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Titolo:
INTEGRATION OF TITIN INTO THE SARCOMERES OF CULTURED DIFFERENTIATING HUMAN SKELETAL-MUSCLE CELLS
Autore:
VANDERLOOP FTL; VANDERVEN PFM; FURST DO; GAUTEL M; VANEYS GJJM; RAMAEKERS FCS;
Indirizzi:
UNIV LIMBURG,CARDIOVASC RES INST,DEPT MOLEC BIOL & GENET,POB 616 6200MD MAASTRICHT NETHERLANDS UNIV NIJMEGEN,DEPT CELL BIOL & HISTOL NIJMEGEN NETHERLANDS MAX PLANCK INST BIOPHYS CHEM,DEPT BIOCHEM W-3400 GOTTINGEN GERMANY EUROPEAN MOLEC BIOL LAB,DIV STRUCT BIOL HEIDELBERG GERMANY
Titolo Testata:
European journal of cell biology
fascicolo: 4, volume: 69, anno: 1996,
pagine: 301 - 307
SICI:
0171-9335(1996)69:4<301:IOTITS>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
FIBER-LIKE STRUCTURES; EARLY CHICK-EMBRYOS; CARDIAC MYOFIBRILLOGENESIS; MONOCLONAL-ANTIBODY; C-PROTEIN; EXPRESSION; MYOFIBRILS; FILAMENTS; MYOSIN; ACTIN;
Keywords:
TITIN; DESMIN; MYOSIN; C-PROTEIN; MYOGENESIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
34
Recensione:
Indirizzi per estratti:
Citazione:
F.T.L. Vanderloop et al., "INTEGRATION OF TITIN INTO THE SARCOMERES OF CULTURED DIFFERENTIATING HUMAN SKELETAL-MUSCLE CELLS", European journal of cell biology, 69(4), 1996, pp. 301-307

Abstract

Titin is amongst the first sarcomeric proteins to be detected in the process of myofibrillogenesis of striated muscle, During embryogenesisthis high molecular weight protein is initially observed in a punctate staining pattern in immunohistochemical studies, while during maturation titin organizes into a cross-striated pattern, The dynamic process of titin assembly up to its integration into the sarcomeres of cultured human skeletal muscle cells has been studied in subsequent stages of differentiation with antibodies to four well-defined titin epitopes. Since in maturated muscle cells these epitopes are clearly distinguishable on the extended titin molecule we wondered how these epitopes reorganize during myofibrillogenesis, and whether such a reorganizationwould reveal important clues about its supramolecular organization during development. Immunofluorescence staining of postmitotic mononuclear myoblasts indicate that the investigated epitopes of the titin molecule are displayed in a punctate pattern with neighboring, but clearlyseparate spots in the cytoplasm of the cells, During elongation and fusion of the cells, these titin spots associate with stress fiber-likestructures to finally reach their position at either the Z-line, the A-I junction or the A-band, We propose that during this transition thelarge titin molecule is unfolded, with the amino terminus of the molecule migrating in the direction of the Z-line and the carboxy terminusmoving towards the M-line, In maturated, fused myotubes the final cross-striated patterns of all investigated titin epitopes are observed, While this process of unfolding of the titin molecule progresses, other compounds of the Z-line and the A-band migrate to their specific positions in the nascent sarcomere, A-band components such as sarcomeric myosin and C-protein, are also observed as dot-like aggregates during initial stages of muscle cell differentiation and organize into a cross-striated pattern in the sarcomere virtually simultaneously with titin. The Z-line associated component desmin organizes into a cross-striated pattern at a later stage.

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Documento generato il 04/12/20 alle ore 21:45:22