Microtubule-dependent polarization and migration of microglia conserved by α-linolenic acid and extracellular Tau-mediated stimulation

Author:

Desale Smita Eknath1,Chinnathambi Subashchandrabose1

Affiliation:

1. National Institute of Mental Health and Neuro Sciences (NIMHANS)

Abstract

Abstract Background The polarized migratory microglia consisting of front edge lamellipodia and rear edge uropod direct migration at the chemotactic gradient. Thus, maintenance of polarized morphology of the cell is utmost to sense the extracellular signal and migrate towards it. During migration, actin provides protrusive forces for the cell; whereas microtubules contribute to directionality. Methods The disruption of microtubule with depolymerizing agent, Colchicine or stabilizing agent, Taxol significantly hampered polarized morphology and subsequent directed migration in response to the extracellular Tau species. Disruption of microtubule dynamics majorly challenge the matrix adhesion; resulting in the reduction of mesenchymal migration of microglia. In neurodegenerative diseases like Alzheimer’s disease, it is necessary to improve the disrupted polarized morphology of microglia as an approach to reduce the burden of extracellular aggregated proteins. Results Incorporation of α-linolenic acid (ALA), an omega-3 fatty acid; had significantly improved the microtubule-disrupted polarized morphology of microglia. The enhanced migration process over to Tau stimulus, which is a significant beneficial property to conserve polarized microglia in Alzheimer’s disease. Conclusion To conclude, the directed migration of microglia is a microtubule-dependent process since microtubule maintains polarized morphology and provides direction according to extracellular stimuli.

Publisher

Research Square Platform LLC

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Cited by 2 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. α-Linolenic Acid Vesicles-Mediated Tau Internalization in Microglia;Methods in Molecular Biology;2024

2. The cross-talk between ApoE and Tau protein in Alzheimer’s disease;Advances in Protein Chemistry and Structural Biology;2024

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