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Heat Shock Proteins and Autoimmunity in Patients with Carotid Atherosclerosis
Author(s) -
RIGANÒ RACHELE,
PROFUMO ELISABETTA,
BUTTARI BRIGITTA,
TAGLIANI ANGELA,
PETRONE LINDA,
D'AMATI GIULIA,
IPPOLITI FLORA,
CAPOANO RAFFAELE,
FUMAGALLI LORENZO,
SALVATI BRUNO,
BUSINARO RITA
Publication year - 2007
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1381.001
Subject(s) - heat shock protein , immune system , peripheral blood mononuclear cell , autoimmunity , antibody , immunology , inflammation , hsp90 , in vitro , downregulation and upregulation , biology , medicine , gene , biochemistry
Studies aimed at elucidating the pathogenetic mechanisms underlying the initiation and progression of human atherosclerosis have emphasized the central role of inflammatory and immune cells. Atherosclerotic plaques are infiltrated by activated macrophages, T and B lymphocytes, plasma cells, and mast cells, releasing inflammatory molecules, which amplify the severity of the disease. Endothelial cells subjected to various stress conditions express increased amounts of heat shock proteins (HSPs), some of the most successfully conserved proteins throughout evolution. Many experimental observations reviewed in this article draw attention to several HSPs targeted by a specific cellular and humoral immune response in patients with atherosclerotic disease. The review also reports preliminary data obtained by our group on the possible role of HSP90 as a candidate autoantigen in carotid atherosclerosis. Our study deals with the presence of specific antibodies and T cells directed against HSP90 in patients with carotid atherosclerotic plaques. In 60% of these subjects' sera but in none of the sera from healthy controls immunoblotting (IB) detected the presence of specific antibodies. Moreover, 20% of peripheral blood mononuclear cells (PBMC) samples from patients but none from healthy subjects proliferated in response to human purified HSP90. In vitro experiments showed an upregulation of HSP90 expression in endothelial cells exposed to oxidative stress by treatment with H 2 O 2 and greater release of soluble HSP90 in culture supernatants from H 2 O 2 ‐treated cells than from untreated cells.