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Tissue factor pathway inhibitor 2 is found in skin and its C-terminal region encodes for antibacterial activity.


ABSTRACT:

Background

Tissue factor pathway inhibitor 2 (TFPI-2) is a matrix-associated serine protease inhibitor with an enigmatic function in vivo. Here, we describe that TFPI-2 is present in fibrin of wounds and also expressed in skin, where it is up-regulated upon wounding.

Methodology and principal findings

Neutrophil elastase cleaved TFPI-2, and a C-terminal fragment was found to bind to bacteria. Similarly, a prototypic peptide representing this C-terminal part, EDC34, bound to bacteria and bacterial lipopolysaccharide, and induced bacterial permeabilization. The peptide also induced leakage in artificial liposomes, and displayed a random coil conformation upon interactions with liposomes as well as lipopolysaccharide. EDC34 was antibacterial against both Gram-negative and Gram-positive bacteria in physiological buffer conditions.

Conclusions/significance

The results demonstrate that the C-terminus of TFPI-2 encodes for antimicrobial activity, and may be released during wounding.

SUBMITTER: Papareddy P 

PROVIDER: S-EPMC3530512 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature

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Publications

Tissue factor pathway inhibitor 2 is found in skin and its C-terminal region encodes for antibacterial activity.

Papareddy Praveen P   Kalle Martina M   Sørensen Ole E OE   Lundqvist Katarina K   Mörgelin Matthias M   Malmsten Martin M   Schmidtchen Artur A  

PloS one 20121226 12


<h4>Background</h4>Tissue factor pathway inhibitor 2 (TFPI-2) is a matrix-associated serine protease inhibitor with an enigmatic function in vivo. Here, we describe that TFPI-2 is present in fibrin of wounds and also expressed in skin, where it is up-regulated upon wounding.<h4>Methodology and principal findings</h4>Neutrophil elastase cleaved TFPI-2, and a C-terminal fragment was found to bind to bacteria. Similarly, a prototypic peptide representing this C-terminal part, EDC34, bound to bacter  ...[more]

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