Inhibition of dendritic spine extension through acrolein conjugation with α-, β-tubulin proteins.
Acrolein
Brain infarction
Cysteine
Dendritic spine
Microtubule
α-, β-tubulins
Journal
The international journal of biochemistry & cell biology
ISSN: 1878-5875
Titre abrégé: Int J Biochem Cell Biol
Pays: Netherlands
ID NLM: 9508482
Informations de publication
Date de publication:
08 2019
08 2019
Historique:
received:
09
03
2019
revised:
24
05
2019
accepted:
27
05
2019
pubmed:
1
6
2019
medline:
18
3
2020
entrez:
1
6
2019
Statut:
ppublish
Résumé
We have recently found that conjugation of acrolein with a 50 kDa protein(s) is strongly associated with tissue damage during brain infarction. In the current study, the identity and function of the 50 kDa protein(s) conjugated with acrolein during brain infarction were investigated. The 50 kDa protein(s) conjugated with acrolein were identified as α- and β-tubulins. Ten cysteine residues in α- and β-tubulins (Cys25, 295, 347 and 376 in α-tubulin and Cys12, 129, 211, 239, 303 and 354 in β-tubulin) were mainly conjugated with acrolein. Since two cysteine residues of α-tubulin (Cys347 and 376) and four cysteine residues of β-tubulin (Cys12, 129, 239 and 354) were located at the interaction site of α- and β-tubulins, association between α- and β-tubulins to form microtubules was strongly inhibited by conjugation with acrolein. Accordingly, dendritic spine extension consisting of microtubules was greatly inhibited in acrolein-treated Neuro2a cells. The results strongly suggest that acrolein contributes to the functional losses in brain signaling through its conjugation with α- and β-tubulins.
Identifiants
pubmed: 31150838
pii: S1357-2725(19)30110-4
doi: 10.1016/j.biocel.2019.05.016
pii:
doi:
Substances chimiques
Tubulin
0
Acrolein
7864XYD3JJ
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
58-66Informations de copyright
Copyright © 2019 Elsevier Ltd. All rights reserved.