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Receptor/Transporter-independent Targeting of Functional Peptides across the Plasma Membrane.

Authors :
Veach, Ruth Ann
Liu, Danya
Yao, Shan
Chen, Yiliu
Xue Yan Liu, Yiliu
Downs, Sheila
Hawiger, Jacek
Source :
Journal of Biological Chemistry. 3/19/2004, Vol. 279 Issue 12, p11425-11431. 7p. 10 Color Photographs, 2 Diagrams, 13 Graphs.
Publication Year :
2004

Abstract

Targeting of peptides, proteins, and other functional cargo into living cells is contingent upon efficient transport across the plasma membrane barrier. We have harnessed the signal sequence hydrophobic region (SSHR) to deliver functional cargoes to cultured cells and to experimental animals. We now report evidence that two chirally distinct forms of SSHR composed of all L or all D amino acids showed similar membrane.translocating activity as assessed by confocal microscopy, flow cytometry, and direct fluorescence measurement. An attached nuclear localization sequence ferried by the SSHR enantiomers displayed similar intracellular function by inhibiting inducible nuclear import of transcription factor nuclear factor κ B and suppressing nuclear factor κ B-dependent gene expression of cytokines. A nuclear localization sequence comprised of a positively charged cluster of amino acids was rapidly translocated by SSHR enantiomers to the interior of unilamellar phospholipid vesicles. These findings indicate that the SSHR translocates functional peptides directly through the plasma membrane phospholipid bilayer without involving chirally specific receptor/transporter mechanisms. This mechanism of SSHR translocation is suitable for facile delivery of biologically active peptides for cell-based and animal-based functional proteomic studies. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00219258
Volume :
279
Issue :
12
Database :
Academic Search Index
Journal :
Journal of Biological Chemistry
Publication Type :
Academic Journal
Accession number :
12918924
Full Text :
https://doi.org/10.1074/jbc.M311089200