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Am J Physiol Cell Physiol 286: C1312-C1323, 2004; doi:10.1152/ajpcell.00426.2002
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EXTRACELLULAR MATRIX, CELL INTERACTIONS

Channel-forming peptide modulates transepithelial electrical conductance and solute permeability

James R. Broughman,1 Robert M. Brandt,2 Christy Hastings,1 Takeo Iwamoto,2 John M. Tomich,2 and Bruce D. Schultz1

1Anatomy and Physiology and 2Biochemistry, Kansas State University, Manhattan, Kansas 66506

Submitted 16 September 2002 ; accepted in final form 14 January 2004

NC-1059, a synthetic channel-forming peptide, transiently increases transepithelial electrical conductance (gTE) and ion transport (as indicated by short-circuit current) across Madin-Darby canine kidney (MDCK) cell monolayers in a time- and concentration-dependent manner when apically exposed. gTE increases from <2 to >40 mS/cm2 over the low to middle micromolar range. Dextran polymer (9.5 but not 77 kDa) permeates the monolayer following apical NC-1059 exposure, suggesting that modulation of the paracellular pathway accounts for changes in gTE. However, concomitant alterations in junctional protein localization (zonula occludens-1, occludin) and cellular morphology are not observed. Effects of NC-1059 on MDCK gTE occur in nominally Cl–- and Na+-free apical media, indicating that permeation by these ions is not required for effects on gTE, although two-electrode voltage-clamp assays with Xenopus oocytes suggest that both Cl– and Na+ permeate NC-1059 channels with a modest Cl– permselectivity (PCl:PNa = 1.3). MDCK monolayers can be exposed to multiple NC-1059 treatments over days to weeks without diminution of response, alteration in the time course, or loss of responsiveness to physiological and pharmacological secretagogues. Together, these results suggest that NC-1059 represents a valuable tool to investigate tight junction regulation and may be a lead compound for therapeutic interventions.

transepithelial resistance; cystic fibrosis; tight junction; epithelial barrier; amphipathic {alpha}-helix


Address for reprint requests and other correspondence: B. D. Schultz, Dept. of Anatomy and Physiology, 228 Coles Hall, Kansas State Univ., Manhattan, KS 66506 (E-mail: bschultz{at}vet.ksu.edu).




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Apical electrolyte concentration modulates barrier function and tight junction protein localization in bovine mammary epithelium
Am J Physiol Cell Physiol, January 1, 2007; 292(1): C305 - C318.
[Abstract] [Full Text] [PDF]


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