Heat shock proteins with an emphasis on HSP 60

Malik, Javid Ahmad; Lone, Rafiq

doi:10.1007/s11033-021-06676-4

Cited by 25 publications

(13 citation statements)

References 106 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…HSPD1 is constitutively expressed in mitochondria and cytoplasm and plays a key role like chaperoning, thermotolerance, apoptosis, cancer, immunology and embryonic development [20]. HSP60 expression promotes Embryonic stem cells (ESCs) differentiation and inhibits ESCs apoptosis [21].…”

Section: Discussionmentioning

confidence: 99%

PRM-based quantitative proteomics analysis of altered HSPs expression in villi and decidua of early missed abortion patients

Chen

Luo

et al. 2022

Preprint

View full text Add to dashboard Cite

Objective: In this study，we aimed to identify differentially expressed heat shock proteins (HSPs) profile in the villi and decidua from early missed abortion(EMA) patients. Methods: By using high-throughput and high-precision Parallel Reaction Monitoring (PRM)-based targeted proteomics technique, this study studied the expressions of HSPs in villi and decidua of 10 EMA patients and 10 controls. Meanwhile, the expressions of 3 HSPs in villi of another 22 EMA patients and 22 controls were verified with Western blotting and immunohistochemistry (IHC). Results:Compared with the control group, there were potential differences in the expressions of 16 HSPs and 42 polypeptides in human villi and decidua. Among them, HSP90AB1, HSPD1 and HSPA13 were down-regulated in expressions in villi of EMA patients, with a statistically significant difference, which was consistent with the verification results of Western blot and IHC. Conclusion: Using PRM- based targeted proteomics technique, this study for the first time screens and quantitatively analyzes the expression profile of HSPs in villi and decidua of patients with EMA. The significant down-regulated expressions of HSP90AB1, HSPD1 and HSPA13 are discovered to have a potentially intimate association with the occurrence of EMA. Findings in our study may provide novel potential research targets related to HSPs for the pathogenesis, prevention and treatment of EMA.

show abstract

Section: Discussionmentioning

confidence: 99%

PRM-based quantitative proteomics analysis of altered HSPs expression in villi and decidua of early missed abortion patients

Chen

Luo

et al. 2022

Preprint

View full text Add to dashboard Cite

show abstract

“…HSP60 is one of the major chaperone molecules that are ubiquitously expressed in all life forms [ 22 ]. HSP60 plays a crucial role in assisting with the folding, assembly, and transport of cellular proteins [ 23 , 24 ].…”

Section: Discussionmentioning

confidence: 99%

Structural Alternation in Heat Shock Proteins of Activated Macrophages

Zhang

Wei

Zhang

et al. 2021

Cells

View full text Add to dashboard Cite

The inflammatory response of macrophages is an orderly and complex process under strict regulation accompanied by drastic changes in morphology and functions. It is predicted that proteins will undergo structural changes during these finely regulated processes. However, changes in structural proteome in macrophages during the inflammatory response remain poorly characterized. In the present study, we applied limited proteolysis coupled mass spectrometry (LiP-MS) to identify proteome-wide structural changes in lipopolysaccharide (LPS)-activated macrophages. We identified 386 structure-specific proteolytic fingerprints from 230 proteins. Using the Gene Ontology (GO) biological process enrichment, we discovered that proteins with altered structures were enriched into protein folding-related terms, in which HSP60 was ranked as the most changed protein. We verified the structural changes in HSP60 by using cellular thermal shift assay (CETSA) and native CETSA. Our results showed that the thermal stability of HSP60 was enhanced in activated macrophages and formed an HSP10-less complex. In conclusion, we demonstrate that in situ structural systems biology is an effective method to characterize proteomic structural changes and reveal that the structures of chaperone proteins vary significantly during macrophage activation.

show abstract

“…However, when cells are faced with hypoxia, the formation of complexes will be reduced and release Bax for translocation into the mitochondria, which results in the release of cytochrome c as an apoptotic signal (35). The HSP60-10 complex responds to oxidative stress and induces apoptosis when cells are under the dual stress of hypoxia and DNA damage (Figure 1B) (36).…”

Section: Responses Of Hsps Under Different Stress Conditionsmentioning

confidence: 99%

Heat shock proteins and viral infection

Zhang

2022

Front. Immunol.

View full text Add to dashboard Cite

Heat shock proteins (HSPs) are a kind of proteins which mostly found in bacterial, plant and animal cells, in which they are involved in the monitoring and regulation of cellular life activities. HSPs protect other proteins under environmental and cellular stress by regulating protein folding and supporting the correctly folded structure of proteins as chaperones. During viral infection, some HSPs can have an antiviral effect by inhibiting viral proliferation through interaction and activating immune pathways to protect the host cell. However, although the biological function of HSPs is to maintain the homeostasis of cells, some HSPs will also be hijacked by viruses to help their invasion, replication, and maturation, thereby increasing the chances of viral survival in unfavorable conditions inside the host cell. In this review, we summarize the roles of the heat shock protein family in various stages of viral infection and the potential uses of these proteins in antiviral therapy.

show abstract

Heat shock proteins with an emphasis on HSP 60

Cited by 25 publications

References 106 publications

PRM-based quantitative proteomics analysis of altered HSPs expression in villi and decidua of early missed abortion patients

PRM-based quantitative proteomics analysis of altered HSPs expression in villi and decidua of early missed abortion patients

Structural Alternation in Heat Shock Proteins of Activated Macrophages

Heat shock proteins and viral infection

Contact Info

Product

Resources

About