Elevated sodium leads to the increased expression of HSP60 and induces apoptosis in HUVECs

Jakic, Bojana; Buszko, Maja; Cappellano, Giuseppe; Wick, Georg

doi:10.1371/journal.pone.0179383

Cited by 51 publications

(49 citation statements)

References 74 publications

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“…(37) Additionally, in endothelial cells, the expression of HSP60 is a marker of chemical stress such as from smoking or free radicals, and increases the risk of atherosclerosis. (35) In contrast to our results, Kleinridders et al (38) reported that mitochondrial dysfunction is induced by downregulation of HSP60 in diabetic mice, and ROS production and insulin resistance are increased. In our previous study, we found that mitochondria accumulate in neurite beading regions (18) and induce superoxide production in hydrogen peroxide-treated neuronal cells.…”

Section: Discussioncontrasting

confidence: 99%

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Proteomic study on neurite responses to oxidative stress: search for differentially expressed proteins in isolated neurites of N1E-115 cells

Fukui

Okihiro

Ohfuchi

et al. 2019

J. Clin. Biochem. Nutr.

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Reactive oxygen species attack several living organs and induce cell death. Previously, we found axonal/dendrite degeneration before the induction of cell death in hydrogen peroxide treated neuro blastoma: N1E 115 cells and primary neurons. This phenomenon may be connected with membrane oxidation, microtubule desta bilization and disruption of intracellular calcium homeostasis. However, its detailed mechanisms are not fully understood. Here, we identified proteins after treatment with hydrogen peroxide using isolated neurites by liquid chromatography matrix assisted laser desorption/ionization time of flight/time of flight analysis. Twenty one proteins were increased after treatment with hydro gen peroxide. Specifically, 5 proteins which were secretogranin 1, heat shock protein family D member 1, Brain acid soluble protein 1, heat shock 70 kDa protein 5 and superoxide dismutase 1, were identified of all experiments and increased in isolated neurites of hydrogen peroxide treated cells compared to the controls. Further more, secretogranin 1 and heat shock protein family D member 1 protein expressions were significantly increased in normal aged and Alzheimer's transgenic mice brains. These results indicate that secretogranin 1 and heat shock protein family D member 1 might contribute to reactive oxygen species induced neurite degeneration. Both proteins have been related to neurodegenerative disorders, so their study may shed light on neurite dysfunction.

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Section: Discussioncontrasting

confidence: 99%

“…(34) Much of the literature on HSP60 is related to immune diseases. (35) However, several studies have demonstrated a relationship between changes in HSP60 and neurodegenerative disorders. (34,36,37) HSP60 binds to amyloid precursor protein and beta-amyloid, and accumulates in the mitochondria of AD transgenic mice brains.…”

Section: Discussionmentioning

confidence: 99%

Proteomic study on neurite responses to oxidative stress: search for differentially expressed proteins in isolated neurites of N1E-115 cells

Fukui

Okihiro

Ohfuchi

et al. 2019

J. Clin. Biochem. Nutr.

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“…An outline was drawn around each cell (100 cells per sample) and the area, integrated density and mean gray value were measured along with adjacent background readings. Next, corrected total cell fluorescence (CTCF) = integrated density (area of selected cell × mean fluorescence of background readings) was calculated as described previously [68].…”

Section: Immunofluorescencementioning

confidence: 99%

Crosstalk between Androgen-ZIP9 Signaling and Notch Pathway in Rodent Sertoli Cells

Kamińska

Marek

Pardyak

et al. 2020

IJMS

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Our recent study demonstrated altered expression of Notch ligands, receptors, and effector genes in testes of pubertal rats following reduced androgen production or signaling. Herein we aimed to explore the role of nuclear androgen receptor (AR) and membrane androgen receptor (Zrt- and Irt-like protein 9; ZIP9) in the regulation of Notch pathway activation in rodent Sertoli cells. Experiments were performed using TM4 and 15P-1 Sertoli cell lines and rat primary Sertoli cells (PSC). We found that testosterone (10−8 M–10−6 M) increased the expression of Notch1 receptor, its active form Notch1 intracellular domain (N1ICD) (p < 0.05, p < 0.01, p < 0.001), and the effector genes Hey1 (p < 0.05, p < 0.01, p < 0.001) and Hes1 (p < 0.05, p < 0.001) in Sertoli cells. Knockdown of AR or ZIP9 as well as antiandrogen exposure experiments revealed that (i) action of androgens via both AR and ZIP9 controls Notch1/N1ICD expression and transcriptional activity of recombination signal binding protein (RBP-J), (ii) AR-dependent signaling regulates Hey1 expression, (iii) ZIP9-dependent pathway regulates Hes1 expression. Our findings indicate a crosstalk between androgen and Notch signaling in Sertoli cells and point to cooperation of classical and non-classical androgen signaling pathways in controlling Sertoli cell function.

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“…Cytosolic HSP60 promotes the activation of procaspase-3 through cytochrome c and dATP in an ATP-dependent manner, suggesting a pro-apoptotic function [15]. Elevated sodium chloride concentration induces apoptosis in human umbilical vein endothelial cells and induces cytosolic and surface expression of HSP60 as well, which triggers autoimmune responses and leads to atherosclerosis [17]. However, in this case, the pro-or anti-apoptotic function of cytosolic HSP60 has not been clearly characterized.…”

Section: Dual Functions Of Hsp60 In Cytosolmentioning

confidence: 99%

“…The contradictory role of cytosolic HSP60 on the regulation of apoptosis has been demonstrated in different studies [14,15]. HSP60 in the cytosol has a pro-survival function, while it also participates in the apoptosis process upon cell death stimuli [15][16][17].…”

Section: Introductionmentioning

confidence: 99%

Functional Compartmentalization of HSP60-Survivin Interaction between Mitochondria and Cytosol in Cancer Cells

Huang

Yeh

2019

Cells

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Heat shock protein 60 (HSP60) and survivin reside in both the cytosolic and mitochondrial compartments under physiological conditions. They can form HSP60-survivin complexes through protein-protein interactions. Their expression levels in cancer tissues are positively correlated and higher expression of either protein is associated with poor clinical prognosis. The subcellular location of HSP60-survivin complex in either the cytosol or mitochondria is cell type-dependent, while the biological significance of HSP60-survivin interaction remains elusive. Current knowledge indicates that the function of HSP60 partly rests on where HSP60-survivin interaction takes place. HSP60 has a pro-survival function when binding to survivin in the mitochondria through interacting with other factors such as CCAR2 and p53. In response to cell death signals, mitochondrial survivin functions through preventing procaspase activation. Degradation of cytosolic survivin leads to the loss of mitochondrial membrane potential and aberrant mitosis processes. On the other hand, HSP60 release from mitochondria to cytosol upon death stimuli might exert a pro-death function, either through stabilizing Bax, enhancing procaspase-3 activation, or increasing protein ubiquitination. Combining the knowledge of mitochondrial HSP60-survivin complex function, cytosolic survivin degradation effect, and pro-death function upon mitochondria release of HSP60, a hypothetical scenario for HSP60-survivin shuttling upon death stimuli is proposed.

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Elevated sodium leads to the increased expression of HSP60 and induces apoptosis in HUVECs

Cited by 51 publications

References 74 publications

Proteomic study on neurite responses to oxidative stress: search for differentially expressed proteins in isolated neurites of N1E-115 cells

Proteomic study on neurite responses to oxidative stress: search for differentially expressed proteins in isolated neurites of N1E-115 cells

Crosstalk between Androgen-ZIP9 Signaling and Notch Pathway in Rodent Sertoli Cells

Functional Compartmentalization of HSP60-Survivin Interaction between Mitochondria and Cytosol in Cancer Cells

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