1978
DOI: 10.1016/0014-4835(78)90031-3
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Evidence for two sodium pumps in the crystalline lens of the rabbit eye

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Cited by 33 publications
(14 citation statements)
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“…Like high extracellular K þ , ouabain has also been shown to inhibit ion and water fluxes measured at the surface of the lens, 21,57,58 and to increase the Na þ content of the lens, but unlike high extracellular K þ it does not, at least initially, reduce to zero either the lens potential, 59 or hydrostatic pressure gradients. 18 In this present study, we show that blocking the circulation system with ouabain also has a different effect on the water gradient than that observed for lenses incubated in AAH-High K þ (Fig.…”
Section: Discussionmentioning
confidence: 99%
“…Like high extracellular K þ , ouabain has also been shown to inhibit ion and water fluxes measured at the surface of the lens, 21,57,58 and to increase the Na þ content of the lens, but unlike high extracellular K þ it does not, at least initially, reduce to zero either the lens potential, 59 or hydrostatic pressure gradients. 18 In this present study, we show that blocking the circulation system with ouabain also has a different effect on the water gradient than that observed for lenses incubated in AAH-High K þ (Fig.…”
Section: Discussionmentioning
confidence: 99%
“…PD is the potential difference between the inside of the lens and the bath ing medium. It is determined by the outer membranes of the lens and is spatially uni form in the surface cells [4,5], PDj , 0 is the PD at which the concentration and electrical gradients are in balance and the current equals zero. It is the potassium equilibrium potential of the system.…”
mentioning
confidence: 99%
“…Also, although anion-dependent ATPases do not generally show activity on ADP, some cation-dependent ATPases have been shown to do so. This is the case for the cal cium-activated ATPase present in basolateral plasma membranes of duodenal epithelia [Ghijsen et al, 1980], The anion-stimulated ATPase activity in the bovine lens is not inhibited by the pres ence of 0.2 mM ouabain and is thus distinct from Na+/K +-ATPase already known to exist in the lens [Bonting et al, 1963;Neville et al, 1978]. The enzyme shows some similarities to the CP/HCOj-activatable ATPase known to exist in other tissues, but also differs strongly from these in being stimulated rather than inhibited by SCN- DeRenzis and Bornancin, 1977;Humphreys and Chou, 1979;Komnick et al, 1980;Bornancin et al, 1980;Gassner and Komnick, 1981a, b].…”
Section: Discussionmentioning
confidence: 99%
“…For example, two clearly differ ent sodium-potassium-activated ATPases have been characterized in the lens, one located in the epithelium and one located in the cortical fibers [Neville et al, 1978]. Each of these cation-dependent ATPases, as well as lens cation transport, is affected by oua bain; and it is quite clear that cation move ment in and out of the lens is an energydependent process [Rae, 1979;Paterson, 1972], In constrast, most researchers have come to the conclusion that anions are pas sively distributed in the lens according to the electrical gradient between the inside and outside of the lens [Rae, 1979].…”
Section: Introductionmentioning
confidence: 99%