Association of Titin and Myosin Heavy Chain in Developing Skeletal Muscle

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 minut...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1992-08, Vol.89 (16), p.7496-7500
Main Authors: Isaacs, W. B., Kim, I. S., Struve, A., Fulton, A. B.
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Animals
Antibodies
Antibodies, Monoclonal
assembly
Biological and medical sciences
Carrier Proteins - metabolism
Cells, Cultured
Cellular biology
Chemical precipitation
Chick Embryo
chickens
Connectin
Contractile proteins
Cross-Linking Reagents - pharmacology
Cytoskeleton
Cytoskeleton - drug effects
Cytoskeleton - metabolism
Electrophoresis, Polyacrylamide Gel
Fluorescent Antibody Technique
formation
Fundamental and applied biological sciences. Psychology
Gels
Holoproteins
Immunoglobulin G
Immunoprecipitation
Methionine - metabolism
Molecules
Muscle development
Muscle Proteins - isolation & purification
Muscle Proteins - metabolism
Muscles - cytology
Muscles - embryology
Muscles - metabolism
Myofibrils
myosin
Myosins - isolation & purification
Myosins - metabolism
Protein Kinases
Proteins
Sarcomeres
skeletal muscle
Succinimides - pharmacology
Sulfur Radioisotopes
synthesis
titin
Vimentin
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Description
Summary: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.89.16.7496