TURNOVER OF CYTOSKELETAL PROTEINS INVIVO

被引:14
|
作者
SAFAEI, R
FISCHER, I
机构
[1] EK SHRIVER CTR,DEPT BIOCHEM,200 TRAPELO RD,WALTHAM,MA 02254
[2] HARVARD UNIV,SCH MED,DEPT BIOL CHEM & MOLEC PHARMACOL,BOSTON,MA 02115
关键词
Biphasic decay rate; Cytoskeleton; Microtubule-associated protein; Neurofilament protein; Spectrin; Tubulin;
D O I
10.1016/0006-8993(90)91799-M
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
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 were 5.8 ± 0.7, 6.9 ± 0.3, 4.8 ± 0.5 and 4.9 ± 0.4 days, respectively, while the slow decay rates of these proteins were 12.0 ± 1.3, 12.4 ± 1.7, 15.0 ± 0.5 and 16.0 ± 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. © 1990.
引用
收藏
页码:83 / 90
页数:8
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