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In vitro polymerization of tau protein monitored by laser light scattering: method and application to the study of FTDP-17 mutants.

Publication ,  Journal Article
Gamblin, TC; King, ME; Dawson, H; Vitek, MP; Kuret, J; Berry, RW; Binder, LI
Published in: Biochemistry
May 23, 2000

Tau polymerization into the filaments that compose neurofibrillary tangles is seminal to the development of many neurodegenerative diseases. It is therefore important to understand the mechanisms involved in this process. However, a consensus method for monitoring tau polymerization in vitro has been lacking. Here we demonstrate that illuminating tau polymerization reactions with laser light and measuring the increased scattering at 90 degrees to the incident beam with a digital camera results in data that closely approximate the mass of tau polymer formation in vitro. The validity of the technique was demonstrated over a range of tau concentrations and through multiple angle scattering measurements. In addition, laser light scattering data closely correlated with quantitative electron microscopy measurements of the mass of tau filaments. Laser light scattering was then used to measure the efficiency with which the mutant tau proteins found in frontotemporal dementia and Parkinsonism linked to chromosome 17 (FTDP-17) form filamentous structures. Several of these mutant proteins display enhanced polymerization in the presence of arachidonic acid, suggesting a direct role for these mutations in tau the filament formation that characterizes FTDP-17.

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Published In

Biochemistry

DOI

ISSN

0006-2960

Publication Date

May 23, 2000

Volume

39

Issue

20

Start / End Page

6136 / 6144

Location

United States

Related Subject Headings

  • tau Proteins
  • Temporal Lobe
  • Sensitivity and Specificity
  • Scattering, Radiation
  • Reproducibility of Results
  • Parkinsonian Disorders
  • Mutation, Missense
  • Mutagenesis, Site-Directed
  • Microscopy, Electron
  • Light
 

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Gamblin, T. C., King, M. E., Dawson, H., Vitek, M. P., Kuret, J., Berry, R. W., & Binder, L. I. (2000). In vitro polymerization of tau protein monitored by laser light scattering: method and application to the study of FTDP-17 mutants. Biochemistry, 39(20), 6136–6144. https://doi.org/10.1021/bi000201f
Gamblin, T. C., M. E. King, H. Dawson, M. P. Vitek, J. Kuret, R. W. Berry, and L. I. Binder. “In vitro polymerization of tau protein monitored by laser light scattering: method and application to the study of FTDP-17 mutants.Biochemistry 39, no. 20 (May 23, 2000): 6136–44. https://doi.org/10.1021/bi000201f.
Gamblin TC, King ME, Dawson H, Vitek MP, Kuret J, Berry RW, et al. In vitro polymerization of tau protein monitored by laser light scattering: method and application to the study of FTDP-17 mutants. Biochemistry. 2000 May 23;39(20):6136–44.
Gamblin, T. C., et al. “In vitro polymerization of tau protein monitored by laser light scattering: method and application to the study of FTDP-17 mutants.Biochemistry, vol. 39, no. 20, May 2000, pp. 6136–44. Pubmed, doi:10.1021/bi000201f.
Gamblin TC, King ME, Dawson H, Vitek MP, Kuret J, Berry RW, Binder LI. In vitro polymerization of tau protein monitored by laser light scattering: method and application to the study of FTDP-17 mutants. Biochemistry. 2000 May 23;39(20):6136–6144.
Journal cover image

Published In

Biochemistry

DOI

ISSN

0006-2960

Publication Date

May 23, 2000

Volume

39

Issue

20

Start / End Page

6136 / 6144

Location

United States

Related Subject Headings

  • tau Proteins
  • Temporal Lobe
  • Sensitivity and Specificity
  • Scattering, Radiation
  • Reproducibility of Results
  • Parkinsonian Disorders
  • Mutation, Missense
  • Mutagenesis, Site-Directed
  • Microscopy, Electron
  • Light