Skip to main content

Focal adhesion integrity is downregulated by the alternatively spliced domain of human tenascin.

Publication ,  Journal Article
Murphy-Ullrich, JE; Lightner, VA; Aukhil, I; Yan, YZ; Erickson, HP; Höök, M
Published in: J Cell Biol
November 1991

Tenascin, together with thrombospondin and SPARC, form a family of matrix proteins that, when added to bovine aortic endothelial cells, caused a dose-dependent reduction in the number of focal adhesion-positive cells to approximately 50% of albumin-treated controls. For tenascin, a maximum response was obtained with 20-60 micrograms/ml of protein. The reduction in focal adhesions in tenascin-treated spread cells was observed 10 min after addition of the adhesion modulator, reached the maximum by 45 min, and persisted for at least 4 h in the continued presence of tenascin. This effect was fully reversible, was independent of de novo protein synthesis, and was neutralized by a polyclonal antibody to tenascin. Monoclonal antibodies to specific domains of tenascin (mAbs 81C6 and 127) were used to localize the active site to the alternatively spliced segment of tenascin. Furthermore, a recombinant protein corresponding to the alternatively spliced segment (fibronectin type III domains 6-12) was expressed in Escherichia coli and was active in causing loss of focal adhesions, whereas a recombinant form of a domain (domain 3) containing the RGD sequence had no activity. Chondroitin-6-sulfate effectively neutralized tenascin activity, whereas dermatan sulfate and chondroitin-4-sulfate were less active and heparan sulfate and heparin were essentially inactive. Studies suggest that galactosaminoglycans neutralize tenascin activity through interactions with cell surface molecules. Overall, our results demonstrate that tenascin, thrombospondin, and SPARC, acting as soluble ligands, are able to provoke the loss of focal adhesions in well-spread endothelial cells.

Duke Scholars

Altmetric Attention Stats
Dimensions Citation Stats

Published In

J Cell Biol

DOI

ISSN

0021-9525

Publication Date

November 1991

Volume

115

Issue

4

Start / End Page

1127 / 1136

Location

United States

Related Subject Headings

  • Vinculin
  • Tenascin
  • RNA Splicing
  • Peptide Fragments
  • Glycosaminoglycans
  • Extracellular Matrix Proteins
  • Extracellular Matrix
  • Endothelium, Vascular
  • Down-Regulation
  • Developmental Biology
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Murphy-Ullrich, J. E., Lightner, V. A., Aukhil, I., Yan, Y. Z., Erickson, H. P., & Höök, M. (1991). Focal adhesion integrity is downregulated by the alternatively spliced domain of human tenascin. J Cell Biol, 115(4), 1127–1136. https://doi.org/10.1083/jcb.115.4.1127
Murphy-Ullrich, J. E., V. A. Lightner, I. Aukhil, Y. Z. Yan, H. P. Erickson, and M. Höök. “Focal adhesion integrity is downregulated by the alternatively spliced domain of human tenascin.J Cell Biol 115, no. 4 (November 1991): 1127–36. https://doi.org/10.1083/jcb.115.4.1127.
Murphy-Ullrich JE, Lightner VA, Aukhil I, Yan YZ, Erickson HP, Höök M. Focal adhesion integrity is downregulated by the alternatively spliced domain of human tenascin. J Cell Biol. 1991 Nov;115(4):1127–36.
Murphy-Ullrich, J. E., et al. “Focal adhesion integrity is downregulated by the alternatively spliced domain of human tenascin.J Cell Biol, vol. 115, no. 4, Nov. 1991, pp. 1127–36. Pubmed, doi:10.1083/jcb.115.4.1127.
Murphy-Ullrich JE, Lightner VA, Aukhil I, Yan YZ, Erickson HP, Höök M. Focal adhesion integrity is downregulated by the alternatively spliced domain of human tenascin. J Cell Biol. 1991 Nov;115(4):1127–1136.

Published In

J Cell Biol

DOI

ISSN

0021-9525

Publication Date

November 1991

Volume

115

Issue

4

Start / End Page

1127 / 1136

Location

United States

Related Subject Headings

  • Vinculin
  • Tenascin
  • RNA Splicing
  • Peptide Fragments
  • Glycosaminoglycans
  • Extracellular Matrix Proteins
  • Extracellular Matrix
  • Endothelium, Vascular
  • Down-Regulation
  • Developmental Biology