Now showing items 1-3 of 3

    • Decreased pulmonary vascular permeability in aquaporin-1-null humans 

      Brown, R H; Agre, P; Nielsen, S; King, L S (National Academy of Sciences, 2002-01-22)
      The molecular determinants of water permeability in the human lung are incompletely defined. Aquaporins (AQP) are water-specific membrane channel proteins. AQP1 is present in endothelial cells in the lung, including those ...
    • Defective Urinary Concentrating Ability Due to a Complete Deficiency of Aquaporin-1 

      Agre, P; Carlton, J P; Fernandez, P C; Choi, M; King, L S (Massachusetts Medical Society, 2001-07-19)
      Aquaporin-1, the archetypal water-channel protein,1 was initially identified in red cells and renal proximal tubular epithelium.2 The gene for aquaporin-1 (AQP1) on chromosome 7 colocalizes with the Colton blood-group ...
    • Reduced arsenic clearance and increased toxicity in aquaglyceroporin-9-null mice 

      Mukhopadhyay, R; Agre, P; Rosen, B P; Nielsen, S; DiCarlo, S E; Lujan, H L; Liu, Y; Wang, Y; Rojek, A; Yoshinaga, M; Zhou, Y; Song, L; Carbrey, J M (National Academy of Sciences, 2009-09-15)
      Expressed in liver, aquaglyceroporin-9 (AQP9) is permeated by glycerol, arsenite, and other small, neutral solutes. To evaluate a possible protective role, AQP9-null mice were evaluated for in vivo arsenic toxicity. After ...