ArticleNucleic acids research2000
Identification, purification and partial characterisation of an oligonucleotide receptor in membranes of HepG2 cells.
Article in Nucleic acids research, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 38 citations in OpenAlex.
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- Canonical and non-canonical barriers facing antimiR cancer therapeutics.Current medicinal chemistry · 2013Review
- Production of an antigenic peptide by insulin-degrading enzyme.Nature immunology · 2010Article
- Article
- Antisense oligonucleotide inhibition of hepatitis C virus genotype 4 replication in HepG2 cells.Cancer cell international · 2006Article
- Phosphorothioate-stimulated uptake of short interfering RNA by human cells.EMBO reports · 2005Article
- Spontaneous uptake of biologically active recombinant DNA by mammalian cells via a selected DNA segment.Gene therapy · 2005Article
- Infection by Mycoplasma hyorhinis strongly enhances uptake of antisense oligonucleotides: a reassessment of receptor-mediated endocytosis in the HepG2 cell line.Nucleic acids research · 2003Article
- Receptor-mediated endocytosis of phosphodiester oligonucleotides in the HepG2 cell line: evidence for non-conventional intracellular trafficking.Nucleic acids research · 2002Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The low and unpredictable uptake and cytosolic transfer of oligonucleotides (ODN) is a major reason for their limited benefit. Improving the ODN potential for therapy and research requires a better understanding of their receptor-mediated endocytosis. We have undertaken to identify a membrane ODN receptor on HepG2 cells by ligand blotting of cell extracts with [(125)I]ODN and by photolabelling of living cells with a [(125)I]ODN-benzophenone conjugate. A major band at 66 kDa was identified by the two methods. Its labelling was saturable and competed for by unlabelled ODN of various sequences and irrespective of the presence of a phosphodiester or phosphoro-thioate backbone. This protein remained sedimentable after carbonate extraction, indicating strong membrane association. About half of the total cell amount resisted extensive surface proteolysis, suggesting a dual localisation at the plasma membrane and cytoplasmic vesicles. The protein was purified using a biotinylated ODN-benzophenone conjugate by photocrosslinking followed by streptavidin affinity purification. A sequence obtained by Edman degradation showed no homology with known proteins. Using anti-peptide antisera, labelling by western blotting revealed at 66 kDa a band with comparable properties as found by ligand blotting. Thus, a new membrane protein acting as an ODN receptor has been demonstrated.
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