Degradation of extracellular matrix and its components by hypobromous acid

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Degradation of extracellular matrix and its components by hypobromous acid. / Rees, Martin D; McNiven, Tane N; Davies, Michael Jonathan.

In: Biochemical Journal, Vol. 401, No. 2, 15.01.2007, p. 587-96.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Rees, MD, McNiven, TN & Davies, MJ 2007, 'Degradation of extracellular matrix and its components by hypobromous acid', Biochemical Journal, vol. 401, no. 2, pp. 587-96. https://doi.org/10.1042/BJ20061236

APA

Rees, M. D., McNiven, T. N., & Davies, M. J. (2007). Degradation of extracellular matrix and its components by hypobromous acid. Biochemical Journal, 401(2), 587-96. https://doi.org/10.1042/BJ20061236

Vancouver

Rees MD, McNiven TN, Davies MJ. Degradation of extracellular matrix and its components by hypobromous acid. Biochemical Journal. 2007 Jan 15;401(2):587-96. https://doi.org/10.1042/BJ20061236

Author

Rees, Martin D ; McNiven, Tane N ; Davies, Michael Jonathan. / Degradation of extracellular matrix and its components by hypobromous acid. In: Biochemical Journal. 2007 ; Vol. 401, No. 2. pp. 587-96.

Bibtex

@article{c0db96ab7b7d42a99fefc1ee887a66e2,
title = "Degradation of extracellular matrix and its components by hypobromous acid",
abstract = "EPO (eosinophil peroxidase) and MPO (myeloperoxidase) are highly basic haem enzymes that can catalyse the production of HOBr (hypobromous acid). They are released extracellularly by activated leucocytes and their binding to the polyanionic glycosa-minoglycan components of extracellular matrix (proteoglycans and hyaluronan) may localize the production of HOBr to these materials. It is shown in the present paper that the reaction of HOBr with glycosaminoglycans (heparan sulfate, heparin, chondroitin sulfate and hyaluronan) generates polymer-derived N-bromo derivatives (bromamines, dibromamines, N-bromosulfon-amides and bromamides). Decomposition of these species, which can occur spontaneously and/or via one-electron reduction by low-valent transition metal ions (Cu+ and Fe2+), results in polymer fragmentation and modification. One-electron reduction of the N-bromo derivatives generates radicals that have been detected by EPR spin trapping. The species detected are consistent with metal ion-dependent polymer fragmentation and modification being initiated by the formation of nitrogen-centred (aminyl, N-bromoaminyl, sulfonamidyl and amidyl) radicals. Previous studies have shown that the reaction of HOBr with proteins generates N-bromo derivatives and results in fragmentation of the polypeptide backbone. The reaction of HOBr with extracellular matrix synthesized by smooth muscle cells in vitro induces the release of carbohydrate and protein components in a time-dependent manner, which is consistent with fragmentation of these materials via the formation of N-bromo derivatives. The degradation of extracellular matrix glycosaminoglycans and proteins by HOBr may contribute to tissue damage associated with inflammatory diseases such as asthma.",
keywords = "Animals, Bromates, Cell Line, Chondroitin Sulfates, Electron Spin Resonance Spectroscopy, Electrophoresis, Polyacrylamide Gel, Extracellular Matrix, Free Radicals, Glycosaminoglycans, Heparin, Heparitin Sulfate, Hyaluronic Acid, Models, Chemical, Muscle, Smooth, Vascular, Rats",
author = "Rees, {Martin D} and McNiven, {Tane N} and Davies, {Michael Jonathan}",
year = "2007",
month = "1",
day = "15",
doi = "10.1042/BJ20061236",
language = "English",
volume = "401",
pages = "587--96",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "2",

}

RIS

TY - JOUR

T1 - Degradation of extracellular matrix and its components by hypobromous acid

AU - Rees, Martin D

AU - McNiven, Tane N

AU - Davies, Michael Jonathan

PY - 2007/1/15

Y1 - 2007/1/15

N2 - EPO (eosinophil peroxidase) and MPO (myeloperoxidase) are highly basic haem enzymes that can catalyse the production of HOBr (hypobromous acid). They are released extracellularly by activated leucocytes and their binding to the polyanionic glycosa-minoglycan components of extracellular matrix (proteoglycans and hyaluronan) may localize the production of HOBr to these materials. It is shown in the present paper that the reaction of HOBr with glycosaminoglycans (heparan sulfate, heparin, chondroitin sulfate and hyaluronan) generates polymer-derived N-bromo derivatives (bromamines, dibromamines, N-bromosulfon-amides and bromamides). Decomposition of these species, which can occur spontaneously and/or via one-electron reduction by low-valent transition metal ions (Cu+ and Fe2+), results in polymer fragmentation and modification. One-electron reduction of the N-bromo derivatives generates radicals that have been detected by EPR spin trapping. The species detected are consistent with metal ion-dependent polymer fragmentation and modification being initiated by the formation of nitrogen-centred (aminyl, N-bromoaminyl, sulfonamidyl and amidyl) radicals. Previous studies have shown that the reaction of HOBr with proteins generates N-bromo derivatives and results in fragmentation of the polypeptide backbone. The reaction of HOBr with extracellular matrix synthesized by smooth muscle cells in vitro induces the release of carbohydrate and protein components in a time-dependent manner, which is consistent with fragmentation of these materials via the formation of N-bromo derivatives. The degradation of extracellular matrix glycosaminoglycans and proteins by HOBr may contribute to tissue damage associated with inflammatory diseases such as asthma.

AB - EPO (eosinophil peroxidase) and MPO (myeloperoxidase) are highly basic haem enzymes that can catalyse the production of HOBr (hypobromous acid). They are released extracellularly by activated leucocytes and their binding to the polyanionic glycosa-minoglycan components of extracellular matrix (proteoglycans and hyaluronan) may localize the production of HOBr to these materials. It is shown in the present paper that the reaction of HOBr with glycosaminoglycans (heparan sulfate, heparin, chondroitin sulfate and hyaluronan) generates polymer-derived N-bromo derivatives (bromamines, dibromamines, N-bromosulfon-amides and bromamides). Decomposition of these species, which can occur spontaneously and/or via one-electron reduction by low-valent transition metal ions (Cu+ and Fe2+), results in polymer fragmentation and modification. One-electron reduction of the N-bromo derivatives generates radicals that have been detected by EPR spin trapping. The species detected are consistent with metal ion-dependent polymer fragmentation and modification being initiated by the formation of nitrogen-centred (aminyl, N-bromoaminyl, sulfonamidyl and amidyl) radicals. Previous studies have shown that the reaction of HOBr with proteins generates N-bromo derivatives and results in fragmentation of the polypeptide backbone. The reaction of HOBr with extracellular matrix synthesized by smooth muscle cells in vitro induces the release of carbohydrate and protein components in a time-dependent manner, which is consistent with fragmentation of these materials via the formation of N-bromo derivatives. The degradation of extracellular matrix glycosaminoglycans and proteins by HOBr may contribute to tissue damage associated with inflammatory diseases such as asthma.

KW - Animals

KW - Bromates

KW - Cell Line

KW - Chondroitin Sulfates

KW - Electron Spin Resonance Spectroscopy

KW - Electrophoresis, Polyacrylamide Gel

KW - Extracellular Matrix

KW - Free Radicals

KW - Glycosaminoglycans

KW - Heparin

KW - Heparitin Sulfate

KW - Hyaluronic Acid

KW - Models, Chemical

KW - Muscle, Smooth, Vascular

KW - Rats

U2 - 10.1042/BJ20061236

DO - 10.1042/BJ20061236

M3 - Journal article

C2 - 17014424

VL - 401

SP - 587

EP - 596

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 2

ER -

ID: 129671379