Chick myotendinous antigen. II. A novel extracellular glycoprotein complex consisting of large disulfide-linked subunits

doi:10.1083/jcb.98.6.1937

This Article

	Full Text (PDF, 1314K)
	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 Chiquet, M.
	Articles by Fambrough, D. M.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Chiquet, M.
	Articles by Fambrough, D. M.


Social Bookmarking

	What's this?

ARTICLES

Chick myotendinous antigen. II. A novel extracellular glycoprotein complex consisting of large disulfide-linked subunits

M Chiquet and DM Fambrough

This report describes the biochemical characterization of a novel extracellular matrix component, " myotendinous antigen," which appears early in chick limb morphogenesis at sites connecting developing muscle fibers, tendons, and bone ( Chiquet , M., and D. Fambrough , 1984; J. Cell Biol., 98:1926-1936). This extracellular matrix antigen is a major component of the secretory proteins released into the medium by fibroblast and muscle cultures; the soluble form is characterized here. This form of myotendinous antigen is a large glycoprotein complex consisting of several disulfide linked subunits (Mr approximately 150,000-240,000). The differently sized antigen subunits are related, since they yielded very similar proteolytic cleavage patterns. M1 antibody can bind to the denatured subunits. The antigen subunits, as well as a Mr approximately 80,000 pepsin-resistant antigenic domain derived from them, are resistant to bacterial collagenase. Despite possessing subunits similar in size to fibronectin, myotendinous antigen appears to be both structurally and antigenically unrelated to fibronectin or to other known extracellular matrix components. About seven times more M1 antigen per cell nucleus was released into the medium in fibroblast as compared to muscle cultures. In muscle conditioned medium, myotendinous antigen is noncovalently complexed to very high molecular weight material that could be heavily labeled by [3H]glucosamine and [35S]sulfate. This material is sensitive to chondroitinase ABC and hence appears to contain sulfated glycosaminoglycans. We speculate that myotendinous antigen might interact with proteoglycans on the surface of muscle fibers, thereby acting as a link to tendons.
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:

Veit, G., Hansen, U., Keene, D. R., Bruckner, P., Chiquet-Ehrismann, R., Chiquet, M., Koch, M. (2006). Collagen XII Interacts with Avian Tenascin-X through Its NC3 Domain. J. Biol. Chem. 281: 27461-27470 [Abstract] [Full Text]
Jaggi, G. P., Laeng, H. R., Muntener, M., Killer, H. E. (2005). The Anatomy of the Muscle Insertion (Scleromuscular Junction) of the Lateral and Medial Rectus Muscle in Humans. IOVS 46: 2258-2263 [Abstract] [Full Text]
Mokone, G. G., Gajjar, M., September, A. V., Schwellnus, M. P., Greenberg, J., Noakes, T. D., Collins, M. (2005). The Guanine-Thymine Dinucleotide Repeat Polymorphism Within the Tenascin-C Gene Is Associated With Achilles Tendon Injuries. Am J Sports Med 33: 1016-1021 [Abstract] [Full Text]
Oldekamp, J., Kraemer, N., Alvarez-Bolado, G., Skutella, T. (2004). bHLH Gene Expression in the Emx2-deficient Dentate Gyrus Reveals Defective Granule Cells and Absence of Migrating Precursors. Cereb Cortex 14: 1045-1058 [Abstract] [Full Text]
Ingham, K. C., Brew, S. A., Erickson, H. P. (2004). Localization of a Cryptic Binding Site for Tenascin on Fibronectin. J. Biol. Chem. 279: 28132-28135 [Abstract] [Full Text]
Fluck, M., Chiquet, M., Schmutz, S., Mayet-Sornay, M.-H., Desplanches, D. (2003). Reloading of atrophied rat soleus muscle induces tenascin-C expression around damaged muscle fibers. Am. J. Physiol. Regul. Integr. Comp. Physiol. 284: R792-R801 [Abstract] [Full Text]
Puente Navazo, M. D., Valmori, D., Ruegg, C. (2001). The Alternatively Spliced Domain TnFnIII A1A2 of the Extracellular Matrix Protein Tenascin-C Suppresses Activation-Induced T Lymphocyte Proliferation and Cytokine Production. J. Immunol. 167: 6431-6440 [Abstract] [Full Text]
Geboes, K., El-Zine, M. Y., Dalle, I., El-Haddad, S., Rutgeerts, P., Van Eyken, P. (2001). Tenascin and Strictures in Inflammatory Bowel Disease: An Immunohistochemical Study. INT J SURG PATHOL 9: 281-286 [Abstract]
Kaarteenaho–Wiik, R., Lakari, E., Soini, Y., Pöllänen, R., Kinnula, V. L., Pääkkö, P. (2000). Tenascin Expression and Distribution in Pleural Inflammatory and Fibrotic Diseases. J. Histochem. Cytochem. 48: 1257-1268 [Abstract] [Full Text]
PAAKKO, P., KAARTEENAHO-WIIK, R., POLLANEN, R., SOINI, Y. (2000). Tenascin mRNA Expression at the Foci of Recent Injury in Usual Interstitial Pneumonia. Am. J. Respir. Crit. Care Med. 161: 967-972 [Abstract] [Full Text]
Talts, J., Wirl, G, Dictor, M, Muller, W., Fassler, R (1999). Tenascin-C modulates tumor stroma and monocyte/macrophage recruitment but not tumor growth or metastasis in a mouse strain with spontaneous mammary cancer. J. Cell Sci. 112: 1855-1864 [Abstract]
Halfter, W., Dong, S., Schurer, B., Cole, G. J. (1998). Collagen XVIII Is a Basement Membrane Heparan Sulfate Proteoglycan. J. Biol. Chem. 273: 25404-25412 [Abstract] [Full Text]
Smith, G. M., Hale, J. H. (1997). Macrophage/Microglia Regulation of Astrocytic Tenascin: Synergistic Action of Transforming Growth Factor-beta and Basic Fibroblast Growth Factor. J. Neurosci. 17: 9624-9633 [Abstract] [Full Text]
Maseruka, H, Bonshek, R E, Tullo, A B (1997). Tenascin-C expression in normal, inflamed, and scarred human corneas. Br J Ophthalmol 81: 677-682 [Abstract] [Full Text]
Schumacher, S., Volkmer, H., Buck, F., Otto, A., Tarnok, A., Roth, S., Rathjen, F. G. (1997). Chicken Acidic Leucine-rich EGF-like Domain Containing Brain Protein (CALEB), a Neural Member of the EGF Family of Differentiation Factors, Is Implicated in Neurite Formation. JCB 136: 895-906 [Abstract] [Full Text]
Chung, C., Erickson, H. (1997). Glycosaminoglycans modulate fibronectin matrix assembly and are essential for matrix incorporation of tenascin-C. J. Cell Sci. 110: 1413-1419 [Abstract]
Jones, P. L., Rabinovitch, M. (1996). Tenascin-C Is Induced With Progressive Pulmonary Vascular Disease in Rats and Is Functionally Related to Increased Smooth Muscle Cell Proliferation. Circ. Res. 79: 1131-1142 [Abstract] [Full Text]
Fischer, D., Chiquet-Ehrismann, R., Bernasconi, C., Chiquet, M. (1995). A Single Heparin Binding Region within the Fibrinogen-like Domain Is Functional in Chick Tenascin-C. J. Biol. Chem. 270: 3378-3384 [Abstract] [Full Text]
Wirl, G, Hermann, M, Ekblom, P, Fassler, R (1995). Mammary epithelial cell differentiation in vitro is regulated by an interplay of EGF action and tenascin-C downregulation. J. Cell Sci. 108: 2445-2456 [Abstract]
Jones, P., Boudreau, N, Myers, C., Erickson, H., Bissell, M. (1995). Tenascin-C inhibits extracellular matrix-dependent gene expression in mammary epithelial cells. Localization of active regions using recombinant tenascin fragments. J. Cell Sci. 108: 519-527 [Abstract]
Baker, L., Daggett, D., Peng, H. (1994). Concentration of pp125 focal adhesion kinase (FAK) at the myotendinous junction. J. Cell Sci. 107: 1485-1497 [Abstract]
Wehrle-Haller, B, Chiquet, M (1993). Dual function of tenascin: simultaneous promotion of neurite growth and inhibition of glial migration. J. Cell Sci. 106: 597-610 [Abstract]
Sriramarao, P, Mendler, M, Bourdon, M. (1993). Endothelial cell attachment and spreading on human tenascin is mediated by alpha 2 beta 1 and alpha v beta 3 integrins. J. Cell Sci. 105: 1001-1012 [Abstract]
Mackie, E. J., Tucker, R. P. (1992). Tenascin in bone morphogenesis: expression by osteoblasts and cell type-specific expression of splice variants. J. Cell Sci. 103: 765-771 [Abstract]
Umbhauer, M, Riou, J., Spring, J, Smith, J., Boucaut, J. (1992). Expression of tenascin mRNA in mesoderm during Xenopus laevis embryogenesis: the potential role of mesoderm patterning in tenascin regionalization. Development 116: 147-157 [Abstract]
Lukinmaa, P.-L., Mackie, E.J., Thesleff, I. (1991). Immunohistochemical Localization of the Matrix Glycoproteins-Tenascin and the ED-sequence-containing Form of Cellular Fibronectin--in Human Permanent Teeth and Periodontal Ligament. JDR 70: 19-26 [Abstract]
Mina, M., Kollar, E. J., Bishop, J. A., Rohrbach, D. H. (1990). Interaction between The Neural Crest and Extracellular Matrix Proteins in Craniofacial Skeletogenesis. CROBM 1: 79-87 [Full Text]
Olin, A. I., Morgelin, M., Sasaki, T., Timpl, R., Heinegard, D., Aspberg, A. (2001). The Proteoglycans Aggrecan and Versican Form Networks with Fibulin-2 through Their Lectin Domain Binding. J. Biol. Chem. 276: 1253-1261 [Abstract] [Full Text]
Schumacher, S., Jung, M., Norenberg, U., Dorner, A., Chiquet-Ehrismann, R., Stuermer, C. A. O., Rathjen, F. G. (2001). CALEB Binds via Its Acidic Stretch to the Fibrinogen-like Domain of Tenascin-C or Tenascin-R and Its Expression Is Dynamically Regulated after Optic Nerve Lesion. J. Biol. Chem. 276: 7337-7345 [Abstract] [Full Text]