Highly homologous filamin polypeptides have different distributions in avian slow and fast muscle fibers

doi:10.1083/jcb.97.3.818

This Article

	Full Text (PDF, 1815K)
	Alert me when this article is cited

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 Gomer, R. H.
	Articles by Lazarides, E.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Gomer, R. H.
	Articles by Lazarides, E.


Social Bookmarking

	What's this?

ARTICLES

Highly homologous filamin polypeptides have different distributions in avian slow and fast muscle fibers

RH Gomer and E Lazarides

The high molecular weight actin-binding protein filamin is located at the periphery of the Z disk in the fast adult chicken pectoral muscle (Gomer, R. H., and E. Lazarides, 1981, Cell, 23: 524-532). In contrast, we have found that in the slow anterior latissimus dorsi (ALD) muscle, filamin was additionally located throughout the l band as judged by immunofluorescence with affinity-purified antibodies on myofibrils and cryosections. The Z line proteins desmin and alpha-actinin, however, had the same distribution in ALD as they do in pectoral muscle. Quantitation of filamin and actin from the two muscle types showed that there was approximately 10 times as much filamin per actin in ALD myofibrils as in pectoral myofibrils. Filamin immunoprecipitated from ALD had an electrophoretic mobility in SDS polyacrylamide gels identical to that of pectoral myofibril filamin and slightly greater than that of chicken gizzard filamin. Two-dimensional peptide maps of filamin immunoprecipitated and labeled with 125I showed that ALD myofibril filamin was virtually identical to pectoral myofibril filamin and was distinct from chicken gizzard filamin.
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Add to Reddit Reddit Add to Technorati Technorati What's this?

This article has been cited by other articles:

van der Flier, A., Kuikman, I., Kramer, D., Geerts, D., Kreft, M., Takafuta, T., Shapiro, S. S., Sonnenberg, A. (2002). Different splice variants of filamin-B affect myogenesis, subcellular distribution, and determine binding to integrin {beta} subunits. JCB 156: 361-376 [Abstract] [Full Text]
van der Ven, P. F.M., Wiesner, S., Salmikangas, P., Auerbach, D., Himmel, M., Kempa, S., Haye{beta}, K., Pacholsky, D., Taivainen, A., Schroder, R., Carpen, O., Furst, D. O. (2000). Indications for a Novel Muscular Dystrophy Pathway: {gamma}-Filamin, the Muscle-specific Filamin Isoform, Interacts with Myotilin. JCB 151: 235-248 [Abstract] [Full Text]
Gomer, R.H., Datta, S., Mehdy, M., Crowley, T., Sivertsen, A., Nellen, W., Reymond, C., Mann, S., Firtel, R.A. (1985). Regulation of Cell-type-specific Gene Expression in Dictyostelium. Cold Spring Harb Symp Quant Biol 50: 801-812 [Abstract]
van der Flier, A., Kuikman, I., Kramer, D., Geerts, D., Kreft, M., Takafuta, T., Shapiro, S. S., Sonnenberg, A. (2002). Different splice variants of filamin-B affect myogenesis, subcellular distribution, and determine binding to integrin {beta} subunits. JCB 156: 361-376 [Abstract] [Full Text]