Properties of a magnesium- or calcium-dependent adenosine triphosphatase from frog rod photoreceptor outer segment disks and its inhibition by illumination

Biochemistry ◽  
1972 ◽  
Vol 11 (25) ◽  
pp. 4679-4686 ◽  
Author(s):  
Thomas J. Ostwald ◽  
Joram Heller ◽  
Marianne Lawrence
Keyword(s):  
Adenosine Triphosphatase ◽  
Outer Segment ◽  
Rod Photoreceptor ◽  
Photoreceptor Outer Segment ◽  
Calcium Dependent

Reliability Assessment of a Rod Photoreceptor Outer Segment Grading System

2001 ◽  
Vol 72 (5) ◽  
pp. 573-579 ◽  
Author(s):  
Monica M Jablonski ◽  
Marshall J Graney ◽  
Stephen B Kritchevsky ◽  
Alessandro Iannaccone
Keyword(s):  
Outer Segment ◽  
Reliability Assessment ◽  
Grading System ◽  
Rod Photoreceptor ◽  
Photoreceptor Outer Segment

scholarly journals RPGRIP1 is essential for normal rod photoreceptor outer segment elaboration and morphogenesis

2009 ◽  
Vol 18 (22) ◽  
pp. 4329-4339 ◽  
Author(s):  
Jungyeon Won ◽  
Elaine Gifford ◽  
Richard S. Smith ◽  
Haiqing Yi ◽  
Paulo A. Ferreira ◽  
...  
Keyword(s):  
Outer Segment ◽  
Rod Photoreceptor ◽  
Photoreceptor Outer Segment

scholarly journals THE OSMOTIC BEHAVIOR OF ROD PHOTORECEPTOR OUTER SEGMENT DISCS

1971 ◽  
Vol 48 (3) ◽  
pp. 633-649 ◽  
Author(s):  
Joram Heller ◽  
Thomas J. Ostwald ◽  
Dean Bok
Keyword(s):  
Electron Microscopy ◽  
Outer Segment ◽  
Volume Measurement ◽  
Rod Photoreceptor ◽  
Photoreceptor Outer Segment ◽  
Bathing Medium ◽  
Intracellular Space ◽  
Disc Membrane ◽  
Osmotic Effects ◽  
Osmotic Behavior

The permeability properties of frog rod photoreceptor outer segment discs were investigated in preparations of purified, dark-adapted, outer segment fragments by the techniques of direct volume measurement and electron microscopy. Outer segment discs were found to swell and contract reversibly in response to changes in the osmotic pressure of the bathing medium in accordance with the Boyle-van't Hoff law. By use of the criterion of reversible osmotic swelling, the disc membrane is impermeable to Na+, K+, Mg+2, Ca+2, Cl-, and (PO4)-3 ions, whereas it is freely permeable to ammonium acetate. The disc membrane is impermeable to sucrose, although its osmotic behavior towards this substance is different from its behavior towards impermeable ions. Electron microscopy showed that the osmotic effects on the rod outer segment fragments represent changes in the intradiscal volume. Fixation with glutaraldehyde did not abolish the permeability properties of the disc membrane, and fixed membranes were still capable of osmotic volume changes. It is concluded from this study that the frog's rod photoreceptor outer segment discs are free-floating membranous organelles with an inside space separate and distinct from the photoreceptor intracellular space.

EM immunocytochemical localization of rhodopsin and IRBP during retinal development

1989 ◽  
Vol 47 ◽  
pp. 800-801
Author(s):  
R. J. Ulshafer ◽  
W.W. Hauswirth ◽  
A. van der Langerijt
Keyword(s):  
Outer Segment ◽  
Electrical Response ◽  
Pigment Epithelium ◽  
Retinal Pigment ◽  
Rabbit Serum ◽  
Subretinal Space ◽  
Rod Photoreceptor ◽  
Photoreceptor Outer Segment ◽  
Thin Sections ◽  
Specific Proteins

Two rod photoreceptor cell-specific proteins, rhodopsin and interphotoreceptor retinoid binding protein (IRBP), were localized during fetal development of the bovine retina using immuncicrytcichemistry. Rhodopsin is the light sensitive protein that, when activated, begins the process of transducing light energy to an electrical response. IRBP is a carrier protein that shuttles light-isomerized vitamin A (retinol) between the rod outer segment and the overlying retinal pigment epithelium where it is recycled to its light-sensitive form. Rhodopsin has been previously imimmocytochemically localized to rod (but not cone) photoreceptor outer segment membranes. IRBP has been localized to the subretinal space using immunocytochemistry.Retinas were obtained from fetuses at approximately 4, 5, 6, 7, and 8 months of gestation, fixed in 4% paraformaldehyde and 0.5% glutaraldehyde, and embedded at 40°C in epoxy resin. Thin sections were mounted on Ni grids and incubated with antibodies raised against the purified antigens: a mouse monoclonal anti-rhodopsin or a rabbit polyclonal anti-IRBP. A second antibody (Goat-anti-mouse or Goat-anti-rabbit) was conjugated with 15 nm Au particles and reacted with the sections. Control incubations were made using pre-immune rabbit serum and mouse monoclonals made against other tissue or bacterial sources.

scholarly journals Distribution of guanylate cyclase within photoreceptor outer segments

1996 ◽  
Vol 109 (7) ◽  
pp. 1803-1812
Author(s):  
M.A. Hallett ◽  
J.L. Delaat ◽  
K. Arikawa ◽  
C.L. Schlamp ◽  
F. Kong ◽  
...  
Keyword(s):  
Guanylate Cyclase ◽  
Actin Filaments ◽  
Outer Segment ◽  
Essential Role ◽  
Photoreceptor Cells ◽  
Rod Photoreceptor ◽  
Light Activation ◽  
Photoreceptor Outer Segment ◽  
Photoreceptor Outer Segments ◽  
Vertebrate Photoreceptor

Guanylate cyclases play an essential role in the recovery of vertebrate photoreceptor cells after light activation. Here, we have investigated how one such guanylate cyclase, RetGC-1, is distributed within light- and dark-adapted rod photoreceptor cells. Guanylate cyclase activity partitioned with the photoreceptor outer segment (OS) cytoskeleton in a light-sensitive manner. RetGC-1 was found to bind actin filaments in actin blot overlays, suggesting a mechanism for its association with the OS cytoskeleton. In retinal sections, this enzyme was immunodetected only in the OSs, where it appeared to be distributed throughout the disk membranes.

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