Korean J Anat.  2005 Apr;38(2):167-172.

Ultrastructural Localization of the Ammonium Transporter Protein, RhBG, in the Intercalated Cell of Rat Kidney Collecting Duct

• Han KH
• Kim WY
• Verlander
• Weiner ID
• Kim J

Abstract

Ammonia excretion in the renal collecting duct is critical in the regulation of the acid-base homeostasis. A novel family of ammonium transporter protein, Rh B Glycoprotein (RhBG) was recently identified in the mouse and rat kidney collecting duct. The purpose of this was to examine the ultrastructural localization of RhBG in the collecting duct. Rat kidneys were processed for light and electron microscope immunocytochemistry using anti-RhBG rabbit polyclonal antibody. Strong RhBG immunolabeling was observed in the basolateral plasma membrane of type A intercalated cells in the collecting duct. In contrast, RhBG labeling was very weak or negative in type B intercalated cells and principal cells. Transmission electron microscopy confirmed that RhBG immunostaining was located mainly in the basolateral plasma membrane and infoldings of type A intercalated cells, but very weak in type B cells. RhBG labeling was not observed in the apical plasma membrane both in type A and B cells. These results demonstrate that RhBG is a basolateral transporter in acid-secreting type A cells and may mediate ammonia excretion in the collecting duct.

Keyword

Acid-base homeostasis; Ammonia; RhBG; Intercalated cell

MeSH Terms

Ammonia
Ammonium Compounds*
Animals
B-Lymphocytes
Cell Membrane
Glycoproteins
Homeostasis
Humans
Immunohistochemistry
Kidney Tubules, Collecting*
Kidney*
Mice
Microscopy, Electron, Transmission
Rats*
Ammonia
Glycoproteins