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Galectin-1 interacts with beta-1 subunit of integrin.

Authors
  • Moiseeva, Elena P
  • Williams, Bryan
  • Goodall, Alison H
  • Samani, Nilesh J
Type
Published Article
Journal
Biochemical and biophysical research communications
Publication Date
Oct 24, 2003
Volume
310
Issue
3
Pages
1010–1016
Identifiers
PMID: 14550305
Source
Medline
License
Unknown

Abstract

Galectin-1, a beta-galactoside-binding dimeric lectin, is involved in adhesion, migration, and proliferation of vascular smooth muscle cells (SMC), the key steps in the development of atherosclerosis and restenosis. Here we investigated the molecular basis of the interactions between galectin-1 and SMCs. Galectin-1 modulated SMC attachment in a dose- and beta-galactoside-dependent manner. Direct binding of galectin-1 to beta1 integrin was detected by the immune precipitation of beta1 integrin after chemical cross-linking of 125I-labelled galectin-1 to the cell surface proteins. Galectin-1 transiently increased availability of beta1 integrins on the cell surface to antibodies against beta1 integrin. Incubation of SMCs with galectin-1 transiently increased the amount of the active form of beta1 integrin and tyrosine phosphorylation of two cytoskeleton-associated proteins; one of them coincided with focal adhesion kinase (FAK). Galectin-1 is likely to affect SMC adhesion by interacting with beta1 integrin on the cell surface of SMCs and inducing outside-in signalling.

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