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      Chloride- and Bicarbonate-Stimulated ATPase Activity in Bovine Lens Epithelium

      ,

      Ophthalmic Research

      S. Karger AG

      Bovine lens capsule, Bovine lens epithelium, ATPase activity, Anion-activated

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          Abstract

          An anion-stimulated, ouabain-insensitive Mg<sup>2+</sup>ATPase activity has been found in fresh homogenates prepared from capsules and epithelia of bovine lenses. Approximately equal activity was observed in the presence of HCO<sub>3</sub><sup>––</sup> or of Cl<sup>––</sup>. The stimulation of each anion obeys saturation kinetics, with an optimum at approximately 20 m M Cl<sup>––</sup> or HCO<sub>3</sub><sup>––</sup>. Whereas SCN<sup>––</sup> inhibits anion-activated ATPase in most other tissues, it failed to inhibit Cl<sup>––</sup> or HCO<sub>3</sub><sup>––</sup>stimulated ATPase activity in the bovine lens. On the contrary, SCN<sup>––</sup> proved a potent activator of the enzyme. However, in keeping with other tissues, OCN<sup>––</sup> and the diuretic drugs, furosemide and ethacrynic acid are inhibitory. ATP is the primary substrate for the enzyme, which also shows some activity on GTP, ITP, and even ADP. Little Na<sup>+</sup>/ K<sup>+</sup>-dependent ATPase activity was observed in the fresh homogenate, but it increased in lyophilized preparations. In contrast, the lyophilized preparations showed no anion-dependent ATPase activity. It is postulated that active bicarbonate ion transport in the lens may be mediated by this anion-dependent ATPase.

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          Author and article information

          Journal
          ORE
          Ophthalmic Res
          10.1159/issn.0030-3747
          Ophthalmic Research
          S. Karger AG
          0030-3747
          1423-0259
          1983
          1983
          04 December 2009
          : 15
          : 2
          : 90-98
          Affiliations
          Institute of Experimental Ophthalmology and Institute of Cytology, University of Bonn, FRG
          Article
          265240 Ophthalmic Res 1983;15:90–98
          10.1159/000265240
          6224119
          © 1983 S. Karger AG, Basel

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          Page count
          Pages: 9
          Categories
          Original Paper

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