Oxidation of lysine side-chains of elastin by the myeloperoxidase system and by stimulated human neutrophils

Robert A. Clark; Susan Szot; Marcia A. Williams; Herbert M. Kagan

doi:10.1016/0006-291X(86)90015-X

Oxidation of lysine side-chains of elastin by the myeloperoxidase system and by stimulated human neutrophils

Robert A. Clark, Susan Szot, Marcia A. Williams, Herbert M. Kagan

Research output: Contribution to journal › Article › peer-review

22 Scopus citations

Abstract

Exposure of [³H]-lysine labeled elastin to either purified myeloper-oxidase plus H₂O₂ and halides or human neutrophils plus phorbol myristate acetate resulted in oxidation of lysine side chains quantitated as ³H₂O release. In both the enzyme and cell systems oxidation was blocked by azide, cyanide or catalase, but not by β-aminopropionitrile, an inhibitor of lysyl oxidase. Myeloperoxidase-deficient neutrophils were ineffective unless exogenous myeloperoxidase was added. These data provide a biochemical basis for inflammatory changes in connective tissue proteins mediated by oxidant secretory products of neutrophils.

Original language	English (US)
Pages (from-to)	451-457
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	135
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(86)90015-X
State	Published - Mar 13 1986
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/0006-291X(86)90015-X

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@article{34cfd961262b48e1981458540d3a83e7,

title = "Oxidation of lysine side-chains of elastin by the myeloperoxidase system and by stimulated human neutrophils",

abstract = "Exposure of [3H]-lysine labeled elastin to either purified myeloper-oxidase plus H2O2 and halides or human neutrophils plus phorbol myristate acetate resulted in oxidation of lysine side chains quantitated as 3H2O release. In both the enzyme and cell systems oxidation was blocked by azide, cyanide or catalase, but not by β-aminopropionitrile, an inhibitor of lysyl oxidase. Myeloperoxidase-deficient neutrophils were ineffective unless exogenous myeloperoxidase was added. These data provide a biochemical basis for inflammatory changes in connective tissue proteins mediated by oxidant secretory products of neutrophils.",

author = "Clark, {Robert A.} and Susan Szot and Williams, {Marcia A.} and Kagan, {Herbert M.}",

note = "Funding Information: ACKNOWLEDGEMENTTSh: is work was supported by grants BL19717, AM18880, and AI20866 from the National Institutes of Health and by a grant from the Veterans Administration. R.A.C. is a Medical Investigator of the Veterans Administration. We thank Cari Malone for preparing the manuscript.",

year = "1986",

month = mar,

day = "13",

doi = "10.1016/0006-291X(86)90015-X",

language = "English (US)",

volume = "135",

pages = "451--457",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "2",

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TY - JOUR

T1 - Oxidation of lysine side-chains of elastin by the myeloperoxidase system and by stimulated human neutrophils

AU - Clark, Robert A.

AU - Szot, Susan

AU - Williams, Marcia A.

AU - Kagan, Herbert M.

N1 - Funding Information: ACKNOWLEDGEMENTTSh: is work was supported by grants BL19717, AM18880, and AI20866 from the National Institutes of Health and by a grant from the Veterans Administration. R.A.C. is a Medical Investigator of the Veterans Administration. We thank Cari Malone for preparing the manuscript.

PY - 1986/3/13

Y1 - 1986/3/13

N2 - Exposure of [3H]-lysine labeled elastin to either purified myeloper-oxidase plus H2O2 and halides or human neutrophils plus phorbol myristate acetate resulted in oxidation of lysine side chains quantitated as 3H2O release. In both the enzyme and cell systems oxidation was blocked by azide, cyanide or catalase, but not by β-aminopropionitrile, an inhibitor of lysyl oxidase. Myeloperoxidase-deficient neutrophils were ineffective unless exogenous myeloperoxidase was added. These data provide a biochemical basis for inflammatory changes in connective tissue proteins mediated by oxidant secretory products of neutrophils.

AB - Exposure of [3H]-lysine labeled elastin to either purified myeloper-oxidase plus H2O2 and halides or human neutrophils plus phorbol myristate acetate resulted in oxidation of lysine side chains quantitated as 3H2O release. In both the enzyme and cell systems oxidation was blocked by azide, cyanide or catalase, but not by β-aminopropionitrile, an inhibitor of lysyl oxidase. Myeloperoxidase-deficient neutrophils were ineffective unless exogenous myeloperoxidase was added. These data provide a biochemical basis for inflammatory changes in connective tissue proteins mediated by oxidant secretory products of neutrophils.

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JO - Biochemical and Biophysical Research Communications

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IS - 2

ER -

Oxidation of lysine side-chains of elastin by the myeloperoxidase system and by stimulated human neutrophils

Abstract

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