4.6 Article

Changes in microtubule-associated protein tau during peripheral nerve injury and regeneration

Journal

NEURAL REGENERATION RESEARCH
Volume 11, Issue 9, Pages 1506-1511

Publisher

MEDKNOW PUBLICATIONS & MEDIA PVT LTD
DOI: 10.4103/1673-5374.191227

Keywords

nerve regeneration; sciatic nerve crush; microtubule-associated protein; tau; phosphorylated tau (Ser 404); tau hyper-phosphorylation; tau tubulin kinase 1; microtubule structure; microtubule assembly and disassembly; peripheral nervous system; neural regeneration

Funding

  1. National Natural Science Foundation of China [81130080, 31300942]
  2. National Key Basic Research Program of China (973 Program) [2014CB542202]
  3. Natural Science Foundation of Jiangsu Province, China [BK20150409]
  4. Natural Science Foundation of Jiangsu Higher Education Institutions of China [15KJB180013]
  5. Scientific Research Foundation of Nantong University of China [14R29]
  6. Natural Science Foundation of Nantong City in China [MS12015043]
  7. Priority Academic Program Development of Jiangsu Higher Education Institutions of China

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Tau, a primary component of microtubule-associated protein, promotes microtubule assembly and/or disassembly and maintains the stability of the microtubule structure. Although the importance of tau in neurodegenerative diseases has been well demonstrated, whether tau is involved in peripheral nerve regeneration remains unknown. In the current study, we obtained sciatic nerve tissue from adult rats 0, 1, 4, 7, and 14 days after sciatic nerve crush and examined tau mRNA and protein expression levels and the location of tau in the sciatic nerve following peripheral nerve injury. The results from our quantitative reverse transcription polymerase chain reaction analysis showed that compared with the uninjured control sciatic nerve, mRNA expression levels for both tau and tau tubulin kinase 1, a serine/threonine kinase that regulates tau phosphorylation, were decreased following peripheral nerve injury. Our western blot assay results suggested that the protein expression levels of tau and phosphorylated tau initially decreased 1 day post nerve injury but then gradually increased. The results of our immunohistochemical labeling showed that the location of tau protein was not altered by nerve injury. Thus, these results showed that the expression of tau was changed following sciatic nerve crush, suggesting that tau may be involved in peripheral nerve repair and regeneration.

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