Modulation of ion channels in rod photoreceptors by nitric oxide

Kurenny, Dmitry E.; Moroz, Leonid L.; Turner, Ray W.; Sharkey, Keith A.; Barnes, Steven

doi:10.1016/0896-6273(94)90349-2

Cited by 184 publications

(116 citation statements)

References 44 publications

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“…The amplitude and voltage dependence of photoreceptor I Ca also are affected by a large number of extrinsic neuromodulators, including dopamine , somatostatin (Akopian et al, 2000), cannabinoids (Straiker and Sullivan, 2003;Fan and Yazulla, 2003), adenosine , nitric oxide (Kurenny et al, 1994), insulin (Stella et al, 2001), polyunsaturated fats (Vellani et al, 2000) and various ions. The list of substances that can modulate photoreceptor I Ca is probably not yet complete.…”

Section: Intrinsic Mechanisms That Regulate I Camentioning

confidence: 99%

“…Tyrosine kinase inhibitors also alter rod I Ca , suggesting that tyrosine phosphorylation might regulate channel activity (Stella et al, 2001). The ineffectiveness of cGMP analogs (Kurenny et al, 1994) argues against modulation by a cGMP-dependent protein kinase. The question of whether other enzymes such as PKC might regulate photoreceptor I Ca remains unanswered.…”

Section: Intrinsic Mechanisms That Regulate I Camentioning

confidence: 99%

“…Nitric oxide-Nitric oxide synthase is present throughout the retina, including horizontal and bipolar cell processes in the OPL and photoreceptor inner segments (e.g., Kurenni et al, 1995;Djamgoz et al, 1996;Blute et al, 1997;Cao and Eldred, 2001;Haverkamp and Eldred, 1998). In addition to stimulating cGMP synthesis and thus CNG channels, application of NO donors inhibit I Ca in salamander cones and produce a negative activation shift in the I Ca of salamander rods (Kurenny et al, 1994;Kurenny et al, 2004). Application of an nNOS inhibitor evokes a relative reduction in rod vs. cone inputs to horizontal cells (Kurenny et al, 2004), consistent with effects of NO donors on I Ca , suggesting that endogenously released NO inhibit cone inputs and stimulate rod inputs into horizontal cells.…”

Section: Insulin-insulin Inhibits Both the Erg B-wavementioning

confidence: 99%

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Synaptic transmission at retinal ribbon synapses

Heidelberger

Thoreson

Witkovsky

2005

Progress in Retinal and Eye Research

209

231

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The molecular organization of ribbon synapses in photoreceptors and ON bipolar cells is reviewed in relation to the process of neurotransmitter release. The interactions between ribbon synapseassociated proteins, synaptic vesicle fusion machinery and the voltage-gated calcium channels that gate transmitter release at ribbon synapses are discussed in relation to the process of synaptic vesicle exocytosis. We describe structural and mechanistic specializations that permit the ON bipolar cell to release transmitter at a much higher rate than the photoreceptor does, under in vivo conditions. We also consider the modulation of exocytosis at photoreceptor synapses, with an emphasis on the regulation of calcium channels.

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Section: Intrinsic Mechanisms That Regulate I Camentioning

confidence: 99%

Section: Intrinsic Mechanisms That Regulate I Camentioning

confidence: 99%

Section: Insulin-insulin Inhibits Both the Erg B-wavementioning

confidence: 99%

See 1 more Smart Citation

Synaptic transmission at retinal ribbon synapses

Heidelberger

Thoreson

Witkovsky

2005

Progress in Retinal and Eye Research

209

231

View full text Add to dashboard Cite

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“…There is also evidence from recent studies that NO is involved in several different processes in the vertebrate retina, for example it influences light responses of amphibian rods [4,5], it activates a soluble guanylyl cyclase and modulates a Ca 2+ channel and a voltage-independent conductance in inner segments of photoreceptors [6,7]. Effects of NO were also recorded on hemi-gap junction channels in horizontal cells [8], on cGMP-gated cation channels in retinal ganglion [9] and on-bipolar cells [10].…”

Section: Introductionmentioning

confidence: 99%

“…Most authors describe staining of subpopulations of amacrine and ganglion cells, but in some reports labelling of photoreceptor inner segments and cone outer segments was also demonstrated [6,7,17,19]. Additionally, NOS activities have been determined biochemically in crude retinal extracts [22,23] and in a photoreceptor preparation of outer segments attached to parts of the inner segment (OS-IS), where the NOS activity was almost *Corresponding author.…”

Section: Introductionmentioning

confidence: 99%

Purified retinal nitric oxide synthase enhances ADP‐ribosylation of rod outer segment proteins

Zoche

Koch

1995

FEBS Letters

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Nitric oxide synthase is present in different cell layers of vertebrate retina and seems to have neuromodulatory functions in the outer retina. The enzyme, when purified from a bovine retina extract, has an apparent molecular mass of 160 kDa and resembles the neuronal constitutive NOS type I with respect to CaZ+-calmodulin sensitivity, K m value and inhibition by analogues of L-arginine. Retinal NOS is present in a preparation of rod outer segments attached to parts of the inner segments, but not in pure outer segments. We describe the enhancement of specific ADP-ribosylation of outer segment proteins by purified retinal NOS.

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Developmental expression of nitric oxide synthase isoform I and III in chick retina

Goureau¹,

Régnier‐Ricard²,

Jonet³

et al. 1997

J. Neurosci. Res.

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During our studies on the multiple possible functions of nitric oxide (NO) in chick retinal development and physiology, we have demonstrated the presence and the activity of NO synthase (NOS-I and III) in certain neuronal populations (photoreceptors, amacrine cells in the inner nuclear and ganglion cells) and also in synaptic-rich regions in the developing chick retina. Both enzymes, detected by nicotinamide adenine dinucleotide phosphate (NADPH)-diaphorase, immunohistochemistry and Western blotting, appeared between embryonic days 6 and 12, and followed a spatial and temporal pattern of expression which correlated with the differentiation of the neuronal layers. Evaluation of the conversion of [3H]-labeled arginine to [3H]-citrulline, confirmed the presence of a calcium-dependent NOS activity in the cytosolic and particulate retinal extracts during the development. This pattern of NOS expression suggests that the regulated release of NO during key phases of development might be one mechanism involved in the regulation of retinal differentiation.

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Modulation of ion channels in rod photoreceptors by nitric oxide

Cited by 184 publications

References 44 publications

Synaptic transmission at retinal ribbon synapses

Synaptic transmission at retinal ribbon synapses

Purified retinal nitric oxide synthase enhances ADP‐ribosylation of rod outer segment proteins

Developmental expression of nitric oxide synthase isoform I and III in chick retina

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