Immunochemical localization of myosin heavy chain isoforms and paramyosin in developmentally and structurally diverse muscle cell types of the nematode Caenorhabditis elegans

doi:10.1083/jcb.105.6.2763

This Article

	Full Text (PDF, 3231K)
	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 Ardizzi, J. P.
	Articles by Epstein, H. F.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Ardizzi, J. P.
	Articles by Epstein, H. F.


Social Bookmarking

	What's this?

ARTICLES

Immunochemical localization of myosin heavy chain isoforms and paramyosin in developmentally and structurally diverse muscle cell types of the nematode Caenorhabditis elegans

JP Ardizzi and HF Epstein
Program in Neuroscience, Baylor College of Medicine, Houston, Texas 77030.

The nematode Caenorhabditis elegans contains two major groups of muscle cells that exhibit organized sarcomeres: the body wall and pharyngeal muscles. Several additional groups of muscle cells of more limited mass and spatial distribution include the vulval muscles of hermaphrodites, the male sex muscles, the anal-intestinal muscles, and the gonadal sheath of the hermaphrodite. These muscle groups do not exhibit sarcomeres and therefore may be considered smooth. Each muscle cell has been shown to have a specific origin in embryonic cell lineages and differentiation, either embryonically or postembryonically (Sulston, J. E., and H. R. Horvitz. 1977. Dev. Biol. 56:110-156; Sulston, J. E., E. Schierenberg, J. White, and J. N. Thomson. 1983. Dev. Biol. 100:64- 119). Each muscle type exhibits a unique combination of lineage and onset of differentiation at the cellular level. Biochemically characterized monoclonal antibodies to myosin heavy chains A, B, C, and D and to paramyosin have been used in immunochemical localization experiments. Paramyosin is detected by immunofluorescence in all muscle cells. Myosin heavy chains C and D are limited to the pharyngeal muscle cells, whereas myosin heavy chains A and B are localized not only within the sarcomeres of body wall muscle cells, as reported previously, but to the smooth muscle cells of the minor groups as well. Myosin heavy chains A and B and paramyosin proteins appear to be compatible with functionally and structurally distinct muscle cell types that arise by multiple developmental pathways.
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:

Ben-Zvi, A., Miller, E. A., Morimoto, R. I. (2009). Collapse of proteostasis represents an early molecular event in Caenorhabditis elegans aging. Proc. Natl. Acad. Sci. USA 106: 14914-14919 [Abstract] [Full Text]
Ono, K., Yamashiro, S., Ono, S. (2008). Essential role of ADF/cofilin for assembly of contractile actin networks in the C. elegans somatic gonad. J. Cell Sci. 121: 2662-2670 [Abstract] [Full Text]
Landsverk, M. L., Li, S., Hutagalung, A. H., Najafov, A., Hoppe, T., Barral, J. M., Epstein, H. F. (2007). The UNC-45 chaperone mediates sarcomere assembly through myosin degradation in Caenorhabditis elegans. JCB 177: 205-210 [Abstract] [Full Text]
Higashibata, A., Szewczyk, N. J., Conley, C. A., Imamizo-Sato, M., Higashitani, A., Ishioka, N. (2006). Decreased expression of myogenic transcription factors and myosin heavy chains in Caenorhabditis elegans muscles developed during spaceflight. J. Exp. Biol. 209: 3209-3218 [Abstract] [Full Text]
Ono, K., Yu, R., Mohri, K., Ono, S. (2006). Caenorhabditis elegans Kettin, a Large Immunoglobulin-like Repeat Protein, Binds to Filamentous Actin and Provides Mechanical Stability to the Contractile Apparatuses in Body Wall Muscle. Mol. Biol. Cell 17: 2722-2734 [Abstract] [Full Text]
Sassi, H. E., Renihan, S., Spence, A. M., Cooperstock, R. L. (2005). Gene CATCHR--Gene Cloning And Tagging for Caenorhabditis elegans using yeast Homologous Recombination: a novel approach for the analysis of gene expression. Nucleic Acids Res 33: e163-e163 [Abstract] [Full Text]
Hooper, S. L., Thuma, J. B. (2005). Invertebrate Muscles: Muscle Specific Genes and Proteins. Physiol. Rev. 85: 1001-1060 [Abstract] [Full Text]
Dixon, S. J., Roy, P. J. (2005). Muscle arm development in Caenorhabditis elegans. Development 132: 3079-3092 [Abstract] [Full Text]
Sasson, I. E., Stern, M. J. (2004). FGF and PI3 kinase signaling pathways antagonistically modulate sex muscle differentiation in C. elegans. Development 131: 5381-5392 [Abstract] [Full Text]
Ono, K., Ono, S. (2004). Tropomyosin and Troponin Are Required for Ovarian Contraction in the Caenorhabditis elegans Reproductive System. Mol. Biol. Cell 15: 2782-2793 [Abstract] [Full Text]
Gaudet, J., Mango, S. E. (2002). Regulation of Organogenesis by the Caenorhabditis elegans FoxA Protein PHA-4. Science 295: 821-825 [Abstract] [Full Text]
Kostas, S. A., Fire, A. (2002). The T-box factor MLS-1 acts as a molecular switch during specification of nonstriated muscle in C. elegans. Genes Dev. 16: 257-269 [Abstract] [Full Text]
Oeda, T., Shimohama, S., Kitagawa, N., Kohno, R., Imura, T., Shibasaki, H., Ishii, N. (2001). Oxidative stress causes abnormal accumulation of familial amyotrophic lateral sclerosis-related mutant SOD1 in transgenic Caenorhabditis elegans. Hum Mol Genet 10: 2013-2023 [Abstract] [Full Text]
Hoppe, P. E., Waterston, R. H. (2000). A Region of the Myosin Rod Important for Interaction With Paramyosin in Caenorhabditis elegans Striated Muscle. Genetics 156: 631-643 [Abstract] [Full Text]
Ao, W., Pilgrim, D. (2000). Caenorhabditis elegans Unc-45 Is a Component of Muscle Thick Filaments and Colocalizes with Myosin Heavy Chain B, but Not Myosin Heavy Chain a. JCB 148: 375-384 [Abstract] [Full Text]
Mullen, G. P., Rogalski, T. M., Bush, J. A., Gorji, P. R., Moerman, D. G. (1999). Complex Patterns of Alternative Splicing Mediate the Spatial and Temporal Distribution of Perlecan/UNC-52 in Caenorhabditis elegans. Mol. Biol. Cell 10: 3205-3221 [Abstract] [Full Text]
Liu, F., Bauer, C. C., Ortiz, I., Cook, R. G., Schmid, M. F., Epstein, H. F. (1998). {beta}-Filagenin, a Newly Identified Protein Coassembling with Myosin and Paramyosin in Caenorhabditis elegans. JCB 140: 347-353 [Abstract] [Full Text]
Kalb, J., Lau, K., Goszczynski, B, Fukushige, T, Moons, D, Okkema, P., McGhee, J. (1998). pha-4 is Ce-fkh-1, a fork head/HNF-3alpha,beta,gamma homolog that functions in organogenesis of the C. elegans pharynx. Development 125: 2171-2180 [Abstract]
Harbinder, S., Tavernarakis, N., Herndon, L. A., Kinnell, M., Xu, S. Q., Fire, A., Driscoll, M. (1997). Genetically targeted cell disruption in elegans. Proc. Natl. Acad. Sci. USA 94: 13128-13133 [Abstract] [Full Text]
Okkema, P., Ha, E, Haun, C, Chen, W, Fire, A (1997). The Caenorhabditis elegans NK-2 homeobox gene ceh-22 activates pharyngeal muscle gene expression in combination with pha-1 and is required for normal pharyngeal development. Development 124: 3965-3973 [Abstract]
Krause, M, Park, M, Zhang, J., Yuan, J, Harfe, B, Xu, S., Greenwald, I, Cole, M, Paterson, B, Fire, A (1997). A C. elegans E/Daughterless bHLH protein marks neuronal but not striated muscle development. Development 124: 2179-2189 [Abstract]
Okkema, P., Fire, A (1994). The Caenorhabditis elegans NK-2 class homeoprotein CEH-22 is involved in combinatorial activation of gene expression in pharyngeal muscle. Development 120: 2175-2186 [Abstract]
Chen, L, Krause, M, Draper, B, Weintraub, H, Fire, A (1992). Body-wall muscle formation in Caenorhabditis elegans embryos that lack the MyoD homolog hlh-1. Science 256: 240-243 [Abstract]