Why proteins without an α-crystallin domain should not be included in the human small heat shock protein family HSPB

Kappé, Guido; Boelens, Wilbert C.; Jong, Wilfried W. de

doi:10.1007/s12192-009-0155-4

Cited by 81 publications

(65 citation statements)

References 30 publications

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“…mRNA and protein levels of HspB11, which is controversially discussed to belong to the HspB family (Bellyei et al 2007;Kappe et al 2010), were not significantly altered in response to tMCAO in our study. This fits to previous data that HspB11 is not stress-responsive after several kinds of cellular stresses (Bartelt- Kirbach and Golenhofen 2014;Bellyei et al 2007;Kirbach and Golenhofen 2011).…”

Section: Other Hspbscontrasting

confidence: 63%

“…This subgroup consists of ten family members, named HspB1 through HspB10, although many of them have alternative names related to their molecular weight or the tissue of their preferential expression. An 11th family member, HspB11, is still controversially discussed to belong to the HspB family or not (Bellyei et al 2007; Kappe et al 2010) but was nevertheless included in our study. The main function of HspBs is to prevent irreversible protein aggregation and denaturation by keeping partially unfolded proteins in a Electronic supplementary material The online version of this article (doi:10.1007/s12192-017-0794-9) contains supplementary material, which is available to authorized users.…”

Section: Introductionmentioning

confidence: 99%

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Upregulation and phosphorylation of HspB1/Hsp25 and HspB5/αB-crystallin after transient middle cerebral artery occlusion in rats

Bartelt-Kirbach

Slowik

Beyer

et al. 2017

Cell Stress and Chaperones

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Ischemic stroke leads to cellular dysfunction, cell death, and devastating clinical outcomes. The cells of the brain react to such a cellular stress by a stress response with an upregulation of heat shock proteins resulting in activation of endogenous neuroprotective capacities. Several members of the family of small heat shock proteins (HspBs) have been shown to be neuroprotective. However, yet no systematic study examined all HspBs during cerebral ischemia. Here, we performed a comprehensive comparative study comprising all HspBs in an animal model of stroke, i.e., 1 h transient middle cerebral artery occlusion followed by 23 h of reperfusion. On the mRNA level out of the 11 HspBs investigated, HspB1/Hsp25, HspB3, HspB4/αA-crystallin, HspB5/αB-crystallin, HspB7/cvHsp, and HspB8/Hsp22 were significantly upregulated in the peri-infarct region of the cerebral cortex of infarcted hemispheres. HspB1 and HspB5 reached the highest mRNA levels and were also upregulated at the protein level, suggesting that these HspBs might be functionally most relevant. Interestingly, in the infarcted cortex, both HspB1 and HspB5 were mainly allocated to neurons and to a lesser extent to glial cells. Additionally, both proteins were found to be phosphorylated in response to ischemia. Our data suggest that among all HspBs, HspB1 and HspB5 might be most important in the neuronal stress response to ischemia/reperfusion injury in the brain and might be involved in neuroprotection.

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Section: Other Hspbscontrasting

confidence: 63%

Section: Introductionmentioning

confidence: 99%

Upregulation and phosphorylation of HspB1/Hsp25 and HspB5/αB-crystallin after transient middle cerebral artery occlusion in rats

Bartelt-Kirbach

Slowik

Beyer

et al. 2017

Cell Stress and Chaperones

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“…Also, sites for post-translational modification appear largely in this portion of the protein. Hence, it is possible that the variability at the N-terminus may have a part to play in cell's unit of sHsps which can recognize a wide range of target proteins [69][70][71][72].…”

Section: Small Heat Shock Proteinsmentioning

confidence: 99%

Cytotoxic or cytoprotective chaperones: An unfolded biology in oral lesions

Kashyap¹,

P²,

Rajguru³

2017

Clin Res Trials

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Heat shock proteins (Hsp) or the molecular chaperones are observed in most cells of humans, microbes, and in extracellular and intracellular fluids. Hsps plays an essential role under most stress conditions at the cellular and subcellular levels. It presents cytoprotective properties by the modulation of cytokine release and immunity and is involved in various physiological and pathological events. A tight regulation of molecular chaperones monitors the folding/misfolding, internal localization, and proteolytic turnover of proteins. Despite their advantageous effects, Hsps also has disadvantageous role in intensifying the inflammation. They are potential mediators of oncogenesis as they are the key regulators of cellular growth and differentiation. The authors reviewed, an overview of the role of chaperones, with respect to the lesions affecting oral and para-oral structures.

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“…Similarly to the rest of families of heat shock proteins (Hsps), their expression can be either constitutive or stress-regulated, in the latter case due to the presence of heat shock elements in their promoters. They also share with other Hsps a general role as chaperones, which basically consists of refolding denatured proteins and preventing thus their aggregation and subsequent cytotoxicity, as well as other functions related to intracellular trafficking, cytoskeletal dynamics or regulation of apoptosis (Franck et al, 2004;Sun and MacRae, 2005a;Kappe et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

Developmental Expression Pattern of Hspb8 mRNA in the Mouse Brain: Analysis Through Online Databases

García-Lax

Tomás‐Roca

Marı́n

2011

The Anatomical Record

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Hspb8 is a member of the Hspb family of chaperone-like proteins. It is involved in several neural disorders such as Alzheimer's disease, amyotrophic lateral sclerosis, hereditary distal motor neuropathy, and CharcotMarie-Tooth's disease. In this work, we aimed to characterize its expression pattern in the mouse brain, by using the information available at online databases of high-throughput in situ hybridization. Therefore, we downloaded and analyzed the image series from these databases showing Hspb8 mRNA expression from embryonic to adult and aging stages. In early gestational embryos, Hspb8 was expressed in the hippocampal anlagen and in the ventricular layer of rhombomere 4. At perinatal stages, there appeared transitory expression in the dentate gyrus and the cerebellar cortex. From perinatal to aging stages, the neurons of the mesencephalic trigeminal nucleus and cranial motor nuclei displayed stable and strong Hspb8 expression. Additionally, along these stages there was moderate and relatively homogenous expression in the anterodorsal thalamic, lateral mammillary, arcuate hypothalamic and medial habenular nuclei, and in the locus coeruleus. In its turn, the basal ganglia, cerebellar inner granular layer and diverse sensory and reticular formation nuclei of the

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Why proteins without an α-crystallin domain should not be included in the human small heat shock protein family HSPB

Cited by 81 publications

References 30 publications

Upregulation and phosphorylation of HspB1/Hsp25 and HspB5/αB-crystallin after transient middle cerebral artery occlusion in rats

Upregulation and phosphorylation of HspB1/Hsp25 and HspB5/αB-crystallin after transient middle cerebral artery occlusion in rats

Cytotoxic or cytoprotective chaperones: An unfolded biology in oral lesions

Developmental Expression Pattern of Hspb8 mRNA in the Mouse Brain: Analysis Through Online Databases

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