Fish muscle cytoskeleton integrity is not dependent on intact thin filaments.
J Muscle Res Cell Motil
; 18(3): 285-94, 1997 Jun.
Article
en En
| MEDLINE
| ID: mdl-9172071
ABSTRACT
Striated muscle cytoskeleton was studied by ultrastructure and electrophoresis. Treatment of sea bass white muscle myofibrils and glycerinated fibres with calpain caused disruption of costameres, intermediate filaments, and Z-line, without altering sarcomeres. V8 protease also caused loss of costameres and Z-line, and disrupted sarcomeres without affecting the intermediate filaments. Recombinant lipase caused loss of Z-lines and also sarcolemma detachment, without changing sarcomeres or intermediate filaments. DNase-1 removed thin filaments and partially removed Z-lines while leaving intact the sarcolemma attachments and intermediate filaments. Calpain, V8 protease, lipase and DNase-1 treatments induced extensive loss of alpha-actinin from the Z-line, which could be related to titin cleavage (calpain, V8), phosphoinositide hydrolysis (lipase), and actin depolymerisation (DNase-1). These results show that the cytoskeletal components are independent of intact thin filaments.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Actinas
/
Músculo Esquelético
/
Hidrolasas
Límite:
Animals
Idioma:
En
Revista:
J Muscle Res Cell Motil
Año:
1997
Tipo del documento:
Article
País de afiliación:
Francia