scholarly journals Heat Shock Protein 22 in Physiological and Pathological Hearts: Small Molecule, Large Potentials

Cells ◽  
2021 ◽  
Vol 11 (1) ◽  
pp. 114
Author(s):  
Xiaonan Sun ◽  
Sharadhi Siri ◽  
Amirah Hurst ◽  
Hongyu Qiu
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Molecular Mechanisms ◽  
Heart Diseases ◽  
Pressure Overload ◽  
Small Heat Shock Protein ◽  
Cardiac Metabolism ◽  
Vital Role ◽  
Post Translational Modification ◽  
Heat Shock Protein 22

Small heat shock protein 22 (HSP22) belongs to the superfamily of heat shock proteins and is predominantly expressed in the heart, brain, skeletal muscle, and different types of cancers. It has been found that HSP22 is involved in variant cellular functions in cardiomyocytes and plays a vital role in cardiac protection against cardiomyocyte injury under diverse stress. This review summarizes the multiple functions of HSP22 in the heart and the underlying molecular mechanisms through modulating gene transcription, post-translational modification, subcellular translocation of its interacting proteins, and protein degradation, facilitating mitochondrial function, cardiac metabolism, autophagy, and ROS production and antiapoptotic effect. We also discuss the association of HSP22 in cardiac pathologies, including human dilated cardiomyopathy, pressure overload-induced heart failure, ischemic heart diseases, and aging-related cardiac metabolism disorder. The collected information would provide insights into the understanding of the HSP22 in heart diseases and lead to discovering the therapeutic targets.

scholarly journals Hsp22 Deficiency Induces Age-Dependent Cardiac Dilation and Dysfunction by Impairing Autophagy, Metabolism, and Oxidative Response

Antioxidants ◽  
2021 ◽  
Vol 10 (10) ◽  
pp. 1550
Author(s):  
Wenqian Wu ◽  
Xiaonan Sun ◽  
Xiaomeng Shi ◽  
Lo Lai ◽  
Charles Wang ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Essential Role ◽  
Early Stage ◽  
Small Heat Shock Protein ◽  
Vital Role ◽  
Physiological Conditions ◽  
Age Related ◽  
And Function ◽  
Heat Shock Protein 22

Heat shock protein 22 (Hsp22) is a small heat shock protein predominantly expressed in skeletal and cardiac muscle. Previous studies indicate that Hsp22 plays a vital role in protecting the heart against cardiac stress. However, the essential role of Hsp22 in the heart under physiological conditions remains largely unknown. In this study, we used an Hsp22 knockout (KO) mouse model to determine whether loss of Hsp22 impairs cardiac growth and function with increasing age under physiological conditions. Cardiac structural and functional alterations at baseline were measured using echocardiography and invasive catheterization in Hsp22 KO mice during aging transition compared to their age-matched wild-type (WT) littermates. Our results showed that Hsp22 deletion induced progressive cardiac dilation along with declined function during the aging transition. Mechanistically, the loss of Hsp22 impaired BCL-2–associated athanogene 3 (BAG3) expression and its associated cardiac autophagy, undermined cardiac energy metabolism homeostasis and increased oxidative damage. This study showed that Hsp22 played an essential role in the non-stressed heart during the early stage of aging, which may bring new insight into understanding the pathogenesis of age-related dilated cardiomyopathy.

Regulation of Sam68 activity by small heat shock protein 22

2006 ◽  
Vol 99 (5) ◽  
pp. 1353-1362 ◽  
Author(s):  
Kameswara R. Badri ◽  
Suhasini Modem ◽  
Herve C. Gerard ◽  
Insia Khan ◽  
Mihir Bagchi ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Small Heat Shock Protein ◽  
Heat Shock Protein 22

scholarly journals Comparative Transcriptomic Analysis of Biological Process and Key Pathway in Three Cotton (Gossypium spp.) Species Under Drought Stress

2019 ◽  
Vol 20 (9) ◽  
pp. 2076 ◽  
Author(s):  
Md Mosfeq-Ul Hasan ◽  
Fanglu Ma ◽  
Faisal Islam ◽  
Muhammad Sajid ◽  
Zakaria H. Prodhan ◽  
...  
Keyword(s):  
Drought Stress ◽  
Heat Shock ◽  
Drought Tolerance ◽  
Heat Shock Protein ◽  
Molecular Mechanisms ◽  
Biological Process ◽  
Expression Profiles ◽  
Gene Expression Profiles ◽  
Small Heat Shock Protein ◽  
Cotton Species

Drought is one of the most important abiotic stresses that seriously affects cotton growth, development, and production worldwide. However, the molecular mechanism, key pathway, and responsible genes for drought tolerance incotton have not been stated clearly. In this research, high-throughput next generation sequencing technique was utilized to investigate gene expression profiles of three cotton species (Gossypium hirsutum, Gossypium arboreum, and Gossypium barbadense L.) under drought stress. A total of 6968 differentially expressed genes (DEGs) were identified, where 2053, 742, and 4173 genes were tested as statistically significant; 648, 320, and 1998 genes were up-regulated, and 1405, 422, and 2175 were down-regulated in TM-1, Zhongmian-16, and Pima4-S, respectively. Total DEGs were annotated and classified into functional groups under gene ontology analysis. The biological process was present only in tolerant species(TM-1), indicating drought tolerance condition. The Kyoto encyclopedia of genes and genomes showed the involvement of plant hormone signal transduction and metabolic pathways enrichment under drought stress. Several transcription factors associated with ethylene-responsive genes (ICE1, MYB44, FAMA, etc.) were identified as playing key roles in acclimatizing to drought stress. Drought also caused significant changes in the expression of certain functional genes linked to abscisic acid (ABA) responses (NCED, PYL, PP2C, and SRK2E), reactive oxygen species (ROS) related in small heat shock protein and 18.1 kDa I heat shock protein, YLS3, and ODORANT1 genes. These results will provide deeper insights into the molecular mechanisms of drought stress adaptation in cotton.

A novel Lys141Thr mutation in small heat shock protein 22 (HSPB8) gene in Charcot–Marie–Tooth disease type 2L

2013 ◽  
Vol 23 (8) ◽  
pp. 656-663 ◽  
Author(s):  
Khriezhanuo Nakhro ◽  
Jin-Mo Park ◽  
Ye Jin Kim ◽  
Bo Ram Yoon ◽  
Jeong Hyun Yoo ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Small Heat Shock Protein ◽  
Disease Type ◽  
Charcot Marie Tooth ◽  
Charcot Marie Tooth Disease ◽  
Heat Shock Protein 22 ◽  
Tooth Disease

scholarly journals The small heat-shock protein αB-crystallin uses different mechanisms of chaperone action to prevent the amorphous versus fibrillar aggregation of α-lactalbumin

2012 ◽  
Vol 448 (3) ◽  
pp. 343-352 ◽  
Author(s):  
Melissa Kulig ◽  
Heath Ecroyd
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Molecular Mechanisms ◽  
Amyloid Fibrils ◽  
Conformational Stability ◽  
Critical Role ◽  
Small Heat Shock Protein ◽  
Αb Crystallin ◽  
Amorphous Aggregation ◽  
Fibril Aggregates

Stress conditions can destabilize proteins, promoting them to unfold and adopt intermediately folded states. Partially folded protein intermediates are unstable and prone to aggregation down off-folding pathways leading to the formation of either amorphous or amyloid fibril aggregates. The sHsp (small heat-shock protein) αB-crystallin acts as a molecular chaperone to prevent both amorphous and fibrillar protein aggregation; however, the precise molecular mechanisms behind its chaperone action are incompletely understood. To investigate whether the chaperone activity of αB-crystallin is dependent upon the form of aggregation (amorphous compared with fibrillar), bovine α-lactalbumin was developed as a model target protein that could be induced to aggregate down either off-folding pathway using comparable buffer conditions. Thus when α-lactalbumin was reduced it aggregated amorphously, whereas a reduced and carboxymethylated form aggregated to form amyloid fibrils. Using this model, αB-crystallin was shown to be a more efficient chaperone against amorphously aggregating α-lactalbumin than when it aggregated to form fibrils. Moreover, αB-crystallin forms high molecular mass complexes with α-lactalbumin to prevent its amorphous aggregation, but prevents fibril formation via weak transient interactions. Thus, the conformational stability of the protein intermediate, which is a precursor to aggregation, plays a critical role in modulating the chaperone mechanism of αB-crystallin.

scholarly journals Hot-spot residue in small heat-shock protein 22 causes distal motor neuropathy

2004 ◽  
Vol 36 (6) ◽  
pp. 597-601 ◽  
Author(s):  
Joy Irobi ◽  
Katrien Van Impe ◽  
Pavel Seeman ◽  
Albena Jordanova ◽  
Ines Dierick ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Hot Spot ◽  
Small Heat Shock Protein ◽  
Motor Neuropathy ◽  
Heat Shock Protein 22
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