Curcumin Upregulate HO-1 Expression but Downregulate HO-2 Expression in SHSY5Y Cell

2010 ◽  
Author(s):  
Xiaodong Shi ◽  
Yu Li
Keyword(s):  
Shsy5y Cell

scholarly journals Study on the influence of G82S RAGE polymorphism on RAGE-Amyloid interaction in AD pathology

2019 ◽  
Author(s):  
Rani Cathrine. C ◽  
Bincy Lukose ◽  
P. Rani
Keyword(s):  
Cell Line ◽  
Binding Affinity ◽  
Structural Changes ◽  
Md Simulations ◽  
Binding Pocket ◽  
Enhanced Expression ◽  
Shsy5y Cell ◽  
High Affinity Receptor ◽  
Aβ42 Peptide

AbstractReceptor for advanced glycation end products (RAGE) has been implicated in the pathophysiology of AD due to its ability to bind amyloid-beta and mediate inflammatory response. G82S RAGE polymorphism is associated with AD but the molecular mechanism for this association is not understood. Our previous in silico study indicated a higher binding affinity for mutated G82S RAGE, which could be caused due to changes in N linked glycosylation at residue N81. To confirm this hypothesis, in the present study molecular dynamics (MD) simulations were used to simulate the wild type (WT) and G82S glycosylated structures of RAGE to identify the global structural changes and to find the binding efficiency with Aβ42 peptide. Binding pocket analysis of the MD trajectory showed that cavity/binding pocket in mutant G82S glycosylated RAGE variants is more exposed and accessible to external ligands compared to WT RAGE, which can enhance the affinity of RAGE for Aβ. To validate the above concept, an in vitro binding study was carried using SHSY5Y cell line expressing recombinant WT and mutated RAGE variant individually to which HiLyte Fluor labeled Aβ42 was incubated at different concentrations. Saturated binding kinetics method was adopted to determine the Kd values for Aβ42 binding to RAGE. The Kd value for Aβ42-WT and Aβ42-mutant RAGE binding were 92±40 nM (95% CI-52 to 152nM; R2-0.92) and 45±20 nM (95% CI −29 to 64nM; R2-0.93), respectively. The Kd value of <100nM observed for both variants implicates RAGE as a high-affinity receptor for Aβ42 and mutant RAGE has higher affinity compared to WT. The alteration in binding affinity is responsible for activation of the inflammatory pathway as implicated by enhanced expression of TNFα and IL6 in mutant RAGE expressing cell line which gives a mechanistic view for the G82S RAGE association with AD.

scholarly journals Neurotoxicity of pre-incubated alpha-synuclein with neutral nanoliposomes on PC12 and SHSY5Y cell lines

2017 ◽  
Vol 0 (0) ◽  
pp. 0-0 ◽  
Author(s):  
Farhang Aliakbari ◽  
Ali. Akbar Shabani ◽  
Hassan Bardania ◽  
Hadieh Alsadat Eslampanah Seyedi ◽  
Hossein Mohammad-Beigi ◽  
...  
Keyword(s):  
Cell Lines ◽  
Alpha Synuclein ◽  
Shsy5y Cell

N-acetylcysteineamide protects against manganese-induced toxicity in SHSY5Y cell line

2015 ◽  
Vol 1608 ◽  
pp. 157-166 ◽  
Author(s):  
Yasaswi Maddirala ◽  
Shakila Tobwala ◽  
Nuran Ercal
Keyword(s):  
Cell Line ◽  
Shsy5y Cell

scholarly journals Protection against Mitochondrial and Metal Toxicity Depends on Functional Lipid Binding Sites in ATP13A2

2016 ◽  
Vol 2016 ◽  
pp. 1-11 ◽  
Author(s):  
Shaun Martin ◽  
Sarah van Veen ◽  
Tine Holemans ◽  
Seyma Demirsoy ◽  
Chris van den Haute ◽  
...  
Keyword(s):  
Binding Sites ◽  
Lipid Binding ◽  
Stress Conditions ◽  
Activation Mechanism ◽  
Mitochondrial Stress ◽  
Cellular Protection ◽  
Shsy5y Cell ◽  
Related Stress ◽  
P Type

The late endo-/lysosomal P-type ATPase ATP13A2 (PARK9) is implicated in Parkinson’s disease (PD) and Kufor-Rakeb syndrome, early-onset atypical Parkinsonism. ATP13A2 interacts at the N-terminus with the signaling lipids phosphatidic acid (PA) and phosphatidylinositol (3,5) bisphosphate (PI(3,5)P2), which modulate ATP13A2 activity under cellular stress conditions. Here, we analyzed stable human SHSY5Y cell lines overexpressing wild-type (WT) or ATP13A2 mutants in which three N-terminal lipid binding sites (LBS1–3) were mutated. We explored the regulatory role of LBS1–3 in the cellular protection by ATP13A2 against mitochondrial stress induced by rotenone and found that the LBS2-3 mutants displayed an abrogated protective effect. Moreover, in contrast to WT, the LBS2 and LBS3 mutants responded poorly to pharmacological inhibition of, respectively, PI(3,5)P2 and PA formation. We further demonstrate that PA and PI(3,5)P2 are also required for the ATP13A2-mediated protection against the toxic metals Mn2+, Zn2+, and Fe3+, suggesting a general lipid-dependent activation mechanism of ATP13A2 in various PD-related stress conditions. Our results indicate that the ATP13A2-mediated protection requires binding of PI(3,5)P2 to LBS2 and PA to LBS3. Thus, targeting the N-terminal lipid binding sites of ATP13A2 might offer a therapeutic approach to reduce cellular toxicity of various PD insults including mitochondrial stress.

scholarly journals Hydrogen sulfide generation from L-cysteine in the human glioblastoma-astrocytoma U-87 MG and neuroblastoma SHSY5Y cell lines

2017 ◽  
Vol 64 (1) ◽  
Author(s):  
Maria Wróbel ◽  
Patrycja Bronowicka-Adamska ◽  
Anna Bentke
Keyword(s):  
Hydrogen Sulfide ◽  
Cell Lines ◽  
Neuroblastoma Cells ◽  
Hplc Method ◽  
Human Glioblastoma ◽  
Astrocytoma Cells ◽  
Shsy5y Cell ◽  
Mercaptopyruvate Sulfurtransferase ◽  
Catalyzed Reactions

Hydrogen sulfide (H2S) is endogenously synthesized from L-cysteine in reactions catalyzed by cystathionine beta-synthase (CBS, EC 4.2.1.22) and gamma-cystathionase (CSE, EC 4.4.1.1). The role of 3-mercaptopyruvate sulfurtransferase (MPST, EC 2.8.1.2) in H2S generation is also considered; it could be important for tissues with low CTH activity, e.g. cells of the nervous system. The expression and the activity of CBS, CTH, and MPST have been detected in the human glioblastoma-astrocytoma (U-87 MG) and neuroblastoma (SHSY5Y) cell lines. In both the cell lines, the expression and activity of MPST were the highest among the investigated enzymes, suggesting its possible role in the generation of H2S. The RP-HPLC method was used to determine cystathionine and alpha-ketobutyrate, products of the CBS and CTH-catalyzed reactions. A difference in cystathionine levels between cell homogenates with totally CTH-inhibiting concentrations of DL-propargylglycine and without the inhibitor was employed to evaluate the activity of CBS. A higher expression and the activities of the CBS, CTH, MPST in the neuroblastoma cells were associated with more an intensive generation of H2S in the presence of 2mM cysteine. A threefold higher level of sulfane sulfur, a potential source of hydrogen sulfide, was detected in the astrocytoma cells in comparison to the neuroblastoma cells.

scholarly journals Investigation of cytotoxicity induced by Nigella sativa and Azadirachta indica using MDA-MB-231, HCT 116 and SHSY5Y cell lines

2017 ◽  
Vol 9 (2) ◽  
pp. 192-195 ◽  
Author(s):  
Sayani Banerjee ◽  
Shefali Pandey ◽  
Purbasha Mukherjee ◽  
Afia Sayeed ◽  
Apoorva Vasant Pandurangi ◽  
...  
Keyword(s):  
Cell Lines ◽  
Azadirachta Indica ◽  
Nigella Sativa ◽  
Shsy5y Cell ◽  
Hct 116
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