Rod cell

Rod cells are photoreceptor cells in the retina of the eye that can function in less intense light than the other type of visual photoreceptor, cone cells. Rods are usually found concentrated at the outer edges of the retina and are used in peripheral vision. On average, there are approximately 92 million rod cells in the human retina.[1] Rod cells are more sensitive than cone cells and are almost entirely responsible for night vision. However, rods have little role in color vision, which is the main reason why colors are much less apparent in dim light, and not at all at night.

Rod cell
Retina-diagram
Cross section of the retina. Rods are visible at far right.
Details
LocationRetina
ShapeRod-shaped
FunctionLow-light photoreceptor
NeurotransmitterGlutamate
Presynaptic connectionsNone
Postsynaptic connectionsBipolar cells and horizontal cells
Identifiers
NeuroLex IDnlx_cell_100212
THH3.11.08.3.01030
Anatomical terms of neuroanatomy

Structure

Rods are a little longer and leaner than cones but have the same basic structure. Opsin-containing disks lie at the end of the cell adjacent to the retinal pigment epithelium, which in turn is attached to the inside of the eye ball. The stacked-disc structure of the detector portion of the cell allows for very high efficiency. Rods are much more common than cones, with about 100 million rod cells compared to 7 million cone cells.[2]

Like cones, rod cells have a synaptic terminal, an inner segment, and an outer segment. The synaptic terminal forms a synapse with another neuron, usually a bipolar cell or a horizontal cell. The inner and outer segments are connected by a cilium,[3] which lines the distal segment.[4] The inner segment contains organelles and the cell's nucleus, while the rod outer segment (abbreviated to ROS), which is pointed toward the back of the eye, contains the light-absorbing materials.[3]

A human rod cell is about 2 microns in diameter and 100 microns long.[5] Rods are not all morphologically the same; in mice, rods close to the outer plexiform synaptic layer display a reduced length due to a shortened synaptic terminal.[6]

Function

Photoreception

Cone2
Anatomy of a Rod Cell[7]

In vertebrates, activation of a photoreceptor cell is a hyperpolarization (inhibition) of the cell. When they are not being stimulated, such as in the dark, rod cells and cone cells depolarize and release a neurotransmitter spontaneously. This neurotransmitter hyperpolarizes the bipolar cell. Bipolar cells exist between photoreceptors and ganglion cells and act to transmit signals from the photoreceptors to the ganglion cells. As a result of the bipolar cell being hyperpolarized, it does not release its transmitter at the bipolar-ganglion synapse and the synapse is not excited.

Activation of photopigments by light sends a signal by hyperpolarizing the rod cell, leading to the rod cell not sending its neurotransmitter, which leads to the bipolar cell then releasing its transmitter at the bipolar-ganglion synapse and exciting the synapse.

Depolarization of rod cells (causing release of their neurotransmitter) occurs because in the dark, cells have a relatively high concentration of cyclic guanosine 3'-5' monophosphate (cGMP), which opens ion channels (largely sodium channels, though calcium can enter through these channels as well). The positive charges of the ions that enter the cell down its electrochemical gradient change the cell's membrane potential, cause depolarization, and lead to the release of the neurotransmitter glutamate. Glutamate can depolarize some neurons and hyperpolarize others, allowing photoreceptors to interact in an antagonistic manner.

When light hits photoreceptive pigments within the photoreceptor cell, the pigment changes shape. The pigment, called rhodopsin (conopsin is found in cone cells) comprises a large protein called opsin (situated in the plasma membrane), attached to which is a covalently bound prosthetic group: an organic molecule called retinal (a derivative of vitamin A). The retinal exists in the 11-cis-retinal form when in the dark, and stimulation by light causes its structure to change to all-trans-retinal. This structural change causes an increased affinity for the regulatory protein called transducin (a type of G protein). Upon binding to rhodopsin, the alpha subunit of the G protein replaces a molecule of GDP with a molecule of GTP and becomes activated. This replacement causes the alpha subunit of the G protein to dissociate from the beta and gamma subunits of the G protein. As a result, the alpha subunit is now free to bind to the cGMP phosphodiesterase (an effector protein).[8] The alpha subunit interacts with the inhibitory PDE gamma subunits and prevents them from blocking catalytic sites on the alpha and beta subunits of PDE, leading to the activation of cGMP phosphodiesterase, which hydrolyzes cGMP (the second messenger), breaking it down into 5'-GMP.[9] Reduction in cGMP allows the ion channels to close, preventing the influx of positive ions, hyperpolarizing the cell, and stopping the release of the neurotransmitter glutamate (Kandel et al., 2000). Though cone cells primarily use the neurotransmitter substance acetylcholine, rod cells use a variety. The entire process by which light initiates a sensory response is called visual phototransduction.

Activation of a single unit of rhodopsin, the photosensitive pigment in rods, can lead to a large reaction in the cell because the signal is amplified. Once activated, rhodopsin can activate hundreds of transducin molecules, each of which in turn activates a phosphodiesterase molecule, which can break down over a thousand cGMP molecules per second (Kandel et al. 2000). Thus, rods can have a large response to a small amount of light.

As the retinal component of rhodopsin is derived from vitamin A, a deficiency of vitamin A causes a deficit in the pigment needed by rod cells. Consequently, fewer rod cells are able to sufficiently respond in darker conditions, and as the cone cells are poorly adapted for sight in the dark, blindness can result. This is night-blindness.

Reversion to the resting state

Rods make use of three inhibitory mechanisms (negative feedback mechanisms) to allow a rapid revert to the resting state after a flash of light.

Firstly, there exists a rhodopsin kinase (RK) which would phosphorylate the cytosolic tail of the activated rhodopsin on the multiple serines, partially inhibiting the activation of transducin. Also, an inhibitory protein - arrestin then binds to the phosphorylated rhodopsins to further inhibit the rhodopsin's activity.

While arrestin shuts off rhodopsin, an RGS protein (functioning as a GTPase-activating proteins(GAPs)) drives the transducin (G-protein) into an "off" state by increasing the rate of hydrolysis of the bounded GTP to GDP.

Also as the cGMP sensitive channels allow not only the influx of sodium ions, but also calcium ions, with the decrease in concentration of cGMP, cGMP sensitive channels are then closed and reducing the normal influx of calcium ions. The decrease in the concentration of calcium ions stimulates the calcium ion-sensitive proteins, which would then activate the guanylyl cyclase to replenish the cGMP, rapidly restoring its original concentration. The restoration opens the cGMP sensitive channels and causes a depolarization of the plasma membrane.[10]

Desensitization

When the rods are exposed to a high concentration of photons for a prolonged period, they become desensitized (adapted) to the environment.

As rhodopsin is phosphorylated by rhodopsin kinase (a member of the GPCR kinases(GRKs)), it binds with high affinity to the arrestin. The bound arrestin can contribute to the desensitization process in at least two ways. First, it prevents the interaction between the G protein and the activated receptor. Second, it serves as an adaptor protein to aid the receptor to the clathrin-dependent endocytosis machinery (to induce receptor-mediated endocytosis).[10]

Sensitivity

A rod cell is sensitive enough to respond to a single photon of light[11] and is about 100 times more sensitive to a single photon than cones. Since rods require less light to function than cones, they are the primary source of visual information at night (scotopic vision). Cone cells, on the other hand, require tens to hundreds of photons to become activated. Additionally, multiple rod cells converge on a single interneuron, collecting and amplifying the signals. However, this convergence comes at a cost to visual acuity (or image resolution) because the pooled information from multiple cells is less distinct than it would be if the visual system received information from each rod cell individually.

Cone-response-en
Wavelength responsiveness of short (S), medium (M) and long (L) wavelength cones compared to that of rods (R).[12]

Rod cells also respond slower to light than cones and the stimuli they receive are added over roughly 100 milliseconds. While this makes rods more sensitive to smaller amounts of light, it also means that their ability to sense temporal changes, such as quickly changing images, is less accurate than that of cones.[3]

Experiments by George Wald and others showed that rods are most sensitive to wavelengths of light around 498 nm (green-blue), and insensitive to wavelengths longer than about 640 nm (red). This is responsible for the Purkinje effect: as intensity dims at twilight, the rods take over, and before color disappears completely, peak sensitivity of vision shifts towards the rods' peak sensitivity (blue-green).

References

  1. ^ Curcio, C. A.; Sloan, K. R.; et al. (1990). "Human photoreceptor topography". The Journal of Comparative Neurology. 292 (4): 497–523. doi:10.1002/cne.902920402. PMID 2324310.
  2. ^ "The Rods and Cones of the Human Eye". hyperphysics.phy-astr.gsu.edu. Retrieved 25 April 2016.
  3. ^ a b c Kandel E.R., Schwartz, J.H., Jessell, T.M. (2000). Principles of Neural Science, 4th ed., pp. 507–513. McGraw-Hill, New York.
  4. ^ "Photoreception" McGraw-Hill Encyclopedia of Science & Technology, vol. 13, p. 460, 2007
  5. ^ "How Big Is a Photoreceptor". Cell Biology By The Numbers. Ron Milo & Rob Philips.
  6. ^ Li, Shuai; Mitchell, Joe; Briggs, Deidrie J.; Young, Jaime K.; Long, Samuel S.; Fuerst, Peter G. (1 March 2016). "Morphological Diversity of the Rod Spherule: A Study of Serially Reconstructed Electron Micrographs". PLOS ONE. 11 (3): e0150024. doi:10.1371/journal.pone.0150024. PMC 4773090. PMID 26930660. Retrieved 25 January 2017 – via PLoS Journals.
  7. ^ Human Physiology and Mechanisms of Disease by Arthur C. Guyton (1992) p. 373
  8. ^ "G Proteins". rcn.com. Retrieved 25 January 2017.
  9. ^ Muradov, Khakim G.; Artemyev, Nikolai O. (10 March 2000). "Loss of the Effector Function in a Transducin-α Mutant Associated with Nougaret Night Blindness". J. Biol. Chem. 275 (10): 6969–6974. doi:10.1074/jbc.275.10.6969. Retrieved 25 January 2017 – via www.jbc.org.
  10. ^ a b Bruce Alberts, Alexander Johnson, Julian Lewis, Martin Raff, Keith Roberts, Peter Walter (2008). Molecular Biology of The Cell, 5th ed., pp.919-921. Garland Science.
  11. ^ Okawa, Haruhisa; Alapakkam P. Sampath. "Optimization of Single-Photon Response Transmission at the Rod-to-Rod Bipolar Synapse". Physiology. Int. Union Physiol. Sci./Am. Physiol. Soc. 22 (4): 279–286. doi:10.1152/physiol.00007.2007.
  12. ^ Bowmaker J.K. and Dartnall H.J.A. (1980). "Visual pigments of rods and cones in a human retina". J. Physiol. 298: 501–511. doi:10.1113/jphysiol.1980.sp013097. PMC 1279132. PMID 7359434.

External links

Absolute threshold

In neuroscience and psychophysics, an absolute threshold was originally defined as the lowest level of a stimulus – light, sound, touch, etc. – that an organism could detect. Under the influence of signal detection theory, absolute threshold has been redefined as the level at which a stimulus will be detected a specified percentage (often 50%) of the time. The absolute threshold can be influenced by several different factors, such as the subject's motivations and expectations, cognitive processes, and whether the subject is adapted to the stimulus.The absolute threshold can be compared to the difference threshold, which is the measure of how different two stimuli must be for the subject to notice that they are not the same.

BBS4

Bardet-Biedl syndrome 4 is a protein that in humans is encoded by the BBS4 gene.This gene encodes a protein which contains tetratricopeptide repeats (TPR), similar to O-linked N-acetylglucosamine transferase. Mutations in this gene have been observed in patients with Bardet-Biedl syndrome type 4. The encoded protein may play a role in pigmentary retinopathy, obesity, polydactyly, renal malformation and mental retardation.

Congenital stationary night blindness

Congenital stationary night blindness (CSNB) is a rare non-progressive retinal disorder. It has two forms, complete, also known as type-1 (CSNB1), and incomplete, also known as type-2 (CSNB2), depending on severity. In the complete form (CSNB1), there is no measurable rod cell response to light, whereas this response is measurable in the incomplete form. Patients with this disorder have difficulty adapting to low light situations due to impaired photoreceptor transmission. These patients also often have reduced visual acuity, myopia, nystagmus and strabismus. CSNB1 can be caused by mutations in various genes, including NYX, which encode proteins involved in retinal synapse formation or synaptic transmission. CSNB2 is caused by mutations in the gene CACNA1F, which encodes a voltage-gated calcium channel CaV1.4.

Congenital stationary night blindness (CSNB) can be inherited in an X-linked, autosomal dominant, or autosomal recessive pattern, depending on the genes involved.

Depolarization

In biology, depolarization is a change within a cell, during which the cell undergoes a shift in electric charge distribution, resulting in less negative charge inside the cell. Depolarization is essential to the function of many cells, communication between cells, and the overall physiology of an organism.

Most cells in higher organisms maintain an internal environment that is negatively charged relative to the cell's exterior. This difference in charge is called the cell's membrane potential. In the process of depolarization, the negative internal charge of the cell temporarily becomes more positive (less negative). This shift from a negative to a more positive membrane potential occurs during several processes, including an action potential. During an action potential, the depolarization is so large that the potential difference across the cell membrane briefly reverses polarity, with the inside of the cell becoming positively charged.

The change in charge typically occurs due to an influx of sodium ions into a cell, although it can be mediated by an influx of any kind of cation or efflux of any kind of anion. The opposite of a depolarization is called a hyperpolarization.

Usage of the term "depolarization" in biology differs from its use in physics. In physics it refers instead to situations in which any form of polarity changes to a value of zero.

Depolarization is sometimes referred to as "hypopolarization".

Dua's layer

Dua's layer, according to a 2013 paper by Harminder Singh Dua's group at the University of Nottingham, is a layer of the cornea that had not been detected previously. It is hypothetically 15 micrometres (0.59 mils) thick, the fourth caudal layer, and located between the corneal stroma and Descemet's membrane. Despite its thinness, the layer is very strong and impervious to air. It is strong enough to withstand up to 2 bars (200 kPa) of pressure. While some scientists welcomed the announcement, other scientists cautioned that time was needed for other researchers to confirm the discovery and its significance. Others have met the claim "with incredulity". The choice of the name Dua's Layer has also been criticized.

Eigengrau

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Flexner–Wintersteiner rosette

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NRL (gene)

Neural retina-specific leucine zipper protein is a protein that in humans is encoded by the NRL gene.

Ora serrata

The ora serrata is the serrated junction between the retina and the ciliary body. This junction marks the transition from the simple, non-photosensitive area of the ciliary body to the complex, multi-layered, photosensitive region of the retina. The pigmented layer is continuous over choroid, ciliary body and iris while the nervous layer terminates just before the ciliary body. This point is the ora serrata. In this region the pigmented epithelium of the retina transitions into the outer pigmented epithelium of the ciliary body and the inner portion of the retina transitions into the non-pigmented epithelium of the cilia. In animals in which the region does not have a serrated appearance, it is called the ora ciliaris retinae.

Outer plexiform layer

The outer plexiform layer (external plexiform layer) is a layer of neuronal synapses in the retina of the eye. It consists of a dense network of synapses between dendrites of horizontal cells from the inner nuclear layer, and photoreceptor cell inner segments from the outer nuclear layer. It is much thinner than the inner plexiform layer, where amacrine cells synapse with retinal ganglion cells.The synapses in the outer plexiform layer are between the rod cell endings or cone cell branched foot plates and horizontal cells. Unlike in most systems, rod and cone cells release neurotransmitters when not receiving a light signal.

PDE6A

Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha is an enzyme that in humans is encoded by the PDE6A gene.PDE6A encodes the cyclic-GMP (cGMP) specific phosphodiesterase 6A alpha subunit, expressed in cells of the retinal rod outer segment. The phosphodiesterase 6 holoenzyme is a heterotrimer composed of an alpha, beta, and two gamma subunits.cGMP is an important regulator of rod cell membrane current, and its dynamic concentration is established by phosphodiesterase 6A cGMP hydrolysis and gunylate cyclase cGMP synthesis. Mutations in PDE6A have been identified as one cause of autosomal recessive retinitis pigmentosa.

PDE6D

Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta is an enzyme that in humans is encoded by the PDE6D gene. PDE6D was originally identified as a fourth subunit of rod cell-specific cGMP phosphodiesterase (PDE) (EC 3.1.4.35). The precise function of PDE delta subunit in the rod specific GMP-PDE complex is unclear. In addition, PDE delta subunit is not confined to photoreceptor cells but is widely distributed in different tissues. PDE delta subunit is thought to be a specific soluble transport factor for certain prenylated proteins and Arl2-GTP a regulator of PDE-mediated transport.

Pars plana

The pars plana (Latin: flat portion) is part of the ciliary body in the uvea (or vascular tunic), the middle layer of the three layers that comprise the eye.

It is about 4 mm long, located near the junction of the iris and sclera, and is scalloped in appearance.

The pars plana may not have a function in the post-fetal period, making this a good site of entry for ophthalmic surgery of the posterior segment of eyeball; this surgery is known as pars plana vitrectomy.

Progressive retinal atrophy

Progressive retinal atrophy (PRA) is a group of genetic diseases seen in certain breeds of dogs and, more rarely, cats. Similar to retinitis pigmentosa in humans, it is characterized by the bilateral degeneration of the retina, causing progressive vision loss culminating in blindness. The condition in nearly all breeds is inherited as an autosomal recessive trait, with the exception of the Siberian Husky (inherited as an X chromosome linked trait) and the Bullmastiff (inherited as an autosomal dominant trait). There is no treatment.

RAR-related orphan receptor beta

RAR-related orphan receptor beta (ROR-beta), also known as NR1F2 (nuclear receptor subfamily 1, group F, member 2) is a nuclear receptor that in humans is encoded by the RORB gene.

RP1

Oxygen-regulated protein 1 also known as retinitis pigmentosa 1 protein (RP1) is a protein that in humans is encoded by the RP1 gene.

SOX8

Transcription factor SOX-8 is a protein that in humans is encoded by the SOX8 gene.This gene encodes a member of the SOX (SRY-related HMG-box) family of transcription factors involved in the regulation of embryonic development and in the determination of the cell fate. The encoded protein may act as a transcriptional activator after forming a protein complex with other proteins. This protein may be involved in brain development and function. Haploinsufficiency for this protein may contribute to the mental retardation found in haemoglobin H-related mental retardation (ATR-16 syndrome).

SOX9

Transcription factor SOX-9 is a protein that in humans is encoded by the SOX9 gene.

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