Now showing items 104-116 of 116

    • Secretin promotes osmotic water transport in rat cholangiocytes by increasing aquaporin-1 water channels in plasma membrane: Evidence for a secretin-induced vesicular translocation of aquaporin-1 

      Pham, Linh; Marinelli, Raul A.; LaRusso, Nicholas F.; Agre, Peter (American Society for Biochemistry and Molecular Biology, 1997-05-16)
      Although secretin is known to stimulate ductal bile secretion by directly interacting with cholangiocytes, the precise cellular mechanisms accounting for this choleretic effect are unknown. We have previously shown that ...
    • Sequence and exon-intron organization of the DNA encoding the alpha I domain of human spectrin. Application to the study of mutations causing hereditary elliptocytosis. 

      Forget, B G; Marchesi, V. T.; Linnenbach, A. J.; Agre, P; Marchesi, S. L.; Laughinghouse, K.; Scarpa, A.; Tobe, T.; Sahr, K. E. (American Society for Clinical Investigation, 1989-10)
      We have determined the exon-intron organization and the nucleotide sequence of the exons and their flanking intronic DNA in cloned genomic DNA that encodes the first 526 amino acids of the alpha I domain of the human red ...
    • 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 ...
    • Structural basis for conductance by the archaeal aquaporin AqpM at 1.68 Å 

      Stroud, Robert; Agre, P; Kitagawa, Y; Remis, J.; Kozono, D; Lee, J K (National Academy of Sciences, 2005-12-27)
      To explore the structural basis of the unique selectivity spectrum and conductance of the transmembrane channel protein AqpM from the archaeon Methanothermobacter marburgensis, we determined the structure of AqpM to 1.68-A ...
    • Structural determinants of water permeation through aquaporin-1 

      Fujiyoshi, Yoshinori; Engel, Andreas; Heymann, J. Bernard; Agre, Peter; Walz, Thomas; Hirai, Teruhisa; Mitsuoka, Kaoru; Murata, Kazuyoshi (Nature Publishing Group, 2000-10-05)
      Human red cell AQP1 is the first functionally defined member of the aquaporin family of membrane water channels. Here we describe an atomic model of AQP1 at 3.8A resolution from electron crystallographic data. Multiple ...
    • Syntrophin-dependent expression and localization of Aquaporin-4 water channel protein 

      Adams, Marvin E.; Agre, Peter; Froehner, Stanley C.; Ottersen, Ole Petter; Amiry-Moghaddam, Mahmood; Neely, John D. (National Academy of Sciences, 2001-11-20)
      The Aquaporin-4 (AQP4) water channel contributes to brain water homeostasis in perivascular astrocyte endfeet where it is concentrated. We postulated that AQP4 is tethered at this site by binding of the AQP4 C terminus to ...
    • Targeted disruption of the Cl−/HCO3− exchanger Ae2 results in osteopetrosis in mice 

      Praetorius, Jeppe; Nielsen, Søren; Agre, Peter; Frische, Sebastian; Gawenis, Lara R.; Kwon, Tae-Hwan; Fejerskov, Ole; Josephsen, Kaj (National Academy of Sciences, 2009-02-03)
      Osteoclasts are multinucleated bone-resorbing cells responsible for constant remodeling of bone tissue and for maintaining calcium homeostasis. The osteoclast creates an enclosed space, a lacuna, between their ruffled ...
    • Targeted disruption of the Cl−/HCO3− exchanger Ae2 results in osteopetrosis in mice 

      Kwon, T; Gawenis, L; Frische, S.; Praetorius, J.; Josephsen, K.; Agre, P (National Academy of Sciences, 2009-02-03)
      Osteoclasts are multinucleated bone-resorbing cells responsible for constant remodeling of bone tissue and for maintaining calcium homeostasis. The osteoclast creates an enclosed space, a lacuna, between their ruffled ...
    • Temporary loss of perivascular aquaporin-4 in neocortex after transient middle cerebral artery occlusion in mice 

      Amiry-Moghaddam, Mahmood; Ottersen, Ole P.; Agre, Peter; Rash, John E.; Haug, Finn-Mogens; Laake, Petter; Skare, Oivind; Zeynalov, Emil; Davidson, Kimberly G. V.; Yasumura, Thomas; Mylonakou, Maria N.; Otsuka, Takashi; Bhardwaj, Anish; Frydenlund, Didrik S. (National Academy of Sciences, 2006-09-05)
      The aquaporin-4 (AQP4) pool in the perivascular astrocyte membranes has been shown to be critically involved in the formation and dissolution of brain edema. Cerebral edema is a major cause of morbidity and mortality in ...
    • The three-dimensional structure of aquaporin-1 

      Engel, Andreas; Agre, Peter; Smith, Barbara L.; Fujiyoshi, Yoshinori; Mitsuoka, Kaoru; Heymann, J. Bernard; Murata, Kazuyoshi; Hirai, Teruhisa; Walz, Thomas (Nature Publishing Group, 1997-06-05)
      The entry and exit of water from cells is a fundamental process of life. Recognition of the high water permeability of red blood cells led to the proposal that specialized water pores exist in the plasma membrane. Expression ...
    • Water and ion permeation of aquaporin-1 in planar lipid bilayers. Major differences in structural determinants and stoichiometry. 

      Pohl, Peter; Agre, Peter; Rothe, Ulrich; Kozono, David; Saparov, S. M. (American Society for Biochemistry and Molecular Biology, 2001-08-24)
      The aquaporin-1 (AQP1) water channel protein is known to facilitate the rapid movement of water across cell membranes, but a proposed secondary role as an ion channel is still unsettled. Here we describe a method to ...
    • 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. ...
    • Water channel properties of major intrinsic protein of lens 

      Guggino, W B; Mulders, S. M.; Preston, G M; Deen, P. M.; Agre, P; Van Os, C. H. (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. ...