Modification of leucine transport across bovine pigment epithelium by metabolic stress

1989 ◽  
Vol 257 (5) ◽  
pp. C940-C947 ◽  
Author(s):  
E. L. Pautler ◽  
C. Tengerdy ◽  
J. Beyer ◽  
D. Beezley
Keyword(s):  
Transport System ◽  
Opposite Direction ◽  
Competitive Inhibition ◽  
Pigment Epithelium ◽  
Retinal Pigment ◽  
Metabolic Stress ◽  
Temperature Sensitive ◽  
Sodium Dependence ◽  
L System ◽  
Leucine Transport

The transport of leucine in the apical-to-basal (retina to choroid) direction across the isolated bovine retinal pigment epithelium is mediated predominantly by the L amino transport system at low carrier (10 microns) concentrations. There is no evidence of an active or facilitated transport system operating in the opposite direction. The identification of the L system is based on the lack of sodium dependence, specific inhibition of leucine transport by 2-aminobicyclo-(2,2,1)-heptane-2-carboxylic acid (BCH), and the demonstration of trans-stimulation. Lysine, glutamate, and 2-methylaminoisobutyric acid (MeAIB) did not provide any competitive inhibition. Ouabain and iodoacetate were also ineffective in modifying leucine transport. The transport mediated by the L system was markedly temperature sensitive, whereas no temperature dependence was apparent in the transport of leucine in the basal-to-apical direction (choroid to retina). When treated with dinitrophenol (DNP), the transport of leucine in the apical-to-basal direction was greatly enhanced, but no effect was observed on the leucine movement in the opposite direction. Azide and rotenone had an effect similar to DNP, as did reducing the partial pressure of O2 to less than 40 Torr. The enhancement of transport appeared to be mediated by the activation of an ancillary system, since it was susceptible to different classes of metabolic and competitive inhibitors as well as the observed ionic dependency. After DNP treatment, the transport of leucine was inhibited by lysine and BCH, revealed a sodium dependence, and could be inhibited by iodoacetate. The characteristics of the enhanced transport appear to be similar to those of the recently described G system(s) of amino acid transport.

scholarly journals Metabolic features of mouse and human retinas: rods vs. cones, macula vs. periphery, retina vs. RPE

2020 ◽  
Author(s):  
Bo Li ◽  
Ting Zhang ◽  
Wei Liu ◽  
Yekai Wang ◽  
Rong Xu ◽  
...  
Keyword(s):  
Aerobic Glycolysis ◽  
Pigment Epithelium ◽  
Retinal Pigment ◽  
Lipid Synthesis ◽  
Metabolic Stress ◽  
Tca Cycle ◽  
High Energy ◽  
Metabolic Dysfunction ◽  
Metabolic Demand ◽  
Energy Demands

AbstractPhotoreceptors, especially cones, which are enriched in the human macula, have high energy demands, making them vulnerable to metabolic stress. Metabolic dysfunction of photoreceptors and their supporting retinal pigment epithelium (RPE) is an important underlying cause of degenerative retinal diseases. However, how cones and the macula support their exorbitant metabolic demand and communicate with RPE is unclear. By profiling metabolite uptake and release and analyzing metabolic genes, we have found cone-rich retinas and human macula share specific metabolic features with upregulated pathways in pyruvate metabolism, mitochondrial TCA cycle and lipid synthesis. Human neural retina and RPE have distinct but complementary metabolic features. Retinal metabolism centers on NADH production and neurotransmitter biosynthesis. The retina needs aspartate to sustain its aerobic glycolysis and mitochondrial metabolism. RPE metabolism is directed toward NADPH production and biosynthesis of acetyl-rich metabolites, serine and others. RPE consumes multiple nutrients, including proline, to produce metabolites for the retina.

scholarly journals Hypoxia-induced metabolic stress in retinal pigment epithelial cells is sufficient to induce photoreceptor degeneration

eLife ◽  
2016 ◽  
Vol 5 ◽  
Author(s):  
Toshihide Kurihara ◽  
Peter D Westenskow ◽  
Marin L Gantner ◽  
Yoshihiko Usui ◽  
Andrew Schultz ◽  
...  
Keyword(s):  
Pigment Epithelium ◽  
Retinal Pigment ◽  
Metabolic Stress ◽  
Retinal Pigment Epithelial Cells ◽  
Age Related Macular Degeneration ◽  
Photoreceptor Degeneration ◽  
Rpe Cells ◽  
Glucose And Lipid Metabolism ◽  
Age Related ◽  
Cellular Stresses

Photoreceptors are the most numerous and metabolically demanding cells in the retina. Their primary nutrient source is the choriocapillaris, and both the choriocapillaris and photoreceptors require trophic and functional support from retinal pigment epithelium (RPE) cells. Defects in RPE, photoreceptors, and the choriocapillaris are characteristic of age-related macular degeneration (AMD), a common vision-threatening disease. RPE dysfunction or death is a primary event in AMD, but the combination(s) of cellular stresses that affect the function and survival of RPE are incompletely understood. Here, using mouse models in which hypoxia can be genetically triggered in RPE, we show that hypoxia-induced metabolic stress alone leads to photoreceptor atrophy. Glucose and lipid metabolism are radically altered in hypoxic RPE cells; these changes impact nutrient availability for the sensory retina and promote progressive photoreceptor degeneration. Understanding the molecular pathways that control these responses may provide important clues about AMD pathogenesis and inform future therapies.

Apical sorting of influenza hemagglutinin by transcytosis in retinal pigment epithelium

1997 ◽  
Vol 110 (15) ◽  
pp. 1717-1727 ◽  
Author(s):  
V.L. Bonilha ◽  
A.D. Marmorstein ◽  
L. Cohen-Gould ◽  
E. Rodriguez-Boulan
Keyword(s):  
Plasma Membrane ◽  
Retinal Pigment Epithelium ◽  
Pigment Epithelium ◽  
Retinal Pigment ◽  
Subretinal Space ◽  
Temperature Sensitive ◽  
Permissive Temperature ◽  
Apical Surface ◽  
Rpe Cells

The retinal pigment epithelium is endowed with a unique distribution of certain plasma membrane proteins. Na+,K+-ATPase, for instance, is polarized to the apical surface of RPE, rather than to the basolateral surface as in most other epithelia. To study the sorting pathways of RPE cells, we used temperature sensitive mutants of influenza and vesicular stomatitis virus (VSV) to synchronize the transport of hemagglutinin (HA) and VSV G protein (VSV G) along the biosynthetic pathway of the RPE cell line RPE-J. After HA and VSV G accumulated in the trans-Golgi network of RPE-J cells kept at 20 degrees C, transfer to the permissive temperature (32 degrees C) resulted in the transport of both HA and VSV G to the basolateral plasma membrane. Later, while VSV G remained basolateral, HA progressively reversed its polarity, eventually becoming apical. Further analysis demonstrated that the reversal of HA polarity was due to transcytosis of HA from the basolateral to the apical surface of RPE-J cells. To determine whether HA followed a transcytotic route in RPE in vivo, influenza and VSV were injected into the subretinal space of rat eyes. Again, both HA and VSV G were initially observed at the basolateral surface of RPE cells. However, whereas VSV G remained there, HA progressively redistributed to the apical surface. These findings demonstrated that RPE cells use a transcytotic pathway for the targeting of at least some apical proteins to their destination.

High-resolution scanning electron microscopy (HRSEM) of mitochondria from various rat tissues

1988 ◽  
Vol 46 ◽  
pp. 14-15
Author(s):  
P.J. Lea ◽  
M.J. Hollenberg
Keyword(s):  
Electron Microscopy ◽  
Pigment Epithelium ◽  
Retinal Pigment ◽  
Rat Hepatocytes ◽  
Three Dimensions ◽  
Objective Lens ◽  
Rat Tissues ◽  
Thin Sections ◽  
Reconstruction Methods ◽  
Scanning Electron

Our current understanding of mitochondrial ultrastructure has been derived primarily from thin sections using transmission electron microscopy (TEM). This information has been extrapolated into three dimensions by artist's impressions (1) or serial sectioning techniques in combination with computer processing (2). The resolution of serial reconstruction methods is limited by section thickness whereas artist's impressions have obvious disadvantages.In contrast, the new techniques of HRSEM used in this study (3) offer the opportunity to view simultaneously both the internal and external structure of mitochondria directly in three dimensions and in detail.The tridimensional ultrastructure of mitochondria from rat hepatocytes, retinal (retinal pigment epithelium), renal (proximal convoluted tubule) and adrenal cortex cells were studied by HRSEM. The specimens were prepared by aldehyde-osmium fixation in combination with freeze cleavage followed by partial extraction of cytosol with a weak solution of osmium tetroxide (4). The specimens were examined with a Hitachi S-570 scanning electron microscope, resolution better than 30 nm, where the secondary electron detector is located in the column directly above the specimen inserted within the objective lens.

Ultrastructural Changes of Smoooth Endoplasmic Reticulum in the Retinal Pigment Epithelium by Choline Chloride

1972 ◽  
Vol 30 ◽  
pp. 58-59
Author(s):  
Kazushige Hirosawa ◽  
Eichi Yamada
Keyword(s):  
Endoplasmic Reticulum ◽  
Epithelial Cell ◽  
Smooth Endoplasmic Reticulum ◽  
Pigment Epithelium ◽  
Choline Chloride ◽  
Retinal Pigment ◽  
Ultrastructural Changes ◽  
Lower Vertebrate ◽  
Visual Cells ◽  
Pigment Epithelial

The pigment epithelium is located between the choriocapillary and the visual cells. The pigment epithelial cell is characterized by a large amount of the smooth endoplasmic reticulum (SER) in its cytoplasm. In addition, the pigment epithelial cell of some lower vertebrate has myeloid body as a specialized form of the SER. Generally, SER is supposed to work in the lipid metabolism. However, the functions of abundant SER and myeloid body in the pigment epithelial cell are still in question. This paper reports an attempt, to depict the functions of these organelles in the frog retina by administering one of phospholipid precursors.

High-voltage electron microscopy of subretinal scar formation

1992 ◽  
Vol 50 (1) ◽  
pp. 486-487
Author(s):  
G.E. Korte ◽  
M. Marko ◽  
G. Hageman
Keyword(s):  
Electron Microscopy ◽  
Monoclonal Antibody ◽  
Retinal Pigment Epithelium ◽  
Glial Cells ◽  
High Voltage ◽  
Pigment Epithelium ◽  
Retinal Pigment ◽  
Sodium Iodate ◽  
High Voltage Electron Microscopy ◽  
Voltage Electron

Sodium iodate iv. damages the retinal pigment epithelium (RPE) in rabbits. Where RPE does not regenerate (e.g., 1,2) Muller glial cells (MC) forma subretinal scar that replaces RPE. The MC response was studied by HVEM in 3D computer reconstructions of serial thick sections, made using the STEREC0N program (3), and the HVEM at the NYS Dept. of Health in Albany, NY. Tissue was processed for HVEM or immunofluorescence localization of a monoclonal antibody recognizing MG microvilli (4).

The photoreceptor cytoskeleton visualized

1992 ◽  
Vol 50 (1) ◽  
pp. 480-481
Author(s):  
Beth Burnside
Keyword(s):  
Outer Segment ◽  
Pigment Epithelium ◽  
Retinal Pigment ◽  
Cell Polarization ◽  
Synaptic Proteins ◽  
Cell Functions ◽  
Vertebrate Photoreceptor ◽  
Numerous Cell ◽  
Turn Over

The vertebrate photoreceptor provides a drammatic example of cell polarization. Specialized to carry out phototransduction at its distal end and to synapse with retinal interneurons at its proximal end, this long slender cell has a uniquely polarized morphology which is reflected in a similarly polarized cytoskeleton. Membranes bearing photopigment are localized in the outer segment, a modified sensory cilium. Sodium pumps which maintain the dark current critical to photosensory transduction are anchored along the inner segment plasma membrane between the outer segment and the nucleus.Proximal to the nucleus is a slender axon terminating in specialized invaginating synapses with other neurons of the retina. Though photoreceptor diameter is only 3-8u, its length from the tip of the outer segment to the synapse may be as great as 200μ. This peculiar linear cell morphology poses special logistical problems and has evoked interesting solutions for numerous cell functions. For example, the outer segment membranes turn over by means of a unique mechanism in which new disks are continuously added at the proximal base of the outer segment, while effete disks are discarded at the tip and phagocytosed by the retinal pigment epithelium. Outer segment proteins are synthesized in the Golgi near the nucleus and must be transported north through the inner segment to their sites of assembly into the outer segment, while synaptic proteins must be transported south through the axon to the synapse.The role of the cytoskeleton in photoreceptor motile processes is being intensely investigated in several laboratories.

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