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Cellular & Molecular Biology Letters logoLink to Cellular & Molecular Biology Letters
. 2008 Apr 18;13(3):452–464. doi: 10.2478/s11658-008-0017-6

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

Tharinee Susantad 1, Duncan R Smith 1,
PMCID: PMC6275979  PMID: 18425431

Abstract

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.

Key words: siRNA, RNA interference, Laminin receptor, p40, Ribosomal, Liver, Silencing, LAMR1

Full Text

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Abbreviations used

GAPDH

glyceraldehyde 3-phosphate dehydrogenase

LBP-p40

laminin-binding protein precursor p40

LRP

laminin receptor precursor

PrPc

cellular prion protein

siRNA

small interfering RNAs

37LBP

37-kDa laminin binding protein

67LR

67-kDa laminin receptor

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