Heat Shock Protein 60 in Hepatocellular Carcinoma: Insights and Perspectives

Hoter, Abdullah; Rizk, Sandra; Naim, Hassan Y.

doi:10.3389/fmolb.2020.00060

Cited by 22 publications

(15 citation statements)

References 95 publications

(98 reference statements)

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“…Studies demonstrated that exosomal HSP60 has high potential for clinical use, such as a potential clinical biomarker for diagnosing, monitoring disease progression, and assessing prognosis of a variety of cancers. 260 , 261 , 262 Research showed that HSP60 is increased in patient tumor–tissue samples or EXs obtained from the blood of patients, and some groups are evaluating the application of potential HSP60 inhibitors for treatment of certain cancers, 262 induced a decrease in the HSP60 levels or its PTMs leading to cell death. 263 These findings suggest HSP60 has potential clinical applications of both diagnosis and therapy for cancers.…”

Section: Hspss As Potential Therapeutic Targetsmentioning

confidence: 99%

Heat shock proteins: Biological functions, pathological roles, and therapeutic opportunities

Yang

Zhou

et al. 2022

MedComm

188

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The heat shock proteins (HSPs) are ubiquitous and conserved protein families in both prokaryotic and eukaryotic organisms, and they maintain cellular proteostasis and protect cells from stresses. HSP protein families are classified based on their molecular weights, mainly including large HSPs, HSP90, HSP70, HSP60, HSP40, and small HSPs. They function as molecular chaperons in cells and work as an integrated network, participating in the folding of newly synthesized polypeptides, refolding metastable proteins, protein complex assembly, dissociating protein aggregate dissociation, and the degradation of misfolded proteins. In addition to their chaperone functions, they also play important roles in cell signaling transduction, cell cycle, and apoptosis regulation. Therefore, malfunction of HSPs is related with many diseases, including cancers, neurodegeneration, and other diseases. In this review, we describe the current understandings about the molecular mechanisms of the major HSP families including HSP90/HSP70/HSP60/HSP110 and small HSPs, how the HSPs keep the protein proteostasis and response to stresses, and we also discuss their roles in diseases and the recent exploration of HSP related therapy and diagnosis to modulate diseases. These research advances offer new prospects of HSPs as potential targets for therapeutic intervention.

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Section: Hspss As Potential Therapeutic Targetsmentioning

confidence: 99%

Heat shock proteins: Biological functions, pathological roles, and therapeutic opportunities

Yang

Zhou

et al. 2022

MedComm

188

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“…HSPD1 assists in proteolytic degradation of misfolded proteins and performs many physiological functions but can also be pathogenic in various conditions. Previous reports highlight the implication of HSP60 in human cancer development [ 24 ]. It was also reported that upregulation of HSPD1 suppressed the activity of mitochondrial complex IV, resulting in an increase in ROS concentration in cardiac muscle [ 25 ].…”

Section: Discussionmentioning

confidence: 99%

Rosavin Ameliorates Hepatic Inflammation and Fibrosis in the NASH Rat Model via Targeting Hepatic Cell Death

Albadawy

Hasanin

Agwa

et al. 2022

IJMS

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Background: Non-alcoholic fatty liver disease (NAFLD) represents the most common form of chronic liver disease that urgently needs effective therapy. Rosavin, a major constituent of the Rhodiola Rosea plant of the family Crassulaceae, is believed to exhibit multiple pharmacological effects on diverse diseases. However, its effect on non-alcoholic steatohepatitis (NASH), the progressive form of NAFLD, and the underlying mechanisms are not fully illustrated. Aim: Investigate the pharmacological activity and potential mechanism of rosavin treatment on NASH management via targeting hepatic cell death-related (HSPD1/TNF/MMP14/ITGB1) mRNAs and their upstream noncoding RNA regulators (miRNA-6881-5P and lnc-SPARCL1-1:2) in NASH rats. Results: High sucrose high fat (HSHF) diet-induced NASH rats were treated with different concentrations of rosavin (10, 20, and 30 mg/kg/day) for the last four weeks of dietary manipulation. The data revealed that rosavin had the ability to modulate the expression of the hepatic cell death-related RNA panel through the upregulation of both (HSPD1/TNF/MMP14/ITGB1) mRNAs and their epigenetic regulators (miRNA-6881-5P and lnc-SPARCL1-1:2). Moreover, rosavin ameliorated the deterioration in both liver functions and lipid profile, and thereby improved the hepatic inflammation, fibrosis, and apoptosis, as evidenced by the decreased protein levels of IL6, TNF-α, and caspase-3 in liver sections of treated animals compared to the untreated NASH rats. Conclusion: Rosavin has demonstrated a potential ability to attenuate disease progression and inhibit hepatic cell death in the NASH animal model. The produced effect was correlated with upregulation of the hepatic cell death-related (HSPD1, TNF, MMP14, and ITGB1) mRNAs—(miRNA-6881-5P—(lnc-SPARCL1-1:2) RNA panel.

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“…HSPs are classified into the HSP27, HSP40, HSP47, HSP60, HSP70, HSP110 and HSP150 families according to their molecular weight. The role of HSPD1 on the growth of cancer cells is highly controversial (18). HSPA1A and HSPA8 are molecular chaperone which are related to various intracellular process (19).…”

Section: Discussionmentioning

confidence: 99%

Proteomic Analysis of Hepatocellular Carcinoma Tissues With Encapsulation Shows Up-regulation of Leucine Aminopeptidase 3 and Phosphoenolpyruvate Carboxykinase 2

Kuhara

Kitagawa

Baron

et al. 2021

Cancer Genomics Proteomics

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Heat Shock Protein 60 in Hepatocellular Carcinoma: Insights and Perspectives

Cited by 22 publications

References 95 publications

Heat shock proteins: Biological functions, pathological roles, and therapeutic opportunities

Heat shock proteins: Biological functions, pathological roles, and therapeutic opportunities

Rosavin Ameliorates Hepatic Inflammation and Fibrosis in the NASH Rat Model via Targeting Hepatic Cell Death

Proteomic Analysis of Hepatocellular Carcinoma Tissues With Encapsulation Shows Up-regulation of Leucine Aminopeptidase 3 and Phosphoenolpyruvate Carboxykinase 2

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