Selective Assembly of V-ATPase Subunit Isoforms in Mouse Kidney |
| |
Authors: | Email author" target="_blank">Ge-Hong?Sun-WadaEmail author Hiroyuki?Tabata Nobuyuki?Kawamura |
| |
Institution: | (1) Department of Biochemistry, Faculty of Pharmaceutical Sciences, Doshisha Women’s College, Kyoto, Japan |
| |
Abstract: | The kidney plays vital roles in acid–base homeostasis, and the reabsorption of water, ions, and proteins. These processes
are achieved through acidification of urine and endosomes of proximal tubule epithelial cells. Multisubunit vacuolar-type
proton ATPase (V-ATPase) is one of the major acidification-machinery proteins that localizes to the apical or basolateral
plasma membranes of intercalated cells in collecting ducts and the endosomal region at the base of brush border microvilli
in proximal tubules. Multiple subunit isoforms of V-ATPase, which are expressed in kidney, have been identified. One obvious
question is whether the pumps at different locations in the kidney have their own unique subunit identities. We have used
a combination of methods to study this enzyme in kidney including immunocytochemical staining and immunoprecipitation analyses.
The subunit isoforms of V-ATPase exhibited selective association/assembly in kidney: kidney-specific isoforms predominantly
formed the intercalated cell proton pump, whereas the pump located in the brush border comprised ubiquitously expressed counterparts. |
| |
Keywords: | V-ATPase acid-base homeostasis subunit isoforms kidney |
本文献已被 PubMed SpringerLink 等数据库收录! |
|