title: Fish muscle cytoskeleton integrity is not dependent on intact thin filaments.
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.
authors.affiliation: INRA, Muscle Biochemistry Unit SRV, St. Genes Champanelle, France.
authors.forename: R G
authors.initials: RG
authors.lastname: Taylor
authors.forename: I
authors.initials: I
authors.lastname: Papa
authors.forename: C
authors.initials: C
authors.lastname: Astier
authors.forename: F
authors.initials: F
authors.lastname: Ventre
authors.forename: Y
authors.initials: Y
authors.lastname: Benyamin
authors.forename: A
authors.initials: A
authors.lastname: Ouali
mesh_terms: D000185:Actinin / Q000032:analysis / Q000187:drug effects; D000199:Actins / Q000032:analysis / Q000187:drug effects / Q000502:physiology*; D000818:Animals; D001492:Bass; D002154:Calpain / Q000494:pharmacology; D003850:Deoxyribonuclease I / Q000494:pharmacology; D004586:Electrophoresis; D006867:Hydrolases / Q000494:pharmacology*; D007382:Intermediate Filaments / Q000187:drug effects; D008049:Lipase / Q000494:pharmacology; D018482:Muscle, Skeletal / Q000187:drug effects / Q000648:ultrastructure*; D012518:Sarcomeres / Q000187:drug effects; D012697:Serine Endopeptidases / Q000494:pharmacology; D013997:Time Factors; D010738:Type C Phospholipases / Q000494:pharmacology
chemical_list: D000199:Actins; D000185:Actinin; D006867:Hydrolases; D008049:Lipase; D003850:Deoxyribonuclease I; D010738:Type C Phospholipases; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase; D002154:Calpain