Identification of the sodium-calcium exchanger as the major ricin-binding glycoprotein of bovine rod outer segments and its localization to the plasma membrane

Biochemistry ◽  
1990 ◽  
Vol 29 (6) ◽  
pp. 1601-1607 ◽  
Author(s):  
Delyth M. Reid ◽  
Ute Friedel ◽  
Robert S. Molday ◽  
Neil J. Cook
Keyword(s):  
Plasma Membrane ◽  
Rod Outer Segments ◽  
Sodium Calcium Exchanger ◽  
Outer Segments ◽  
Sodium Calcium ◽  
Binding Glycoprotein

scholarly journals MEMBRANE CHARACTERISTICS AND OSMOTIC BEHAVIOR OF ISOLATED ROD OUTER SEGMENTS

1973 ◽  
Vol 56 (2) ◽  
pp. 389-398 ◽  
Author(s):  
Juan I. Korenbrot ◽  
Dennis T. Brown ◽  
Richard A. Cone
Keyword(s):  
Plasma Membrane ◽  
Outer Segment ◽  
Receptor Cell ◽  
Water Flux ◽  
Rod Outer Segments ◽  
Repeat Distance ◽  
Permeability Constant ◽  
Outer Segments ◽  
Length Reduction ◽  
Osmotic Behavior

Freshly isolated frog rod outer segments are sensitive osmometers which retain their photosensitivity; their osmotic behavior reveals essentially the same light-sensitive Na+ influx observed electrophysiologically in the intact receptor cell. Using appropriate osmotic conditions we have examined freeze-etch replicas of freshly isolated outer segments to identify the membrane which regulates the flow of water and ions. Under isosmotic conditions we find that the disc to disc repeat distance is almost exactly twice the thickness of a disc. This ratio appears to be the same in a variety of vertebrate rod outer segments and can be reliably measured in freeze-etch images. Under all our osmotic conditions the discs appear nearly collapsed. However, when the length of the outer segment is reduced by hyperosmotic shocks the discs move closer together. This markedly reduces the ratio of repeat distance to disc thickness since disc thickness remains essentially constant. Thus, the length reduction of isolated outer segments after hyperosmotic shocks primarily results from reduction of the extradisc volume. Since the discs are free floating and since they undergo negligibly small changes in volume, the plasma membrane alone must be primarily responsible for regulating the water flux and the light-sensitive Na+ influx in freshly isolated outer segments. On this basis we calculate, from the osmotic behavior, that the plasma membrane of frog rod outer segment has a Na+ permeability constant of about 2.8 x 10-6 cm/s and an osmotic permeability coefficient of greater than 2 x 10-3 cm/s.

scholarly journals Transmembrane Regulation of Intracellular Calcium by a Plasma Membrane Sodium/Calcium Exchanger in Mouse Ova1

1999 ◽  
Vol 60 (5) ◽  
pp. 1137-1143 ◽  
Author(s):  
J.R. Pepperell ◽  
K. Kommineni ◽  
S. Buradagunta ◽  
P.J.S. Smith ◽  
D.L. Keefe
Keyword(s):  
Plasma Membrane ◽  
Intracellular Calcium ◽  
Sodium Calcium Exchanger ◽  
Sodium Calcium

Stable Inhibition of Brain Synaptic Plasma Membrane Calcium ATPase in Rats Anesthetized with Halothane 

1995 ◽  
Vol 82 (1) ◽  
pp. 118-128 ◽  
Author(s):  
John J. Franks ◽  
Jean-Louis Horn ◽  
Piotr K. Janicki ◽  
Gurkeerat Singh
Keyword(s):  
Plasma Membrane ◽  
Hydrolytic Activity ◽  
Synaptic Plasma Membrane ◽  
Sodium Calcium Exchanger ◽  
Halothane Anesthesia ◽  
Treatment Groups ◽  
Sodium Calcium ◽  
Recovery From Anesthesia ◽  
Anesthetic Exposure

Background The authors recently showed that plasma membrane Ca(2+)-ATPase (PMCA) activity in cerebral synaptic plasma membrane (SPM) is diminished in a dose-related fashion during exposure in vitro to halothane, isoflurane, xenon, and nitrous oxide at clinically relevant partial pressures. They have now extended their work to in vivo studies, examining PMCA pumping in SPM obtained from control rats decapitated without anesthetic exposure, from rats decapitated during halothane anesthesia, and from rats decapitated after recovery from halothane anesthesia. Methods Three treatment groups were studied: 1) C, control rats that were decapitated without anesthetic exposure, 2) A, anesthetized rats exposed to 1 minimum effective dose (MED) for 20 min and then decapitated, and 3) R, rats exposed to 1 MED for 20 min and then decapitated after recovery from anesthesia, defined as beginning to groom. Plasma membrane Ca(2+)-ATPase pumping and Ca(2+)-dependent ATPase hydrolytic activity, as well as sodium-calcium exchanger activity and Na+-K+-ATPase hydrolytic activity, were assessed in cerebral SPM. In addition, halothane effect on smooth endoplasmic reticulum Ca(2+)-ATPase (SERCA) was examined. Results Plasma membrane Ca(2+)-ATPase transport of Ca2+ into SPM vesicles from anesthetized rats was reduced to 71% of control (P < 0.01) compared with 113% of control for the recovered group (NS). No depression by halothane of SERCA activity, sodium-calcium exchanger, or Na+-K+-ATPase activity was noted among the CAR treatment groups. Conclusions Plasma membrane Ca(2+)-ATPase is selectively and stably inhibited in cerebral SPM from rats killed while anesthetized with halothane, compared with rats killed without anesthesia or after recovery from anesthesia. The studies described in this report, in conjunction with previously reported inhibition of PMCA activity in vitro by a wide range of anesthetic agents, indicate a relationship between inhibition of PMCA and action of inhalational anesthetics.

Patch electrode recording of currents from the plasma membrane of rod outer segments of the frog

1982 ◽  
Vol 394 (S1) ◽  
pp. R45-R45 ◽  
Author(s):  
G. Nöll ◽  
E. Neher ◽  
Ch Baumann
Keyword(s):  
Plasma Membrane ◽  
Rod Outer Segments ◽  
Outer Segments ◽  
Electrode Recording

Letter to the editor: Squalene is Localized to the Plasma Membrane in Bovine Retinal Rod Outer Segments

1997 ◽  
Vol 64 (2) ◽  
pp. 279-282 ◽  
Author(s):  
STEVEN J. FLIESLER ◽  
KATHLEEN BOESZE-BATTAGLIA ◽  
ZOPHIA PAW ◽  
R.KENNEDY KELLER ◽  
ARLENE D. ALBERT
Keyword(s):  
Plasma Membrane ◽  
Rod Outer Segments ◽  
Outer Segments ◽  
Letter To The Editor ◽  
Retinal Rod ◽  
Retinal Rod 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.

Sign in / Sign up

Export Citation Format

Share Document