Human heat shock protein 60 (409–424) fragment is recognized by serum antibodies of patients with acute coronary syndromes

Wysocki, Jan; Karawajczyk, Bożena; Górski, Jacek; Korzeniowski, A.; Maćkiewicz, Zbigniew; Kupryszewski, Gotfryd; Głośnicka, R

doi:10.1016/s1054-8807(02)00109-6

Cited by 17 publications

(14 citation statements)

References 23 publications

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“…There have been numerous previous reports on the (Xu et al 1999(Xu et al , 2000Burian et al 2001;Zhu et al 2001;Kocsis et al 2002;Wysocki et al 2002). For instance, a prospective study has indicated that antibody titers to Hsp60 are predictive of cardiovascular events (Huittinen et al 2002).…”

Section: Discussionmentioning

confidence: 99%

Serum antibody titers against heat shock protein 27 are associated with the severity of coronary artery disease

Pourghadamyari

Moohebati

Parizadeh³

et al. 2011

Cell Stress and Chaperones

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Section: Discussionmentioning

confidence: 99%

Serum antibody titers against heat shock protein 27 are associated with the severity of coronary artery disease

Pourghadamyari

Moohebati

Parizadeh³

et al. 2011

Cell Stress and Chaperones

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“…[11][12][13][14] Antibodies against heat shock proteins have also been reported to be associated with atherosclerotic vascular diseases. [15][16][17][18] During our comparative examination of the proteome between the atheromatous plaque core area and nearby normal-appearing area in the same vessel specimens from carotid endarterectomy, we found a differential expression of heat shock protein 27 (Hsp27). Because there has not been a thorough examination of Hsp27 in atherosclerotic lesions or in the plasma of patients with coronary artery disease, we identified its localization in the atherosclerotic plaques and assessed the level of its soluble form in the plasma of patients with acute coronary syndrome (ACS).…”

Section: Editorial P 870 Clinical Perspective P 893mentioning

confidence: 98%

Expression of Heat Shock Protein 27 in Human Atherosclerotic Plaques and Increased Plasma Level of Heat Shock Protein 27 in Patients With Acute Coronary Syndrome

et al. 2006

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Background-We intended to identify proteins that are differentially expressed in human atherosclerotic plaques. Methods and Results-Comparative 2-dimensional electrophoretic analysis on carotid atherosclerotic endarterectomy specimens (nϭ10) revealed that heat shock protein 27 (Hsp27) expression was significantly increased in the nearby normal-appearing area compared with the plaque core area from the same vessel specimen, which was further confirmed by Western blot analysis. The Hsp27 expression in the adjacent normal-appearing vessel areas was much higher than that in nonatherosclerotic reference arteries. The phosphorylation of Hsp27 showed a gradation in the degree of phosphorylation: greatest in the reference arteries, intermediate in the adjacent normal-appearing area, and lowest in plaque core area. Immunohistochemical analysis showed that the phosphorylation of Hsp27 of smooth muscle cells in the carotid endarterectomy specimens was decreased compared with that in the reference artery specimen. The mean plasma level of Hsp27 was significantly higher in patients with acute coronary syndrome (ACS) (nϭ27; 106.1Ϯ74.1 ng/mL) than in the normal reference subjects (nϭ29; 45.8Ϯ29.5 ng/mL; PϽ0.005). The plasma levels of Hsp27 were significantly correlated with those of heat shock protein 70 (Hsp70) (rϭ0.422, PϽ0.0005), with adjustment for ACS/reference status. Conclusions-In the atherosclerotic lesion, Hsp27 expression is increased in the normal-appearing vessel adjacent to atherosclerotic plaque, whereas levels in the plaque itself are significantly decreased. Both plaque and adjacent artery show decreased Hsp27 phosphorylation compared with reference vessel. In ACS, plasma Hsp27 and Hsp70 are increased, and levels of Hsp27 correlate with Hsp70, C-reactive protein, and CD40L levels.

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“…With other peptides, we did not observe significant differences between the CHD and HP sera. To our best knowledge, only one report (Wysocki et al 2002) dealt with the epitope specificity of the anti-HSP60 antibody in coronary heart disease. Unfortunately, the CHD-specific epitope (409-424) of HSP60 described by the paper of Wysocki et al (2002) was only partly represented among the peptides we used (five amino acid overlap in peptide 404-413).…”

Section: Disease-specific Differencesmentioning

confidence: 99%

“…Therefore, the analysis of epitope specificity of these antibodies in health and disease is most important. Such analysis was performed in different infections [Rickettsia tsutsugamushi (Lachumanan et al 1993), Porphyromonas gingivalis (Maeda et al 2000), Chlamydia trachomatis (Yi et al 1993), Helicobacter pylori (Yamaguchi et al 2000)], picornaviruses (Harkonen et al 2000), and other diseases including adjuvant arthritis (Ulmansky et al 2002), carotid atherosclerosis (Metzler et al 1997;Perschinka et al 2003), acute coronary syndrome (Wysocki et al 2002), children with type 1 diabetes mellitus .…”

Section: Introductionmentioning

confidence: 99%

Comparison of epitope specificity of anti-heat shock protein 60/65 IgG type antibodies in the sera of healthy subjects, patients with coronary heart disease and inflammatory bowel disease

Füst

Uray

Bene

et al. 2012

Cell Stress and Chaperones

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Previously, we reported on the presence of antibodies to linear epitopes of human and mycobacterial 60 kD heat shock proteins (HSP) in the sera of healthy blood donors. Since many recent findings indicate that the levels of these antibodies may be altered in coronary heart disease (CHD) and also inflammatory bowel diseases (IBD), it seemed worthwhile to compare the epitope specificity of the anti-HSP60 and anti-HSP65 antibodies in the sera of patients with these diseases to those in healthy subjects. The multipin enzyme-linked immunosorbent assay method was applied with a large overlapping set of synthetic 10-mer peptides covering selected regions of human HSP60 and Mycobacterium bovis HSP65. Sera of 12 healthy persons (HP), 14 CHD, and 14 IBD patients with the same concentration of total anti-HSP60 and HSP65 IgG antibodies were tested. We have identified CHDspecific epitopes in the equatorial domain of the HSP60 protein but in neither region of the HSP65 molecule, indicating that the formation of anti-HSP60 antibodies is not or only partially due to the cross-reaction between human HSP60 and bacterial HSP65. IBD-specific epitopes were found in many regions of the HSP60 and in even more regions of the HSP65 molecule including an IBD-specific T cell epitope in region X as well. These findings indicate that the epitope specificity of the anti-human and antimycobacterial HSP60 antibodies associated with various diseases is different.

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Human heat shock protein 60 (409–424) fragment is recognized by serum antibodies of patients with acute coronary syndromes

Cited by 17 publications

References 23 publications

Serum antibody titers against heat shock protein 27 are associated with the severity of coronary artery disease

Serum antibody titers against heat shock protein 27 are associated with the severity of coronary artery disease

Expression of Heat Shock Protein 27 in Human Atherosclerotic Plaques and Increased Plasma Level of Heat Shock Protein 27 in Patients With Acute Coronary Syndrome

Comparison of epitope specificity of anti-heat shock protein 60/65 IgG type antibodies in the sera of healthy subjects, patients with coronary heart disease and inflammatory bowel disease

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