Na+-Ca2+-K+ Currents Measured in Insect Cells Transfected with the Retinal Cone or Rod Na+-Ca2+-K+ Exchanger cDNA
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The recently cloned retinal cone Na(+)-Ca(2+)-K(+) exchanger (NCKX) was expressed in cultured insect cells, and whole-cell patch clamp was used to measure transmembrane currents generated by this transcript and compare them with currents generated by retinal rod NCKX or by a deletion mutant rod NCKX from which the two large hydrophilic loops were removed. We have characterized the ionic currents generated by both the forward (Ca(2+) extrusion) and reverse (Ca(2+) influx) modes of all three NCKX proteins. Reverse NCKX exchange generated outward current that required the simultaneous presence of both external Ca(2+) and external K(+). Forward NCKX exchange carried inward current with Na(+), but not with Li(+) in the bath solution. The cation dependencies of the three NCKX tested (external K(+), external Na(+), internal Ca(2+)) were very similar to each other and to those reported previously for the in situ rod NCKX. These findings provide the first electrophysiological characterization of cone NCKX and the first electrophysiological characterization of potassium-dependent Na(+)-Ca(+) exchangers in heterologous systems. Our results demonstrate the feasibility of combining heterologous expression and biophysical measurements for detailed NCKX structure/function studies.
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All other NCKX proteins traffic to the plasma membrane where they remove Ca2+ from the cytoplasm to the extracellular space.
“These data, supporting an intracellular, partial TGN localization, are surprising since all other NCKX proteins have been shown to traffic to the plasma membrane where they operate to remove Ca 2ϩ from the cytoplasm to the extracellular space (26 -28).”
From SLC24A5 encodes a trans-Golgi network protein with potassium-dependent sodium-calcium exchange activity that regulates human epidermal melanogenesis (2008) · cites this paper as [27]
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ISOFORM 2 (NCKX2) IN THE DEVELOPMENT OF FOCAL CEREBRAL ISCHEMIA
Ciclo, X. (2008)
- Authors
- Sheng, J.-Z., Prinsen, C. F. M., Clark, R. B., Giles, W. R., & Schnetkamp, P. P. M.
- Affiliations
- University of Calgary (CA)
- Corresponding author
- Schnetkamp, P.P.M.
- Venue
- Biophysical Journal
- Publisher
- Elsevier BV
- Published
- 2000-10
- Volume
- 79
- Issue
- 4
- Pages
- 1945-1953
- ISSN
- 0006-3495 (ISSN-L)
- PMC
- PMC1301085
- OpenAlex
- W1991413812
- Cited by
- 30
- References
- 26
- Citations by year
- 2020: 1 · 2017: 1 · 2015: 1 · 2014: 1 · 2013: 2 · 2012: 3
- FWCI
- 0.72
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biophysical Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
- Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
- Keywords
- cone photoreceptors, rod photoreceptors, calcium efflux, calcium influx, ion selectivity, structure-function analysis
- MeSH terms
- Amino Acid Sequence, Animals, Biophysics, Carrier Proteins, Cattle, Cell Line, Chickens, Dolphins, Humans, Insecta, Molecular Sequence Data, Transfection, Ion Transport, Retinal Rod Photoreceptor Cells, Retinal Cone Photoreceptor Cells, DNA, Complementary, Patch-Clamp Techniques, Sodium-Calcium Exchanger, Biophysical Phenomena
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