Small Heat Shock Proteins Induce a Cerebral Inflammatory Reaction

Bruinsma, Ilona B.; Jager, Mieke de; Carrano, Anna; Versleijen, Alexandra A M; Veerhuis, Robert; Boelens, Wilbert C.; Rozemüller, Annemieke; Waal, R.M.W. de; Verbeek, Marcel M.

doi:10.1523/jneurosci.0945-11.2011

Cited by 36 publications

(33 citation statements)

References 52 publications

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“…Glial cells have also been reported to release Hsp70, conferring protection to neighboring neurons (81). Extracellular hsp have been observed to interact with amyloid β peptides, which are involved in the pathology of Alzheimer’s disease (82, 83). Moreover, Hsp70 and Hsp90 inhibited amyloid β aggregation in vitro conditions (84).…”

Section: The Export Of Hspmentioning

confidence: 99%

Extracellular Heat Shock Proteins

Maio¹,

Vázquez

2013

Shock

151

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The expression of heat shock proteins (hsp) is a basic and well conserved cellular response to an array of stresses. These proteins are involved in the repair of cellular damage induced by the stress, which is necessary for the salutary resolution from the insult. Moreover, they confer protection from subsequent insults, which has been coined stress tolerance. Since these proteins are expressed in subcellular compartments, it was thought that their function during stress conditions was circumscribed to the intracellular environment. However, it is now well established that hsp can also be present outside cells where they appear to display a function different than the well understood chaperone role. Extracellular hsp act as alert stress signals priming other cells, particularly of the immune system, to avoid the propagation of the insult and favor resolution. Since the majority of hsp do not possess a secretory peptide signal, they are likely be exported by a non-classical secretory pathway. Different mechanisms have been proposed to explain the export of hsp, including translocation across the plasma membrane and release associated with lipid vesicles, as well as the passive release after cell death by necrosis. Extracellular hsp appear in various flavors, including membrane-bound and membrane-free forms. All of these variants of extracellular hsp suggest that their interactions with cells may be quite diverse, both in target cell types and the activation signaling pathways. This review addresses some of our current knowledge about the release and relevance of extracellular hsp.

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Section: The Export Of Hspmentioning

confidence: 99%

Extracellular Heat Shock Proteins

Maio¹,

Vázquez

2013

Shock

151

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“…These data suggest a potential role for αB-crystallin in directing substrate ubiquitination in the ubiquitin proteasome pathway, which may assist in maintaining cellular homeostasis by degrading proteins that will not refold properly. Activation of autophagy or the infl ammatory response may also be a role for αB-crystallin in protein quality control as has been suggested for other sHSPs (Carra et al 2008(Carra et al , 2009Bruinsma et al 2011 ).…”

Section: Chaperonementioning

confidence: 87%

Multifunctional Roles of αB-Crystallin in Skeletal and Cardiac Muscle Homeostasis and Disease

Mitzelfelt

Benjamin

2015

Heat Shock Proteins

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αB-Crystallin, or HspB5, is a small molecular-weight heat shock protein expressed highly in cardiac and skeletal muscle with multifaceted cellular roles including, chaperone function towards essential myofi brillar components. Insights into protective roles played by αB-crystallin, as well as mutations in the gene encoding αB-crystallin, CRYAB , which resulted in human pathologies, have highlighted the critical functions of αB-crystallin in both skeletal and cardiac muscle, inter alia . Various human mutations in CRYAB appear to have tissue-specifi c effects, with loss of αB-crystallin only impacting skeletal muscle under basal conditions. This review aims to highlight the roles of αB-crystallin in skeletal and cardiac muscle homeostasis as well as under conditions of stress and disease, drawing insights from human pathologies resulting from CRYAB mutations, and to discuss the potential of using induced pluripotent stem cells to model αB-crystallin-opathies in vitro.

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“…Interestingly, Cellular Physiology and Biochemistry Cellular Physiology and Biochemistry the proinflammatory effect of HSP6 does not seem to be limited to a single parameter, it also modulates multiple inflammatory factors including ICAM-1, IL-8 and MCP-1 [99]. According to these findings, HSPB6 not only affects Aβ accumulation and aggregation, but also may contribute to the neuropathology by actively triggering the inflammatory reactions in both AD and HCHWA-D.…”

Section: Role Of Hspb6 In Neuronal Diseasesmentioning

confidence: 99%

Study of HSPB6: Insights into the Properties of the Multifunctional Protective Agent

Xiao

Zhou

et al. 2017

Cell Physiol Biochem

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HSPB6(Heat shock protein B6), is also referred to as P20/HSP20. Unlike other many other members of sHSP(small Heat shock protein) family, which tend to form high-molecular-mass oligomers, in solution, human HSPB6 only forms dimers. However, it still exhibits chaperon-like activity comparable with that of HSPB5. It is expressed ubiquitously, with high and constitutive expression in muscular tissues. sHSPs characteristically function as molecular chaperones and HSPB6 also has a molecular chaperone activity. HSPB6 is up-regulated in response to diverse cellular stress or damage and protect cells from otherwise lethal conditions. HSPB6 is widely recognized as a principle mediator of cardioprotective signaling and recent studies have unraveled the protective role of HSPB6 in disease or injury to the central nervous system. Moreover, accumulating evidence has implicated HSPB6 as a key mediator of diverse vital physiological processes, such as smooth muscle relaxation, platelet aggregation. The versatility of HSPB6 can be explained by its direct involvement in regulating different client proteins and its ability to form heterooligomer with other sHSPs, which seems to be dependent on HSPB6 phosphorylation. This review focuses on the properties including expression and regulation pattern, phosphorylation, chaperon activity, multiple cellular targets of HSPB6, as well as its possible role in physical and pathological conditions.

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Small Heat Shock Proteins Induce a Cerebral Inflammatory Reaction

Cited by 36 publications

References 52 publications

Extracellular Heat Shock Proteins

Extracellular Heat Shock Proteins

Multifunctional Roles of αB-Crystallin in Skeletal and Cardiac Muscle Homeostasis and Disease

Study of HSPB6: Insights into the Properties of the Multifunctional Protective Agent

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