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Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C.

Publication ,  Journal Article
Chung, CY; Erickson, HP
Published in: J Cell Biol
July 1994

We have investigated the binding of soluble tenascin-C (TN-C) to several cell lines using a radioligand binding assay. Specific binding was demonstrated to U-251MG human glioma cells and to a line of bovine aortic endothelial cells, but hamster fibroblasts showed no specific binding. Recombinant proteins corresponding to specific domains of TN-C were used to map the binding site(s) in TN-C. The alternatively spliced segment (TNfnA-D) inhibited the binding of native TN-C most strongly, and itself bound to glioma and endothelial cells. Scatchard analysis of TNfnA-D binding indicated 2-5 x 10(5) binding sites per cell, with an apparent 2 nM dissociation constant. The cell surface receptor for TNfnA-D was identified as a 35-kD protein on the basis of blot binding assays and affinity chromatography of membrane extracts on native TN-C and TNfnA-D columns. Protein sequencing indicated that this 35-kD receptor was annexin II. Annexin II is well characterized as a cytoplasmic protein, so it was surprising to find it as a presumably extracellular receptor for TN-C. To confirm that it was the 35-kD receptor, we obtained purified annexin II and demonstrated its binding to TNfnA-D and TN-C at nM concentrations. Antibodies to annexin II prominently stained the external surface of live endothelial cells and blocked the binding of TNfnA-D to the cells. Thus annexin II appears to be a receptor for the alternatively spliced segment of TN-C, and may mediate cellular responses to soluble TN-C in the extracellular matrix.

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Published In

J Cell Biol

DOI

ISSN

0021-9525

Publication Date

July 1994

Volume

126

Issue

2

Start / End Page

539 / 548

Location

United States

Related Subject Headings

  • Tumor Cells, Cultured
  • Tenascin
  • Sequence Analysis
  • Recombinant Proteins
  • Receptors, Cell Surface
  • Radioligand Assay
  • Nerve Tissue Proteins
  • Molecular Sequence Data
  • Lung
  • Kinetics
 

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Chung, C. Y., & Erickson, H. P. (1994). Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C. J Cell Biol, 126(2), 539–548. https://doi.org/10.1083/jcb.126.2.539
Chung, C. Y., and H. P. Erickson. “Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C.J Cell Biol 126, no. 2 (July 1994): 539–48. https://doi.org/10.1083/jcb.126.2.539.
Chung, C. Y., and H. P. Erickson. “Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C.J Cell Biol, vol. 126, no. 2, July 1994, pp. 539–48. Pubmed, doi:10.1083/jcb.126.2.539.

Published In

J Cell Biol

DOI

ISSN

0021-9525

Publication Date

July 1994

Volume

126

Issue

2

Start / End Page

539 / 548

Location

United States

Related Subject Headings

  • Tumor Cells, Cultured
  • Tenascin
  • Sequence Analysis
  • Recombinant Proteins
  • Receptors, Cell Surface
  • Radioligand Assay
  • Nerve Tissue Proteins
  • Molecular Sequence Data
  • Lung
  • Kinetics