{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ming X"],"funding":["NIGMS NIH HHS"],"pagination":["6567-76"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2965246"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["38(19)"],"pubmed_abstract":["Gastrin-releasing peptide receptor (GRPR), a member of the G protein-coupled receptor superfamily, has been utilized for receptor-mediated targeting of imaging and therapeutic agents; here we extend its use to oligonucleotide delivery. A splice-shifting antisense oligonucleotide was conjugated to a bombesin (BBN) peptide, and its intracellular delivery was tested in GRPR expressing PC3 cells stably transfected with a luciferase gene interrupted by an abnormally spliced intron. The BBN-conjugate produced significantly higher luciferase expression compared to unmodified oligonucleotide, and this increase was reversed by excess BBN peptide. Kinetic studies revealed a combination of saturable, receptor-mediated endocytosis and non-saturable pinocytosis for uptake of the conjugate. The K(m) val"],"journal":["Nucleic acids research"],"pubmed_title":["Intracellular delivery of an antisense oligonucleotide via endocytosis of a G protein-coupled receptor."],"pmcid":["PMC2965246"],"funding_grant_id":["P01GM059299"],"pubmed_authors":["Fisher M","Juliano RL","Alam MR","Chen X","Yan Y","Ming X"],"additional_accession":[]},"is_claimable":false,"name":"Intracellular delivery of an antisense oligonucleotide via endocytosis of a G protein-coupled receptor.","description":"Gastrin-releasing peptide receptor (GRPR), a member of the G protein-coupled receptor superfamily, has been utilized for receptor-mediated targeting of imaging and therapeutic agents; here we extend its use to oligonucleotide delivery. A splice-shifting antisense oligonucleotide was conjugated to a bombesin (BBN) peptide, and its intracellular delivery was tested in GRPR expressing PC3 cells stably transfected with a luciferase gene interrupted by an abnormally spliced intron. The BBN-conjugate produced significantly higher luciferase expression compared to unmodified oligonucleotide, and this increase was reversed by excess BBN peptide. Kinetic studies revealed a combination of saturable, receptor-mediated endocytosis and non-saturable pinocytosis for uptake of the conjugate. The K(m) val","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Oct","modification":"2025-04-22T05:22:45.76Z","creation":"2019-03-27T00:35:13Z"},"accession":"S-EPMC2965246","cross_references":{"pubmed":["20551131"],"doi":["10.1093/nar/gkq534"]}}