Tolerization against atherosclerosis using heat shock protein 60

Wick, Cecilia

doi:10.1007/s12192-015-0659-z

Cited by 35 publications

(28 citation statements)

References 109 publications

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“…Finally, another immune cell type involved in atheroprogression (albeit to a lesser degree) are T-regulatory cells, which mediate atheroprotection by amplifying the release of IL-10, thereby resulting in immune suppression ( 139 – 142 ). However, the role of HSP27 in T-regulatory function during atheroprogression is uncertain ( 143 ). Mast cells, a key cell type that populates atherosclerotic plaque, are classically known to react immediately to allergens via cross-linking of cell surface IgE resulting in degranulation, histamine release, and synthesis of arachidonic acid metabolites, which can activate stress-signaling and pro-apoptotic pathways ( 144 ).…”

Section: Hsp27 In Atherosclerosismentioning

confidence: 99%

Extracellular Release and Signaling by Heat Shock Protein 27: Role in Modifying Vascular Inflammation

et al. 2016

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Heat shock protein 27 (HSP27) is traditionally viewed as an intracellular chaperone protein with anti-apoptotic properties. However, recent data indicate that a number of heat shock proteins, including HSP27, are also found in the extracellular space where they may signal via membrane receptors to alter gene transcription and cellular function. Therefore, there is increasing interest in better understanding how HSP27 is released from cells, its levels and composition in the extracellular space, and the cognate cell membrane receptors involved in effecting cell signaling. In this paper, the knowledge to date, as well as some emerging paradigms about the extracellular function of HSP27 is presented. Of particular interest is the role of HSP27 in attenuating atherogenesis by modifying lipid uptake and inflammation in the plaque. Moreover, the abundance of HSP27 in serum is an emerging new biomarker for ischemic events. Finally, HSP27 replacement therapy may represent a novel therapeutic opportunity for chronic inflammatory disorders, such as atherosclerosis.

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Section: Hsp27 In Atherosclerosismentioning

confidence: 99%

Extracellular Release and Signaling by Heat Shock Protein 27: Role in Modifying Vascular Inflammation

et al. 2016

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“…It is thought that T-cell reactivity to Hsp60 is less prominent in men age 50 and over because the majority of the T-cells have already formed from blood to the site of inflammation in atherosclerotic plaques and lymphocytes from peripheral blood may no longer present the specific antigen repertoire of cells in vessel walls [ 55 ]. This T-cell reactivity to Hsp60 is capable of triggering both innate and adaptive immune responses that initiate the earliest inflammatory stage of atherosclerosis, and mitochondrial Hsp60 is increasingly being recognised as a key autoantigen at the sites of endothelial inflammation [ 56 , 57 ]. However, the mechanisms leading to expression of Hsp60 during the initiation of arteriosclerosis due to T-cell reactivity to Hsp60 are still not well understood.…”

Section: Hsp60 and Inflammationmentioning

confidence: 99%

Does Hsp60 Provide a Link between Mitochondrial Stress and Inflammation in Diabetes Mellitus?

Juwono

Martinus

2016

Journal of Diabetes Research

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The focus of this review is to summarise the known relationships between the expression of heat shock protein 60 (Hsp60) and its association with the pathogenesis of Type 1 and Type 2 diabetes mellitus. Hsp60 is a mitochondrial stress protein that is induced by mitochondrial impairment. It is known to be secreted from a number of cell types and circulating levels have been documented in both Types 1 and 2 diabetes mellitus patients. The biological significance of extracellular Hsp60, however, remains to be established. We will examine the links between Hsp60 and cellular anti- and proinflammatory processes and specifically address how Hsp60 appears to affect immune inflammation by at least two different mechanisms: as a ligand for innate immune receptors and as an antigen recognised by adaptive immune receptors. We will also look at the role of Hsp60 during immune cell activation in atherosclerosis, a significant risk factor during the pathogenesis of diabetes mellitus.

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“…It has been reported that administration route of HSP60 immunization could affect the progression of atherosclerosis [31]. The current understanding is that HSP60 oral administration protects from atherosclerosis due to the HSP60-induced mucosal immune tolerance, whereas subcutaneous injection promotes atherosclerosis progression [12,[31][32][33]. Oral administrations of HSP60 increase MSDCs (myeloid derived suppressor cells) that suppress the progression of atherosclerosis [31].…”

Section: Plos Onementioning

confidence: 99%

Humoral immune response to heat shock protein 60 of Aggregatibacter actinomycetemcomitans and cross-reactivity with malondialdehyde acetaldehyde-modified LDL

et al. 2020

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Atherosclerosis is a chronic inflammatory disease and major cause of mortality worldwide. One of the crucial steps for atherosclerotic plaque development is oxidation of low-density lipoprotein (LDL). Through the oxidation, highly immunogenic epitopes are created and the immune system is activated. Association between atherosclerosis and periodontal diseases is well documented, and one of the main oral pathogens common in periodontitis is Aggregatibacter actinomycetemcomitans (Aa). Heat shock protein 60 (HSP60) is an important virulence factor for Aa bacteria and a strong activator of the immune system. Cross-reactivity of HSP60 and oxidized LDL (OxLDL) antibodies could be a potential mechanism in the progression of atherosclerosis and one possible link between atherosclerosis and periodontitis. Human plasma samples from neonates and mothers were analyzed to determine if antibody titer to Aa-HSP60 protein is already present in newborns. Further objectives were to characterize antibody response in Aa-HSP60 immunized mice and to determine possible antibody cross-reaction with oxidized LDL. We demonstrated that newborns already have IgM antibody levels to Aa-HSP60. We also showed that in mice, Aa-HSP60 immunization provoked IgG and IgM antibody response not only to Aa-HSP60 but also to malondialdehyde acetaldehyde-modified LDL (MAA-LDL). Competition assay revealed that the antibodies were specific to Aa-HSP60 and cross-reacted with MAA-LDL. Our results suggest a possibility of molecular mimicry between Aa-HSP60 and MAA-LDL, making it intriguing to speculate on the role of HSP60 protein in atherosclerosis that manifests at young age.

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Tolerization against atherosclerosis using heat shock protein 60

Cited by 35 publications

References 109 publications

Extracellular Release and Signaling by Heat Shock Protein 27: Role in Modifying Vascular Inflammation

Extracellular Release and Signaling by Heat Shock Protein 27: Role in Modifying Vascular Inflammation

Does Hsp60 Provide a Link between Mitochondrial Stress and Inflammation in Diabetes Mellitus?

Humoral immune response to heat shock protein 60 of Aggregatibacter actinomycetemcomitans and cross-reactivity with malondialdehyde acetaldehyde-modified LDL

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