Key result
Titin and myosin heavy chain can be chemically cross-linked into very large, detergent-resistant complexes within minutes of synthesis, suggesting coordinated assembly in nascent myofibrils.
Titin and myosin heavy chain synthesis and assembly are temporally and spatially coordinated in nascent myofibrils, supporting the hypothesis that titin helps organize sarcomere formation.
Supports titin-mediated sarcomere organization in animal models; leaves open relevance to human cardiomyocyte maturation or repair.
To understand molecular interactions that organize developing myofibrils, we examined the biosynthesis and interaction of titin and myosin heavy chain in cultures of developing muscle. Use of pulse-labeling, immunoprecipitation, and a reversible cross-linking procedure demonstrates that within minutes of synthesis, titin and myosin heavy chain can be chemically cross-linked into very large, detergent-resistant complexes retaining many features of intact myotubes. These complexes, predominantly of titin and myosin, occur very early in myofibrillogenesis as well as later. These data suggest that synthesis and assembly of titin and myosin are temporally and spatially coordinated in nascent myofibrils and support the hypothesis that titin molecules help to organize sarcomere formation.
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Isaacs et al. (1992) studied this question. Chemical cross-linking with EGS vs. Uncross-linked control was evaluated on Formation of titin and myosin heavy chain complexes. Titin and myosin heavy chain can be chemically cross-linked into very large, detergent-resistant complexes within minutes of synthesis, suggesting coordinated assembly in nascent myofibrils.
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