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siRNA-mediated silencing of the 37/67-kDa high affinity laminin receptor in Hep3B cells induces apoptosis


The laminin-binding protein, variously called the 37/67-kDa high affinity laminin receptor or p40, mediates the attachment of normal cells to the laminin network, and also has a role as a ribosomal protein. Over-expression of this protein has been strongly correlated with the metastatic phenotype. However, few studies have investigated the cellular consequence of the ablation of this gene’s expression. To address this issue, the expression of the 37/67-kDa high affinity laminin receptor was knocked out with several siRNA constructs via RNA interference in transformed liver (Hep3B) cells. In each case where the message was specifically ablated, apoptosis was induced, as determined by annexin V/propidium iodide staining, and by double staining with annexin V and an antibody directed against the 37/67-kDa high affinity laminin receptor. These results suggest that this protein plays a critical role in maintaining cell viability.



glyceraldehyde 3-phosphate dehydrogenase


laminin-binding protein precursor p40


laminin receptor precursor

PrPc :

cellular prion protein


small interfering RNAs


37-kDa laminin binding protein


67-kDa laminin receptor


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Correspondence to Duncan R. Smith.

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Susantad, T., Smith, D.R. siRNA-mediated silencing of the 37/67-kDa high affinity laminin receptor in Hep3B cells induces apoptosis. Cell Mol Biol Lett 13, 452–464 (2008).

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Key words

  • siRNA
  • RNA interference
  • Laminin receptor
  • p40
  • Ribosomal
  • Liver
  • Silencing
  • LAMR1