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Johansson HJ, El-Andaloussi S, Holm T, et al. Characterization of a Novel Cytotoxic Cell-penetrating Peptide Derived From p14ARF Protein. Mol Ther. 2016;16(1):115-123doi: 10.1038/sj.mt.6300346.
Johansson, H. J., El-Andaloussi, S., Holm, T., Mäe, M., Jänes, J., Maimets, T., & Langel, �. �. (2008). Characterization of a Novel Cytotoxic Cell-penetrating Peptide Derived From p14ARF Protein. Molecular therapy : the journal of the American Society of Gene Therapy, 16(1), 115-123. https://doi.org/10.1038/sj.mt.6300346
Johansson, Henrik J, et al. "Characterization of a Novel Cytotoxic Cell-penetrating Peptide Derived From p14ARF Protein." Molecular therapy : the journal of the American Society of Gene Therapy vol. 16,1 (2008): 115-123. doi: https://doi.org/10.1038/sj.mt.6300346
Johansson HJ, El-Andaloussi S, Holm T, Mäe M, Jänes J, Maimets T, Langel Ü. Characterization of a Novel Cytotoxic Cell-penetrating Peptide Derived From p14ARF Protein. Mol Ther. 2008 Jan;16(1):115-123. doi: 10.1038/sj.mt.6300346. Epub 2016 Dec 07. PMID: 28192705.
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Mol Ther. 2008 Jan;16(1):115-123. doi: 10.1038/sj.mt.6300346. Epub 2016 Dec 07.

Characterization of a Novel Cytotoxic Cell-penetrating Peptide Derived From p14ARF Protein.

Molecular therapy : the journal of the American Society of Gene Therapy

Henrik J Johansson, Samir El-Andaloussi, Tina Holm, Maarja Mäe, Jaak Jänes, Toivo Maimets, Ülo Langel

Affiliations

  1. Department of Neurochemistry, Stockholm University, Stockholm, Sweden. Electronic address: [email protected].
  2. Department of Neurochemistry, Stockholm University, Stockholm, Sweden.
  3. Department of Cell Biology, Institute of Molecular and Cell Biology, Tartu University, Tartu, Estonia.

PMID: 28192705 DOI: 10.1038/sj.mt.6300346

Abstract

The tumor suppressor p14ARF is widely deregulated in many types of cancers and is believed to function as a failsafe mechanism, inhibiting proliferation and inducing apoptosis as cellular response to a high oncogene load. We have found that a 22-amino-acid-long peptide derived from the N-terminal part of p14ARF, denoted ARF(1-22), which has previously been shown to mimic the function of p14ARF, has cell-penetrating properties. This peptide is internalized to the same extent as the cell-penetrating peptide (CPP) TP10 and dose-dependently decreases proliferation in MCF-7 and MDA MB 231 cells. Uptake of the ARF(1-22) peptide is associated with low membrane disturbance, measured by deoxyglucose and lactate dehydrogenase (LDH) leakage, as compared to its scrambled peptide. Also, flow cytometric analysis of annexin V/propidium iodide (PI) binding and Hoechst staining of nuclei suggest that ARF(1-22) induces apoptosis, whereas scrambled or inverted peptide sequences have no effect. The ARF(1-22) peptide mainly translocates cells through endocytosis, and is found intact inside cells for at least 3 hours. To our knowledge, this is the first time a CPP having pro-apoptopic activity has been designed from a protein.

Copyright © 2007 The American Society of Gene Therapy. Published by Elsevier Inc. All rights reserved.

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