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S100A8 and S100A9 in human arterial wall

McCormick, Michelle M; Rahimi, Ahmed (Farid); Bobryshev, Yuri V; Gaus, Katharina; Zreiqat, Hala; Cai, Hong; Lord, Reginald S A; Geczy, Carolyn

Description

Atherogenesis is a complex process involving inflammation. S100A8 and S100A9, the Ca2+-binding neutrophil cytosolic proteins, are associated with innate immunity and regulate processes leading to leukocyte adhesion and transmigration. In neutrophils and monocytes the S100A8-S100A9 complex regulates phosphorylation, NADPH-oxidase activity, and fatty acid transport. The proteins have anti-microbial properties, and S100A8 may play a role in oxidant defense in inflammation. Murine S100A8 is...[Show more]

dc.contributor.authorMcCormick, Michelle M
dc.contributor.authorRahimi, Ahmed (Farid)
dc.contributor.authorBobryshev, Yuri V
dc.contributor.authorGaus, Katharina
dc.contributor.authorZreiqat, Hala
dc.contributor.authorCai, Hong
dc.contributor.authorLord, Reginald S A
dc.contributor.authorGeczy, Carolyn
dc.date.accessioned2015-12-10T22:14:05Z
dc.identifier.issn0021-9258
dc.identifier.urihttp://hdl.handle.net/1885/50103
dc.description.abstractAtherogenesis is a complex process involving inflammation. S100A8 and S100A9, the Ca2+-binding neutrophil cytosolic proteins, are associated with innate immunity and regulate processes leading to leukocyte adhesion and transmigration. In neutrophils and monocytes the S100A8-S100A9 complex regulates phosphorylation, NADPH-oxidase activity, and fatty acid transport. The proteins have anti-microbial properties, and S100A8 may play a role in oxidant defense in inflammation. Murine S100A8 is regulated by inflammatory mediators and recruits macrophages with a proatherogenic phenotype. S100A9 but not S100A8 was found in macrophages in ApoE-/- murine atherosclerotic lesions, whereas both proteins are expressed in human giant cell arteritis. Here we demonstrate S100A8 and S100A9 protein and mRNA in macrophages, foam cells, and neovessels in human atheroma. Monomeric and complexed forms were detected in plaque extracts. S100A9 was strongly expressed in calcifying areas and the surrounding extracellular matrix. Vascular matrix vesicles contain high levels of Ca2+-binding proteins and phospholipids that regulate calcification. Matrix vesicles characterized by electron microscopy, x-ray micro-analysis, nucleoside triphosphate pyrophosphohydrolase assay and cholesterol/phospholipid analysis contained predominantly S100A9. We propose that S100A9 associated with lipid structures in matrix vesicles may influence phospholipid-Ca2+ binding properties to promote dystrophic calcification. S100A8 and S100A9 were more sensitive to hypochlorite oxidation than albumin or low density lipoprotein and immunoaffinity confirmed S100A8-S100A9 complexes; some were resistant to reduction, suggesting that hypochlorite may contribute to protein cross-linking. S100A8 and S100A9 in atherosclerotic plaque and calcifying matrix vesicles may significantly influence redox- and Ca2+-dependent processes during atherogenesis and its chronic complications, particularly dystrophic calcification.
dc.publisherAmerican Society for Biochemistry and Molecular Biology Inc
dc.sourceJournal of Biological Chemistry
dc.subjectKeywords: Binding energy; Cells; Diseases; Fatty acids; Immunology; Monomers; Proteins; Cytosolic proteins; Inflammatory mediators; Monocytes; Phosphorylation; Blood vessels; albumin; calcium binding protein; calcium ion; calgranulin; hypochlorite; low density lipo
dc.titleS100A8 and S100A9 in human arterial wall
dc.typeJournal article
local.description.notesImported from ARIES
local.identifier.citationvolume280
dc.date.issued2005
local.identifier.absfor110799 - Immunology not elsewhere classified
local.identifier.absfor110201 - Cardiology (incl. Cardiovascular Diseases)
local.identifier.absfor110316 - Pathology
local.identifier.ariespublicationu8611701xPUB197
local.type.statusPublished Version
local.contributor.affiliationMcCormick, Michelle M, University of New South Wales
local.contributor.affiliationRahimi, Ahmed (Farid), College of Medicine, Biology and Environment, ANU
local.contributor.affiliationBobryshev, Yuri V, University of New South Wales
local.contributor.affiliationGaus, Katharina, University of New South Wales
local.contributor.affiliationZreiqat, Hala, University of New South Wales
local.contributor.affiliationCai, Hong, University of New South Wales
local.contributor.affiliationLord, Reginald S A, University of New South Wales
local.contributor.affiliationGeczy, Carolyn, University of New South Wales
local.description.embargo2037-12-31
local.bibliographicCitation.startpage41521
local.bibliographicCitation.lastpage41529
local.identifier.doi10.1074/jbc.M509442200
local.identifier.absseo920108 - Immune System and Allergy
local.identifier.absseo920103 - Cardiovascular System and Diseases
dc.date.updated2015-12-09T08:03:32Z
local.identifier.scopusID2-s2.0-29244446785
CollectionsANU Research Publications

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