Abstract:
:The cellular uptake of a model antisense oligonucleotide complementary to 21 bases of the bovine GLUT-1 glucose transporter mRNA and a model vasopressin peptide that were biotinylated, was markedly stimulated by the presence of avidin, a cationic protein. Conversely, the bacteria homologue of avidin, streptavidin, which is a slightly acidic protein, did not facilitate cellular uptake. The avidin-mediated uptake of biotinylated derivatives was competitively inhibited by another cationic protein, protamine, with a Ki of 5 micrograms/ml; was saturable, temperature- and time-dependent; and was associated with endocytosis. The use of the avidin-biotin system provides a new approach to increasing the cellular uptake of antisense oligonucleotides or peptides.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Pardridge WM,Boado RJdoi
10.1016/0014-5793(91)80996-gsubject
Has Abstractpub_date
1991-08-19 00:00:00pages
30-2issue
1-2eissn
0014-5793issn
1873-3468pii
0014-5793(91)80996-Gjournal_volume
288pub_type
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