Translocation of acylated pardaxin into cells

Yasmin Paul, Aryeh Weiss, Knut Adermann, Georg Erdmann, Carola Kassebaum, Philip Lazarovici, Jacob Hochman, Hans Wellhöner

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

Acylated pardaxin is translocated through the cytoplasmic membrane and is accumulated in the nucleoli of NG108-15 and chromaffin cells. The uptake is time- and dose-dependent and temperature-sensitive. However, the binding of acylated 125I-pardaxin cannot be reduced by competition with pardaxin acylated with Rudinger's reagent. In this respect, acylated pardaxin resembles the Tat protein 37-71 fragment. Metabolic inhibitors do not significantly reduce the uptake of acylated 125I-pardaxin. Acylated pardaxin might be useful as a vector to translocate other molecules. Copyright (C) 1998 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)131-134
Number of pages4
JournalFEBS Letters
Volume440
Issue number1-2
DOIs
StatePublished - 27 Nov 1998
Externally publishedYes

Bibliographical note

Funding Information:
This work was supported in part by a grant from the Lower Saxony-Israel Research Fund to J.H., P.L., and H.W.

Funding

This work was supported in part by a grant from the Lower Saxony-Israel Research Fund to J.H., P.L., and H.W.

FundersFunder number
Lower Saxony-Israel Research Fund

    Keywords

    • Pardaxin uptake
    • Peptide uptake

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