Analysis of oligo-arginine cell-permeable peptides uptake by prostate cells

Jian Zhou, Wei Liu, Rey Chen Pong, Guiyang Hao, Xiankai Sun, Jer Tsong Hsieh

Research output: Contribution to journalArticle

16 Scopus citations

Abstract

Recently, we have shown that oligo-arginine peptide (i.e., R11), a unique cell-permeable peptide (CPP), can be used as an imaging probe for prostate cancer detection. In this study, the mechanism(s) of oligo-arginine peptide in prostate cells was further analyzed. The length of the oligo-arginine peptide appears to be critical for the efficiency of uptake by prostate cells: poly (11)-arginine (R11) > poly (9)-arginine (R9) > poly (13)-arginine peptide (R13). The uptake of R11 peptide by prostate cells is mediated by macropinocytosis as evidenced by the fact that uptake can be blocked by a macropinocytosis inhibitor. However, the use of an inhibitor for carbohydrate chain elongation of glycosaminoglycan or inhibitors for carbohydrate synthesis of glycoprotein via either O-link or N-link showed minimal effects on R11 uptake. Nevertheless, pentosan sulfate (PentS) or dextran sulfate (DS) exhibited the highest inhibitory effect on R11 uptake in several prostate cells treated with various soluble glycosaminoglycans (GAGs) or anionic polymers. It is known that laminin receptor has been characterized as a PentS binding partner. Knocking down 37LRP (laminin receptor precursor) expression in prostate cells showed a reduction in their ability to uptake R11 peptides. In conclusion, laminin receptor is one of the initial binding site(s) responsible for R11 peptide uptake in prostate cells.

Original languageEnglish (US)
Pages (from-to)1253-1260
Number of pages8
JournalAmino Acids
Volume42
Issue number4
DOIs
StatePublished - Apr 2012

Keywords

  • Cell-permeable peptide
  • Laminin receptor
  • Oligo-arginine peptide
  • Prostate cells

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry
  • Organic Chemistry

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