Lithium preserves F-actin from the disarrangement induced by either DNase I or cytochalasin D.
Biochem Cell Biol
; 71(9-10): 440-6, 1993.
Article
de En
| MEDLINE
| ID: mdl-8192896
ABSTRACT
Light scattering at 546 nm, which is mainly related to the presence of rodlike particles longer than 50 nm, showed that Li+ accelerates the formation of actin filaments. Intermolecular cross-linking with N,N'-1,4-phenylene-bismaleimide proved that the observed enhancement in the light-scattering intensity is caused by the increase in the concentration of actin oligomers, which gradually elongate to form longer filaments. DNase-I-related F-actin disassembly was reduced in the presence of lithium ions, as demonstrated by fluorimetric and viscometric experiments. Li(+)-F-actin showed an apparently similar behaviour when exposed to cytochalasin D. We confirm that Li+ acts on actin polymerization by stabilizing actin nuclei and polymers. The stabilization of cytoskeletal polymers really appears as one of the mechanisms by which lithium ions influence some of the cell activities.
Recherche sur Google
Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Cytochalasine D
/
Actines
/
Deoxyribonuclease I
/
Lithium
Limites:
Animals
Langue:
En
Journal:
Biochem Cell Biol
Sujet du journal:
BIOQUIMICA
Année:
1993
Type de document:
Article
Pays d'affiliation:
Italie