The protective role of yeast Cathepsin D in acetic acid-induced apoptosis depends on ANT (Aac2p) but not on the voltage-dependent channel (Por1p)

Abstract Mitochondrial reactive oxygen species (mtROS)-induced apoptosis has been suggested to contribute to myocardial ischemia/reperfusion injury. Interleukin 35 (IL-35), a novel anti-inflammatory cytokine, has been shown to protect the myocardium and inhibit mtROS production. However, its effect on cardiomyocytes upon exposure to hypoxia/reoxygenation (H/R) damage has not yet been elucidated. The present study aimed to investigate the potential protective role and underlying mechanisms of IL-35 in H/R-induced mouse neonatal cardiomyocyte injury. Mouse neonatal cardiomyocytes were challenged to H/R in the presence of IL-35, and we found that IL-35 dose dependently promotes cell viability, diminishes mtROS, maintains mitochondrial membrane potential, and decreases the number of apoptotic cardiomyocytes. Meanwhile, IL-35 remarkably activates mitochondrial STAT3 (mitoSTAT3) signaling, inhibits cytochrome c release, and reduces apoptosis signaling. Furthermore, co-treatment of the cardiomyocytes with the STAT3 inhibitor AG490 abrogates the IL-35-induced cardioprotective effects. Our study identified the protective role of IL-35 in cardiomyocytes following H/R damage and revealed that IL-35 protects cardiomyocytes against mtROS-induced apoptosis through the mitoSTAT3 signaling pathway during H/R.

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Caspase-6 mediated cleavage of guanylate cyclase alpha 1 during deoxycholate-induced apoptosis: Protective role of the nitric oxide signaling module

Cell Biology and Toxicology ◽

10.1023/b:cbto.0000013331.70391.0e ◽

2003 ◽

Vol 19 (6) ◽

pp. 373-392 ◽

Cited By ~ 15

Author(s):

C.M. Payne ◽

C.N. Waltmire ◽

C. Crowley ◽

C.L. Crowley-Weber ◽

K. Dvorakova ◽

...

Keyword(s):

Nitric Oxide ◽

Guanylate Cyclase ◽

Protective Role ◽

Nitric Oxide Signaling ◽

Caspase 6 ◽

Induced Apoptosis

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Autophagic proteins regulate cigarette smoke induced apoptosis: Protective role of heme oxygenase-1

Autophagy ◽

10.4161/auto.6767 ◽

2008 ◽

Vol 4 (7) ◽

pp. 887-895 ◽

Cited By ~ 151

Author(s):

Hong Pyo Kim ◽

Xue Wang ◽

Seon-Jin Lee ◽

Min-Hsin Huang ◽

Yong Wan ◽

...

Keyword(s):

Cigarette Smoke ◽

Heme Oxygenase ◽

Protective Role ◽

Heme Oxygenase 1 ◽

Induced Apoptosis ◽

Autophagic Proteins

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Autophagy plays a protective role during Pseudomonas aeruginosa-induced apoptosis via ROS–MAPK pathway

Innate Immunity ◽

10.1177/1753425920952156 ◽

2020 ◽

Vol 26 (7) ◽

pp. 580-591

Author(s):

Lu Han ◽

Qinmei Ma ◽

Jialin Yu ◽

Zhaoqian Gong ◽

Chenjie Ma ◽

...

Keyword(s):

Pseudomonas Aeruginosa ◽

Mapk Pathway ◽

Protective Role ◽

Vital Role ◽

Raw264.7 Cells ◽

Cellular Reactive Oxygen Species ◽

Induced Apoptosis ◽

Related Proteins ◽

The Impact

Pseudomonas aeruginosa infection can induce alveolar macrophage apoptosis and autophagy, which play a vital role in eliminating pathogens. These two processes are usually not independent. Recently, autophagy has been found to interact with apoptosis during pathogen infections. Nevertheless, the role of autophagy in P. aeruginosa-infected cell apoptosis is unclear. In this study, we explored the impact of P. aeruginosa infection on autophagy and apoptosis in RAW264.7 cells. The autophagy activator rapamycin was used to stimulate autophagy and explore the role of autophagy on apoptosis in P. aeruginosa-infected RAW264.7 cells. The results indicated that P. aeruginosa infection induced autophagy and apoptosis in RAW264.7 cells, and that rapamycin could suppress P. aeruginosa-induced apoptosis by regulating the expression of apoptosis-related proteins. In addition, rapamycin scavenged the cellular reactive oxygen species (ROS) and diminished p-JNK, p-ERK1/2 and p-p38 expression of MAPK pathways in RAW264.7 cells infected with P. aeruginosa. In conclusion, the promotion of autophagy decreased P. aeruginosa-induced ROS accumulation and further attenuated the apoptosis of RAW264.7 cells through MAPK pathway. These results provide novel insights into host–pathogen interactions and highlight a potential role of autophagy in eliminating P. aeruginosa.

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In Vitro Evidence for the Protective role of Sida rhomboidea. Roxb Extract Against LDL Oxidation and Oxidized LDL-Induced Apoptosis in Human Monocyte–Derived Macrophages

Cardiovascular Toxicology ◽

10.1007/s12012-011-9110-6 ◽

2011 ◽

Vol 11 (2) ◽

pp. 168-179 ◽

Cited By ~ 14

Author(s):

Menaka C. Thounaojam ◽

Ravirajsinh N. Jadeja ◽

Ranjisinh V. Devkar ◽

A. V. Ramachandran

Keyword(s):

Oxidized Ldl ◽

Human Monocyte ◽

Protective Role ◽

Ldl Oxidation ◽

Induced Apoptosis

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Autophagy Protects Advanced Glycation End Product-Induced Apoptosis and Expression of MMP-3 and MMP-13 in Rat Chondrocytes

BioMed Research International ◽

10.1155/2017/6341919 ◽

2017 ◽

Vol 2017 ◽

pp. 1-9 ◽

Cited By ~ 5

Author(s):

Wenzhou Huang ◽

Peng Ao ◽

Jian Li ◽

Tianlong Wu ◽

Libiao Xu ◽

...

Keyword(s):

Western Blotting ◽

Annexin V ◽

Protective Role ◽

Autophagic Flux ◽

Advanced Glycation ◽

Age Related ◽

Glycation End Products ◽

Induced Apoptosis ◽

Related Proteins

Aging is one of the most prominent risk factors for the pathological progression of osteoarthritis (OA). One feature of age-related changes in OA is advanced glycation end products (AGEs) accumulation in articular cartilage. Autophagy plays a cellular housekeeping role by removing dysfunctional cellular organelles and proteins. However, the relationship between autophagy and AGE-associated OA is unknown. The aim of this study is to determine whether autophagy participates in the pathology of AGE-treated chondrocytes and to investigate the exact role of autophagy in AGE-induced cell apoptosis and expression of matrix metalloproteinase- (MMP-) 3 and MMP-13. AGEs induced notable apoptosis that was detected by Annexin V/PI double-staining, and the upregulation of MMP-3 and MMP-13 was confirmed by Western blotting. Autophagy-related proteins were also determined by Western blotting, and chondrocytes were transfected with mCherry-GFP-LC3B-adenovirus to monitor autophagic flux. As a result, autophagy significantly increased in chondrocytes and peaked at 6 h. Furthermore, rapamycin (RA) attenuated AGE-induced apoptosis and expression of MMP-3 and MMP-13 by autophagy activation. In contrast, pretreatment with autophagy inhibitor 3-methyladenine (3-MA) enhanced the abovementioned effects of AGEs. We therefore demonstrated that autophagy is linked with AGE-related pathology in rat chondrocytes and plays a protective role in AGE-induced apoptosis and expression of MMP-3 and MMP-13.

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