Inactivation of epidermal growth factor by Porphyromonas gingivalis as a potential mechanism for periodontal tissue damage

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Inactivation of epidermal growth factor by Porphyromonas gingivalis as a potential mechanism for periodontal tissue damage. / Pyrc, Krzysztof; Milewska, Aleksandra; Kantyka, Tomasz; Sroka, Aneta; Maresz, Katarzyna; Koziel, Joanna; Nguyen, Ky-Anh; Enghild, Jan Johannes; Knudsen, Anders Dahl; Potempa, Jan.

I: Infection and Immunity, Bind 81, Nr. 1, 01.2013, s. 55-64.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Pyrc, K, Milewska, A, Kantyka, T, Sroka, A, Maresz, K, Koziel, J, Nguyen, K-A, Enghild, JJ, Knudsen, AD & Potempa, J 2013, 'Inactivation of epidermal growth factor by Porphyromonas gingivalis as a potential mechanism for periodontal tissue damage', Infection and Immunity, bind 81, nr. 1, s. 55-64. https://doi.org/10.1128/IAI.00830-12

APA

Pyrc, K., Milewska, A., Kantyka, T., Sroka, A., Maresz, K., Koziel, J., ... Potempa, J. (2013). Inactivation of epidermal growth factor by Porphyromonas gingivalis as a potential mechanism for periodontal tissue damage. Infection and Immunity, 81(1), 55-64. https://doi.org/10.1128/IAI.00830-12

CBE

Pyrc K, Milewska A, Kantyka T, Sroka A, Maresz K, Koziel J, Nguyen K-A, Enghild JJ, Knudsen AD, Potempa J. 2013. Inactivation of epidermal growth factor by Porphyromonas gingivalis as a potential mechanism for periodontal tissue damage. Infection and Immunity. 81(1):55-64. https://doi.org/10.1128/IAI.00830-12

MLA

Vancouver

Pyrc K, Milewska A, Kantyka T, Sroka A, Maresz K, Koziel J o.a. Inactivation of epidermal growth factor by Porphyromonas gingivalis as a potential mechanism for periodontal tissue damage. Infection and Immunity. 2013 jan;81(1):55-64. https://doi.org/10.1128/IAI.00830-12

Author

Pyrc, Krzysztof ; Milewska, Aleksandra ; Kantyka, Tomasz ; Sroka, Aneta ; Maresz, Katarzyna ; Koziel, Joanna ; Nguyen, Ky-Anh ; Enghild, Jan Johannes ; Knudsen, Anders Dahl ; Potempa, Jan. / Inactivation of epidermal growth factor by Porphyromonas gingivalis as a potential mechanism for periodontal tissue damage. I: Infection and Immunity. 2013 ; Bind 81, Nr. 1. s. 55-64.

Bibtex

@article{63a111d9a0204648b72d03a0b071e3da,
title = "Inactivation of epidermal growth factor by Porphyromonas gingivalis as a potential mechanism for periodontal tissue damage",
abstract = "Porphyromonas gingivalis is a Gram-negative bacterium associated with the development of periodontitis. The evolutionary success of this pathogen results directly from the presence of numerous virulence factors, including a peptidylarginine deiminase (PPAD), an enzyme, which converts arginine to citrulline in proteins and peptides. Such posttranslational modification is thought to affect the function of many different signaling molecules. Taking into account the importance of tissue remodeling and repair mechanisms for periodontal homeostasis, which are orchestrated by ligands of the epidermal growth factor receptor (EGFR), we investigated the ability of PPAD to distort cross-talk between the epithelium and the EGF signaling pathway. We found that EGF preincubation with purified recombinant PPAD, or a wild-type strain of P. gingivalis, but not with a PPAD-deficient isogenic-mutant, efficiently hindered the ability of the growth factor to stimulate epidermal cell proliferation and migration. In addition, PPAD abrogated EGFR-EGF interaction-dependent stimulation of expression of Suppressor of Cytokine Signaling 3 (SOCS3) and Interferon Regulatory Factor 1 (IRF-1). Biochemical analysis clearly showed that the PPAD-exerted effects on EGF activities were solely due to deimination of the C-terminal arginine. Interestingly, citrullination of two internal Arg residues with human endogenous peptidylarginine deiminases did not alter EFG function, arguing that the C-terminal arginine is essential for EGF biological activity. Cumulatively, these data suggest that PPAD-activity-abrogating EGF function in gingival pockets may at least partially contribute to tissue damage and delayed healing within P. gingivalis-infected periodontia.",
author = "Krzysztof Pyrc and Aleksandra Milewska and Tomasz Kantyka and Aneta Sroka and Katarzyna Maresz and Joanna Koziel and Ky-Anh Nguyen and Enghild, {Jan Johannes} and Knudsen, {Anders Dahl} and Jan Potempa",
year = "2013",
month = "1",
doi = "10.1128/IAI.00830-12",
language = "English",
volume = "81",
pages = "55--64",
journal = "Infection and Immunity",
issn = "0019-9567",
publisher = "American Society for Microbiology",
number = "1",

}

RIS

TY - JOUR

T1 - Inactivation of epidermal growth factor by Porphyromonas gingivalis as a potential mechanism for periodontal tissue damage

AU - Pyrc, Krzysztof

AU - Milewska, Aleksandra

AU - Kantyka, Tomasz

AU - Sroka, Aneta

AU - Maresz, Katarzyna

AU - Koziel, Joanna

AU - Nguyen, Ky-Anh

AU - Enghild, Jan Johannes

AU - Knudsen, Anders Dahl

AU - Potempa, Jan

PY - 2013/1

Y1 - 2013/1

N2 - Porphyromonas gingivalis is a Gram-negative bacterium associated with the development of periodontitis. The evolutionary success of this pathogen results directly from the presence of numerous virulence factors, including a peptidylarginine deiminase (PPAD), an enzyme, which converts arginine to citrulline in proteins and peptides. Such posttranslational modification is thought to affect the function of many different signaling molecules. Taking into account the importance of tissue remodeling and repair mechanisms for periodontal homeostasis, which are orchestrated by ligands of the epidermal growth factor receptor (EGFR), we investigated the ability of PPAD to distort cross-talk between the epithelium and the EGF signaling pathway. We found that EGF preincubation with purified recombinant PPAD, or a wild-type strain of P. gingivalis, but not with a PPAD-deficient isogenic-mutant, efficiently hindered the ability of the growth factor to stimulate epidermal cell proliferation and migration. In addition, PPAD abrogated EGFR-EGF interaction-dependent stimulation of expression of Suppressor of Cytokine Signaling 3 (SOCS3) and Interferon Regulatory Factor 1 (IRF-1). Biochemical analysis clearly showed that the PPAD-exerted effects on EGF activities were solely due to deimination of the C-terminal arginine. Interestingly, citrullination of two internal Arg residues with human endogenous peptidylarginine deiminases did not alter EFG function, arguing that the C-terminal arginine is essential for EGF biological activity. Cumulatively, these data suggest that PPAD-activity-abrogating EGF function in gingival pockets may at least partially contribute to tissue damage and delayed healing within P. gingivalis-infected periodontia.

AB - Porphyromonas gingivalis is a Gram-negative bacterium associated with the development of periodontitis. The evolutionary success of this pathogen results directly from the presence of numerous virulence factors, including a peptidylarginine deiminase (PPAD), an enzyme, which converts arginine to citrulline in proteins and peptides. Such posttranslational modification is thought to affect the function of many different signaling molecules. Taking into account the importance of tissue remodeling and repair mechanisms for periodontal homeostasis, which are orchestrated by ligands of the epidermal growth factor receptor (EGFR), we investigated the ability of PPAD to distort cross-talk between the epithelium and the EGF signaling pathway. We found that EGF preincubation with purified recombinant PPAD, or a wild-type strain of P. gingivalis, but not with a PPAD-deficient isogenic-mutant, efficiently hindered the ability of the growth factor to stimulate epidermal cell proliferation and migration. In addition, PPAD abrogated EGFR-EGF interaction-dependent stimulation of expression of Suppressor of Cytokine Signaling 3 (SOCS3) and Interferon Regulatory Factor 1 (IRF-1). Biochemical analysis clearly showed that the PPAD-exerted effects on EGF activities were solely due to deimination of the C-terminal arginine. Interestingly, citrullination of two internal Arg residues with human endogenous peptidylarginine deiminases did not alter EFG function, arguing that the C-terminal arginine is essential for EGF biological activity. Cumulatively, these data suggest that PPAD-activity-abrogating EGF function in gingival pockets may at least partially contribute to tissue damage and delayed healing within P. gingivalis-infected periodontia.

U2 - 10.1128/IAI.00830-12

DO - 10.1128/IAI.00830-12

M3 - Journal article

C2 - 23090954

VL - 81

SP - 55

EP - 64

JO - Infection and Immunity

JF - Infection and Immunity

SN - 0019-9567

IS - 1

ER -