Although significant progress has been made regarding the structure and function of titin, little data exist on the biosynthesis of this large protein in developing muscle. Using pulse-labeling with [35S]methionine and immunoprecipitation with an anti-titin mAb, we have examined the biosynthesis of titin in synchronized cultures of skeletal muscle cells derived from day 12 chicken embryos. We find that: (a) titin synthesis increases greater than 4-fold during the first week in culture and during this same time period, synthesis of muscle-specific myosin heavy chain increases greater than 12-fold; (b) newly synthesized titin has a t1/2 of approximately 70 h; (c) titin is resistant to extraction with Triton X-100 both during and immediately after its synthesis. These observations suggest that newly synthesized titin molecules are stable proteins that rapidly associate with the cytoskeleton of developing myotubes.
Article|
November 01 1989
Biosynthesis of titin in cultured skeletal muscle cells.
W B Isaacs,
W B Isaacs
Department of Biochemistry, University of Iowa, Iowa City 52242.
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I S Kim,
I S Kim
Department of Biochemistry, University of Iowa, Iowa City 52242.
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A Struve,
A Struve
Department of Biochemistry, University of Iowa, Iowa City 52242.
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A B Fulton
A B Fulton
Department of Biochemistry, University of Iowa, Iowa City 52242.
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W B Isaacs
Department of Biochemistry, University of Iowa, Iowa City 52242.
I S Kim
Department of Biochemistry, University of Iowa, Iowa City 52242.
A Struve
Department of Biochemistry, University of Iowa, Iowa City 52242.
A B Fulton
Department of Biochemistry, University of Iowa, Iowa City 52242.
Online Issn: 1540-8140
Print Issn: 0021-9525
J Cell Biol (1989) 109 (5): 2189–2195.
Citation
W B Isaacs, I S Kim, A Struve, A B Fulton; Biosynthesis of titin in cultured skeletal muscle cells.. J Cell Biol 1 November 1989; 109 (5): 2189–2195. doi: https://doi.org/10.1083/jcb.109.5.2189
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