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

Morphogenesis and Differentiation Program

22 Citations (Scopus)

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
Journal	The Journal of Biological Chemistry
Volume	289
Issue number	21
Pages (from-to)	14740-14749
Number of pages	10
ISSN	0021-9258
DOIs	https://doi.org/10.1074/jbc.M113.541318
Publication status	Published - 2014

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The Membrane-anchored Serine Protease Prostasin (CAP1/PRSS8) Supports Epidermal Development and Postnatal Homeostasis Independent of Its Enzymatic Activity. / Peters, Diane E; Szabo, Roman; Friis, Stine et al.

In: The Journal of Biological Chemistry, Vol. 289, No. 21, 2014, p. 14740-14749.

Research output: Contribution to journal › Journal article › Research › peer-review

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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 {Uzzun Sales}, Katiuchia and Kenn Holmbeck and Bugge, {Thomas H}",

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AU - Peters, Diane E

AU - Szabo, Roman

AU - Friis, Stine

AU - Shylo, Natalia A

AU - Uzzun Sales, Katiuchia

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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DO - 10.1074/jbc.M113.541318

M3 - Journal article

C2 - 24706745

SN - 0021-9258

VL - 289

SP - 14740

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JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 21

ER -

The Membrane-anchored Serine Protease Prostasin (CAP1/PRSS8) Supports Epidermal Development and Postnatal Homeostasis Independent of Its Enzymatic Activity

Abstract

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