Retinal ganglion cells express a cGMP-gated cation conductance activatable by nitric oxide donors

Iqbal Ahmad; Trese Leinders-Zufall; Jeffery D. Kocsis; Gordon M. Shepherd; Frank Zufall; Colin J. Barnstable

doi:10.1016/0896-6273(94)90160-0

Retinal ganglion cells express a cGMP-gated cation conductance activatable by nitric oxide donors

Iqbal Ahmad
, Trese Leinders-Zufall
, Jeffery D. Kocsis
, Gordon M. Shepherd
, Frank Zufall
, Colin J. Barnstable

Research output: Contribution to journal › Article › peer-review

232 Scopus citations

Abstract

We have identified a putative cGMP-gated cation conductance in rat retinal ganglion cells. Both in situ hybridization and polymerase chain reaction amplification detected transcripts in ganglion cells that were highly homologous to the cGMP-gated cation channel expressed in rod photoreceptors. Whole-cell patch-clamp recordings detected a current stimulated by cGMP due to activation of nonselective cation channels. This current had a reversal potential near 0 mV, showed some outward rectification, and could be blocked by Cd²⁺. The current could also be activated by a phosphodiesterase inhibitor and the nitric oxide donors sodium nitroprusside and S-nitrosocysteine. We propose that nitric oxide released from an identified subpopulation of amacrine cells may activate this channel to modulate ganglion cell activity.

Original language	English (US)
Pages (from-to)	155-165
Number of pages	11
Journal	Neuron
Volume	12
Issue number	1
DOIs	https://doi.org/10.1016/0896-6273(94)90160-0
State	Published - Jan 1994

All Science Journal Classification (ASJC) codes

General Neuroscience

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10.1016/0896-6273(94)90160-0

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@article{2d8ea82cff0842b19fb140d8b854f4e1,

title = "Retinal ganglion cells express a cGMP-gated cation conductance activatable by nitric oxide donors",

abstract = "We have identified a putative cGMP-gated cation conductance in rat retinal ganglion cells. Both in situ hybridization and polymerase chain reaction amplification detected transcripts in ganglion cells that were highly homologous to the cGMP-gated cation channel expressed in rod photoreceptors. Whole-cell patch-clamp recordings detected a current stimulated by cGMP due to activation of nonselective cation channels. This current had a reversal potential near 0 mV, showed some outward rectification, and could be blocked by Cd2+. The current could also be activated by a phosphodiesterase inhibitor and the nitric oxide donors sodium nitroprusside and S-nitrosocysteine. We propose that nitric oxide released from an identified subpopulation of amacrine cells may activate this channel to modulate ganglion cell activity.",

author = "Iqbal Ahmad and Trese Leinders-Zufall and Kocsis, \{Jeffery D.\} and Shepherd, \{Gordon M.\} and Frank Zufall and Barnstable, \{Colin J.\}",

note = "Funding Information: The first two authors made equal contributions to this study. We thank Dean Cummins and Shigeto Kitano for help in early stages of this project, Adrienne La Rue for technical assistance, and Bob Brown for photography. This work was supported by grants from the National Institutes of Health, a Browne-Coxe Postdoctoral Fellowship (I. A.), and the Darien Lions. C. J. B. is a Jules and Doris Stein Research to Prevent Blindness Professor.",

year = "1994",

month = jan,

doi = "10.1016/0896-6273(94)90160-0",

language = "English (US)",

volume = "12",

pages = "155--165",

journal = "Neuron",

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publisher = "Cell Press",

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TY - JOUR

T1 - Retinal ganglion cells express a cGMP-gated cation conductance activatable by nitric oxide donors

AU - Ahmad, Iqbal

AU - Leinders-Zufall, Trese

AU - Kocsis, Jeffery D.

AU - Shepherd, Gordon M.

AU - Zufall, Frank

AU - Barnstable, Colin J.

N1 - Funding Information: The first two authors made equal contributions to this study. We thank Dean Cummins and Shigeto Kitano for help in early stages of this project, Adrienne La Rue for technical assistance, and Bob Brown for photography. This work was supported by grants from the National Institutes of Health, a Browne-Coxe Postdoctoral Fellowship (I. A.), and the Darien Lions. C. J. B. is a Jules and Doris Stein Research to Prevent Blindness Professor.

PY - 1994/1

Y1 - 1994/1

N2 - We have identified a putative cGMP-gated cation conductance in rat retinal ganglion cells. Both in situ hybridization and polymerase chain reaction amplification detected transcripts in ganglion cells that were highly homologous to the cGMP-gated cation channel expressed in rod photoreceptors. Whole-cell patch-clamp recordings detected a current stimulated by cGMP due to activation of nonselective cation channels. This current had a reversal potential near 0 mV, showed some outward rectification, and could be blocked by Cd2+. The current could also be activated by a phosphodiesterase inhibitor and the nitric oxide donors sodium nitroprusside and S-nitrosocysteine. We propose that nitric oxide released from an identified subpopulation of amacrine cells may activate this channel to modulate ganglion cell activity.

AB - We have identified a putative cGMP-gated cation conductance in rat retinal ganglion cells. Both in situ hybridization and polymerase chain reaction amplification detected transcripts in ganglion cells that were highly homologous to the cGMP-gated cation channel expressed in rod photoreceptors. Whole-cell patch-clamp recordings detected a current stimulated by cGMP due to activation of nonselective cation channels. This current had a reversal potential near 0 mV, showed some outward rectification, and could be blocked by Cd2+. The current could also be activated by a phosphodiesterase inhibitor and the nitric oxide donors sodium nitroprusside and S-nitrosocysteine. We propose that nitric oxide released from an identified subpopulation of amacrine cells may activate this channel to modulate ganglion cell activity.

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DO - 10.1016/0896-6273(94)90160-0

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AN - SCOPUS:0028178804

SN - 0896-6273

VL - 12

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EP - 165

JO - Neuron

JF - Neuron

IS - 1

ER -

Retinal ganglion cells express a cGMP-gated cation conductance activatable by nitric oxide donors

Abstract

All Science Journal Classification (ASJC) codes

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