Internalization of the Extracellular Full-Length Tau Inside Neuro2A and Cortical Cells Is Enhanced by Phosphorylation

• Published in: Biomolecules (Basel, Switzerland) Vol. 6; no. 3; p. 36
• Main Authors: Wauters, Mathilde, Wattiez, Ruddy, Ris, Laurence
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI 19-08-2016; MDPI AG
• Subjects: Alzheimer Disease - metabolism; Animals; Brain - metabolism; Cell Line; Cells, Cultured; Communication; Humans; internalization; Mice; Neurons - metabolism; Phosphorylation; Rats, Wistar; Recombinant Proteins - metabolism; spreading; Tau; tau Proteins - metabolism; spreading; Tau; internalization; phosphorylation
• ISSN: 2218-273X; 2218-273X
• DOI: 10.3390/biom6030036

Tau protein is mainly intracellular. However, several studies have demonstrated that full-length Tau can be released into the interstitial fluid of the brain. The physiological or pathological function of this extracellular Tau remains unknown. Moreover, as evidence suggests, extracellular Tau aggregates can be internalized by neurons, seeding Tau aggregation. However, much less is known about small species of Tau. In this study, we hypothesized that the status of phosphorylation could alter the internalization of recombinant Tau in Neuro2A and cortical cells. Our preliminary results revealed that the highly phosphorylated form of Tau entered the cells ten times more easily than a low phosphorylated one. This suggests that hyperphosphorylated Tau protein could spread between neurons in pathological conditions such as Alzheimer's disease.