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Titolo:
I-band titin in cardiac muscle is a three-element molecular spring and is critical for maintaining thin filament structure
Autore:
Linke, WA; Rudy, DE; Centner, T; Gautel, M; Witt, C; Labeit, S; Gregorio, CC;
Indirizzi:
Univ Heidelberg, Inst Physiol 2, D-69120 Heidelberg, Germany Univ Heidelberg Heidelberg Germany D-69120 , D-69120 Heidelberg, Germany Univ Arizona, Dept Anat & Cell Biol, Tucson, AZ 85724 USA Univ Arizona Tucson AZ USA 85724 t Anat & Cell Biol, Tucson, AZ 85724 USA European Mol Biol Lab, D-69012 Heidelberg, Germany European Mol Biol Lab Heidelberg Germany D-69012 012 Heidelberg, Germany Max Planck Inst Mol Physiol, D-44202 Dortmund, Germany Max Planck Inst MolPhysiol Dortmund Germany D-44202 2 Dortmund, Germany Univ Heidelberg, Klinikum Mannheim, Inst Anasthesiol & Operat Intensivmed,D-68167 Mannheim, Germany Univ Heidelberg Mannheim Germany D-68167 ivmed,D-68167 Mannheim, Germany Univ Arizona, Dept Mol & Cellular Biol, Tucson, AZ 85721 USA Univ ArizonaTucson AZ USA 85721 ol & Cellular Biol, Tucson, AZ 85721 USA
Titolo Testata:
JOURNAL OF CELL BIOLOGY
fascicolo: 3, volume: 146, anno: 1999,
pagine: 631 - 644
SICI:
0021-9525(19990809)146:3<631:ITICMI>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
GIANT PROTEIN TITIN; ACTIN-FILAMENTS; IMMUNOELECTRON MICROSCOPY; MONOCLONAL-ANTIBODIES; ELASTICITY; TROPOMYOSIN; IMMUNOGLOBULIN; MYOFIBRILLOGENESIS; STABILITY; MYOCYTES;
Keywords:
heart muscle; connectin; elasticity; transfection; sarcomere;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
52
Recensione:
Indirizzi per estratti:
Indirizzo: Linke, WA Univ Heidelberg, Inst Physiol 2, Im Neuenheimer Feld 326, D-69120 Heidelberg, Germany Univ Heidelberg Im Neuenheimer Feld 326 Heidelberg Germany D-69120
Citazione:
W.A. Linke et al., "I-band titin in cardiac muscle is a three-element molecular spring and is critical for maintaining thin filament structure", J CELL BIOL, 146(3), 1999, pp. 631-644

Abstract

In cardiac muscle, the giant protein titin exists in different length isoforms expressed in the molecule's I-band region. Both isoforms, termed N2-A and N2-B, comprise stretches of Ig-like modules separated by the PEVK domain. Central I-band titin also contains isoform-specific Ig-motifs and nonmodular sequences, notably a longer insertion in N2-B. We investigated the elastic behavior of the I-band isoforms by using single-myofibril mechanics, immunofluorescence microscopy, and immunoelectron microscopy of rabbit cardiac sarcomeres stained with sequence-assigned antibodies. Moreover, we overexpressed constructs from the N2-B region in chick cardiac cells to search for possible structural properties of this cardiac-specific segment,We found that cardiac titin contains three distinct elastic elements: poly-Ig regions, the PEVK domain, and the N2-B sequence insertion, which extends similar to 60 nm at high physiological stretch. Recruitment of all three elements allows cardiac titin to extend fully reversibly at physiological sarcomere lengths, without the need to unfold Ig domains. Overexpressing theentire N2-B region or its NH2 terminus in cardiac myocytes greatly disrupted thin filament, but not thick filament structure. Our results strongly suggest that the NH2-terminal N2-B domains are necessary to stabilize thin filament integrity. N2-B-titin emerges as a unique region critical for both reversible extensibility and structural maintenance of cardiac myofibrils.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 22:17:52