Disk membrane initiation and insertion are not required for axial disk displacement in Xenopus laevis rod outer segments

1998 ◽  
Vol 17 (1) ◽  
pp. 73-78 ◽  
Author(s):  
Michael W. Kaplan
Keyword(s):  
Xenopus Laevis ◽  
Rod Outer Segments ◽  
Disk Displacement ◽  
Outer Segments ◽  
Disk Membrane

scholarly journals Targeting of mouse guanylate cyclase 1 (Gucy2e) to Xenopus laevis rod outer segments

2011 ◽  
Vol 51 (21-22) ◽  
pp. 2304-2311 ◽  
Author(s):  
Sukanya Karan ◽  
Beatrice M. Tam ◽  
Orson L. Moritz ◽  
Wolfgang Baehr
Keyword(s):  
Xenopus Laevis ◽  
Guanylate Cyclase ◽  
Rod Outer Segments ◽  
Outer Segments

scholarly journals Localization of peripherin/rds in the disk membranes of cone and rod photoreceptors: relationship to disk membrane morphogenesis and retinal degeneration.

1992 ◽  
Vol 116 (3) ◽  
pp. 659-667 ◽  
Author(s):  
K Arikawa ◽  
L L Molday ◽  
R S Molday ◽  
D S Williams
Keyword(s):  
Plasma Membrane ◽  
Retinal Degeneration ◽  
Outer Segment ◽  
Photoreceptor Cells ◽  
Growth Stages ◽  
Rod Outer Segments ◽  
Rod Photoreceptor ◽  
Outer Segments ◽  
Disk Membrane ◽  
Membrane Morphogenesis

The outer segments of vertebrate rod photoreceptor cells consist of an ordered stack of membrane disks, which, except for a few nascent disks at the base of the outer segment, is surrounded by a separate plasma membrane. Previous studies indicate that the protein, peripherin or peripherin/rds, is localized along the rim of mature disks of rod outer segments. A mutation in the gene for this protein has been reported to be responsible for retinal degeneration in the rds mouse. In the present study, we have shown by immunogold labeling of rat and ground squirrel retinas that peripherin/rds is present in the disk rims of cone outer segments as well as rod outer segments. Additionally, in the basal regions of rod and cone outer segments, where disk morphogenesis occurs, we have found that the distribution of peripherin/rds is restricted to a region that is adjacent to the cilium. Extension of its distribution from the cilium coincides with the formation of the disk rim. These results support the model of disk membrane morphogenesis that predicts rim formation to be a second stage of growth, after the first stage in which the ciliary plasma membrane evaginates to form open nascent disks. The results also indicate how the proteins of the outer segment plasma membrane and the disk membranes are sorted into their separate domains: different sets of proteins may be incorporated into membrane outgrowths during different growth stages of disk morphogenesis. Finally, the presence of peripherin/rds protein in both cone and rod outer segment disks, together with the phenotype of the rds mouse, which is characterized by the failure of both rod and cone outer segment formation, suggest that the same rds gene is expressed in both types of photoreceptor cells.

scholarly journals Correlation of rhodopsin biogenesis with ultrastructural morphogenesis in the chick retina.

1975 ◽  
Vol 64 (1) ◽  
pp. 235-241 ◽  
Author(s):  
W T Mason ◽  
K J Bighouse
Keyword(s):  
Outer Segment ◽  
Receptor Cell ◽  
Rod Outer Segments ◽  
Membrane Biogenesis ◽  
Rod Outer Segment ◽  
Rods And Cones ◽  
Outer Segments ◽  
Chick Retina ◽  
Disk Membrane ◽  
Detergent Extraction

The developing chick retina from stages 39-45 has been examined by biochemical and electron microscope techniques. The levels of rhodopsin contained in the maturing chick retina were evaluated by detergent extraction and correlated with rod outer segment formation. It was found that the appearance of rhodopsin in significant levels preceded outer segment formation by at least 2 days, thus implying that rhodopsin is synthesized in the receptor cell inner segment and translocated to the outer limb when disk membrane biogenesis occurs. The level of rhodopsin continues to rise as the rod outer segment develops. Development of both rods and cones originates and proceeds most rapidly in the fundus or central region and proceeds toward the periphery. In general, rod outer segments were noted to develop far more rapidly than cone outer segments.

scholarly journals Surfaces of rod photoreceptor disk membranes: light-activated enzymes.

1982 ◽  
Vol 95 (2) ◽  
pp. 501-509 ◽  
Author(s):  
D J Roof ◽  
J I Korenbrot ◽  
J E Heuser
Keyword(s):  
Particle Density ◽  
Rod Outer Segments ◽  
Rod Photoreceptor ◽  
Outer Segments ◽  
Cytoplasmic Surface ◽  
Bright Flash ◽  
Large Particles ◽  
Disk Membrane ◽  
Rule Out ◽  
Number Of Particles

The light-activated GTP-binding protein (GBP) in toad rod outer segments has been located on the cytoplasmic surface (CS) of rod disk membranes by correlating biochemical results with images of quick-frozen, freeze-fractured, and deep-etched rod outer segments. This has been accomplished by selectively removing and replacing the 8-12-nm particles that are found on the CS of disk membranes, exactly in parallel with the GBP. In contrast, the large particles are not correlated with another major disk enzyme, the light-activated cGMP phosphodiesterase. We have been unable to visualize this protein. The surface density of large particles, one particle per eleven rhodopsins in isolated rod outer segments and one particle per nine rhodopsins in intact retina, correlates well with previous biochemical estimates of GBP numbers based on enzyme activity. After the identification of the large particles, we tested the effects of light on the density of particles on the surface of disk membranes in intact retinas. Retinas quick-frozen at various intervals after a bright flash of light show a modest increase (approximately 30%) in particle density by 10 s after the flash but no increase before 1 s. The number of particles on the disk membrane returns to dark levels between 1 and 10 min after the flash. The 1-s latency in the change of particle binding would appear to rule out this process as a mechanism for initiating phototransduction in the rod.

Electron Microscopy of Frog Photoreceptor Outer Segments after Fixation with Aldehydes

1974 ◽  
Vol 16 (1) ◽  
pp. 199-219
Author(s):  
G. J. JONES
Keyword(s):  
Electron Microscopy ◽  
Osmium Tetroxide ◽  
Ringer Solution ◽  
Rod Outer Segments ◽  
Buffer Concentration ◽  
Glutaraldehyde Fixation ◽  
Photoreceptor Outer Segments ◽  
Outer Segments ◽  
Cytoplasmic Material ◽  
Disk Membrane

The appearance of the outer segments of isolated retinae fixed with glutaraldehyde or formaldehyde alone, or with these aldehydes and postfixed with osmium tetroxide, is described. Rod outer segments and, to a lesser extent, cone outer segments of retinae fixed only with glutaraldehyde show shrinkage or swelling artifacts which are dependent on the fixative buffer concentration. The rod outer segments are most normal with a fixative phosphate buffer about 50% isotonic with retinal Ringer solution. The disks fixed with glutaraldehyde alone have a granular pentalaminar structure. At the edge of the rod disks, the loops formed by folding over of the disk membranes are seen after glutaraldehyde fixation alone to be filled with stainable material and the edges of adjacent loops to be in contact. The edge of the disk stack thus appears to be a more solid structure than previously thought, and it only partly survives osmium tetroxide treatment, even after glutaraldehyde fixation. Similarly, the arrangement of the disk membranes after glutaraldehyde fixation also appears to be weakened by postfixation with osmium tetroxide. For rod outer segments showing severe shrinkage after glutaraldehyde fixation alone, the interdisk clear spaces are lost and stainable cytoplasmic material, probably protein, is trapped between the disks. The disk membranes then appear as light lines on a dark background, since the central, unstained hydrophobic regions of each disk membrane become prominent.

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