Cysteine mutagenesis to study the structure of claudin-2 paracellular pores

Ann N Y Acad Sci. 2009 May:1165:143-7. doi: 10.1111/j.1749-6632.2009.04038.x.

Abstract

The structure and transport mechanism of paracellular pores are only poorly understood. Here we describe for the first time how the substituted cysteine accessibility method (SCAM), previously developed to study transmembrane transport, can be applied to analyze the pathway of paracellular ion permeation. Using stable transfected Madin Darby canine kidney type I cells, induced to express claudin-2, we show that paracellular cation transport can be blocked by sulfhydryl-specific methanethiosulfonate (MTS) and that SCAM can be used to identify residues that line paracellular pores.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Membrane Permeability
  • Cells, Cultured
  • Cysteine / genetics*
  • Cysteine / metabolism
  • Dogs
  • Fluorescent Antibody Technique
  • Membrane Proteins / chemistry*
  • Membrane Proteins / genetics*
  • Membrane Proteins / metabolism
  • Mutagenesis

Substances

  • Membrane Proteins
  • Cysteine