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At least 973 records · Page 54Linked to original sources
PubMed2006

Characterization of semenogelin proteins in the human retina.

Semenogelin I and II are the major proteins present in semen coagulum. In the present study, semenogelin I and II were detected in human RPE lysates by proteomic analysis. We further analyzed the expression of these proteins in the retinal cells in vivo and in vitro. Western blots detected semenogelin I and II in both RPE and neural retina while the vitreous contained only SgII. Cryo and paraffin sections of human retina were processed for both immunofluorescence and DAB reaction with an antibody that recognizes both forms of semenogelin proteins. Retina and RPE total lysates were evaluated for the presence of these proteins and in a human RPE cell line (D407). Both proteins were detected by western blot in human RPE and in D407 cell lysates. Immunoreactivity was detected in the ganglion cell and photoreceptor layer of the retina. Our data support the expression of semenogelin I and II in the human retina in several different compartments. Further studies towards addressing the function of these proteins in the retina are in progress.

Aged↗
PubMed2005

Immunohistochemical localization of phospholipase D1 in the retina of pigs.

The expression of phospholipase D1 (PLD1) was examined in the retinas of pigs. Western blot analysis detected the expression of PLD1 in the retinas of 1-day-old piglets and showed that it was enhanced in the retinas of 2 years old adult pigs. Immunohistochemically, PLD1 was mainly immunostained in ganglion cell bodies in the ganglion cell layer, in some radial processes of Muller cells in the retinal layer and in the inner and outer segments of the rod and cone layer in newborn and adult pigs, but not in astrocytic bundles in nerve fiber layers. The immunoreactivity of PLD1 in the radial processes of Muller cells across the retinal layers was enhanced in adult pig retinas compared to those of newborn piglets. This was the first demonstration to show that PLD1 is constitutively expressed in the retina of pigs, implying that retinal PLD1 expression is enhanced in radial fibers of Muller cells with age. This finding suggests that PLD1 plays an important role in signal transduction of glial cells and neuronal cells in the retina.

Animals↗
PubMed2006

Immunohistochemical localization of heat shock protein 27 in the retina of pigs.

The expression of heat shock protein 27 (HSP27) was examined in the retinas of pigs. Western blot analysis detected the expression of HSP27 in the retinas of 1-day-old piglets and showed that it was enhanced in the retinas of 6-month-old adult pigs. Immunohistochemically, HSP27 immunostaining was seen mainly in ganglion cell bodies in the ganglion cell layer, and in some processes of astrocytes in the innermost nerve fiber layer. In 1-day-old piglets, HSP27 was detected weakly in the inner plexiform, inner nuclear cell, outer plexiform, and rod and cone layers. The HSP27 immunoreactivity across the retinal layers was enhanced in the retinas of 6-month-old pigs compared with newborn piglets. The HSP27 immunoreactivity in the radial processes of Müller cells was particularly prominent in adult pig retinas. In summary, this finding suggests that HSP27 plays an important role in signal transduction of glial cells and neuronal cells in the retina.

Animals↗
PubMed2006

Association of connexin36 and zonula occludens-1 with zonula occludens-2 and the transcription factor zonula occludens-1-associated nucleic acid-binding protein at neuronal gap junctions in rodent retina.

Most gap junctions between neurons in mammalian retina contain abundant connexin36, often in association with the scaffolding protein zonula occludens-1. We now investigate co-association of connexin36, zonula occludens-1, zonula occludens-2 and Y-box transcription factor 3 (zonula occludens-1-associated nucleic acid-binding protein) in mouse and rat retina. By immunoblotting, zonula occludens-1-associated nucleic acid-binding protein and zonula occludens-2 were both detected in retina, and zonula occludens-2 in retina was found to co-immunoprecipitate with connexin36. By immunofluorescence, the four proteins appeared as puncta distributed in the plexiform layers. In the inner plexiform layer, most connexin36-puncta were co-localized with zonula occludens-1, and many were co-localized with zonula occludens-1-associated nucleic acid-binding protein. Moreover, zonula occludens-1-associated nucleic acid-binding protein was often co-localized with zonula occludens-1. Nearly all zonula occludens-2-puncta were positive for connexin36, zonula occludens-1 and zonula occludens-1-associated nucleic acid-binding protein. In the outer plexiform layer, connexin36 was also often co-localized with zonula occludens-1-associated nucleic acid-binding protein. In connexin36 knockout mice, labeling of zonula occludens-1 was slightly reduced in the inner plexiform layer, zonula occludens-1-associated nucleic acid-binding protein was decreased in the outer plexiform layer, and both zonula occludens-1-associated nucleic acid-binding protein and zonula occludens-2 were markedly decreased in the inner sublamina of the inner plexiform layer, whereas zonula occludens-1, zonula occludens-2 and zonula occludens-1-associated nucleic acid-binding protein puncta persisted and remained co-localized in the outer sublamina of the inner plexiform layer. By freeze-fracture replica immunogold labeling, connexin36 was found to be co-localized with zonula occludens-2 within individual neuronal gap junctions. In addition, zonula occludens-1-associated nucleic acid-binding protein was abundant in a portion of ultrastructurally-defined gap junctions throughout the inner plexiform layer, and some of these junctions contained both connexin36 and zonula occludens-1-associated nucleic acid-binding protein. These distinct patterns of connexin36 association with zonula occludens-1, zonula occludens-2 and zonula occludens-1-associated nucleic acid-binding protein in different sublaminae of retina, and differential responses of these proteins to connexin36 gene deletion suggest differential regulatory and scaffolding roles of these gap junction accessory proteins. Further, the persistence of a subpopulation of zonula occludens-1/zonula occludens-2/zonula occludens-1-associated nucleic acid-binding protein co-localized puncta in the outer part of the inner plexiform layer of connexin36 knockout mice suggests close association of these proteins with other structures in retina, possibly including gap junctions composed of an as-yet-unidentified connexin.

Animals↗
PubMed2005

Redefining the limit of the outer retina in optical coherence tomography scans.

OBJECTIVE: A highly reflective layer seen in retinal optical coherence tomography (OCT) has been believed to correspond to the choriocapillaris (CHC) and retinal pigment epithelium (RPE). On gray-scale scans of OCT-2000, and on Stratus OCT, this layer by the outer retinal limit can be resolved into 2 distinct laminae. We analyzed these 2 laminae in normal and abnormal maculae to infer their anatomic correlate. DESIGN: Retrospective study. METHODS: Analysis of macular OCT scans was performed in 44 patients using OCT-2000, and in 39 patients using Stratus OCT. Thirty of these patients had no ocular disease, and their OCT was normal. The other 53 patients had several macular diseases of different etiologies. Both color and gray-scale images were analyzed. RESULTS: Macular OCT scans showed a double laminae at the level where the retina interfaces the RPE in normal subjects using both OCT-2000 and Stratus OCT. In 2-dimensional scans, this laminar structure appears as a double line. It is best distinguished on the Stratus OCT and gray-scale images of OCT-2000. This double line consisted of a thin inner line and a thicker outer line. Similar analysis in patients with macular pathology showed a discernible double line at the retina/RPE interface in at least part of the scan. However, in patients with macular hole, the area corresponding to the absent retina showed only a single line. The inner line component appeared to follow the contour of the retina. This phenomenon was also seen in eyes with neurosensory detachment secondary to central serous chorioretinopathy and other etiologies. In contrast, in macular pathologies where the outer retina did not lose contiguity with the RPE, such as in lamellar macular hole and in cystoid macular edema, the double line persisted. Software for retinal thickness measurements regularly place the outer limit of the retina at the internal aspect of the inner line, probably underestimating the retinal thickness by about 24 to 34 mum. CONCLUSIONS: A double laminar structure at the outer retina/RPE/CHC interface can be consistently distinguished on commercially available OCT of normal eyes. In eyes with macular pathology, OCT analysis of the inner lamina leads us to conclude it is most likely part of the neurosensory retina and not part of the RPE/CHC complex as previously thought.

Adult↗
PubMedDate not supplied

Photochemical damage of the retina.

Visual perception occurs when radiation with a wavelength between 400 and 760 nm reaches the retina. The retina has evolved to capture photons efficiently and initiate visual transduction. The retina, however, is vulnerable to damage by light, a vulnerability that has long been recognized. Photochemical damage has been widely studied, because it can cause retinal damage within the intensity range of natural light. Photochemical lesions are primarily located in the outer layers at the central region of the retina. Two classes of photochemical damage have been recognized: Class I damage, which is characterized by the rhodopsin action spectrum, is believed to be mediated by visual pigments, with the primary lesions located in the photoreceptors; whereas Class II damage is generally confined to the retinal pigment epithelium. The action spectrum peaks in the short wavelength region, providing the basis for the concept of blue light hazard. Several factors can modify the susceptibility of the retina to photochemical damage. Photochemical mechanisms, in particular mechanisms that arise from illumination with blue light, are responsible for solar retinitis and for iatrogenic retinal insult from ophthalmological instruments. Further, blue light may play a role in the pathogenesis of age-related macular degeneration. Laboratory studies have suggested that photochemical damage includes oxidative events. Retinal cells die by apoptosis in response to photic injury, and the process of cell death is operated by diverse damaging mechanisms. Modern molecular biology techniques help to study in-depth the basic mechanism of photochemical damage of the retina and to develop strategies of neuroprotection.

Animals↗
PubMed2004

Genetic analysis of the homeodomain transcription factor Chx10 in the retina using a novel multifunctional BAC transgenic mouse reporter.

Chx10 is a homeobox-containing transcription factor critical for progenitor cell proliferation and bipolar cell determination in the developing retina. Its expression in the retina has been reported to be restricted to these cell populations. To further understand Chx10 regulation and function, a multifunctional reporter construct consisting of GFP, alkaline phosphatase, and Cre recombinase was integrated into a BAC encoding Chx10. Stable lines of transgenic mice expressing this BAC were generated and analyzed. The reporter expression was faithful to the endogenous retinal Chx10 expression pattern and revealed a previously unappreciated locus of Chx10 expression in a subset of Müller glial cells. In addition, Chx10 reporter activity was identified in mature orJ-Chx10 mutant retinas, although these retinas lack Chx10-expressing bipolar cells. Reporter and molecular analysis showed that the reporter-expressing cells in the mutant had hallmarks of progenitor cells or partially differentiated Müller glial cells. These results strongly suggest that Chx10 promotes bipolar fate by affecting differentiation of late progenitor cells. Crosses of the Chx10 BAC reporter mice to R26R mice for fate-mapping experiments revealed that Chx10 reporter-expressing progenitor cells contribute to all mature cell types of the retina. These results demonstrate the utility of these lines for generation of mosaic or complete genetic manipulations of the retina.

Alkaline Phosphatase↗
PubMed2004

CYP26A1 and CYP26C1 cooperate in degrading retinoic acid within the equatorial retina during later eye development.

In the embryonic mouse retina, retinoic acid (RA) is unevenly distributed along the dorsoventral axis: RA-rich zones in dorsal and ventral retina are separated by a horizontal RA-poor stripe that contains the RA-inactivating enzyme CYP26A1. To explore the developmental role of this arrangement, we studied formation of the retina and its projections in Cyp26a1 null-mutant mice. Expression of several dorsoventral markers was not affected, indicating that CYP26A1 is not required for establishing the dorsoventral retina axis. Analysis of the mutation on a RA-reporter mouse background confirmed, as expected, that the RA-poor stripe was missing in the retina and its projections at the time when the optic axons first grow over the diencephalon. A day later, however, a gap appeared both in retina and retinofugal projections. As explanation, we found that CYP26C1, another RA-degrading enzyme, had emerged centrally in a narrower domain within the RA-poor stripe. While RA applications increased retinal Cyp26a1 expression, they slightly reduced Cyp26c1. These observations indicate that the two enzymes function independently. The safeguard of the RA-poor stripe by two distinct enzymes during later development points to a role in maturation of a significant functional feature like an area of higher visual acuity that develops at its location.

Animals↗
PubMed2004

2-[125I]-melatonin binding sites in the central nervous system and neural retina of the frog Rana perezi: regulation by light and temperature.

The objective of the present study is to test daily and seasonal changes in 2-[125I]-Melatonin ([125I]-Mel) binding in different brain areas and the retina of the frog Rana perezi as well as the possible effect of light and temperature on melatonin receptors. During the day-night cycle, binding of [125I]-Mel showed a clear rhythm in the optic tectum, diencephalon, telencephalon, and neural retina, the binding being higher in the light phase than in the dark phase. By contrast, melatonin receptors did not show any significant summer-winter differences in any of the four tissues studied. In the neural retina, but not in the brain, exposure of frogs to 24 h darkness for one week leads to significantly less [125I]-Mel binding than 24 h light exposure. This darkness-induced reduction of [125I]-Mel binding is not due to a desensitisation of binding sites by high melatonin levels. Thermal acclimation to either 5 or 22 degrees C for one month did not change the affinity (Kd) and density (Bmax) of [125I]-Mel binding sites either in the brain or the retina. All these results indicate that there is a daily rhythm in melatonin receptors in the frog brain and retina, and that the light/dark cycle can drive this rhythm in [125I]-Mel binding in the retina. Temperature apparently did not modify [125I]-Mel binding in frogs.

Animals↗
PubMed2005

Diurnal and circadian rhythms in melatonin synthesis in the turkey pineal gland and retina.

The pineal gland and retina of the turkey rhythmically produce melatonin. In birds kept under a daily light-dark (LD) illumination cycle melatonin concentrations in the pineal gland and retina were low during the light phase and high during the dark phase. A similar melatonin rhythm with high night-time values was also observed in the plasma. The pineal and retinal melatonin rhythms mirror oscillations in the activity of serotonin N-acetyltransferase (AANAT; the penultimate enzyme in the melatonin biosynthetic pathway). In contrast, in both the pineal gland and retina the activity of the enzyme hydroxyindole-O-methyltransferase (HIOMT) did not exhibit significant changes throughout the 24-h period. Acute exposure of turkeys to light at night dramatically decreased melatonin levels in the pineal gland, retina and plasma. The rhythms in AANAT activity and melatonin concentrations in the turkey pineal gland and retina were circadian in nature as they persisted under conditions of constant darkness (DD). Under DD, however, the amplitudes of AANAT and melatonin rhythms were significantly lower (by 50-80%) than those found under the LD cycle. The findings indicate that melatonin rhythmicity in the turkey pineal gland and retina is regulated both by light and the endogenous circadian clock. The rapid dampening of the rhythms under DD suggests that of these two regulatory factors, environmental light may be the primary stimulus in the maintenance of the high amplitude melatonin rhythms in the turkey.

Acetylserotonin O-Methyltransferase↗
PubMed2002

Vole retina is a target for gonadotropin-releasing hormone.

Gonadotropin-releasing hormone (GnRH) projections from the terminal nerve to the retina are common in fish, but have not been reported in mammals. However, GnRH fibers have been seen previously in the optic nerves (but not retinas) of rats and monkeys. Using prairie voles, we tested the hypotheses that (1) GnRH-immunoreactive (-ir) neurons project into the optic nerve and (2) the retina expresses GnRH receptor mRNA as determined by reverse transcription-polymerase chain reaction (RT-PCR) combined with Southern blotting. In both adult and postnatal-day-2 voles, GnRH-ir fibers were observed within the optic nerve. In adult voles, GnRH-ir fibers projected only a short distance into the optic nerve compared with the much longer length of projections in neonates. Fibers immunoreactive for GnRH were not seen in the retinas of neonates or adults. However, RT-PCR-Southern blotting demonstrated GnRH receptor expression in the retina of adult voles. This study supports the hypothesis that GnRH has the potential of modulating visual processing in the retina of mammals.

Animals↗
PubMed1998

Calretinin-immunoreactive elements in the retina and optic tectum of the frog, Rana esculenta.

The frog retina contains numerous 28 kDa calbindin positive elements in its every layer. At the same time, parvalbumin has been observed only in a few elements in the visual system of amphibian species, whilst calretinin immunoreactivity could be detected in salamander retina and the optic tectum of tench. However, the presence and distribution of calretinin have been described to date neither in the retina nor in the other parts of the visual system of anurans. Therefore, the aim of this study is to describe the calretinin immunoreactive elements in the retina and the optic tectum of the frog and to establish whether or not the expression of this calcium-binding protein is transmitter-related and/or cell type specific in these parts of the central nervous system. In the retina, numerous bipolar cells showed calretinin immunoreactivity. The axon terminals of the bipolar cells branched in both the OFF and ON sublayers of the inner plexiform layer. The few labeled amacrine cells were larger than 10 microns in diameter. Over 50% of the cells in the ganglion cell layer contained calretinin. The labeled cells in the ganglion cell layer were of usually 16-22 microns in diameter, although a few smaller cells were also seen. Accordingly, many optic fibers were also labeled. In colocalization experiments, gamma-aminobutyric acid and calretinin were found in partially overlapping amacrine cell populations, cells with the former marker being much more numerous. At the same time, all the gamma-aminobutyric acid positive bipolar cells also contained calretinin. Most of the calretinin positive neurons in the ganglion cell layer however were only single-labeled. Axons of ganglion cells terminated in B, C and F sublayers of layer 9 in the optic tectum. Local tectal neuron populations in layer 4, 6, 8 and 9 were also labeled and a few calretinin positive cells were detected also in layer 2. Approximately 10% of the tectal cells were found to be immunoreactive for calretinin. Layer 4 and 6 cells were mostly large pear-shaped neurons while cells in the 8th layer were small pear-shaped and ganglion cells labeled too. Coexistence of gamma-aminobutyric acid and calretinin was characteristic in cells of the upper tectal layers while they were not detected in neurons of deep layers of the tectum. After monocular enucleation, contralateral to the removed eye, calretinin-immunoreactivity disappeared almost completely from F sublayer and became less pronounced in sublayers B and C after 90 days. Calretinin-immunoreactivity remained mostly unchanged in local tectal cells. The results show that, although its function remains undetermined, calretinin is the major EF-hand calcium-binding protein in the frog retina and optic tectum.

Animals↗
PubMed1998

Centrifugal fibers are the only GABAergic structures of the retina of the larval sea lamprey: an immunocytochemical study.

The structures of the retina immunoreactive to GABA are described in larval lamprey. Although GABAergic cells develop early in the retinas of vertebrates, no GABA-immunoreactive perikarya were observed in the retina of lamprey larvae. The only GABA-immunoreactive structures were beaded fibers of the centrifugal system, which produced a dense plexus at the level of the optic fiber/inner plexiform layer in both the central (photoreceptor-bearing) and lateral (no-photoreceptor) parts of the retina. These fibers do not ascend toward the outer plexiform layer. Nerve fibers in the optic nerve and neuronal perikarya of the M5 nucleus of the mesencephalon, which is known to project to the retina, were also GABA-immunoreactive. The distribution of centrifugal fibers closely matches that of ganglion cells revealed by retrograde labelling with fluorescein-coupled dextran-amine, and the presence of biplexiform ganglion cells in larvae is confirmed. That the ganglion cells and the centrifugal fibers appears to be the only structures differentiated in the lateral retina of the larva suggests that the GABAergic centrifugal fibers may have a role, perhaps the neurotrophic maintenance of retinal ganglion cells, during the very long larval phase of lampreys.

Animals↗
PubMed2004

Age-related changes in the human retina.

BACKGROUND: In a previous study, scanning electron microscopy (SEM) showed age-related changes in the rat retina. We carried out a study to evaluate age-related changes in the human retina. METHODS: Samples of fresh retinal tissue obtained from younger (age 22 years or less) and older (age 66 years or more) donors were studied by means of traditional histologic methods and by SEM. Eight retinas were obtained from four donors whose corneas had been used for transplantation, and four retinas were obtained from four subjects whose eyes had been enucleated owing to injury. All morphologic results were subjected to quantitative analysis of images. The concentration of cytoplasmic (free) and structural (tissue-associated) protein in retinal tissue homogenates was determined by means of biochemical methods. RESULTS: There was a decrease in all features studied with the exception of structural protein concentration. The mean retinal thickness (and standard error of the mean) was 426 (34.2) microm in the younger subjects and 261 (18.9) microm in the older subjects. The mean numbers of ganglion cells (and standard error of the mean) were 413.5/mm2 (32.3/mm2) and 256.2/mm2 (26.8/mm2) respectively, of capillaries 3.6/mm2 (1.4/mm2) and 1.8/mm2 (1.2/mm2) respectively, of synaptic bodies 122.4 (4.9) conventional units (CU)/area observed and 38.5 (1.6) CU/area observed respectively, of cellular processes 82.3 (3.1) CU/area observed and 13.1 (1.5) CU/ area observed respectively, and of intercellular connections 36.4 (2.5) CU/area observed and 14.3 (1.4) CU/area observed respectively. The mean concentration of total protein per milligram of fresh tissue (and standard error of the mean) was 92.1 (1.8) microg in the younger subjects and 78.7 (1.3) microg in the older subjects; the corresponding values for cytoplasmic protein were 27.6 (1.3) microg and 11.8 (0.8) microg, and for structural protein, 64.4 (1.6) microg and 86.9 (1.4) microg. All differences between the younger and older subjects were significant (p < 0.001) with the exception of mean concentration of cytoplasmic and of structural protein. INTERPRETATION: The human retina undergoes specific changes with aging. SEM provides new morphometric information regarding age-related changes in photoreceptor cells, bipolar cells and ganglion cells that increases our understanding of this topic. Our results may be adopted as a model or as normal values when studying other changes that may occur in the human retina in pathological conditions.

Adolescent↗
PubMed2003

Expression and activation of STAT proteins during mouse retina development.

Cytokines and growth factors play important roles in mammalian ocular development and maintenance. Recent studies have indicated that some of these ligands can activate signal transducer and activator of transcription factors (STATs) and modulate gene transcription. The purpose of this study was to investigate the expression and activation of STAT proteins in the developing mouse retina. Anti-STAT and anti-phosphorylated STAT antibodies were used to detect the expression and activation of STATs in embryonic and postnatal neuronal retina, ciliary margin, and retinal pigment epithelium (RPE). In situ hybridization and Western blot were also employed. In embryonic stages, all STAT proteins were expressed in the neuronal retina in distinct cell populations at different embryonic stages. For example, Stat3 expression and activation gradually increased in the inner neuroblast layer and ciliary margin during development. In adult retina, Stat3 was detected in the inner nuclear layer and ganglion cells layers. Stat1 was strongly expressed in both outer and inner plexiform layers. Stat5a was clearly expressed in the outer/inner nuclear layer, the ganglion cell layer, and the inner plexiform layer. Strong expression of Stat3, Stat5a, and Stat6 was observed in the RPE. Activated Stat3 and Stat5a were found in the neural retina and the RPE. Distinct STAT proteins were present in different cell populations in neuronal retina and RPE suggesting multiple functions of STATs in mammalian eye development. Studies of STAT signal pathways in the eye may contribute to the understanding of molecular mechanisms in control of ocular development and pathogenesis.

Animals↗
PubMed1995

Vascular lesions in diabetes are distributed non-uniformly within the retina.

Microaneurysms, acellular capillaries and pericyte ghosts are characteristic of diabetic retinopathy, but it is not clear what causes these lesions or whether they are causally related to each other. The distribution of microaneurysms, acellular capillaries and pericyte ghosts has been evaluated in two animal models of diabetic retinopathy, diabetic dogs (n = 25) and galactose-fed dogs (n = 12). After 5 years of diabetes or galactosemia, retinas were divided into four quadrants at the optic disk, prepared by the trypsin-digest method, and the frequency of the lesions compared among the quadrants. Numbers of lesions were expressed relative to area of trypsin-digested retina examined or to total number of capillary cells examined. Microaneurysms and acellular capillaries were not uniformly distributed across the retina in diabetes or in galactosemia, both lesions being significantly (more than two-fold) more prevalent in the superior temporal retina than in the inferior nasal quadrant of retina. In contrast, the distribution of pericyte ghosts in these same eyes was not significantly different between the quadrants. These findings suggest that pericyte loss may not be sufficient to account for the development of microaneurysms and acellular (occluded) capillaries in diabetes, and raise a possibility that the lesions occur by different mechanisms. Currently available hypotheses regarding the pathogenesis of diabetic retinopathy fail to account for regional differences in the distribution of the vascular lesions within the same retina. Local factors within the eye apparently play an important role in the response of the retinal microvasculature to hyperglycemia.

Animals↗
PubMed1986

Alterations in the differentiation of chick retina caused by an intraocular injection of an alkaline phosphatase inhibitor.

Intense alkaline phosphatase (ALPase) activity has been localized in the outer plexiform layer of the developing chick retina. To elucidate the functional significance of this enzymatic activity, we have injected an ALPase inhibitor, levamisole, into embryonic eyes on either the 13th or 15th day of incubation. The retina was fixed between the 15th and 20th day of incubation and examined by electron microscopy. Levamisole injection on the 13th day caused various morphological alterations in retinal development, including the appearance of solitary photoreceptor cells in the subretinal space as well as folding of both the outer plexiform and outer nuclear layers. Pedicles of photoreceptor cells in the outer plexiform layer displayed rather smooth configurations with a reduced number of invaginations by post-synaptic neurites. The outer plexiform layer was thinned and the neuritic extensions in this layer appeared much less developed than in the control (PBS-injected) retina. Photoreceptor outer segments were seldom observed. Besides these alterations, layers of optic fibers and ganglion cells were also affected, as shown by evidence of degeneration in the ganglion cells and thinning of the nerve-fiber layer. Injection of levamisole into day 15 embryonic eyes exerted less influence on retinal development, but some photoreceptor cells were still found in the subretinal space. Some of these observations have been reported in the retinas of aged normal animals or in retinas with hereditary or induced retinal dystrophy. It is suggested that ALPase activity in the outer plexiform layer of the developing chick retina may be important for the onset of normal development of synapses in the outer plexiform layer and differentiation of the photoreceptor cells.

Alkaline Phosphatase↗
PubMed1987

Cholinergic neurons in the human retina.

Choline acetyltransferase (ChAT)-like immunoreactivity in the human retina can be demonstrated using a polyclonal antiserum to ChAT isolated from chick brain. There is a population of ChAT-like immunoreactive cells along both margins of the inner plexiform layer (IPL). The labeled cells have a morphology and position characteristic of the cholinergic amacrine- and displaced amacrine cells demonstrated by other workers in the mammalian retina. Non-immune rabbit serum or pre-absorbed antiserum, used in place of the primary antiserum, verified the specificity of the method. Human retinas can also be labeled with the fluorescent dye 4',6-diamidino-2-phenylindole (DAPI), which has been reported to bind selectively to DNA in the nuclei of cholinergic cells. The fluorescent cells are similar in morphology, position, and distribution to the cells which show ChAT-like immunoreactivity. In addition, we have localized the presence of [3H]choline and [3H]choline metabolites in freeze-dried, vapor-fixed tissue using 'dry' autoradiographic techniques. Incubation in [3H]choline was followed by either stimulation or inhibition of calcium-dependent transmitter release during a 1-hr 'chase' period. Using tissue incubated in a chase designed to retain labeled neurotransmitters, silver grains were concentrated over a population of cell bodies at either margin of the IPL (i.e. in the same position as putative ChAT-immunoreactive cells and DAPI-labeled cells). In contrast, tissue incubated in a chase designed to release labeled acetylcholine was labeled uniformly throughout the neural retina, with a heavy band of label over the pigment epithelium. Taken together, the results presented here indicate that three independent markers for cholinergic cells (i.e. ChAT immunoreactivity, DAPI binding, and choline uptake) are present in a population of cells in the human retina. This suggests that acetylcholine may be a neurotransmitter synthesized by amacrine and displaced amacrine cells in the retina.

Acetylcholine↗