5 results on '"Chia-Yuan Lin"'
Search Results
2. PINK1/parkin-mediated mitophagy pathway is related to neuroprotection by carnosic acid in SH-SY5Y cells
- Author
-
Chia-Yuan Lin and Chia-Wen Tsai
- Subjects
Small interfering RNA ,Mitochondrial Diseases ,Ubiquitin-Protein Ligases ,Phosphatase ,PINK1 ,Toxicology ,Parkin ,03 medical and health sciences ,chemistry.chemical_compound ,0404 agricultural biotechnology ,Cell Line, Tumor ,Mitophagy ,Humans ,Tensin ,RNA, Small Interfering ,Oxidopamine ,030304 developmental biology ,Membrane Potential, Mitochondrial ,0303 health sciences ,Chemistry ,Voltage-Dependent Anion Channel 1 ,Cytochromes c ,Carnosic acid ,04 agricultural and veterinary sciences ,General Medicine ,040401 food science ,Mitochondria ,nervous system diseases ,Cell biology ,Neuroprotective Agents ,Abietanes ,Protein Kinases ,VDAC1 ,Food Science - Abstract
Impairment in mitophagy contributes to the pathology of Parkinson's disease. This study investigated whether Phosphatase and tensin homologue (PTEN)-induced kinase 1 (PINK1)/parkin-mediated mitophagy is linked to the protective effect of carnosic acid (CA) from rosemary. Treatment of SH-SY5Y cells with 6-hydroxydopamine (6-OHDA) disrupted the mitochondrial membrane potential, inhibited voltage-dependent anion channel 1 (VDAC1) protein, and induced cytosolic cytochrome c, but CA pretreatment reversed these findings. By immunofluorescence, CA pretreatment was shown to increase the co-localization of red fluorescence (parkin) and MitoTracker green FM fluorescence (mitochondria), indicating that CA promoted the translocation of parkin into mitochondria. Immunoprecipitation with VDAC1 antibody showed that 6-OHDA treatment decreased the interaction of ubiquitinated protein with VDAC1. However, CA pretreatment reversed this reduction in the interaction of ubiquitinated protein with VDAC1. Silencing of PINK1 and parkin by use of small interfering RNA (siRNA) attenuated the ability of CA to reverse 6-OHDA-inhibited autophagic vacuoles. Moreover, in PINK1 siRNA-transfected cells, CA no longer reversed these actions of 6-OHDA on the inhibition of mitophagy-related proteins (PINK1, parkin, VDAC1, and LC3-II) and anti-apoptotic Bcl-2 protein, as well as the induction of apoptotic-related proteins, and nuclear condensation. In conclusion, CA appears to counteract the neurotoxicity of 6-OHDA by activating PINK1/parkin-mediated mitophagy.
- Published
- 2019
3. Inhibition of JNK by pi class of glutathione S -transferase through PKA/CREB pathway is associated with carnosic acid protection against 6-hydroxydopamine-induced apoptosis
- Author
-
Chi-Rei Wu, Ruey Hwang Chou, Chia-Wen Tsai, Shu-Wei Chang, Ru Huei Fu, Jing Hsien Chen, and Chia Yuan Lin
- Subjects
0301 basic medicine ,MAP Kinase Kinase 4 ,Poly ADP ribose polymerase ,Apoptosis ,Toxicology ,CREB ,Cell Line ,03 medical and health sciences ,chemistry.chemical_compound ,0302 clinical medicine ,Humans ,Enzyme Inhibitors ,Phosphorylation ,RNA, Small Interfering ,Cyclic AMP Response Element-Binding Protein ,Oxidopamine ,Sulfonamides ,Hydroxydopamine ,biology ,Kinase ,Carnosic acid ,General Medicine ,Isoquinolines ,Cyclic AMP-Dependent Protein Kinases ,Molecular biology ,Neuroprotective Agents ,030104 developmental biology ,Glutathione S-transferase ,Glutathione S-Transferase pi ,chemistry ,Abietanes ,biology.protein ,030217 neurology & neurosurgery ,Signal Transduction ,Food Science - Abstract
Pi class of glutathione S-transferase (GST) is known to suppress c-Jun N-terminal kinase (JNK)-related apoptosis through protein-protein interactions. Moreover, signaling by PKA/cAMP response element binding protein (CREB) is necessary for GSTP up-regulation. This study explored whether carnosic acid (CA) from rosemary prevents 6-hydroxydopamine (6-OHDA)-induced neurotoxicity by inhibition of JNK through GSTP via PKA/CREB signaling. Results indicated that the GSTP protein was increased in SH-SY5Y cells treated with CA for 18 and 24 h. However, CA had no significant effect on alpha or mu class of GST. Treatment of CA increased the induction of p-PKAα, nuclear p-CREB, and CRE-DNA binding activity. These effects of CA were attenuated in cells pretreated with the PKA inhibitor H89. CA pretreatment suppressed 6-OHDA-induced apoptosis by inhibition of JNK phosphorylation, poly(ADP)-ribose polymerase cleavage, and nuclear condensation. Pretreatment with H89 and GSTP siRNA attenuated the ability of CA to reverse 6-OHDA-induced apoptosis. By use of immunoprecipitation with JNK antibody to examine the interaction of GSTP-JNK with CA, we showed that CA pretreatment increased the immunoprecipitation of GSTP after 6-OHDA treatment, which suggests that CA promoted the interaction between GSTP and JNK. Conclusion: CA prevents 6-OHDA-induced apoptosis via inhibition of JNK by GSTP through the PKA/CREB pathway.
- Published
- 2017
4. Upregulation of OPA1 by carnosic acid is mediated through induction of IKKγ ubiquitination by parkin and protects against neurotoxicity
- Author
-
Wen Jiun Chen, Ru Huei Fu, Chia Yuan Lin, and Chia-Wen Tsai
- Subjects
endocrine system ,Small interfering RNA ,Ubiquitin-Protein Ligases ,Neurotoxins ,Apoptosis ,IκB kinase ,Mitochondrion ,Toxicology ,Mitochondrial Dynamics ,Parkin ,GTP Phosphohydrolases ,03 medical and health sciences ,Mitofusin-2 ,DNM1L ,0404 agricultural biotechnology ,Downregulation and upregulation ,Cell Line, Tumor ,medicine ,Humans ,Oxidopamine ,030304 developmental biology ,0303 health sciences ,Base Sequence ,Chemistry ,Transcription Factor RelA ,Ubiquitination ,04 agricultural and veterinary sciences ,General Medicine ,medicine.disease ,040401 food science ,eye diseases ,I-kappa B Kinase ,Mitochondria ,Up-Regulation ,Cell biology ,Neuroprotective Agents ,Abietanes ,Optic Atrophy 1 ,Food Science - Abstract
An imbalance in mitochondrial dynamics is strongly associated with Parkinson's disease. The fusion protein optic atrophy 1 (OPA1) is up-regulated through the activation of parkin-mediated IκB kinase γ (IKKγ)/p65 signaling. This study investigated whether the neuroprotection of carnosic acid (CA) from rosemary is involved in mitochondrial dynamics and OPA1 protein induction by parkin/IKKγ/p65 signaling. The neurotoxin 6-hydroxydopamine (6-OHDA) treated with SH-SY5Y cells decreased OPA1 and mitofusin 2 fusion proteins, but increased fission 1 and dynamin related protein 1 (DRP1) fission proteins. By immunofluorescence, 6-OHDA induced the fluorescence of green spots outside the mitochondria, indicating that cytochrome c was released to the cytoplasm. Except for the effects on DRP1 protein, CA pretreatment reversed these effects of 6-OHDA. Additionally, CA treatment increased the ubiquitination of IKKγ, nuclear p65 protein, OPA1-p65 DNA binding activity, and OPA1 protein. However, transfection of parkin small interfering RNA (siRNA) attenuated these effects of CA. Furthermore, transfection of OPA1 siRNA abolished the action of CA to reverse 6-OHDA-increased cytosolic cytochrome c protein, apoptotic-related protein cleavage, and cell death. In conclusion, the mechanism by which CA counteracts the toxicity of 6-OHDA is through modulation of mitochondrial dynamics and upregulation of OPA1 via activation of the parkin/IKKγ/p65 pathway.
- Published
- 2020
5. Inhibition of 12-lipoxygenase during baicalein-induced human lung nonsmall carcinoma H460 cell apoptosis
- Author
-
Henry W.-C. Leung, M.-Y. Lai, Hong-Zin Lee, W.H. Yang, and Chia-Yuan Lin
- Subjects
Programmed cell death ,Lung Neoplasms ,Blotting, Western ,Cell ,Apoptosis ,Biology ,Toxicology ,chemistry.chemical_compound ,Carcinoma, Non-Small-Cell Lung ,Cell Line, Tumor ,medicine ,Humans ,Lipoxygenase Inhibitors ,Fragmentation (cell biology) ,DNA Primers ,Cyclin-dependent kinase 1 ,Reverse Transcriptase Polymerase Chain Reaction ,General Medicine ,Cell cycle ,Flow Cytometry ,Apoptotic body ,Antineoplastic Agents, Phytogenic ,respiratory tract diseases ,Baicalein ,medicine.anatomical_structure ,chemistry ,Biochemistry ,Flavanones ,Cancer research ,RNA ,Phytotherapy ,Scutellaria baicalensis ,Food Science - Abstract
Baicalein is known as a 12-lipoxygenase (12-LOX) inhibitor. The 12-LOX is found to be involved in the progression of human cancers and the inhibitor of 12-LOX offers a target for the prevention cancer. We demonstrated the inhibitory effect of baicalein on the gene and protein expression of 12-LOX in H460 human lung nonsmall carcinoma cell line. Treatment of baicalein inhibited the growth of H460 cells in a dose-dependent manner. Following 24 h exposure to 50 μM baicalein, cell cycle analysis revealed an increase in the cell population in S-phase. During the S-phase arrest, baicalein decreased the protein levels of cdk1 and cyclin B1, which are the regulating proteins of S-phase transition to G2/M-phase, in this study. Furthermore, baicalein induced the most of H460 cell apoptosis after treatment for 48 h. H460 cells formed vesicles and apoptotic body, and then floated after treatment with baicalein. Baicalein-induced H460 cell apoptosis was confirmed by DNA condensation and fragmentation. Baicalein-induced apoptosis were also accompanied by decreasing in Bcl-2 and proform of caspase-3 and increasing p53 and Bax protein levels. Pretreatment with a specific caspase-3 inhibitor, Ac-DEVD-CHO, partially reduced baicalein-induced cell death, indicating baicalein induces apoptosis is partially dependent on caspase-3 pathway in H460 cells. These data suggest that baicalein, a 12-LOX inhibitor, inhibits the proliferation of H460 cells via S-phase arrest and induces apoptosis in association with the regulation of molecules in the cell cycle and apoptosis-related proteins.
- Published
- 2007
Catalog
Discovery Service for Jio Institute Digital Library
For full access to our library's resources, please sign in.