Molecular cloning, primary structure, and orientation of the vertebrate photoreceptor cell protein peripherin in the rod outer segment disk membrane

Biochemistry ◽  
1990 ◽  
Vol 29 (19) ◽  
pp. 4691-4698 ◽  
Author(s):  
Gregory J. Connell ◽  
Robert S. Molday
1994 ◽  
Vol 302 (2) ◽  
pp. 455-461 ◽  
Author(s):  
R M Goraczniak ◽  
T Duda ◽  
A Sitaramayya ◽  
R K Sharma

In the vertebrate photoreceptor cell, rod outer segment (ROS) is the site of visual signal-transduction process, and a pivotal molecule that regulates this process is cyclic GMP. Cyclic GMP controls the cationic conductance into the ROS, and light causes a decrease in the conductance by activating hydrolysis of the cyclic nucleotide. The identity of the granylate cyclase (ROS-GC) that synthesizes this pool of cyclic GMP is unknown. We now report the cloning, expression and functional characterization of a DNA from bovine retina that encodes ROS-GC.


1979 ◽  
Vol 29 (4) ◽  
pp. 661-670 ◽  
Author(s):  
E. A. Dratz ◽  
G. P. Miljanich ◽  
P. P. Nemes ◽  
J. E. Gaw ◽  
S. Schwartz

1983 ◽  
Vol 8 (4) ◽  
pp. 128-131 ◽  
Author(s):  
Edward A. Dratz ◽  
Paul A. Hargrave

1996 ◽  
Vol 16 (4) ◽  
pp. 289-297 ◽  
Author(s):  
Kathleen Boesze-Battaglia ◽  
Arlene D. Albert ◽  
James S. Frye ◽  
Philip L. Yeagle

The outer segment portion of photoreceptor rod cells is composed of a stacked array of disk membranes. Newly formed disks are found at the base of the rod outer segment (ROS) and are relatively high in membrane cholesterol. Older disks are found at the apical tip of the ROS and are low in membrane cholesterol. Disk membranes were separated based on their membrane cholesterol content and the extent of membrane protein phosphorylation determined. Light induced phosphorylation of ROS disk membrane proteins was investigated using magic angle spinning31P NMR. When intact rod outer segment preparations were stimulated by light, in the presence of endogenously available kinases, membrane proteins located in disks at the base of the ROS were more heavily phosphorylated than those at the tip. SDS-gel electrophoresis of the phosphorylated disk membranes subpopulations identified a phosphoprotein species with a molecular weight of approximately 68–72 kDa that was more heavily phosphorylated in newly formed disks than in old disks. The identity of this phosphoprotein is presently under investigation. When the phosphorylation reaction was carried out in isolated disk membrane preparations with exogenously added co-factors and kinases, there was no preferential protein phosphorylation. Taken collectively, these results suggest that within the ROS there is a protein phosphorylation gradient that maybe indicative of co-factor or kinase heterogeneity.


1975 ◽  
Vol 64 (1) ◽  
pp. 235-241 ◽  
Author(s):  
W T Mason ◽  
K J Bighouse

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.


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