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. 1992 Aug 15;89(16):7496–7500. doi: 10.1073/pnas.89.16.7496

Association of titin and myosin heavy chain in developing skeletal muscle.

W B Isaacs 1, I S Kim 1, A Struve 1, A B Fulton 1
PMCID: PMC49737  PMID: 1502160

Abstract

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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