scholarly journals Caveolin-1 plays a key role in the oleanolic acid-induced apoptosis of HL-60 cells

2014 ◽  
Vol 32 (1) ◽  
pp. 293-301 ◽  
Author(s):  
WEI MA ◽  
DI-DI WANG ◽  
LI LI ◽  
YU-KUAN FENG ◽  
HONG-MEI GU ◽  
...  
2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Qingqiang Xu ◽  
Wenwen Shi ◽  
Pan Lv ◽  
Wenqi Meng ◽  
Guanchao Mao ◽  
...  

AbstractAflatoxin B1 (AFB1) is a potent hepatocarcinogen in humans and exposure to AFB1 is known to cause both acute and chronic hepatocellular injury. As the liver is known to be the main target organ of aflatoxin, it is important to identify the key molecules that participate in AFB1-induced hepatotoxicity and to investigate their underlying mechanisms. In this study, the critical role of caveolin-1 in AFB1-induced hepatic cell apoptosis was examined. We found a decrease in cell viability and an increase in oxidation and apoptosis in human hepatocyte L02 cells after AFB1 exposure. In addition, the intracellular expression of caveolin-1 was increased in response to AFB1 treatment. Downregulation of caveolin-1 significantly alleviated AFB1-induced apoptosis and decreased cell viability, whereas overexpression of caveolin-1 reversed these effects. Further functional analysis showed that caveolin-1 participates in AFB1-induced oxidative stress through its interaction with Nrf2, leading to the downregulation of cellular antioxidant enzymes and the promotion of oxidative stress-induced apoptosis. In addition, caveolin-1 was found to regulate AFB1-induced autophagy. This finding was supported by the effect that caveolin-1 deficiency promoted autophagy after AFB1 treatment, leading to the inhibition of apoptosis, whereas overexpression of caveolin-1 inhibited autophagy and accelerated apoptosis. Interestingly, further investigation showed that caveolin-1 participates in AFB1-induced autophagy by regulating the EGFR/PI3K-AKT/mTOR signaling pathway. Taken together, our data reveal that caveolin-1 plays a crucial role in AFB1-induced hepatic cell apoptosis via the regulation of oxidation and autophagy, which provides a potential target for the development of novel treatments to combat AFB1 hepatotoxicity.


Oncotarget ◽  
2017 ◽  
Vol 8 (15) ◽  
pp. 24314-24326 ◽  
Author(s):  
Qingmei Kang ◽  
Yue Xiang ◽  
Dan Li ◽  
Jie Liang ◽  
Xiong Zhang ◽  
...  

2009 ◽  
Vol 378 (1) ◽  
pp. 21-26 ◽  
Author(s):  
Xiangxuan Zhao ◽  
Yong Liu ◽  
Qi Ma ◽  
Xiaohui Wang ◽  
Haijing Jin ◽  
...  

2008 ◽  
Vol 294 (1) ◽  
pp. H392-H401 ◽  
Author(s):  
Daniela Volonte ◽  
Charles F. McTiernan ◽  
Marek Drab ◽  
Michael Kasper ◽  
Ferruccio Galbiati

Caveolae are 50- to 100-nm invaginations of the plasma membrane. Caveolins are the structural protein components of caveolar membranes. The caveolin gene family is composed of three members: caveolin-1, caveolin-2, and caveolin-3. Caveolin-1 and caveolin-2 are coexpressed in many cell types, including adipocytes, endothelial cells, epithelial cells, and fibroblasts. In contrast, caveolin-3 expression is essentially restricted to skeletal and smooth muscle cells as well as cardiac myocytes. While the interaction between caveolin-1 and caveolin-2 has been documented previously, the reciprocal interaction between endogenous caveolin-1 and caveolin-3 and their functional role in cell types expressing both isoforms have yet to be identified. Here we demonstrate for the first time that caveolin-1 and caveolin-3 are coexpressed in mouse and rat cardiac myocytes of the atria but not ventricles. We also found that caveolin-1 and caveolin-3 can interact and form heterooligomeric complexes in this cell type. Doxorubicin is an effective anticancer agent, but its use is limited by the possible development of cardiotoxicity. Using caveolin-1- and caveolin-3-null mice, we show that both caveolin-1 and caveolin-3 expression are required for doxorubicin-induced apoptosis in the atria through activation of caspase 3. Together, these results bring new insight into the functional role of caveolae and suggest that caveolin-1/caveolin-3 heterooligomeric complexes may play a key role in chemotherapy-induced cardiotoxicity in the atria.


Tumor Biology ◽  
2010 ◽  
Vol 31 (6) ◽  
pp. 643-650 ◽  
Author(s):  
Juwon Park ◽  
Eunkyung Bae ◽  
Chansu Lee ◽  
Sung-Soo Yoon ◽  
Yang Seok Chae ◽  
...  

2010 ◽  
Vol 126 (2) ◽  
pp. 426-436 ◽  
Author(s):  
Oscar M. Tirado ◽  
Caitlin M. MacCarthy ◽  
Naheed Fatima ◽  
Joaquín Villar ◽  
Silvia Mateo-Lozano ◽  
...  

Molecules ◽  
2016 ◽  
Vol 21 (11) ◽  
pp. 1599 ◽  
Author(s):  
Siling Bi ◽  
Fuhao Chu ◽  
Mina Wang ◽  
Bi Li ◽  
Pei Mao ◽  
...  

Oncogene ◽  
2000 ◽  
Vol 19 (29) ◽  
pp. 3256-3265 ◽  
Author(s):  
Terry L Timme ◽  
Alexei Goltsov ◽  
Salahaldin Tahir ◽  
Likun Li ◽  
Jianxiang Wang ◽  
...  
Keyword(s):  

2001 ◽  
Vol 280 (4) ◽  
pp. C823-C835 ◽  
Author(s):  
Jun Liu ◽  
Peiyee Lee ◽  
Ferruccio Galbiati ◽  
Richard N. Kitsis ◽  
Michael P. Lisanti

The potential role of caveolin-1 in apoptosis remains controversial. Here, we investigate whether caveolin-1 expression is proapoptotic or antiapoptotic using a well-defined antisense approach. We show that NIH/3T3 cells harboring antisense caveolin-1 are resistant to staurosporine-induced apoptosis, as assessed using cell morphology, DNA content, caspase 3 activation, and focal adhesion kinase cleavage. Importantly, sensitivity to apoptosis is recovered when caveolin-1 levels are restored. Conversely, recombinant stable expression of caveolin-1 in T24 bladder carcinoma cells sensitizes these cells to caspase 3 activation. Consistent with the observations using NIH/3T3 cells, downregulation of caveolin-1 in T24 cells substantially diminishes caspase 3-like activity. Loss of sensitivity to apoptotic stimulation is recovered by inhibition of the phosphatidylinositol 3-kinase pathway using LY-294002, suggesting a possible mechanism for the sensitizing effect of caveolin-1. Thus our results suggest that caveolin-1 may act as a coupling or sensitizing factor in signaling apoptotic cell death in both fibroblastic (NIH/3T3) and epithelial (T24) cells.


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