Abstract
PURPOSE
The specific activity of sodium-potassium-adenosine triphosphatase (Na-K-ATPase) in lens fiber cells is lower than the specific activity in lens epithelium. To test whether there is a reduction in the expression of Na-K-ATPase molecules in lens fibers, a Western blot technique was used.
METHODS
Membrane material was isolated from different regions of the rabbit lens. Na-K-ATPase (adenosine triphosphate hydrolysis) activity was measured in each membrane sample and Western blots were performed using an antibody to rabbit kidney Na-K-ATPase.
RESULTS
By immunoblotting, Na-K-ATPase polypeptide was detected in all lens cells. In contrast, adenosine triphosphate hydrolysis by the Na-K-ATPase (Na-K-ATPase activity) was not detectable or was detectable only at very low levels in fiber membranes from the lens nucleus and in cortex.
CONCLUSION
These findings suggest that plasma membrane adenosine triphosphatase enzyme responsible for sodium-potassium transport is expressed in newly formed lens fibers and the transport molecules are retained as the fibers age and are compressed toward the center of the lens. However, with fiber aging there is a loss of functional ability of the Na-K-ATPase to hydrolyze adenosine triphosphate.
Pub Type(s)
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
TY - JOUR
T1 - Distribution of lens sodium-potassium-adenosine triphosphatase.
AU - Delamere,N A,
AU - Dean,W L,
PY - 1993/6/1/pubmed
PY - 1993/6/1/medline
PY - 1993/6/1/entrez
SP - 2159
EP - 63
JF - Investigative ophthalmology & visual science
JO - Invest Ophthalmol Vis Sci
VL - 34
IS - 7
N2 - PURPOSE: The specific activity of sodium-potassium-adenosine triphosphatase (Na-K-ATPase) in lens fiber cells is lower than the specific activity in lens epithelium. To test whether there is a reduction in the expression of Na-K-ATPase molecules in lens fibers, a Western blot technique was used. METHODS: Membrane material was isolated from different regions of the rabbit lens. Na-K-ATPase (adenosine triphosphate hydrolysis) activity was measured in each membrane sample and Western blots were performed using an antibody to rabbit kidney Na-K-ATPase. RESULTS: By immunoblotting, Na-K-ATPase polypeptide was detected in all lens cells. In contrast, adenosine triphosphate hydrolysis by the Na-K-ATPase (Na-K-ATPase activity) was not detectable or was detectable only at very low levels in fiber membranes from the lens nucleus and in cortex. CONCLUSION: These findings suggest that plasma membrane adenosine triphosphatase enzyme responsible for sodium-potassium transport is expressed in newly formed lens fibers and the transport molecules are retained as the fibers age and are compressed toward the center of the lens. However, with fiber aging there is a loss of functional ability of the Na-K-ATPase to hydrolyze adenosine triphosphate.
SN - 0146-0404
UR - https://www.unboundmedicine.com/medline/citation/8389341/Distribution_of_lens_sodium_potassium_adenosine_triphosphatase_
L2 - https://iovs.arvojournals.org/article.aspx?volume=34&issue=7&page=2159
DB - PRIME
DP - Unbound Medicine
ER -