Swelling-activated amino acid efflux in the human neuroblastoma cell line CHP-100. Basavappa, S., Huang, C., Mangel, A., Lebedev, D., Knauf, P., & Ellory, J. Journal of Neurophysiology, 76(2):764-769, American Physiological Society, 1996. cited By 32
Paper doi abstract bibtex 1. The effects of hypoosmotic stress on cell volume and amino acid efflux were evaluated in the human neuroblastoma cell line CHP-100 with the Coulter Counter Multisizer and radiolabeled amino acid efflux, respectively. 2. CHP-100 cells swelled by 35 ± 5% (means ± SE) when the osmolarity of the solution was decreased from 290 to 190 mOsm/kg H2O. The rapid swelling was followed by a biphasic regulatory volume decrease (RVD). 3. In cells loaded with 14C-taurine, hypoosmotic stress induced a 300 ± 22% (n = 23. P < 0.05) increase in taurine efflux compared with controls. This efflux was inhibited by the chloride channel blockers 5-nitro-2-(3-phenylpropylamino)- benzoic acid (NPPB). 4,4'-diisothio-cyanostilbene-2,2'-disulfonic acid (DIDS), niflumic acid and by the volume activated anion channel blocker tamoxifen. In addition, the swelling-activated taurine efflux was dependent upon extracellular calcium. 4. Similarly, in cells loaded with 14C-glycine, hypoosmotic stress significantly increased glycine efflux, which was also sensitive to NPPB. In contrast, efflux of 3H-glutamate was not significantly altered after hypoosmotic stress. 5. With the use of patch clamp recording techniques, Cl- channels were activated in cell attached patches after exposure to hypoosmotic solutions. 6. In nystatin perforated patches, permeability of the hypoosmotically activated anion channel was observed to be SCN > I > Br > Cl >> Glutamate. 7. It is concluded that in CHP-100 cells, anion channels are activated during hypoosmotic stress and these channels represent a pathway for efflux of amino acids.
@ARTICLE{Basavappa1996764,
author={Basavappa, S. and Huang, C.-C. and Mangel, A.W. and Lebedev, D.V. and Knauf, P.A. and Ellory, J.C.},
title={Swelling-activated amino acid efflux in the human neuroblastoma cell line CHP-100},
journal={Journal of Neurophysiology},
year={1996},
volume={76},
number={2},
pages={764-769},
doi={10.1152/jn.1996.76.2.764},
note={cited By 32},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029813762&doi=10.1152%2fjn.1996.76.2.764&partnerID=40&md5=6062bad593f7a224da629e608419d38a},
affiliation={Department of Physiology, University of Oxford, Parks Road, Oxford OX1 3PT, United Kingdom},
abstract={1. The effects of hypoosmotic stress on cell volume and amino acid efflux were evaluated in the human neuroblastoma cell line CHP-100 with the Coulter Counter Multisizer and radiolabeled amino acid efflux, respectively. 2. CHP-100 cells swelled by ~35 ± 5% (means ± SE) when the osmolarity of the solution was decreased from 290 to 190 mOsm/kg H2O. The rapid swelling was followed by a biphasic regulatory volume decrease (RVD). 3. In cells loaded with 14C-taurine, hypoosmotic stress induced a 300 ± 22% (n = 23. P < 0.05) increase in taurine efflux compared with controls. This efflux was inhibited by the chloride channel blockers 5-nitro-2-(3-phenylpropylamino)- benzoic acid (NPPB). 4,4'-diisothio-cyanostilbene-2,2'-disulfonic acid (DIDS), niflumic acid and by the volume activated anion channel blocker tamoxifen. In addition, the swelling-activated taurine efflux was dependent upon extracellular calcium. 4. Similarly, in cells loaded with 14C-glycine, hypoosmotic stress significantly increased glycine efflux, which was also sensitive to NPPB. In contrast, efflux of 3H-glutamate was not significantly altered after hypoosmotic stress. 5. With the use of patch clamp recording techniques, Cl- channels were activated in cell attached patches after exposure to hypoosmotic solutions. 6. In nystatin perforated patches, permeability of the hypoosmotically activated anion channel was observed to be SCN > I > Br > Cl >> Glutamate. 7. It is concluded that in CHP-100 cells, anion channels are activated during hypoosmotic stress and these channels represent a pathway for efflux of amino acids.},
correspondence_address1={Basavappa, S.; Department of Physiology, University of Oxford, Parks Road, Oxford OX1 3PT, United Kingdom},
publisher={American Physiological Society},
issn={00223077},
coden={JONEA},
pubmed_id={8871197},
language={English},
abbrev_source_title={J. NEUROPHYSIOL.},
document_type={Article},
source={Scopus},
}
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The effects of hypoosmotic stress on cell volume and amino acid efflux were evaluated in the human neuroblastoma cell line CHP-100 with the Coulter Counter Multisizer and radiolabeled amino acid efflux, respectively. 2. CHP-100 cells swelled by 35 ± 5% (means ± SE) when the osmolarity of the solution was decreased from 290 to 190 mOsm/kg H2O. The rapid swelling was followed by a biphasic regulatory volume decrease (RVD). 3. In cells loaded with 14C-taurine, hypoosmotic stress induced a 300 ± 22% (n = 23. P < 0.05) increase in taurine efflux compared with controls. This efflux was inhibited by the chloride channel blockers 5-nitro-2-(3-phenylpropylamino)- benzoic acid (NPPB). 4,4'-diisothio-cyanostilbene-2,2'-disulfonic acid (DIDS), niflumic acid and by the volume activated anion channel blocker tamoxifen. In addition, the swelling-activated taurine efflux was dependent upon extracellular calcium. 4. Similarly, in cells loaded with 14C-glycine, hypoosmotic stress significantly increased glycine efflux, which was also sensitive to NPPB. In contrast, efflux of 3H-glutamate was not significantly altered after hypoosmotic stress. 5. With the use of patch clamp recording techniques, Cl- channels were activated in cell attached patches after exposure to hypoosmotic solutions. 6. In nystatin perforated patches, permeability of the hypoosmotically activated anion channel was observed to be SCN > I > Br > Cl >> Glutamate. 7. It is concluded that in CHP-100 cells, anion channels are activated during hypoosmotic stress and these channels represent a pathway for efflux of amino acids.","correspondence_address1":"Basavappa, S.; Department of Physiology, University of Oxford, Parks Road, Oxford OX1 3PT, United Kingdom","publisher":"American Physiological Society","issn":"00223077","coden":"JONEA","pubmed_id":"8871197","language":"English","abbrev_source_title":"J. 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