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  • 1
    Electronic Resource
    Electronic Resource
    Ultracytochemical localization of Ca++-ATPase activity in the paraphyseal epithelial cells of the frog, Rana esculenta (1984)
    Springer
    Cell & tissue research 235 (1984), S. 3-11 
    Details
    ISSN: 1432-0878
    Keywords: Ca++-ATPase ; Mg++-ATPase ; Paraphysis cerebri(frog) ; Ca++-transport ; Ultracytochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Ca++-ATPase activity was studied ultracytochemically (cf. Ando et al. 1981) in the paraphysis cerebri of the frog. An intense reaction was demonstrated on the plasmalemma of the microvilli at the apical pole of paraphyseal cells; in contrast, the basolateral plasmalemma showed only a slight staining. In addition, mitochondria, gap junctions, cilia, and cytoplasmic elements (e.g., microfilaments) displayed Ca++-ATPase activity. Variation of the Ca++-concentration in the incubation medium from 0.1 mM to 100 mM altered the Ca++-ATPase activity of the cell organelles. The substitution of Ca-by Mg-ions resulted in a conspicuous decrease in the enzyme activity, especially on the apical plasmalemma. Ca++-ATPase activity is claimed to be involved in a number of extra-and intracellular functions. In comparison to the epithelium of the adjacent choroid plexus the paraphyseal epithelial cell is thought to be a principal Ca-ion regulator of the cerebrospinal fluid in frogs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00213716
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  • 2
    Electronic Resource
    Electronic Resource
    Localization and function of cyclic guanosine monophosphate-phosphodiesterase activity in the retinal rods of the rat by means of a newly developed cytochemical method (1984)
    Springer
    Cell & tissue research 238 (1984), S. 453-457 
    Details
    ISSN: 1432-0878
    Keywords: Cyclic guanosine monophosphate-phosphodiesterase (cGMP-PDEase) ; New cytochemical method ; Retina ; Rods, outer segments ; Light perception ; 5′GMPase ; Rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Cyclic guanosine monophosphate-phosphodiesterase (cGMP-PDEase) activity was studied histo- and cytochemically in the retinal rods of the rat with the use of a newly developed technique. Intense activity of cGMP-PDEase was evenly distributed over the outer segments of the rods. Reaction product was observed on the plasmalemma and on the disk membranes of the outer segments. A weak reaction product occurred also on the plasmalemma of the inner segments; however, no precipitate was found in the perinuclear and synaptic portions of the rod cells. The enzyme activity was strongly inhibited by 2 mM theophilline and by 2 mM 3-isobutyl-1-methylxanthine (IBMX). To confirm the specificity of this new cGMP-PDEase method, the localization of 5′nucleotidase (5′GMPase) was also studied. In contrast to the activity of cGMP-PDEase, the activity of 5′GMPase was distributed on the plasma membrane of the photoreceptor cells extending over a wide range from the synaptic endings in the outer plexiform layer to the tip of the outer segments.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00219860
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  • 3
    Electronic Resource
    Electronic Resource
    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 (1983)
    Springer
    Cell & tissue research 234 (1983), S. 225-230 
    Details
    ISSN: 1432-0878
    Keywords: Guanosine triphosphatase (GTPase) ; Retina (rat) ; Rod outer segment ; Light perception
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00217416
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