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PMID: 7518469 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

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

The Journal of cell biology ·Vol. 126 ·No. 2 ·1994-07-00 ·Pages 539-48

Chung CY, Erickson HP

Abstract

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.

MeSH Terms
Alternative Splicing Amino Acid Sequence Animals Annexin A2/chemistry,isolation & purification,metabolism Binding Sites Cattle Cell Adhesion Molecules, Neuronal/genetics,metabolism Cells, Cultured Endothelium/cytology Extracellular Matrix Proteins/genetics,metabolism Glioma Humans Kinetics Lung/chemistry Molecular Sequence Data Nerve Tissue Proteins/genetics,metabolism Radioligand Assay Receptors, Cell Surface/chemistry,isolation & purification,metabolism Recombinant Proteins/metabolism Sequence Analysis Tenascin Tumor Cells, Cultured
Chemicals
Annexin A2 Cell Adhesion Molecules, Neuronal Extracellular Matrix Proteins Nerve Tissue Proteins Receptors, Cell Surface Recombinant Proteins Tenascin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Chung C Y
Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710.
Erickson H P
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.126.2.539
Published
1994-07-00
Pages
539-48
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2200039
Subset
IM
Grants
NCI NIH HHS · R37-CA47056 · United States
External Links
PubMed source DOI: 10.1083/jcb.126.2.539 PMC Full Text View journal details
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