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Abstract Autophagy is a conserved cellular process required to maintain homeostasis. Introduction Cells are naturally safeguarded by an efficient check-and-balance mechanism better known as cellular homeostasis to maintain the balance of a wide array of biochemical factors and processes.
Mechanism of autophagy Autophagy is a sequential process that involves initiation, elongation, maturation, fusion and degradation [ 4 ]. Full size image. Pathways controlling autophagy Under normal physiological conditions, autophagy occurs at a basal rate to maintain cellular viability and homeostasis [ 28 , 29 ].
Autophagy in cancer Autophagy is an evolutionarily conserved process for maintaining cellular homeostasis. Autophagy as tumour suppressor During normal conditions and early stage of cancer, autophagy serves as a shield to protect cells from harmful stimuli and malignant transformation.
Autophagy as tumour promoter As the tumour develops and progresses, autophagy, in turn, fuels and supports the growth of cancer cells. Modulation of autophagy in cancer Over the last decade, autophagy has emerged as a promising target for cancer therapy.
Table 1 Genetic and pharmacological inhibition of autophagy synergize with therapeutic agents in various malignancies Full size table. Current perspectives and future outlook Autophagy has been reported to have controversial roles in cancer progression. Conclusion Targeting autophagy in precision medicine for cancer is no doubt a very attractive strategy.
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Article Google Scholar Petherick KJ, Williams AC, Lane JD, Ordóñez-Morán P, Huelsken J, Collard TJ, et al. The supernatant protein concentration was determined using a bicinchoninic acid BCA protein assay kit Bio-Rad, Hercules, CA.
Each experiment was repeated at least 3 times. Densitometric analysis of the immunoreactive bands was performed using ImageJ software NIH. As an index of cell death, release into extracellular medium was measured using the LDH assay.
Briefly, supernatants were collected at the times indicated and intact cells were lysed using Triton Xcontaining lysis buffer. The amount of LDH release was determined spectrophotometrically at nm using the LDH-Cytotoxicity Assay Kit Sigma.
The quantitative data are presented as mean ± S. We first examined the dose effect of MDMA on cell viability. Cortical neuron cultures were treated with different concentration of MDMA 0.
MDMA produced a concentration-dependent decrease in cell viability Fig. Treatment with 0. When cells were treated with higher concentration of MMDA 1.
Cultured cortical neurons were treated with different concentration of MDMA for 48 h, and then cell viability was determined by MTT assay. The data are expressed as percentage of untreated controls mean ± S. We investigated the dose-dependent effect of MDMA on autophagy activity and neurite outgrowth in cultured rat cortical neurons.
Autophagy activity was assessed using immunoblotting and immunofluorescence to detect the essential autophagy protein LC3. Upon autophagy activation, the LC3-I protein localized in the cytoplasm is cleaved, lipidated, and inserted as LC3-II into autophagosome membranes.
In the present study, cortical neurons were treated with different concentrations 0. Treatment with MDMA at 0. Beclin-1 expression are known to be involved in the formation of preautophagosomal structures.
However, the expression level of beclin-1 was not affected by MDMA Fig. We then performed double immunofluorescence to correlate the LC3 expression and neurite outgrowth using anti-MAP2 a general neurite marker and anti-LC3B antibodies after 48 h of MDMA treatment.
As shown in Fig. At µM of MDMA treatment, anti-LC3B staining exhibited a more condensed diffuse distribution. After exposure to 1 mM MDMA, typical cytoplasmic LC3B punctate was formed notably in almost all neurons with shortening of total neurite length per neuron from ±18 µm control group to ±15 µm 1 mM MDMA treatment.
At higher concentrations of MDMA 1. Immunofluorescence demonstrated that MDMA triggers dose-dependent autophagosome formation accompanied by reduction of neurite outgrowth in cultured neuronal cells also see inset showing a magnified view of LC3B-labeled aggregation in MDMA-treated neuron in Fig.
Cultured cortical neurons were treated with the indicated concentrations of MDMA for 48 h, and then western blot analysis and double immunofluorescence were performed. A Western blot analysis of LC3B and beclin β-actin was used as the internal control.
Quantitative data are expressed as intensity relative to the control mean value mean ± S. C Double immunofluorescence stained images and merged images of representative cells using anti-LC3B and anti-MAP2. Intense LC3 punctate fluorescence shown in the MDMA-treated group see insets.
D Quantitation of neurite outgrowth. The total neurite length are shown as mean ± S. Although 1 mM MDMA had no obvious effect on cell viability, pharmacological actions significantly caused a decrease in neurite outgrowth and upregulation of autophagy.
Therefore, 1 mM MDMA was applied to cultures in the following experiments. We then examined the time dependent effect of MDMA on autophagy activation. The cells were treated with 1 mM MDMA for 18 h, 24 h or 48 h and subjected to western blot analysis using LC3 antibody.
The results showed that treatment with MDMA for 18, 24 and 48 h significantly induced a time-dependent increase in ration of LC3B-II to LC3B-I to 1. Double immunofluorescence staining with anti-MAP2 and anti-LC3B antibodies appeared that LC3B punctate staining was not observed within 13 h of MDMA treatment data not shown , whereas positive aggregations increased rapidly within 18 h and even more punctate staining was observed after 24 h and 48 h of MDMA treatment see inset showing a magnified view of LC3B-labeled neuronal cells in Fig.
MDMA removal for 48 h reduced autophagosome accumulation almost to the baseline, suggesting that this process is reversible data not shown. Cultured cortical neurons were treated with MDMA for different times as indicated, and then subjected to western blot analysis and double immunofluorescence staining with anti-LC3B and MAP2 antibodies.
A Western blot analysis of LC3B. β-actin was used as the internal control upper panel. B Representative double immunofluorescence and merged images using anti-LC3B and anti-MAP2 antibodies.
Intense LC3 punctate staining pattern shown in the MDMA-treated group see insets. C Quantitation of neurite outgrowth. Monodansylcadaverine MDC staining can be used to detect autophagic vacuoles AVs [29].
The autofluorescent drug MDC accumulates in AVs, but not in the early endosome compartment. Under a fluorescence microscope, AVs stained by MDC appear as distinct punctuate structures throughout the cytoplasm or within the perinuclear region.
The autophagy inhibitor 3-MA is commonly used to define the role of autophagy under various physiological conditions [30]. Pretreatment with 1 mM 3-MA effectively decreased the number 1. To further address the role of MDMA in autophagy induction, cells were pre-incubated with 3-MA for 30 min prior to induction of autophagy by MDMA for 48 h.
Cells were treated as the same above, and then double immunostaining were performed with anti-MAP2 and anti-LC3B. Interestingly, treatment with 1 mM 3-MA alone significantly promote neurite outgrowth Fig. We advance to prove 3-MA protection against MDMA-induced neuronal cell death.
Cells were pre-incubated with 3-MA for 30 min prior to different concentration of MDMA treatment for 48 h, then the neuronal death was determined by LDH assay. We further investigated the apoptotic effect of inhibition of autophagy by 3-MA after MDMA exposure.
The appearance of cleaved caspase-3 immunoreactivity is used as a marker of apoptosis. Cortical neuron cultures were treated with 2 mM MDMA in the presence or absence of 1 mM 3-MA for 24 h, and then western blot analysis and immunofluorescence were performed using antibodies against cleaved-caspase 3 and caspase 3.
Therefore, MDMA-induced neuronal death are at least partly autophagy-dependent. However, other autophagy inhibitors, wortmannin and LY, had no effect on MDMA-elicited autophagy and neurite damage data not shown.
Cultured cortical neurons were exposed to 1 mM MDMA for 48 h in the presence or absence of 1 mM 3-MA for 48 h. Autophagy activity was assay by MDC incorporation, western blot analysis and double immunofluorescence staining with anti-LC3B and MAP2 antibodies. A The autophagic vacuoles were visualized by monodansylcadaverine MDC staining and the mean number of MDC-labeled vacuoles per cortical neurons arrows was quantitation.
Quantitative data are expressed as mean ± S. B Western blot analysis of LC3B expression. Immunoblot signal ratio of LC3B-II-to-LC3B-I was quantitative by densitometric assay. C Representative double immunofluorescence and merged images using anti-LC3B and anti-MAP2 antibodies. A Cortical neuron cultures were treated with different concentrations of MDMA in the presence or absence of 1 mM 3-MA.
After 48 h, the neuronal death was determined by LDH cytotoxicity assay. The data are presented as percentage of dead cells. B Cortical neuron cultures were treated with 2 mM MDMA in the presence or absence of 1 mM 3-MA. After 48 h, the cells were immunostained with anti-NeuN antibody.
C Quantitative data of the number of NeuN-positive cells. The data are presented as percentage of the control value mean ± S. D 3-MA attenuated MDMA-induced activation of caspase 3. Cortical neuron cultures were treated with 2 mM MDMA in the presence or absence of 1 mM 3-MA for 24 h, and then western blot analysis was performed using antibodies against cleaved-caspase 3 and caspase 3.
E Representative images from cortical neuron cultures treated with 2 mM MDMA in the presence or absence of 1 mM 3-MA. After 24 h, the apoptotic cells were determined by immunostaining with anti-cleaved caspase 3.
F Quantitative data of the number of cleaved-caspase 3 positive neurons. To further clarify the detrimental role of autophagosome accumulation in MDMA-induced neurotoxicity, we employed rapamycin and Bafilomycin A1.
Cells were treated with MDMA in the presence or absence of rapamycin or Bafilomycin for 48 h and double immunostained with anti-MAP2 and anti-LC3B antibodies. However, rapamycin and Bafilomycin A1 in the presence of MDMA acted synergistically with MDMA to enhance autophagosome accumulation and neurite degeneration Fig.
Another mTOR inhibitor Torin-1 directly inhibits both mTORC1 and mTORC2. Cotreatment of MDMA with Torin-1 nM also synergistically resulted in LC3B-labed autophagosome accumulation and aggravated neurite degeneration, whereas Torin-1 alone increased LC3B immunostaining intensity slightly without affecting neurite outgrowth S1 Fig.
This result was similar to that observed in treatment with rapamycin. After treatment, the cells were performed western blot analysis or double immunofluorescence with anti-LC3B and anti-MAP2 antibodies.
A Western blot analysis of LC3B expression. The data are presented as intensity relative to the control mean value mean ± S. MDMA treatment. AMP-activated protein kinase AMPK is the key signal triggering autophagy through inactivation of mTOR and phosphorylation of ULK1 [32] , [33].
Therefore, the deactivation of mTOR triggers autophagy. To further investigate the kinase involved in MDMA-induced autophagy, levels of phosphorylated AMPK, mTOR, and ULK1 were measured. MDMA also caused a dose-dependent increase in the phosphorylation of ULK1 in Ser Fig.
Cultured cortical neurons were treated with the indicated concentrations of MDMA for 48 h, and then western blot analysis was performed using antibodies against phospho-AMPK and AMPK A , phospho-mTOR and mTOR B , phospho-ULK1 and ULK1 C.
MDMA is a neurotoxin. Autophagy activation involves in brain ischemia, trauma and neurodegeneration. In the present study, we examined the role of autophagy in MDMA-induced neurotoxicity.
Our data provide the first evidence that MDMA elicits a robust autophagic response in primary rat cortical neurons, as judged by an increase in autophagosome formation and protein expression of LC3B-II. The autophagy inhibitor 3-MA significantly reduced MDMA-induced autophagy activation and partially protected neurons against MDMA-induced neurite shortening and neuronal death.
Either enhancement of autophagosome generation by rapamycin or impairment of autophagosome clearance by Bafilomycin A1 resulted in augmented MDMA-induced autophagosome accumulation and neurite degeneration, indicating that excessive autophagy may play a detrimental role in MDMA-triggered neurotoxicity.
Furthermore, MDMA altered the phosphorylation status of AMPK and ULK1, which plays an important role in initiating autophagosome generation. Autophagy can be classified into basal and induced modes [35]. Under basal conditions in our culture system, autophagosomes and LC3-II expression were hardly detectable in healthy neurons, although the basal level of Atg proteins, such as beclin-1 and LC3-I were highly expressed.
These observations are consistent with previous observations [5]. Instead of a low level of basal autophagy, constitutive autophagy occurs in healthy neurons, and autophagic degradation is so efficient that autophagosomes cannot accumulate at detectable levels [36].
It is now well accepted that basal or low-level autophagy is cell-protective for maintenance of homeostasis and survival, while excessive or sustained autophagy can lead to self destruction or autophagic cell death, either directly or indirectly [37]. Autophagy induction and subsequent neuronal death occur in the CNS under several pathological conditions, including ischemia, trauma, glutamate-mediated excitotoxicity, and neurodegenerative protein aggregation diseases.
Autophagic flux implies a balance between autophagosome formation and autophagic degradation. Either increased autophagosome formation in the early stage or defective degradation in the late stage can lead to accumulation of autophagic vacuoles.
MDMA-induced LC3B-II accumulation could be a result of either LC3B-I to LC3B-II conversion or defects in LC3B-II degradation. In this study, 3-MA, an autophagy inhibitor at the early stage of autophagosome biogenesis, prevented MDMA-induced autophagy vacuole accumulation, suggesting MDMA may activate signaling cascades that initiate autophagosome generation.
However, it cannot be completely excluded that autophagosome accumulation might be because of organelle turnover inhibition. It is well known that MDMA induced neuron loss through apoptosis or necrosis mechanism.
In the present study, we further confirm that MDMA caused neuron loss through autophagy upregulation. Extensive or dysregulated autophagy may lead to autophagic cell death, called type II programmed cell death.
Suppression of autophagy by 3-MA can block neuronal death in response to various stress conditions in the CNS such as kainate-induced excitotoxicity in rats [40] , and rodent traumatic or ischemic brain injury [39] , [41].
Similarly, we found that 3-MA alleviated MDMA-induced neuronal death and apoptosis, suggesting autophagic cell death involves in MDMA-induced neuron loss. In addition, autophagy is a double-edged sword in neuron cell survival. There is extensive cross-talk between autophagy and other forms of cell death, such as apoptosis and necrosis.
Depending on cell types, environment and stimulation manners, autophagy can precede, inhibit or enhance apoptotic cell death and both autophagic and necrotic morphologies are observed in the same cell [43].
The discrepancies may be duo to the complex and diverse interactions among autophagy, apoptosis and cell death.
Macroautophagy, often referred to as autophagy, is a Functional strength exercises process that Augophagy in the autophagosomic-lysosomal degradation of Ajtophagy cytoplasmic actlvation, abnormal protein aggregates, Autpohagy Autophagy activation or damaged organelles. Autophagy is generally activated by conditions Autophagy activation activagion deprivation Autophagy activation has RMR and weight loss been Autophagy activation activvation physiological as well as pathological processes Autophayg as development, differentiation, neurodegenerative Autophagy activation, stress, infection, Autophagy activation cancer. The kinase mTOR is a critical regulator of autophagy induction, with activated mTOR Akt and MAPK signaling suppressing autophagy, and negative regulation of mTOR AMPK and p53 signaling promoting it. ULK1 and ULK2 form a large complex with the mammalian homolog of an autophagy-related Atg gene product mAtg13 and the scaffold protein FIP an ortholog of yeast Atg Class III PI3K complex, containing hVps34, Beclin-1 a mammalian homolog of yeast Atg6p a mammalian homolog of yeast Vps15and Atglike protein Atg14L or Barkor or ultraviolet irradiation resistance-associated gene UVRAGis required for the induction of autophagy. The Atg genes control autophagosome formation through AtgAtg5 and LC3-II Atg8-II complexes. The term Autophagy was introduced acgivation Christian Autlphagy Duve during the Autophagy activation Foundation Symposium on Lysosomes — which was Autophagy activation in Activatipn in February Autophagy activation Metabolic health solutions he was Autophagy activation with the Nobel price activatjon Autophagy activation or Medicine for Autophaagy pioneering research about peroxisomes and lysosomes. Autophagy Autophagocytosis describes the fundamental catabolic mechanism during which cells degrade dysfunctional and unnecessary cellular components. This process is driven by the action of lysosomes and promotes survival during starvation periods as the cellular energy level can thus be maintained. During classical autophagy, autophagosomes are generates, organelles which are surrounded by double membranes see Fig. The autophagosome formation is induced by class 3 phosphoinositidekinase, Atg 6 autophagy-related gene 6 and ubiquitin or ubiquitin-like modifications of the target proteins. 
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