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Anion sensitive ATPase in human cornea.

H Ebel, W Ruf

    Current Eye Research
    |April 1, 1985
    PubMed
    Summary
    This summary is machine-generated.

    A human cornea enzyme, anion-sensitive ATPase, shows highest activity in the endothelium and is stimulated by bicarbonate. Most of this enzyme is found in mitochondria, with some in plasma membranes.

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    Area of Science:

    • Ocular Biochemistry
    • Enzymology
    • Cellular Biology

    Background:

    • The cornea's physiological functions rely on active transport mechanisms.
    • Adenosine Triphosphatases (ATPases) are crucial enzymes involved in cellular energy.
    • Understanding corneal enzyme activity is vital for comprehending its health and disease.

    Purpose of the Study:

    • To characterize the anion-sensitive ATPase in the human cornea.
    • To determine the enzyme's distribution and specific activity within corneal layers.
    • To investigate the enzyme's kinetic properties and cellular localization.

    Main Methods:

    • Enzyme assays were performed on human cornea tissue.
    • Specific activity and total activity were measured in epithelial and endothelial layers.

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  • Subcellular fractionation identified enzyme localization (mitochondria, plasma membranes).

    • Main Results:

    • An anion-sensitive ATPase was identified in the human cornea.
    • Highest specific activity was observed in the corneal endothelium; highest total activity in the epithelium.
    • The enzyme was stimulated by bicarbonate and sulfite, inhibited by thiocyanate, and primarily localized to mitochondria.

    Conclusions:

    • The human cornea possesses a distinct anion-sensitive ATPase.
    • Mitochondrial localization suggests a role in corneal energy metabolism.
    • Differential distribution between epithelium and endothelium indicates layer-specific functions.