Emerging role of heat shock proteins in cardiovascular diseases

Hazra, Joyita; Vijayakumar, Anupama; Mahapatra, Nitish R.

doi:10.1016/bs.apcsb.2022.10.008

Cited by 3 publications

(2 citation statements)

References 185 publications

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“…17 HSP27 and HSP60 are stress-responsive proteins that can protect cells from apoptosis. 18 TRAIL-Rs can mediate apoptotic signaling during cancer development. 19 Survivin can regulate caspase activation to promote cell apoptosis.…”

Section: Discussionmentioning

confidence: 99%

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TMED3 stabilizes SMAD2 by counteracting NEDD4‐mediated ubiquitination to promote ovarian cancer

Chen,

Zhang,

Han

et al. 2024

Molecular Carcinogenesis

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Ovarian cancer is a major cause of death among cancer patients. Recent research has shown that the transmembrane emp24 domain (TMED) protein family plays a role in the progression of various types of cancer. In this study, we investigated the expression of TMED3 in ovarian cancer tumors compared to nontumor tissues using immunohistochemical staining. We found that TMED3 was overexpressed in ovarian cancer tumors, and its high expression was associated with poor disease‐free and overall survival. To understand the functional implications of TMED3 overexpression in ovarian cancer, we conducted experiments to knockdown TMED3 using short hairpin RNA (shRNA). We observed that TMED3 knockdown resulted in reduced cell viability and migration, as well as increased cell apoptosis. Additionally, in subcutaneous xenograft models in BALB‐c nude mice, TMED3 knockdown inhibited tumor growth. Further investigation revealed that SMAD family member 2 (SMAD2) was a downstream target of TMED3, driving ovarian cancer progression. TMED3 stabilized SMAD2 by inhibiting the E3 ligase NEDD4‐mediated ubiquitination of SMAD2. To confirm the importance of SMAD2 in TMED3‐mediated ovarian cancer, we performed functional rescue experiments and found that SMAD2 played a critical role in this process. Moreover, we discovered that the PI3K‐AKT pathway was involved in the promoting effects of TMED3 overexpression on ovarian cancer cells. Overall, our study identifies TMED3 as a prognostic indicator and tumor promoter in ovarian cancer. Its function is likely mediated through the regulation of the SMAD2 and PI3K‐AKT signaling pathway. These findings contribute to our understanding of the molecular mechanisms underlying ovarian cancer progression and provide potential targets for therapeutic intervention.

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Section: Discussionmentioning

confidence: 99%

“…IGFBP‐1 has been shown to enhance IGF‐independent IGF‐1 actions by sequestrating IGFs within tissues, leading to activation of Akt phosphorylation 17 . HSP27 and HSP60 are stress‐responsive proteins that can protect cells from apoptosis 18 . TRAIL‐Rs can mediate apoptotic signaling during cancer development 19 .…”

Section: Discussionmentioning

confidence: 99%

TMED3 stabilizes SMAD2 by counteracting NEDD4‐mediated ubiquitination to promote ovarian cancer

Chen,

Zhang,

Han

et al. 2024

Molecular Carcinogenesis

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A Systematic Review of Proteomics in Obesity: Unpacking the Molecular Puzzle

Rodriguez-Muñoz,

Motahari-Rad,

Martin-Chaves

et al. 2024

Curr Obes Rep

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Purpose of Review The present study aims to review the existing literature to identify pathophysiological proteins in obesity by conducting a systematic review of proteomics studies. Proteomics may reveal the mechanisms of obesity development and clarify the links between obesity and related diseases, improving our comprehension of obesity and its clinical implications. Recent Findings Most of the molecular events implicated in obesity development remain incomplete. Proteomics stands as a powerful tool for elucidating the intricate interactions among proteins in the context of obesity. This methodology has the potential to identify proteins involved in pathological processes and to evaluate changes in protein abundance during obesity development, contributing to the identification of early disease predisposition, monitoring the effectiveness of interventions and improving disease management overall. Despite many non-targeted proteomic studies exploring obesity, a comprehensive and up-to-date systematic review of the molecular events implicated in obesity development is lacking. The lack of such a review presents a significant challenge for researchers trying to interpret the existing literature. Summary This systematic review was conducted following the PRISMA guidelines and included sixteen human proteomic studies, each of which delineated proteins exhibiting significant alterations in obesity. A total of 41 proteins were reported to be altered in obesity by at least two or more studies. These proteins were involved in metabolic pathways, oxidative stress responses, inflammatory processes, protein folding, coagulation, as well as structure/cytoskeleton. Many of the identified proteomic biomarkers of obesity have also been reported to be dysregulated in obesity-related disease. Among them, seven proteins, which belong to metabolic pathways (aldehyde dehydrogenase and apolipoprotein A1), the chaperone family (albumin, heat shock protein beta 1, protein disulfide-isomerase A3) and oxidative stress and inflammation proteins (catalase and complement C3), could potentially serve as biomarkers for the progression of obesity and the development of comorbidities, contributing to personalized medicine in the field of obesity. Our systematic review in proteomics represents a substantial step forward in unravelling the complexities of protein alterations associated with obesity. It provides valuable insights into the pathophysiological mechanisms underlying obesity, thereby opening avenues for the discovery of potential biomarkers and the development of personalized medicine in obesity

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STAP2 promotes the progression of renal fibrosis via HSP27

Yuan,

Wei,

Xiong

et al. 2024

J Transl Med

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Background Renal fibrosis is a key process in the progression from acute kidney injury (AKI) to chronic kidney disease (CKD), while the intricate mechanisms of renal fibrosis remain obscure. While the signal-transducing adaptor protein 2 (STAP2) was well-studied for its notable function in inflammation and immune-related disorders, its specific implication in renal fibrosis remains unclear. This study assessed the mechanism by which STAP2 could promote the progression of renal fibrosis. Methods The expression level of STAP2 in fibrotic human samples, murine fibrosis models, and cellular fibrosis models was measured, respectively. Subsequently, immunoprecipitation (IP), mass spectrometry, and RNA sequencing (RNA-seq) were employed to identify HSP27 as an interacting protein and the PI3K-AKT signaling pathway. STAP2 was thereafter knocked down or overexpressed in both in vivo and in vitro models to assess the expression levels of pathway-related and fibrosis-related proteins. Finally, the important role of STAP2 in the fibrosis process in animal models induced by ischemia-reperfusion injury (IRI) and cisplatin was validated. Results Functionally, in vivo assays demonstrated that the genetic knockout of STAP2 could remarkably mitigate epithelial-mesenchymal transition (EMT), diminish inflammatory cell infiltration, and reduce collagen deposition in mice with renal fibrosis. Conversely, in vitro assays employing STAP2-overexpressing cell models exacerbated the expression levels of fibrosis markers. The outcomes uncovered a potential mechanism by which STAP2 could modulate renal fibrosis through its impact on the expression level of phosphorylated HSP27, as well as modulating the PI3K/AKT signaling pathway. Conclusions This comprehensive investigation delineated the noticeable function of STAP2 in the advancement of renal fibrosis, and the outcomes might contribute to the development of targeted therapies concentrated on STAP2 to mitigate renal fibrosis. Supplementary Information The online version contains supplementary material available at 10.1186/s12967-024-05776-6.

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Emerging role of heat shock proteins in cardiovascular diseases

Cited by 3 publications

References 185 publications

TMED3 stabilizes SMAD2 by counteracting NEDD4‐mediated ubiquitination to promote ovarian cancer

TMED3 stabilizes SMAD2 by counteracting NEDD4‐mediated ubiquitination to promote ovarian cancer

A Systematic Review of Proteomics in Obesity: Unpacking the Molecular Puzzle

STAP2 promotes the progression of renal fibrosis via HSP27

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