Interaction of beta-amyloid peptides with integrins in a human nerve cell line

S. Sabo, M. P. Lambert, K. Kessey, W. Wade, G. Krafft, W. L. Klein*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

61 Scopus citations


β-Amyloid accumulates as extracellular aggregates in Alzheimer's-afflicted brain tissue, but it also is secreted by healthy tissue, for reasons not yet established. One possibility is that β-amyloid, which contains a sequence (RHDS) homologous to the cell-binding domain of fibronectin, may modulate integrin function, a possibility supported by previous data from non-neuronal cells (Ghiso et al., Biochem. J., 288 (1992) 1053-1059). The current work shows that functional interaction with β-amyloid peptides is also supported by integrins in neuronal cells. Experiments used the SH-SY5Y human neuroblastoma cell line, which was shown to contain integrins that mediated cell adhesion to substratum-bound fibronectin. Adhesion to fibronectin was partially blocked by synthetic β-amyloid peptides containing the RHDS sequence. β-Amyloid sequences adsorbed to substratum themselves were found to mediate cell adhesion, although less effectively than fibronectin. Anti-integrin blocked the peptide-mediated adhesion, at doses commensurate with those blocking fibronectin-mediated adhesion. The data support the hypothesis that β-amyloid peptides could physiologically, and perhaps pathogenically, modulate the activity of neuronal integrins, important cell surface receptors known to control protein kinase activities, Ca2+ levels, gene expression and organization of the cytoskeleton.

Original languageEnglish (US)
Pages (from-to)25-28
Number of pages4
JournalNeuroscience Letters
Issue number1
StatePublished - Jan 16 1995


  • Adhesion
  • Alzheimer's
  • Amyloid
  • Fibronectin
  • Laminin
  • Neuroblastoma
  • SH-SY5Y

ASJC Scopus subject areas

  • General Neuroscience


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