Online citations, reference lists, and bibliographies.
Please confirm you are human
(Sign Up for free to never see this)
← Back to Search

Cell Internalization Of The Third Helix Of The Antennapedia Homeodomain Is Receptor-independent*

D. Derossi, S. Calvet, A. Trembleau, A. Brunissen, G. Chassaing, A. Prochiantz
Published 1996 · Medicine, Biology

Save to my Library
Download PDF
Analyze on Scholarcy
Share
We have recently reported that a 16-amino acid long polypeptide corresponding to the third helix of the DNA binding domain (homeodomain) of Antennapedia, a Drosophila transcription factor, is internalized by cells in culture (Derossi, D., Joliot, A. H., Chassaing, G., and Prochiantz, A. (1994) J. Biol. Chem. 269, 10444-10450). The capture of the homeodomain and of its third helix at temperatures below 10°C raised the problem of the mechanism of internalization. The present demonstration, that a reverse helix and a helix composed of D-enantiomers still translocate across biological membranes at 4 and 37°C strongly suggests that the third helix of the homeodomain is internalized by a receptor-independent mechanism. The finding that introducing 1 or 3 prolines in the structure does not hamper internalization also demonstrates that the α-helical structure is not necessary. The data presented are compatible with a translocation process based on the establishment of direct interactions with the membrane phospholipids. The third helix of the homeodomain has been used successfully to address biologically active substances to the cytoplasm and nucleus of cells in culture (Théodore, L., Derossi, D., Chassaing, G., Llirbat, B., Kubes, M., Jordan, P., Chneiweiss, H., Godement, P., and Prochiantz, A. (1995) J. Neurosci. 15, 7158-7167). Therefore, in addition to their physiological implications (Prochiantz, A., and Théodore, L. (1995) BioEssays 17, 39-45), the present results open the way to the molecular design of cellular vectors.
This paper references
Chassaing, manuscript in preparation. Homeodomain Peptide Internalization
A. Joliot (1991)
10.1523/JNEUROSCI.16-01-00253.1996
Downregulation of Cu/Zn superoxide dismutase leads to cell death via the nitric oxide-peroxynitrite pathway
C. Troy (1996)
10.1073/PNAS.87.12.4761
All-D amino acid-containing channel-forming antibiotic peptides.
D. Wade (1990)
The third helix of the Antennapedia homeodomain translocates through biological membranes.
D. Derossi (1994)
In vitro control of neuronal polarity by glycosaminoglycans.
F. Lafont (1992)
10.1073/PNAS.88.5.1864
Antennapedia homeobox peptide regulates neural morphogenesis.
A. Joliot (1991)
10.1083/JCB.128.5.919
Downregulation of amyloid precursor protein inhibits neurite outgrowth in vitro
B. Allinquant (1995)
10.1073/PNAS.93.11.5635
The contrasting roles of ICE family proteases and interleukin-1beta in apoptosis induced by trophic factor withdrawal and by copper/zinc superoxide dismutase down-regulation.
C. Troy (1996)
10.1073/PNAS.88.13.5572
Delivery of macromolecules into living cells: a method that exploits folate receptor endocytosis.
C. P. Leamon (1991)
10.1016/0962-8924(94)90211-9
Endocytosis without clathrin.
K. Sandvig (1994)
10.1016/0014-5793(95)00681-X
Promoter‐specific regulation of gene expression by an exogenously added homeodomain that promotes neurite growth
I. Le Roux (1995)
10.1002/j.1460-2075.1990.tb08268.x
A novel secretory pathway for interleukin‐1 beta, a protein lacking a signal sequence.
A. Rubartelli (1990)
10.1016/0248-4900(91)90095-5
Fluid phase endocytosis investigated by fluorescence with trimethylamino‐diphenylhexatriene in L929 cells; the influence of temperature and of cytoskeleton depolymerizing drugs
D. Illinger (1991)
10.1016/S0960-9822(02)00425-6
Inhibition of pRb phosphorylation and cell-cycle progression by a 20-residue peptide from p16CDKN2/INK4A
R. Fahraeus (1996)
10.1016/0925-4773(95)00478-5
Transcription factor Hoxa-5 is taken up by cells in culture and conveyed to their nuclei
L. Chatelin (1996)
10.1073/PNAS.90.19.9120
Neurotrophic activity of the Antennapedia homeodomain depends on its specific DNA-binding properties.
I. Le Roux (1993)
10.1523/JNEUROSCI.15-11-07158.1995
Intraneuronal delivery of protein kinase C pseudosubstrate leads to growth cone collapse
L. Theodore (1995)
10.1083/JCB.120.2.485
Antennapedia homeobox peptide enhances growth and branching of embryonic chicken motoneurons in vitro
E. Bloch-Gallego (1993)
10.1073/PNAS.87.18.6954
Homeodomain of yeast repressor alpha 2 contains a nuclear localization signal.
M. Hall (1990)
10.1002/BIES.950170109
Nuclear/growth factors
A. Prochiantz (1995)



This paper is referenced by
10.1021/BI0346805
Protein transduction domains of HIV-1 and SIV TAT interact with charged lipid vesicles. Binding mechanism and thermodynamic analysis.
A. Ziegler (2003)
10.1099/mic.0.2008/021964-0
Plasmodium falciparum and Hyaloperonospora parasitica effector translocation motifs are functional in Phytophthora infestans.
S. Grouffaud (2008)
10.1073/pnas.1811520115
Arginine-rich cell-penetrating peptides induce membrane multilamellarity and subsequently enter via formation of a fusion pore
Christoph Allolio (2018)
Structures, toxicity and internalization of cell-penetrating peptides
Emelía Eiríksdóttir (2010)
Cell-Penetrating Penetratin Peptides - Mechanistic Studies on Uptake Pathways and DNA Delivery Efficiency
Helene L. Åmand (2012)
New fluorine-labelled amino acids as ¹⁹F-NMR reporters for structural peptide studies: Design, synthesis, and applications
Pavlo Mykhailiuk (2008)
10.1038/nprot.2006.30
A direct approach to quantification of the cellular uptake of cell-penetrating peptides using MALDI-TOF mass spectrometry
F. Burlina (2006)
10.1016/j.nano.2011.04.009
A peptide derived from herpes simplex virus type 1 glycoprotein H: membrane translocation and applications to the delivery of quantum dots.
A. Falanga (2011)
10.1016/S0014-5793(01)02843-5
Penetratin‐induced aggregation and subsequent dissociation of negatively charged phospholipid vesicles
D. Persson (2001)
10.1046/J.0014-2956.2001.02653.X
Growth inhibition of mammalian cells by eosinophil cationic protein.
T. Maeda (2002)
10.1016/S0006-2952(98)00243-3
Selective cytotoxicity of topoisomerase-directed protoberberines against glioblastoma cells.
M. Sanders (1998)
10.1517/17530050902824829
Transport molecules using reverse sequence HIV-Tat polypeptides: not just any old Tat? (WO200808225)
J. Howl (2009)
10.1016/S0169-409X(00)00082-X
Novel non-endocytic delivery of antisense oligonucleotides.
S. Dokka (2000)
10.1080/17425247.2018.1517750
Mitochondrial-targeted penetrating peptide delivery for cancer therapy
Jiao Wu (2018)
10.1016/B978-0-12-384935-9.10010-0
Peptide and Protein Delivery with Cell-penetrating Peptides
Helin Räägel (2011)
Highly sensitive fluorescent methods for the detection of enzymes and the determination of their activity by means of specific hydrolases
S. Henkenjohann (2009)
10.1016/J.BBAMEM.2004.07.008
Vesicle size-dependent translocation of penetratin analogs across lipid membranes.
D. Persson (2004)
Recent applicable delivery approaches of peptide nucleic acids to the target cells
Reyhane Alidousti (2019)
10.3109/09537100903324219
Inhibition of platelet activation by peptide analogs of the β3-intracellular domain of platelet integrin αIIbβ3 conjugated to the cell-penetrating peptide Tat(48–60)
Andromaxi A. Dimitriou (2009)
10.1021/BI0491604
The cationic cell-penetrating peptide CPP(TAT) derived from the HIV-1 protein TAT is rapidly transported into living fibroblasts: optical, biophysical, and metabolic evidence.
A. Ziegler (2005)
10.1007/978-1-4939-2806-4_1
Classes of Cell-Penetrating Peptides.
M. Pooga (2015)
10.1007/s40005-016-0253-0
Cell penetrating peptides as an innovative approach for drug delivery; then, present and the future
Santosh K Bashyal (2016)
10.1016/j.jcis.2020.05.121
Shuffled lipidation pattern and degree of lipidation determines the membrane interaction behavior of a linear cationic membrane-active peptide.
Sofie Fogh Hedegaard (2020)
10.1006/EXCR.2001.5316
VE-cadherin-derived cell-penetrating peptide, pVEC, with carrier functions.
A. Elmquist (2001)
10.1002/PAT.3432
Polymers in gene therapy technology
H. Hosseinkhani (2015)
10.1016/j.ijpharm.2007.12.003
Octaarginine-modified liposomes: enhanced cellular uptake and controlled intracellular trafficking.
I. Khalil (2008)
10.1016/j.jcis.2019.05.087
Adsorption and insertion of polyarginine peptides into membrane pores: The trade-off between electrostatics, acid-base chemistry and pore formation energy.
P. G. Ramírez (2019)
Role of Otx2 in mature retinal photoreceptors
Pasquale Pensieri (2019)
10.1016/j.chemphyslip.2013.02.011
Early stages of interactions of cell-penetrating peptide penetratin with a DPPC bilayer.
M. Pourmousa (2013)
10.1016/j.bbamem.2012.11.014
Structure and dynamics of the two amphipathic arginine-rich peptides RW9 and RL9 in a lipid environment investigated by solid-state NMR and MD simulations.
K. Witte (2013)
10.1016/j.pharmthera.2015.07.003
Cell-penetrating peptides transport therapeutics into cells.
J. Ramsey (2015)
10.1038/srep09882
Efficient in vitro generation of functional thymic epithelial progenitors from human embryonic stem cells
M. Su (2015)
See more
Semantic Scholar Logo Some data provided by SemanticScholar