Now showing items 1-5 of 5

    • Arsenite transport by mammalian aquaglyceroporins AQP7 and AQP9 

      Rosen, Barry P.; Agre, Peter; Mukhopadhyay, Rita; Carbrey, Jennifer M.; Shen, Jian; Liu, Zijuan (National Academy of Sciences, 2002-04-30)
      Much is known about the transport of arsenite and antimonite into microbes, but the identities of mammalian transport proteins are unknown. The Saccharomyces cerevisiae FPS1 gene encodes a membrane protein homologous to ...
    • Cholangiocytes express the aquaporin CHIP and transport water via a channel-mediated mechanism 

      LaRusso, Nicholas F.; Agre, Peter; Alpini, Gianfranco; Pham, Linh; Ueno, Yoshiyuki; Yano, Motoyoshi; Roberts, Stuart K. (National Academy of Sciences, 1994-12-20)
      Cholangiocytes line the intrahepatic bile ducts and regulate salt and water secretion during bile formation, but the mechanism(s) regulating ductal water movement remains obscure. A water-selective channel, the aquaporin ...
    • Direct immunogold labeling of aquaporin-4 in square arrays of astrocyte and ependymocyte plasma membranes in rat brain and spinal cord 

      Nielsen, Soren; Agre, Peter; Hudson, C. Sue; Yasumura, Thomas; Rash, John E. (National Academy of Sciences, 1998-09-29)
      Aquaporin (AQP) water channels are abundant in the brain and spinal cord, where AQP1 and AQP4 are believed to play major roles in water metabolism and osmoregulation. Immunocytochemical analysis of the brain recently ...
    • Specialized membrane domains for water transport in glial cells: high resolution immunogold cytochemistry of aquaporin-4 in rat brain 

      Ottersen, Ole Petter; Agre, Peter; Bourque, Charles; Amiry-Moghaddam, Mahmood; Nagelhus, Erlend Arnulf; Nielsen, Søren (Copyright held by the original publisher: Journal of Neuroscience, 1997-01-01)
      Membrane water transport is critically involved in brain volume homeostasis and in the pathogenesis of brain edema. The cDNA encoding aquaporin-4 (AQP4) water channel protein was recently isolated from rat brain. We used ...
    • Water channel properties of major intrinsic protein of lens 

      Agre, Peter; Van Os, Carel H.; Guggino, William B.; Deen, Peter M. T.; Preston, Gregory M.; Mulders, Sabine M. (American Society for Biochemistry and Molecular Biology, 1995-04-14)
      The functions of major intrinsic protein (MIP) of lens are still unresolved; however the sequence homology with channel-forming integral membrane protein (CHIP) and other Aquaporins suggests that MIP is a water channel. ...