| Literature DB >> 12422412 |
Yuki Tajika1, Toshiyuki Matsuzaki, Takeshi Suzuki, Takeo Aoki, Haruo Hagiwara, Shigeyasu Tanaka, Eiki Kominami, Kuniaki Takata.
Abstract
Aquaporin-2 (AQP2) is a member of water channel proteins expressed in the kidney collecting duct cells, where it is stored in the intracellular compartment. Upon stimulation of antidiuretic hormone (ADH), AQP2 is recruited to the plasma membrane, and plays a critical role in urine concentration. We immunohistochemically characterized the intracellular compartment harboring AQP2 in the rat kidney using antibodies to the endoplasmic reticulum, Golgi apparatus, trans-Golgi network, lysosome, and endosome. Aquaporin-2 did not colocalize with calnexin, TGN38, Golgi 58K, cathepsin D or Igp-110. Small portions of AQP2-bearing vesicles were positive for early endosome antigen 1. These localization patterns were basically the same in water-loaded and ADH-treated animals. These results indicate that AQP2-bearing vesicles constitute a unique intracellular compartment distinct from the endoplasmic reticulum, Golgi apparatus, trans-Golgi network and lysosome. Partial colocalization of AQP2 with early endosomes suggests that the endosomal system might be involved in the trafficking of AQP2.Entities:
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Year: 2002 PMID： 12422412 DOI： 10.1046/j.0022-7722.2002.00028.x
Source DB: PubMed Journal: Anat Sci Int ISSN： 1447-073X Impact factor: 1.741