Toggle Main Menu Toggle Search

Open Access padlockePrints

Na+-independent lysine transport in human intestinal Caco-2 cells

Lookup NU author(s): Professor David Thwaites, Professor Nicholas Simmons

Downloads

Full text for this publication is not currently held within this repository. Alternative links are provided below where available.


Abstract

The nature of transepithelial and cellular transport of the dibasic amino acid lysine in human intestinal epithelial Caco-2 cells has been characterized. Intracellular accumulation of lysine across both the apical and basolateral membranes consists of a Na+-independent, membrane potential-sensitive uptake. Na+-independent lysine uptake at the basolateral membrane exceeds that at the apical membrane. Lysine uptake consists of both saturable and nonsaturable components. Na+-independent lysine uptake at both membranes is inhibited by lysine, arginine, alanine, histidine, methionine, leucine, cystine, cysteine and homoserine. In contrast, proline and taurine are without inhibitory effects at both membranes. Fractional Na+-independent lysine efflux from preloaded epithelial layers is greater at the basolateral membrane and shows trans-stimulation across both epithelial borders by lysine, arginine, alanine, histidine, methionine, and leucine but not proline and taurine. Na+-independent lysine influx (10 μM) in the presence of 10 mM homoserine shows further concentration dependent inhibition by lysine. Taken together, these data are consistent with lysine transport being mediated by systems b0,+, y+ and a component of very low affinity (nonsaturable) at both membranes. The relative contribution to lysine uptake at each membrane surface (at 10 μM lysine), normalized to total apical uptake (100%), is apical b0,+ (47%), y+ (27%) and the nonsaturable component (26%), and basal b0,+ (446%), y+ (276%) and the nonsaturable component (20%). Northern analysis shows hybridization of Caco-2 poly(A)+RNA with a human rBAT cDNA probe.


Publication metadata

Author(s): Simmons NL; Thwaites DT; Markovich D; Murer H

Publication type: Article

Publication status: Published

Journal: Journal of Membrane Biology

Year: 1996

Volume: 151

Issue: 3

Pages: 215-224

Print publication date: 01/01/1996

ISSN (print): 0022-2631

ISSN (electronic): 1432-1424

Publisher: Springer New York LLC

URL: http://dx.doi.org/10.1007/s002329900072

DOI: 10.1007/s002329900072

PubMed id: 8661509


Altmetrics

Altmetrics provided by Altmetric


Actions

Find at Newcastle University icon    Link to this publication


Share