PMID- 19707187
OWN - NLM
STAT- MEDLINE
DCOM- 20100113
LR  - 20211020
IS  - 1525-0024 (Electronic)
IS  - 1525-0016 (Print)
IS  - 1525-0016 (Linking)
VI  - 17
IP  - 11
DP  - 2009 Nov
TI  - Cell-surface accumulation of flock house virus-derived peptide leads to efficient 
      internalization via macropinocytosis.
PG  - 1868-76
LID - 10.1038/mt.2009.192 [doi]
AB  - Arginine-rich cell-penetrating peptides (CPPs), including human immunodeficiency 
      virus type 1 (HIV-1) Tat (48-60) and oligoarginines, have been applied as 
      carriers for delivery of cargo molecules, because of their capacity to 
      internalize into cells and penetrate biological membranes. Despite the fact that 
      they have been extensively studied, the factors required for the efficient 
      internalization of CPPs are still unclear. In this report, we evaluated the 
      internalization efficiencies of seven CPPs derived from DNA/RNA-binding peptides, 
      and discovered that a peptide derived from the flock house virus (FHV) coat 
      protein was internalized most efficiently into Chinese hamster ovary (CHO-K1), 
      HeLa, and Jurkat cells. Comparison of the factors facilitating the 
      internalization with those of the Tat peptide revealed that the FHV peptide 
      induces macropinocytosis much more efficiently than the Tat peptide, which leads 
      to its high cellular uptake efficiency. Additionally, the strong adsorption of 
      the FHV peptide on cell membranes via glycosaminoglycans (GAGs) was shown to be a 
      key factor for induction of macropinocytosis, and these steps were successfully 
      monitored by live imaging of the peptide internalization into cells in relation 
      to the actin organization. The remarkable methods of FHV peptide internalization 
      thus highlighted the critical factors for internalizations of the arginine-rich 
      CPPs.
FAU - Nakase, Ikuhiko
AU  - Nakase I
AD  - Institute for Chemical Research, Kyoto University, Kyoto, Japan.
FAU - Hirose, Hisaaki
AU  - Hirose H
FAU - Tanaka, Gen
AU  - Tanaka G
FAU - Tadokoro, Akiko
AU  - Tadokoro A
FAU - Kobayashi, Sachiko
AU  - Kobayashi S
FAU - Takeuchi, Toshihide
AU  - Takeuchi T
FAU - Futaki, Shiroh
AU  - Futaki S
LA  - eng
PT  - Journal Article
DEP - 20090825
PL  - United States
TA  - Mol Ther
JT  - Molecular therapy : the journal of the American Society of Gene Therapy
JID - 100890581
RN  - 0 (Capsid Proteins)
RN  - 0 (Glycosaminoglycans)
RN  - 0 (Nucleic Acid Synthesis Inhibitors)
RN  - 0 (Peptide Fragments)
RN  - 0 (tat Gene Products, Human Immunodeficiency Virus)
RN  - 22144-77-0 (Cytochalasin D)
SB  - IM
MH  - Animals
MH  - CHO Cells
MH  - Capsid Proteins/*metabolism
MH  - Cricetinae
MH  - Cricetulus
MH  - Cytochalasin D/pharmacology
MH  - Flow Cytometry
MH  - Glycosaminoglycans/metabolism
MH  - HeLa Cells
MH  - Humans
MH  - Microscopy, Confocal
MH  - Nucleic Acid Synthesis Inhibitors/pharmacology
MH  - Peptide Fragments/*metabolism
MH  - Pinocytosis/drug effects/*physiology
MH  - Protein Transport/physiology
MH  - tat Gene Products, Human Immunodeficiency Virus/metabolism
PMC - PMC2835031
EDAT- 2009/08/27 09:00
MHDA- 2010/01/14 06:00
PMCR- 2010/11/01
CRDT- 2009/08/27 09:00
PHST- 2009/08/27 09:00 [entrez]
PHST- 2009/08/27 09:00 [pubmed]
PHST- 2010/01/14 06:00 [medline]
PHST- 2010/11/01 00:00 [pmc-release]
AID - S1525-0016(16)30798-5 [pii]
AID - 10.1038/mt.2009.192 [doi]
PST - ppublish
SO  - Mol Ther. 2009 Nov;17(11):1868-76. doi: 10.1038/mt.2009.192. Epub 2009 Aug 25.