Physico-chemical properties of two point mutants of small heat shock protein HspB6 (Hsp20) with abrogated cardioprotection

Shatov, Vladislav M.; Gusev, Nikolai B.

doi:10.1016/j.biochi.2020.04.021

Cited by 8 publications

(3 citation statements)

References 39 publications

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“…In this study, HSPB6 and HSPA6 were upregulated in the heat-stressed groups. The HSPB6 is a multifunctional protein involved in regulating smooth muscle contraction and demonstrating cardioprotective activity [ 40 ]. Under HS, the HSPB6 is heavily upregulated to maintain the cells’ homeostasis conditions and improve the cell survival functions [ 41 ].…”

Section: Discussionmentioning

confidence: 99%

Transcriptomic Analysis of the Porcine Gut in Response to Heat Stress and Dietary Soluble Fiber from Beet Pulp

Kim

Roura

Choi

et al. 2022

Genes

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This study aimed to investigate the impact of heat stress (HS) and the effects of dietary soluble fiber from beet pulp (BP) on gene expression (differentially expressed genes, DEGs) of the porcine jejunum. Out of the 82 DEGs, 47 genes were up-regulated, and 35 genes were downregulated between treatments. The gene ontology (GO) enrichment analysis showed that the DEGs were related mainly to the actin cytoskeleton organization and muscle structure development in biological processes, cytoplasm, stress fibers, Z disc, cytoskeleton, and the extracellular regions in cellular composition, and actin binding, calcium ion binding, actin filament binding, and pyridoxal phosphate binding in the molecular function. The KEGG pathway analysis showed that the DEGs were involved in hypertrophic cardiomyopathy, dilated cardiomyopathy, vascular smooth muscle contraction, regulation of actin cytoskeleton, mucin type O-glycan biosynthesis, and African trypanosomiasis. Several of the genes (HSPB6, HSP70, TPM1, TAGLN, CCL4) in the HS group were involved in cellular oxidative stress, immune responses, and cellular differentiation. In contrast, the DEGs in the dietary BP group were related to intestinal epithelium integrity and immune response to pathogens, including S100A2, GCNT3, LYZ, SCGB1A1, SAA3, and ST3GAL1. These findings might help understand the HS response and the effect of dietary fiber (DF) regarding HS and be a valuable reference for future studies.

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Section: Discussionmentioning

confidence: 99%

Transcriptomic Analysis of the Porcine Gut in Response to Heat Stress and Dietary Soluble Fiber from Beet Pulp

Kim

Roura

Choi

et al. 2022

Genes

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show abstract

“…This effect appears to be mediated by a direct interaction of HSPB6 with BECN1 ( 127 ). These ideas concerning the role of HSPB6 in autophagy were generated in the context of the description of a novel human mutation in the gene encoding HSPB6 (HSPB6S10F) identified in patients with dilated cardiomyopathy (DCM) ( 128 , 129 ). Negative effects of HSPB6S10F were associated with autophagy dysregulation.…”

Section: The Role Of Hsps In Regulated Cell Deathmentioning

confidence: 99%

The role of heat shock proteins in the pathogenesis of heart failure (Review)

Sklifasovskaya,

Blagonravov,

Ryabinina

et al. 2023

Int J Mol Med

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The influence of heat shock proteins (HSPs) on protein quality control systems in cardiomyocytes is currently under investigation. The effect of HSPs on the regulated cell death of cardiomyocytes (CMCs) is of great importance, since they play a major role in the implementation of compensatory and adaptive mechanisms in the event of cardiac damage. HSPs mediate a number of mechanisms that activate the apoptotic cascade, playing both pro- and anti-apoptotic roles depending on their location in the cell. Another type of cell death, autophagy, can in some cases lead to cell death, while in other situations it acts as a cell survival mechanism. The present review considered the characteristics of the expression of HSPs of different molecular weights in CMCs in myocardial damage caused by heart failure, as well as their role in the realization of certain types of regulated cell death.

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“…HSPB6 is widely expressed in different tissues with the highest levels in smooth muscles and in cardiac and skeletal muscles [ 153 , 154 ]. Similar to other HSPBs, HSPB6 can form homodimers and tetramers in solution [ 155 , 156 , 157 , 158 ], but it is also able to form complexes with HSPB1, HSPB5, and HSPB7 [ 159 , 160 , 161 , 162 , 163 , 164 , 165 ], and to bind the co-chaperone BAG3 [ 103 , 113 , 166 , 167 , 168 , 169 ]. Like HSPB1, HSPB4, and HSPB5, HSPB6 not only has a strong chaperone activity, but it is also implicated in the regulation of apoptosis, due to its capability to inhibit Bax translocation to mitochondria [ 170 ].…”

Section: The Family Of the Small Hsps (Hspbs) And Their Role In Prote...mentioning

confidence: 99%

The Role of Small Heat Shock Proteins in Protein Misfolding Associated Motoneuron Diseases

Tedesco

Ferrari

Cozzi

et al. 2022

IJMS

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Motoneuron diseases (MNDs) are neurodegenerative conditions associated with death of upper and/or lower motoneurons (MNs). Proteostasis alteration is a pathogenic mechanism involved in many MNDs and is due to the excessive presence of misfolded and aggregated proteins. Protein misfolding may be the product of gene mutations, or due to defects in the translation process, or to stress agents; all these conditions may alter the native conformation of proteins making them prone to aggregate. Alternatively, mutations in members of the protein quality control (PQC) system may determine a loss of function of the proteostasis network. This causes an impairment in the capability to handle and remove aberrant or damaged proteins. The PQC system consists of the degradative pathways, which are the autophagy and the proteasome, and a network of chaperones and co-chaperones. Among these components, Heat Shock Protein 70 represents the main factor in substrate triage to folding, refolding, or degradation, and it is assisted in this task by a subclass of the chaperone network, the small heat shock protein (sHSPs/HSPBs) family. HSPBs take part in proteostasis by bridging misfolded and aggregated proteins to the HSP70 machinery and to the degradative pathways, facilitating refolding or clearance of the potentially toxic proteins. Because of its activity against proteostasis alteration, the chaperone system plays a relevant role in the protection against proteotoxicity in MNDs. Here, we discuss the role of HSPBs in MNDs and which HSPBs may represent a valid target for therapeutic purposes.

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Physico-chemical properties of two point mutants of small heat shock protein HspB6 (Hsp20) with abrogated cardioprotection

Cited by 8 publications

References 39 publications

Transcriptomic Analysis of the Porcine Gut in Response to Heat Stress and Dietary Soluble Fiber from Beet Pulp

Transcriptomic Analysis of the Porcine Gut in Response to Heat Stress and Dietary Soluble Fiber from Beet Pulp

The role of heat shock proteins in the pathogenesis of heart failure (Review)

The Role of Small Heat Shock Proteins in Protein Misfolding Associated Motoneuron Diseases

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