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Effects of AcSDKP on apoptosis induced by β-amyloid protein
ZHAIWanying, QIANYihua, MAKaige, CHANGKewei, ZONGHangfan, YANGWeina, HANHua
Chinese Journal of Alzheimer's Disease and Related Disorders ›› 2020, Vol. 3 ›› Issue (1) : 56-60.
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Abbreviation (ISO4): Chinese Journal of Alzheimer's Disease and Related Disorders
Editor in chief: Jun WANG
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Effects of AcSDKP on apoptosis induced by β-amyloid protein
Objective: To establish Alzheimer’s disease (AD)-like cellular model induced by Oligomeric Amyloid-beta1-42 (oAβ1-42) and explore the effects of acetyl-Ser-Asp-Lys-Pro (AcSDKP) on apoptosis induced by β-amyloid protein. Methods: SH-SY5Y cells were treated with oAβ1-42 and AcSDKP. The viability of SH-SY5Y cells was examined, the expression of BCL2 and BAX protein, the release of cytochrome C (Cyt c) and the signal molecular NF-κB were assayed by Western blot The neuroprotection of AcSDKP was explored on the cells. Results: SH-SY5Y cells were treated with oAβ1-42 for 24 hours, MTT assay showed that the toxicity of oAβ1-42 to SH-SY5Y cells was concentration-dependent, more than 2.5 μmol oAβ1-42 could significantly decrease the viability of cells, while viability was decreased by about 50% after treatment with 5 μmol of oAβ1-42 for 24 h. Western blot showed that the level of BAX in AcSDKP group was significantly lower than that in Aβ treatment group, and the level of BCL2 in AcSDKP treatment group was significantly higher than that in Aβ treatment group. The results also showed that AcSDKP significantly decreased the release of Cytc. At the same time, it was observed that oAβ1-42 promoted the expression of NF-κB, while AcSDKP could significantly inhibit the expression of NF-κB. Conclusion: AcSDKP could inhibit apoptosis induced by oAβ1-42, which may be due to the inhibition of NF-κB signaling pathway.
Alzheimer’s disease / Oligomeric Amyloid-beta / AcSDKP / Aoptosis / NF-κB
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Alzheimer's disease (AD) is a devastative neurodegenerative disorder with complex etiology. Neuroinflammation has been found to be an underlying cause of the disease, although it demonstrates significant defensive role and renders the brain immunologically secured. This review focuses on the physiology and pathology of this crucial biological process and the diverse factors involved in and acting in a concerted manner to play a pivotal role either in the physiology or pathology of the disease. We used Pubmed, Pubmed Central, and Medline databases for a period of 3 months. It also summarizes the recent advances in neuroinflammation in both in vitro and in vivo. This review eventually warrants further studies on animal models of AD to unravel the complete pathophysiology of the disease and also accentuates the burgeoning need to protect astrocytes which can become a substantial therapeutic avenue.
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Thymosin beta 4 is acknowledged as a major G-actin binding protein maintaining a pool of unassembled actin in motile vertebrate cells. We have examined the function of Tbeta 4 in actin assembly in the high range of concentrations (up to 300 micron) at which Tbeta 4 is found in highly motile blood cells. Tbeta 4 behaves as a simple G-actin sequestering protein only in a range of low concentrations (<20 micron). As the concentration of Tbeta 4 increases, its ability to depolymerize F-actin decreases, due to its interaction with F-actin. The Tbeta 4-actin can be incorporated, in low molar ratios, into F-actin, and can be cross-linked in F-actin using 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide. As a result of the copolymerization of actin and Tbeta 4-actin complex, the critical concentration is the sum of free G-actin and Tbeta 4-G-actin concentrations at steady state, and the partial critical concentration of G-actin is decreased by Tbeta 4-G-actin complex. The incorporation of Tbeta 4-actin in F-actin is associated to a structural change of the filaments and eventually leads to their twisting around each other. In conclusion, Tbeta 4 is not a simple passive actin-sequestering agent, and at high concentrations the ability of Tbeta 4-actin to copolymerize with actin reduces the sequestering activity of G-actin-binding proteins. These results question the evaluation of the unassembled actin in motile cells. They account for observations made on living fibroblasts overexpressing beta-thymosins.
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