Forskning ved Københavns Universitet - Københavns Universitet

Forside

Iodide modulates protein damage induced by the inflammation-associated heme enzyme myeloperoxidase

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Standard

Iodide modulates protein damage induced by the inflammation-associated heme enzyme myeloperoxidase. / Gamon, Luke F.; Dieterich, Simon; Ignasiak, Marta T.; Schrameyer, Verena; Davies, Michael J.

I: Redox Biology, Bind 28, 101331, 2020.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Gamon, LF, Dieterich, S, Ignasiak, MT, Schrameyer, V & Davies, MJ 2020, 'Iodide modulates protein damage induced by the inflammation-associated heme enzyme myeloperoxidase', Redox Biology, bind 28, 101331. https://doi.org/10.1016/j.redox.2019.101331

APA

Gamon, L. F., Dieterich, S., Ignasiak, M. T., Schrameyer, V., & Davies, M. J. (2020). Iodide modulates protein damage induced by the inflammation-associated heme enzyme myeloperoxidase. Redox Biology, 28, [101331]. https://doi.org/10.1016/j.redox.2019.101331

Vancouver

Gamon LF, Dieterich S, Ignasiak MT, Schrameyer V, Davies MJ. Iodide modulates protein damage induced by the inflammation-associated heme enzyme myeloperoxidase. Redox Biology. 2020;28. 101331. https://doi.org/10.1016/j.redox.2019.101331

Author

Gamon, Luke F. ; Dieterich, Simon ; Ignasiak, Marta T. ; Schrameyer, Verena ; Davies, Michael J. / Iodide modulates protein damage induced by the inflammation-associated heme enzyme myeloperoxidase. I: Redox Biology. 2020 ; Bind 28.

Bibtex

@article{855e9362ccf1456b9bef82fbb567d759,
title = "Iodide modulates protein damage induced by the inflammation-associated heme enzyme myeloperoxidase",
abstract = "Iodide ions (I−) are an essential dietary mineral, and crucial for mental and physical development, fertility and thyroid function. I− is also a high affinity substrate for the heme enzyme myeloperoxidase (MPO), which is involved in bacterial cell killing during the immune response, and also host tissue damage during inflammation. In the presence of H2O2 and Cl−, MPO generates the powerful oxidant hypochlorous acid (HOCl), with excessive formation of this species linked to multiple inflammatory diseases. In this study, we have examined the hypothesis that elevated levels of I− would decrease HOCl formation and thereby protein damage induced by a MPO/Cl−/H2O2 system, by acting as a competitive substrate. The presence of increasing I− concentrations (0.1–10 μM; i.e. within the range readily achievable by oral supplementation in humans), decreased damage to both model proteins and extracellular matrix components as assessed by gross structural changes (SDS-PAGE), antibody recognition of parent and modified protein epitopes (ELISA), and quantification of both parent amino acid loss (UPLC) and formation of the HOCl-biomarker 3-chlorotyrosine (LC-MS) (reduced by ca. 50{\%} at 10 μM I−). Elevated levels of I− ( > 1 μM) also protected against functional changes as assessed by a decreased loss of adhesion (eg. 40{\%} vs. < 22{\%} with >1 μM I−) of primary human coronary artery endothelial cells (HCAECs), to MPO-modified human plasma fibronectin. These data indicate that low micromolar concentrations of I−, which can be readily achieved in humans and are readily tolerated, may afford protection against cell and tissue damage induced by MPO.",
keywords = "3-Chlorotyrosine, Fibronectin, Hypochlorous acid, Inflammation, Iodide, Myeloperoxidase",
author = "Gamon, {Luke F.} and Simon Dieterich and Ignasiak, {Marta T.} and Verena Schrameyer and Davies, {Michael J.}",
year = "2020",
doi = "10.1016/j.redox.2019.101331",
language = "English",
volume = "28",
journal = "Redox Biology",
issn = "2213-2317",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Iodide modulates protein damage induced by the inflammation-associated heme enzyme myeloperoxidase

AU - Gamon, Luke F.

AU - Dieterich, Simon

AU - Ignasiak, Marta T.

AU - Schrameyer, Verena

AU - Davies, Michael J.

PY - 2020

Y1 - 2020

N2 - Iodide ions (I−) are an essential dietary mineral, and crucial for mental and physical development, fertility and thyroid function. I− is also a high affinity substrate for the heme enzyme myeloperoxidase (MPO), which is involved in bacterial cell killing during the immune response, and also host tissue damage during inflammation. In the presence of H2O2 and Cl−, MPO generates the powerful oxidant hypochlorous acid (HOCl), with excessive formation of this species linked to multiple inflammatory diseases. In this study, we have examined the hypothesis that elevated levels of I− would decrease HOCl formation and thereby protein damage induced by a MPO/Cl−/H2O2 system, by acting as a competitive substrate. The presence of increasing I− concentrations (0.1–10 μM; i.e. within the range readily achievable by oral supplementation in humans), decreased damage to both model proteins and extracellular matrix components as assessed by gross structural changes (SDS-PAGE), antibody recognition of parent and modified protein epitopes (ELISA), and quantification of both parent amino acid loss (UPLC) and formation of the HOCl-biomarker 3-chlorotyrosine (LC-MS) (reduced by ca. 50% at 10 μM I−). Elevated levels of I− ( > 1 μM) also protected against functional changes as assessed by a decreased loss of adhesion (eg. 40% vs. < 22% with >1 μM I−) of primary human coronary artery endothelial cells (HCAECs), to MPO-modified human plasma fibronectin. These data indicate that low micromolar concentrations of I−, which can be readily achieved in humans and are readily tolerated, may afford protection against cell and tissue damage induced by MPO.

AB - Iodide ions (I−) are an essential dietary mineral, and crucial for mental and physical development, fertility and thyroid function. I− is also a high affinity substrate for the heme enzyme myeloperoxidase (MPO), which is involved in bacterial cell killing during the immune response, and also host tissue damage during inflammation. In the presence of H2O2 and Cl−, MPO generates the powerful oxidant hypochlorous acid (HOCl), with excessive formation of this species linked to multiple inflammatory diseases. In this study, we have examined the hypothesis that elevated levels of I− would decrease HOCl formation and thereby protein damage induced by a MPO/Cl−/H2O2 system, by acting as a competitive substrate. The presence of increasing I− concentrations (0.1–10 μM; i.e. within the range readily achievable by oral supplementation in humans), decreased damage to both model proteins and extracellular matrix components as assessed by gross structural changes (SDS-PAGE), antibody recognition of parent and modified protein epitopes (ELISA), and quantification of both parent amino acid loss (UPLC) and formation of the HOCl-biomarker 3-chlorotyrosine (LC-MS) (reduced by ca. 50% at 10 μM I−). Elevated levels of I− ( > 1 μM) also protected against functional changes as assessed by a decreased loss of adhesion (eg. 40% vs. < 22% with >1 μM I−) of primary human coronary artery endothelial cells (HCAECs), to MPO-modified human plasma fibronectin. These data indicate that low micromolar concentrations of I−, which can be readily achieved in humans and are readily tolerated, may afford protection against cell and tissue damage induced by MPO.

KW - 3-Chlorotyrosine

KW - Fibronectin

KW - Hypochlorous acid

KW - Inflammation

KW - Iodide

KW - Myeloperoxidase

U2 - 10.1016/j.redox.2019.101331

DO - 10.1016/j.redox.2019.101331

M3 - Journal article

C2 - 31568923

AN - SCOPUS:85072645338

VL - 28

JO - Redox Biology

JF - Redox Biology

SN - 2213-2317

M1 - 101331

ER -

ID: 228207065