Related Experiment Video

Updated: Aug 13, 2026

Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays
12:48

Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays

Published on: February 19, 2013

Localization of Na+/K(+)-ATPase in the bovine corneal endothelium

J A Guggenheim1, S A Hodson

  • 1Department of Optometry and Vision Sciences, University of Wales College of Cardiff, UK.

Biochimica Et Biophysica Acta
|January 19, 1994
PubMed

Insights

Researchers identified the location of sodium-potassium adenosine triphosphatase (Na+/K+-ATPase) in bovine corneal endothelial cells. The enzyme is present on both basal and lateral membranes, challenging previous assumptions.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Ophthalmology

Background:

  • The sodium-potassium adenosine triphosphatase (Na+/K+-ATPase) is crucial for maintaining cellular ion gradients.
  • Its precise localization within the bovine corneal endothelium has been a subject of debate.

Purpose of the Study:

  • To precisely localize Na+/K+-ATPase in the bovine corneal endothelium.
  • To characterize the antibody used for localization and confirm its specificity.

Main Methods:

  • Western blotting and immunoprecipitation to identify and characterize the target protein.
  • Peptide N-Glycanase F treatment to analyze glycosylation patterns.
  • Immunocytochemistry at light and electron microscopic levels for cellular localization.

Main Results:

  • A monoclonal antibody specifically recognized the alpha subunit of Na+/K+-ATPase (100 kDa).
  • Deglycosylation analysis revealed a 33 kDa core protein with three N-linked glycans.
  • Immunolabeling showed Na+/K+-ATPase distributed on both basal and lateral membranes of corneal endothelial cells.

Conclusions:

  • The study confirms a basolateral distribution of Na+/K+-ATPase in bovine corneal endothelium.
  • This finding refines our understanding of ion transport mechanisms in the cornea.

More Related Videos

Mechanical Stimulation-induced Calcium Wave Propagation in Cell Monolayers: The Example of Bovine Corneal Endothelial Cells10:46

Mechanical Stimulation-induced Calcium Wave Propagation in Cell Monolayers: The Example of Bovine Corneal Endothelial Cells

Published on: July 16, 2013

In Vitro and In Vivo Models to Study Corneal Endothelial-mesenchymal Transition09:05

In Vitro and In Vivo Models to Study Corneal Endothelial-mesenchymal Transition

Published on: August 20, 2016

Related Concept Videos

ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

The P-type pumps are a large family of integral membrane transporter ATPases. They are divided into five major types based on substrate specificity, from I to V.
A typical P-type pump has three cytosolic domains: nucleotide-binding (N), phosphorylation (P), and activator (A) domains. These domains are connected to the membrane-spanning helices by short amino acid segments. ATP hydrolysis and covalent phosphoenzyme intermediate formation are crucial parts of the catalytic cycle. At the highly...
ATP Driven Pumps III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

V-type pumps are ATP-driven pumps found in the vacuolar membranes of plants, yeast, endosomal and lysosomal membranes of animal cells, plasma membranes of a few specialized eukaryotic cells, and some prokaryotes. They are also known as the V1Vo-ATPase, that couple ATP hydrolysis to transport protons against a concentration gradient.
The peripheral or cytosolic V1 domain with eight subunits is involved in ATP hydrolysis. The integral or transmembrane V0 domain containing at least five subunits...