You are seeing this message because your Web browser does not support basic Web standards. Find out more about why this message is appearing and what you can do to make your experience on this site better.


ABOUT ARCHIVES
Advanced Search

Welcome   | My Account | E-mail Alerts | Access Rights | Sign In


  Vol. 133 No. 6, June 2007 TABLE OF CONTENTS
  Archives
  •  Online Features
  Original Article
 This Article
 •Full text
 •PDF
 • Reply to article
 •Send to a friend
 • Save in My Folder
 •Save to citation manager
 •Permissions
 Citing Articles
 •Citation map
 •Contact me when this article is cited
 Related Content
 •Similar articles in this journal
 Topic Collections
 •Pathology of Head & Neck
 •Voice Disorders
 •Alert me on articles by topic

Immunolocalization of Aquaporins in Vocal Fold Epithelia

Danielle Lodewyck, PhD; Bert Menco, PhD; Kimberly Fisher, PhD

Arch Otolaryngol Head Neck Surg. 2007;133(6):557-563.

Objective  To investigate the presence of aquaporin (AQP) water channels 1, 2, and 3 in stratified squamous vocal fold epithelium.

Design  Immunolocalization analysis of excised ovine vocal fold epithelia.

Subjects  Sheep.

Interventions  Ovine vocal fold epithelia were prepared for immunoelectron microscopy using primary antibodies directed against AQP-1, AQP-2, and AQP-3. Photographic profiles of epithelium exposed to each antibody were used to calculate the immunogold labeling density of the plasma membrane and cytoplasm.

Main Outcome Measures  Density of immunolabeling was compared across 3 regions that represent cell layers closest to the glottal lumen for the plasma membrane and cytoplasm, respectively.

Results  Labeling densities of AQP-1 and AQP-2 were significantly greater for the plasma membrane region of the luminal cells than for deeper cell layers. Cytoplasmic labeling and labeling of circular structures was greatest for cell layers 2 through 5 beneath the vocal fold surface compared with the surface cell layer. Immunogold labeling of AQP-3, an aquaglyceroporin, in vocal fold epithelium was inconclusive.

Conclusion  Aquaporins 1 and 2, associated with the plasma membrane region of ovine vocal fold epithelial cells, demonstrate the presence of an intrinsic mechanism to permit transcellular water flux in response to osmotic gradients.


Author Affiliations: Department of Communication Sciences and Disorders, Northwestern University, Evanston, Ill.







HOME | CURRENT ISSUE | PAST ISSUES | TOPIC COLLECTIONS | CME | SUBMIT | SUBSCRIBE | HELP
CONDITIONS OF USE | PRIVACY POLICY | CONTACT US | SITE MAP
 
© 2007 American Medical Association. All Rights Reserved.