Premium
S‐100 proteins and microtubules: analysis of the effects of rat brain S‐100 (S‐100b) and ox brain S‐100a 0 , S‐100a and S‐100b on microtubule assembly‐diassembly (FEBS 2657)
Author(s) -
Donato R.,
Isobe T.,
Okuyama T.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)81340-5
Subject(s) - microtubule , gene isoform , biophysics , tubulin , in vitro , chemistry , microbiology and biotechnology , biology , biochemistry , gene
Rat brain S-100 (S-100b) and ox brain S-100a0, S-100a and S-100b have been tested for their ability to control the assembly and disassembly of brain microtubule proteins in the presence of either Ca2+ or Zn2+, in vitro. In the presence of Ca2+, single S-100 isoforms have similar, if not identical, effects, i.e. they inhibit assembly and promote disassembly. In the presence of Zn2+ from 0.1 to 1 mM (free concentration), rat S-100 and ox S-100a and S-100b inhibit assembly, while S-100a0 is without effect. These data are briefly discussed in relation to the cellular localization of single S-100 isoforms in the brain.