Biosynthesis of titin in cultured skeletal muscle cells

doi:10.1083/jcb.109.5.2189

This Article

	Full Text (PDF, 1279K)
	Alert me when this article is cited
	Citation Map

Services

	Email this article
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new content in the JCB
	Download to citation manager

Citing Articles

	Citing Articles via HighWire
	Citing Articles via CrossRef
	Citing Articles via Google Scholar

Google Scholar

	Articles by Isaacs, W. B.
	Articles by Fulton, A. B.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Isaacs, W. B.
	Articles by Fulton, A. B.


Social Bookmarking

	What's this?

ARTICLES

Biosynthesis of titin in cultured skeletal muscle cells

WB Isaacs, IS Kim, A Struve and AB Fulton
Department of Biochemistry, University of Iowa, Iowa City 52242.

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.
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Facebook Add to Reddit Reddit Add to Technorati Technorati Twitter What's this?

This article has been cited by other articles:

Kramerova, I., Kudryashova, E., Tidball, J.G., Spencer, M. J. (2004). Null mutation of calpain 3 (p94) in mice causes abnormal sarcomere formation in vivo and in vitro. Hum Mol Genet 13: 1373-1388 [Abstract] [Full Text]
Kontrogianni-Konstantopoulos, A., Jones, E. M., van Rossum, D. B., Bloch, R. J. (2003). Obscurin Is a Ligand for Small Ankyrin 1 in Skeletal Muscle. Mol. Biol. Cell 14: 1138-1148 [Abstract] [Full Text]
Wu, Y., Bell, S. P., Trombitas, K., Witt, C. C., Labeit, S., LeWinter, M. M., Granzier, H. (2002). Changes in Titin Isoform Expression in Pacing-Induced Cardiac Failure Give Rise to Increased Passive Muscle Stiffness. Circulation 106: 1384-1389 [Abstract] [Full Text]
Kontrogianni-Konstantopoulos, A., Huang, S.-C., Benz, E. J. Jr. (2000). A Nonerythroid Isoform of Protein 4.1R Interacts with Components of the Contractile Apparatus in Skeletal Myofibers. Mol. Biol. Cell 11: 3805-3817 [Abstract] [Full Text]
Morris, E., Fulton, A. (1994). Rearrangement of mRNAs for costamere proteins during costamere development in cultured skeletal muscle from chicken. J. Cell Sci. 107: 377-386 [Abstract]
van der Ven, P., Schaart, G, Croes, H., Jap, P., Ginsel, L., Ramaekers, F. (1993). Titin aggregates associated with intermediate filaments align along stress fiber-like structures during human skeletal muscle cell differentiation. J. Cell Sci. 106: 749-759 [Abstract]
Fulton, A., L'Ecuyer, T (1993). Cotranslational assembly of some cytoskeletal proteins: implications and prospects. J. Cell Sci. 105: 867-871