Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

Efficiency of protein transduction is cell type-dependent and is enhanced by dextran sulfate

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Mai, J. C.
  • Shen, H. M.
  • Watkins, S. C.
  • Cheng, T.
  • Robbins, Paul D.

publication date

  • August 2002

journal

  • Journal of Biological Chemistry  Journal

abstract

  • Protein transduction domains (PTDs), both naturally occurring and synthetic, have been increasingly utilized to deliver biologically active agents to a variety of cell types in vitro and in vivo. We report that in addition to previously characterized arginine-rich PTDs, including TAT, lysine homopolymers were able to mediate transduction of a wide variety of cell types, as measured by flow cytometric and enzymatic assays. The efficiency of PTD-mediated transduction was influenced by the cell type tested, although polylysine homopolymers demonstrate levels of internalization that consistently exceeded those of TAT and arginine homopolymers. Transduction of arginine/lysine-rich PTDs occurred at 4 degrees C and following depletion of cellular ATP pools, albeit generally at reduced levels. Although transduction was reduced in Chinese hamster ovary mutant lines deficient in either heparan sulfate or glycosaminoglycan synthesis, uptake was restored to wild-type levels by incubating target cells with dextran sulfate. The enhancement of transduction by dextran sulfate suggests that electrostatic interactions play an important first step in the process by which PTDs and their cargo traverse the plasma membrane.

subject areas

  • Animals
  • CHO Cells
  • Cricetinae
  • Dextran Sulfate
  • Glycosaminoglycans
  • HeLa Cells
  • Humans
  • Proteins
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.M204202200

PubMed ID

  • 12034749
scroll to property group menus

Additional Document Info

start page

  • 30208

end page

  • 30218

volume

  • 277

issue

  • 33

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support