.541318

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title = "The membrane-anchored serine protease Prostasin (CAP1/PRSS8) supports epidermal development and postnatal homeostasis independent of its enzymatic activity",

abstract = "Background: Prostasin is a membrane-anchored serine protease with essential functions in epithelial development and homeostasis. Results: Mice expressing enzymatically inactive endogenous prostasin, unlike prostasin null mice, display normal tissue development and homeostasis. Conclusion: Essential in vivo functions of prostasin are independent of the catalytic activity of prostasin. Significance: Prostasin may have a unique role as an allosteric regulator of other membrane-anchored proteases.",

author = "Peters, {Diane E.} and Roman Szabo and Stine Friis and Shylo, {Natalia A.} and Sales, {Katiuchia Uzzun} and Kenn Holmbeck and Bugge, {Thomas H.}",

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T1 - The membrane-anchored serine protease Prostasin (CAP1/PRSS8) supports epidermal development and postnatal homeostasis independent of its enzymatic activity

AU - Peters, Diane E.

AU - Szabo, Roman

AU - Friis, Stine

AU - Shylo, Natalia A.

AU - Sales, Katiuchia Uzzun

AU - Holmbeck, Kenn

AU - Bugge, Thomas H.

PY - 2014

Y1 - 2014

N2 - Background: Prostasin is a membrane-anchored serine protease with essential functions in epithelial development and homeostasis. Results: Mice expressing enzymatically inactive endogenous prostasin, unlike prostasin null mice, display normal tissue development and homeostasis. Conclusion: Essential in vivo functions of prostasin are independent of the catalytic activity of prostasin. Significance: Prostasin may have a unique role as an allosteric regulator of other membrane-anchored proteases.

AB - Background: Prostasin is a membrane-anchored serine protease with essential functions in epithelial development and homeostasis. Results: Mice expressing enzymatically inactive endogenous prostasin, unlike prostasin null mice, display normal tissue development and homeostasis. Conclusion: Essential in vivo functions of prostasin are independent of the catalytic activity of prostasin. Significance: Prostasin may have a unique role as an allosteric regulator of other membrane-anchored proteases.

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JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

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The membrane-anchored serine protease Prostasin (CAP1/PRSS8) supports epidermal development and postnatal homeostasis independent of its enzymatic activity

Abstract

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