ULTRACYTOCHEMICAL LOCALIZATION OF OUABAIN-SENSITIVE, POTASSIUM-DEPENDENT &lt;i&gt;P&lt;/i&gt;-NITROPHENYLPHOSPHATASE ACTIVITY IN THE GUINEA PIG RETINA

Ueno, Satoki; Mayahara, Hiroshi; Tsukahara, I; Ogawa, Kazuo

doi:10.1267/ahc.13.679

Cited by 27 publications

(9 citation statements)

References 85 publications

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“…This is also the most likely interpretation, since studies employing radiolabeled ouabain, which reports active enzyme, also detect highest levels oflabel in the upper portion of the inner segment region, with little or no label on the outer segments (Stirling and Sarthy, 1985;Stirling and Lee, 1980;Bok and Filerman, 1979). The results presented here are consistent with previous localizations of Na,K-ATPase which detected either the holoenzyme or the a-subunit at high concentrations in the inner segment, but these earlier studies either lacked reagents specific for the various isoforms or were conducted at the light microscopic level (Yazulla and Studholme, 1987;McGrail and Sweadner, 1986;Stirling and Sarthy, 1985;Stahl and Baskin, 1984;Stirling and Lee, 1980;Ueno et al, 1980 1988;Kashgarian et al, 1985;Baskin and Stahl, 1982;Louyard, 1980;Kyte, 1976 et al, 1990;Morrow et al, 1989;Nelson and Hammerton, 1989;Nelson and Veshnock, 1987 J Histochem…”

Section: Immunoblotssupporting

confidence: 91%

Co-localization and polarized distribution of Na,K-ATPase alpha 3 and beta 2 subunits in photoreceptor cells.

Schneider¹,

Shyjan²,

Levenson³

1991

J Histochem Cytochem.

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Na,K-ATPase plays a central role in the visual sensitivity of photoreceptors by driving the dark current of vision. The alpha 3 and beta 2 isoforms of Na,K-ATPase were previously shown to be the major alpha and beta subunit mRNAs expressed in photoreceptors. Here we compared the distribution of beta-subunits of the enzyme in the retina and kidney, using electron microscopic immunocytochemistry with specific antibodies against alpha 3, beta 1, and beta 2 isoforms as well as with an antibody (Ax2) that binds to alpha 2 and/or alpha 3 isoforms. Both the alpha 3 and beta 2 isoforms were localized to photoreceptor inner segments at highest labeling density between the base of the connecting cilium and the outer limiting membrane (OLM). Quantitative analysis of Ax2 antibody binding to alpha 3 revealed a significant decrease in labeling density below the OLM and above the base of the connecting cilium. Although the beta 2-subunit has been reported to have adhesive functions in glial cells in cerebellum, we detected beta 2 in the photoreceptor, a cell of neural origin, but not in the Mueller cell, the glial cell of the retina. Moreover, anti-beta 2 antibodies bound maximally to portions of photoreceptor cells not involved in cell-cell contact.

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Section: Immunoblotssupporting

confidence: 91%

Co-localization and polarized distribution of Na,K-ATPase alpha 3 and beta 2 subunits in photoreceptor cells.

Schneider¹,

Shyjan²,

Levenson³

1991

J Histochem Cytochem.

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“…Such processes may act as stores of Ca2+ or Na+ (Ellisman et al, 1980: rat Schwann cells;Gambetti et al, 1975: frog ependymoglia, human astrocytes;Krishnan and Singer, 1974: amphibian and reptilian Schwrann cells; SpaCek and Lieberman, 1980: rat oligodendrocytes and astrocytes; Wagner and Pilgrim, 1978: rat astrocytes). The membrane of such processes has rather high Na,K-pump activity (Ariyasu et al, 1985: mouse astrocytes and Schwann cells; Mrsulja et al, 1985: rat Schwann cells; Ueno et al, 1981: guinea pig Muller cells; Wood et al, 1977: fish astrocytes and oligodendrocytes; Reichenbach et al, 198813: rabbit Muller cells) and may be dominated by inward-rectifying K+ channels (Nilius and Reichenbach, 1988: rabbit Muller cells), although these were not yet found in cultured astrocytes. It is likely that receptors and uptake systems for neurotransmitters are also concentrated within this membrane.…”

Section: Classification and Determination Of Glial Processesmentioning

confidence: 99%

Attempt to classify glial cells by means of their process specialization using the rabbit retinal Müller cell as an example of cytotopographic specialization of glial cells

Reichenbach

1989

Glia

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The rabbit retinal Müller cell is one of the most widely studied glial cell types, and it has all forms of contacts that a glial cell can express, viz. 1) to a (ventricular) fluid space, 2) to a mesenchymal borderline (basal lamina), and 3) to neuronal compartments. This cell demonstrates the local adaptation of cell processes to the microenvironment with which they are in contact. Summarizing available data on Müller cells and other glial cell types, it is concluded that the structure with which the process is in contact determines the type of glial cell process that develops. The type I process has microvilli, desmosome-like junctions, and high Na+,K+-ATPase activity; this type of process is in direct contact with a fluid such as cerebrospinal fluid. The type II endfoot-bearing process contains gliofilaments and has a high K+ conductivity; this type of process is covered by a basal lamina and is in contact with mesenchyme. The type III sheath-bearing process insulates neuronal compartments and expresses suitable membrane properties for glia-neuronal communication. Since structurally similar processes have been shown to have similar physiological properties, a new systematic classification of glial cells is proposed, based on the presence or absence of defined types of cell processes. This approach is believed to provide new insights into the function of neuroglia in both the central and peripheral nervous systems, in vertebrates and invertebrates, and even during ontogenetic development.

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“…Recently, a new one-step cytochcmical method for both ATPases was developed [I, 14]. Instead of the cytochcmical detec tion of the Na-K-ATPase activity, the ouabain-sensi tive, K-dcpcndent p-nitrophenylphosphatase activity (K-NPPase) was examined: the K-NPPasc activity reflects the secondary déphosphorylation step of the Na-K-ATPase complex [for methodological details, see 17,18].…”

Section: Methodsmentioning

confidence: 99%

“…Concerning the results of several physiologi cal studies, it is widely accepted that in the dark phase a steady Na ion current flows between the outer segment and the proximal part of the photoreceptor cells; this current is caused by a continuous diffusion of Na ions through Na channels of the outer seg ment plasmalemma [17,18]. When the photon is absorbed by the visual pigment of the disk membrane, the steady dark current flow of Na ions is reduced, and a hyper polarization of the plasmalemma occurs [6], This event is considered to be the initial con dition for the electrical response of the photoreceptor after light perception.…”

Section: Introductionmentioning

confidence: 99%

Localization of ATPases in Retinal Receptor Cells

et al. 1984

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Ouabain-sensitive, K-dependent p-nitrophenylphosphatase (K-NPPase) activity of the Na-K-ATPase complex and the Ca-ATPase activity were studied ultracytochemically in the inner and outer segments of guinea pig photoreceptor cells by means of newly developed methods. The K-NPPase activity was demonstrated on the plasmalemma of the inner segments, whereas the Ca-ATPase activity was restricted to the matrix side of the inner membrane of the mitochondria which were accumulated in the inner segments. In contrast to the enzyme activities in the inner segments no such activity could be detected on the plasma and disk membranes of the outer segments. The functional meaning of the enzyme activities is discussed.

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ULTRACYTOCHEMICAL LOCALIZATION OF OUABAIN-SENSITIVE, POTASSIUM-DEPENDENT <i>P</i>-NITROPHENYLPHOSPHATASE ACTIVITY IN THE GUINEA PIG RETINA

Cited by 27 publications

References 85 publications

Co-localization and polarized distribution of Na,K-ATPase alpha 3 and beta 2 subunits in photoreceptor cells.

Co-localization and polarized distribution of Na,K-ATPase alpha 3 and beta 2 subunits in photoreceptor cells.

Attempt to classify glial cells by means of their process specialization using the rabbit retinal Müller cell as an example of cytotopographic specialization of glial cells

Localization of ATPases in Retinal Receptor Cells

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