FASEB J. Avanti Polar Lipids
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF) Free
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Chiquet-Ehrismann, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Chiquet-Ehrismann, R.

The FASEB Journal, Vol 4, 2598-2604, Copyright © 1990 by The Federation of American Societies for Experimental Biology

REVIEWS

What distinguishes tenascin from fibronectin?

R Chiquet-Ehrismann
Friedrich Miescher Institute, Basel, Switzerland.

Tenascin and fibronectin are two major extracellular matrix glycoproteins. They both consist of large disulfide-linked subunits composed of multiple structural domains. More than half of each molecule consists of so-called fibronectin type III repeats, but the other domains differ. Fibronectin is a dimer, whereas tenascin is a hexamer. Often fibronectin and tenascin are colocalized in tissues, but the occurrence of tenascin is much more restricted when compared with fibronectin. Tenascin is transiently expressed in many developing organs such as connective tissues, the mesenchyme of epithelial organs, and also the central and peripheral nervous systems, and it reappears in the stroma of many tumors. The distinctive and highly regulated expression of tenascin has provoked interest in trying to identify possible functions of tenascin in cell-cell and cell-substratum adhesion, cell migration, growth, and cell differentiation during morphogenesis.


This article has been cited by other articles:


Home page
 Clin. Cancer Res.Home page
S. Suwiwat, C. Ricciardelli, R. Tammi, M. Tammi, P. Auvinen, V.-M. Kosma, R. G. LeBaron, W. A. Raymond, W. D. Tilley, and D. J. Horsfall
Expression of Extracellular Matrix Components Versican, Chondroitin Sulfate, Tenascin, and Hyaluronan, and Their Association with Disease Outcome in Node-Negative Breast Cancer
Clin. Cancer Res., April 1, 2004; 10(7): 2491 - 2498.
[Abstract] [Full Text] [PDF]

Home page
 J. Histochem. Cytochem.Home page
R. Kaarteenaho–Wiik, E. Lakari, Y. Soini, R. Pöllänen, V. L. Kinnula, and P. Pääkkö
Tenascin Expression and Distribution in Pleural Inflammatory and Fibrotic Diseases
J. Histochem. Cytochem., September 1, 2000; 48(9): 1257 - 1268.
[Abstract] [Full Text]

Home page
 Am. J. Respir. Crit. Care Med.Home page
P. PAAKKO, R. KAARTEENAHO-WIIK, R. POLLANEN, and Y. SOINI
Tenascin mRNA Expression at the Foci of Recent Injury in Usual Interstitial Pneumonia
Am. J. Respir. Crit. Care Med., March 1, 2000; 161(3): 967 - 972.
[Abstract] [Full Text] [PDF]

Home page
 Mol Hum ReprodHome page
S.C. Bell, J.H. Pringle, D.J. Taylor, and T.M. Malak
Alternatively spliced tenascin-C mRNA isoforms in human fetal membranes
Mol. Hum. Reprod., November 1, 1999; 5(11): 1066 - 1076.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
A. Minet, B. Rubin, R. Tucker, S Baumgartner, and R Chiquet-Ehrismann
Teneurin-1, a vertebrate homologue of the Drosophila pair-rule gene ten-m, is a neuronal protein with a novel type of heparin-binding domain
J. Cell Sci., January 6, 1999; 112(12): 2019 - 2032.
[Abstract] [PDF]

Home page
 Am. J. Respir. Cell Mol. Bio.Home page
V. L. Kinnula, A. Linnala, E. Viitala, K. Linnainmaa, and I. Virtanen
Tenascin and Fibronectin Expression in Human Mesothelial Cells and Pleural Mesothelioma Cell-Line Cells
Am. J. Respir. Cell Mol. Biol., September 1, 1998; 19(3): 445 - 452.
[Abstract] [Full Text]

Home page
 J. Cell Sci.Home page
T Sakai, Y Furukawa, R Chiquet-Ehrismann, M Nakamura, S Kitagawa, T Ikemura, and K Matsumoto
Tenascin-X expression in tumor cells and fibroblasts: glucocorticoids as negative regulators in fibroblasts
J. Cell Sci., January 8, 1996; 109(8): 2069 - 2077.
[Abstract] [PDF]

Home page
 J. Cell Sci.Home page
P Pesheva, R Probstmeier, A. Skubitz, J. McCarthy, L. Furcht, and M Schachner
Tenascin-R (J1 160/180 inhibits fibronectin-mediated cell adhesion--functional relatedness to tenascin-C
J. Cell Sci., January 8, 1994; 107(8): 2323 - 2333.
[Abstract] [PDF]

Home page
 J. Cell Sci.Home page
P Sriramarao, M Mendler, and M. Bourdon
Endothelial cell attachment and spreading on human tenascin is mediated by alpha 2 beta 1 and alpha v beta 3 integrins
J. Cell Sci., January 8, 1993; 105(4): 1001 - 1012.
[Abstract] [PDF]

Home page
 J. Cell Sci.Home page
C. M. Kielty, S. P. Whittaker, M. E. Grant, and C. A. Shuttleworth
Attachment of human vascular smooth muscles cells to intact microfibrillar assemblies of collagen VI and fibrillin
J. Cell Sci., October 1, 1992; 103(2): 445 - 451.
[Abstract] [PDF]

Home page
 DevelopmentHome page
M Umbhauer, J. Riou, J Spring, J. Smith, and J. Boucaut
Expression of tenascin mRNA in mesoderm during Xenopus laevis embryogenesis: the potential role of mesoderm patterning in tenascin regionalization
Development, January 9, 1992; 116(1): 147 - 157.
[Abstract] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1990 by The Federation of American Societies for Experimental Biology.