December 1987
Volume 28, Issue 12
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Articles  |   December 1987
ATPase pump site density in human dysfunctional corneal endothelium.
Author Affiliations
  • M D McCartney
    Department of Anatomy, College of Medicine, University of Tennessee at Memphis 38163.
  • D P Robertson
    Department of Anatomy, College of Medicine, University of Tennessee at Memphis 38163.
  • T O Wood
    Department of Anatomy, College of Medicine, University of Tennessee at Memphis 38163.
  • B J McLaughlin
    Department of Anatomy, College of Medicine, University of Tennessee at Memphis 38163.
Investigative Ophthalmology & Visual Science December 1987, Vol.28, 1955-1962. doi:
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      M D McCartney, D P Robertson, T O Wood, B J McLaughlin; ATPase pump site density in human dysfunctional corneal endothelium.. Invest. Ophthalmol. Vis. Sci. 1987;28(12):1955-1962.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract

Proper corneal hydration is maintained by a Na, K-ATPase pump located in the lateral membranes of the endothelial cells. In dysfunctional corneas this pumping action appears to break down as the corneas become edematous. In order to provide quantitative and qualitative data on the Na, K-ATPase pump site density on dysfunctional and functional human corneal endothelial cells, the present study has employed both autoradiographic and histochemical techniques. Computer-assisted morphometrics and statistical analysis showed that there was a significant reduction (P less than 0.001) in 3H-ouabain binding, and thus ATPase pump sites, in the three types of corneas (Fuchs' endothelial dystrophy, aphakic and pseudophakic bullous keratopathy) with dysfunctional endothelia as compared to both types of corneas (eye bank, keratoconus) with functional endothelial cells. There were no significant differences amongst the dysfunctional types or between the two functional types of corneal endothelial cells in respect to density of silver grains. Histochemical staining for ATPase showed less p-nitro-phenylphosphatase histochemical reaction product present on dysfunctional endothelial lateral membranes than in the functional cells.

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