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Turnover of cytoskeletal proteins in vivo
Journal article   Peer reviewed

Turnover of cytoskeletal proteins in vivo

Roohangiz Safaei and Itzhak Fischer
Brain research, v 533(1), pp 83-90
1990
DOI: https://doi.org/10.1016/0006-8993(90)91799-M
PMID: 2085737
Featured in Collection :   UN Sustainable Development Goals @ Drexel

Abstract

Biphasic decay rate Cytoskeleton Microtubule-associated protein Neurofilament protein Spectrin Tubulin
The turnover of the microtubule-associated proteins 1B and 2 (MAP1B and MAP2), tubulin, high molecular weight neurofilament protein (NF-H), and spectrin were studied by in vivo labeling. Radiolabeled [ 35S]methionine was injected intracranially to 10-day-old rats and the rate of turnover was measured for total and specific brain proteins. The turnover of total brain proteins was biphasic and consisted of a fast and a slow component with half lives of 6.5 ± 0.4 and 14.2 ± 0.7 (mean ±S.E.M.) days, respectively. The turnover of individual cytoskeletal brain proteins was also biphasic. The fast decay rates of MAP1B, MAP2, tubulin and spectrin were5.8 ± 0.7, 6.9 ± 0.3, 4.8 ± 0.5 and4.9 ± 0.4 days, respectively, while the slow decay rates of these proteins were12.0 ± 1.3, 12.4 ± 1.7, 15.0 ± 0.5 and16.0 ± 1.2 days, respectively. In addition, the Triton X-100 insoluble fraction of MAP1B, tubulin, spectrin and NF-H showed monophasic decay rates of 29.0 ± 2.3, 15.0 ± 1.4, 16.0 ± 0.9 and 18.5 ± 1.5 days, respectively, which were similar to their slow decay rates in whole brain homogenates, suggesting that incorporation of these proteins into the cytoskeletal lattice increases their stability.

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