Myeloperoxidase interacts with endothelial cell-surface cytokeratin 1 and modulates bradykinin production by the plasma Kallikrein-Kinin system.

Myeloperoxidase interacts with endothelial cell-surface cytokeratin 1 and modulates bradykinin production by the plasma Kallikrein-Kinin system. Research Abstract Details 

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Myeloperoxidase interacts with endothelial cell-surface cytokeratin 1 and modulates bradykinin production by the plasma Kallikrein-Kinin system. Abstract Text:

Joshua M Astern,William F Pendergraft,Ronald J Falk,J Charles Jennette,Alvin H Schmaier,Fakhri Mahdi,Gloria A Preston,

During an inflammatory state, functional myeloperoxidase (MPO) is released into the vessel as a result of intravascular neutrophil degradation. One mechanism of resulting cellular injury involves endothelial internalization of MPO, which causes oxidative damage and impairs endothelial signaling. We report the discovery of a protein that facilitates MPO internalization, cytokeratin 1 (CK1), identified using affinity chromatography and mass spectrometry. CK1 interacts with MPO in vitro, even in the presence of 100% human plasma, thus substantiating biological relevance. Immunofluorescent microscopy confirmed that MPO added to endothelial cells can co-localize with endogenously expressed CK1. CK1 acts as a scaffolding protein for the assembly of the vasoregulatory plasma kallikrein-kinin system; thus we explored whether MPO and high molecular weight kininogen (HK) reside on CK1 together or whether they compete for binding. The data support cooperative binding of MPO and HK on cells such that MPO masked the plasma kallikrein cleavage site on HK, and MPO-generated oxidants caused inactivation of both HK and kallikrein. Collectively, interactions between MPO and the components of the plasma kallikrein-kinin system resulted in decreased bradykinin production. This study identifies CK1 as a facilitator of MPO-mediated vascular responses and thus provides a new paradigm by which MPO affects vasoregulatory systems.

Myeloperoxidase interacts with endothelial cell-surface cytokeratin 1 and modulates bradykinin production by the plasma Kallikrein-Kinin system. Publishing Authors By Initials

JM Astern,WF Pendergraft,RJ Falk,JC Jennette,AH Schmaier,F Mahdi,GA Preston,

For similar enzymes and coenzymes: enzymes: oxidoreductases: peroxidases: peroxidase research abstracts see: enzymes and coenzymes: enzymes: oxidoreductases: peroxidases: peroxidase research

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Myeloperoxidase interacts with endothelial cell-surface cytokeratin 1 and modulates bradykinin production by the plasma Kallikrein-Kinin system. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: The American journal of pathology

VOLUME: 171

Page Numbers: 349-60

Journal Abbreviation: Am. J. Pathol.

ISSN: 0002-9440

DAY: 3

MONTH: Jul

YEAR: 2007

Myeloperoxidase interacts with endothelial cell-surface cytokeratin 1 and modulates bradykinin production by the plasma Kallikrein-Kinin system. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 370502

Myeloperoxidase interacts with endothelial cell-surface cytokeratin 1 and modulates bradykinin production by the plasma Kallikrein-Kinin system. Keywords Mesh Terms:

KEYWORDS: Peroxidase

MESH TERMS: physiology

Chemical & Substance for Abstract: Myeloperoxidase interacts with endothelial cell-surface cytokeratin 1 and modulates bradykinin production by the plasma Kallikrein-Kinin system. Information

Substance Name: Peroxidase

Registry Number: EC 1.11.1.7

Grant and Affiliation Information for Myeloperoxidase interacts with endothelial cell-surface cytokeratin 1 and modulates bradykinin production by the plasma Kallikrein-Kinin system.

AFFILIATION: Burnett-Womack, UNC Kidney Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7155, USA. jastern@med.unc.edu

Country: United States

AGENCY: United States NHLBI

GRANT: HL052779-10

ACRONYM: HL

MEDLINETA: Am J Pathol

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