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Cargo-dependent mode of uptake and bioavailability of TAT-containing proteins and peptides in living cells.

Tünnemann, Gisela and Martin, Robert M. and Haupt, Simone and Patsch, Christoph and Edenhofer, Frank and Cardoso, M Cristina (2006):
Cargo-dependent mode of uptake and bioavailability of TAT-containing proteins and peptides in living cells.
In: The FASEB journal : official publication of the Federation of American Societies for Experimental Biology, pp. 1775-84, 20, (11), ISSN 1530-6860,
[Online-Edition: http://www.cardoso-lab.org/publications/Tunnemann_2006.pdf],
[Article]

Abstract

Cell-penetrating peptides (CPPs) are capable of introducing a wide range of cargoes into living cells. Descriptions of the internalization process vary from energy-independent cell penetration of membranes to endocytic uptake. To elucidate whether the mechanism of entry of CPP constructs might be influenced by the properties of the cargo, we used time lapse confocal microscopy analysis of living mammalian cells to directly compare the uptake of the well-studied CPP TAT fused to a protein (>50 amino acids) or peptide (<50 amino acids) cargo. We also analyzed various constructs for their subcellular distribution and mobility after the internalization event. TAT fusion proteins were taken up largely into cytoplasmic vesicles whereas peptides fused to TAT entered the cell in a rapid manner that was dependent on membrane potential. Despite their accumulation in the nucleolus, photobleaching of TAT fusion peptides revealed their mobility. The bioavailability of internalized TAT peptides was tested and confirmed by the strong inhibitory effect on cell cycle progression of two TAT fusion peptides derived from the tumor suppressor p21(WAF/Cip) and DNA Ligase I measured in living cells.

Item Type: Article
Erschienen: 2006
Creators: Tünnemann, Gisela and Martin, Robert M. and Haupt, Simone and Patsch, Christoph and Edenhofer, Frank and Cardoso, M Cristina
Title: Cargo-dependent mode of uptake and bioavailability of TAT-containing proteins and peptides in living cells.
Language: German
Abstract:

Cell-penetrating peptides (CPPs) are capable of introducing a wide range of cargoes into living cells. Descriptions of the internalization process vary from energy-independent cell penetration of membranes to endocytic uptake. To elucidate whether the mechanism of entry of CPP constructs might be influenced by the properties of the cargo, we used time lapse confocal microscopy analysis of living mammalian cells to directly compare the uptake of the well-studied CPP TAT fused to a protein (>50 amino acids) or peptide (<50 amino acids) cargo. We also analyzed various constructs for their subcellular distribution and mobility after the internalization event. TAT fusion proteins were taken up largely into cytoplasmic vesicles whereas peptides fused to TAT entered the cell in a rapid manner that was dependent on membrane potential. Despite their accumulation in the nucleolus, photobleaching of TAT fusion peptides revealed their mobility. The bioavailability of internalized TAT peptides was tested and confirmed by the strong inhibitory effect on cell cycle progression of two TAT fusion peptides derived from the tumor suppressor p21(WAF/Cip) and DNA Ligase I measured in living cells.

Journal or Publication Title: The FASEB journal : official publication of the Federation of American Societies for Experimental Biology
Volume: 20
Number: 11
Divisions: 10 Department of Biology > Cell Biology and Epigenetics
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10 Department of Biology
Date Deposited: 06 Mar 2010 08:00
Official URL: http://www.cardoso-lab.org/publications/Tunnemann_2006.pdf
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