Localization of Na(+)-K(+)-ATPase α/β, Na(+)-K(+)-2Cl-cotransporter 1 and aquaporin-5 in human eccrine sweat glands

Acta Histochem. 2014 Oct;116(8):1374-81. doi: 10.1016/j.acthis.2014.08.010. Epub 2014 Sep 11.

Abstract

In order to evaluate the function of the repaired or regenerated eccrine sweat glands, we must first localize the proteins involved in sweat secretion and absorption in normal human eccrine sweat glands. In our studies, the cellular localization of Na(+)-K(+)-ATPase α/β, Na(+)-K(+)-2Cl-cotransporter 1 (NKCC1) and aquaporin-5 (AQP5) in eccrine sweat glands were detected by immunoperoxidase labeling. The results showed that Na(+)-K(+)-ATPase α was immunolocalized in the cell membrane of the basal layer and suprabasal layer cells of the epidermis, the basolateral membrane of the secretory coils, and the cell membrane of the outer cells and the basolateral membrane of the luminal cells of the ducts. The localization of Na(+)-K(+)-ATPase β in the secretory coils was the same as Na(+)-K(+)-ATPase α, but Na(+)-K(+)-ATPase β labeling was absent in the straight ducts and epidermis. NKCC1 labeling was seen only in the basolateral membrane of the secretory coils. AQP5 was strongly localized in the apical membrane and weakly localized in the cytoplasm of secretory epithelial cells. The different distribution of these proteins in eccrine sweat glands was related to their functions in sweat secretion and absorption.

Keywords: Eccrine sweat gland; Immunohistochemistry; Na(+)–K(+)-ATPase α/β; Na(+)–K(+)–2Cl-cotransporter 1, Aquaporin-5.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Aquaporin 5 / metabolism*
  • Eccrine Glands / metabolism*
  • Female
  • Humans
  • Immunohistochemistry
  • Male
  • Sodium-Potassium-Exchanging ATPase / metabolism*
  • Solute Carrier Family 12, Member 2 / metabolism*

Substances

  • Aquaporin 5
  • SLC12A2 protein, human
  • Solute Carrier Family 12, Member 2
  • Sodium-Potassium-Exchanging ATPase