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Histo- and Cytochemical Demonstration of Guanosine Triphosphatase Activity in the Outer Segments of Rods in the Rat Retina by Means of a Newly Developed Method

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Journal Cell Tissue Res
Date 1983 Jan 1
PMID 6139170
Citations 2
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Abstract

Guanosine triphosphatase (GTPase) activity was studied histo- and cytochemically in the rod outer segments of the rat retina by means of a newly developed method. Differences in the distribution pattern of the enzyme activity exist within the outer segment: the activity is more intense at the tip of the rod outer segments near the pigment epithelium than in their proximal portion. Ultracytochemically, the new procedure reveals the reaction product of GTPase activity partly (i) on the extradisk membrane side and (ii) on the disk membranes. This result is in contrast to the cytochemical localization of guanylate cyclase (GCLase), an enzyme also localized at the tip of the rod outer segments: GCLase activity is restricted to the intradisk membrane area of the rod outer segments. The functional role of GTPase activity in the outer segments of rods is discussed.

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Ultracytochemical study of Ca++-ATPase and K+-NPPase activities in retinal photoreceptors of the guinea pig.

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PMID: 6207924 DOI: 10.1007/BF00228432.


Localization and function of cyclic guanosine monophosphate-phosphodiesterase activity in the retinal rods of the rat by means of a newly developed cytochemical method.

Ueno S, Bambauer H, Umar H, Ueck M Cell Tissue Res. 1984; 238(3):453-7.

PMID: 6084553 DOI: 10.1007/BF00219860.

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