Electrophysiological properties of AQP6 in mouse parotid acinar cells

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  • Ichikawa Hideki
    Oral Health Science Center, hrc7, Tokyo Dental College Department of Physiology, Tokyo Dental College
  • Shibukawa Yoshiyuki
    Oral Health Science Center, hrc7, Tokyo Dental College Department of Physiology, Tokyo Dental College
  • Sahara Yoshinori
    Department of Physiology, Iwate Medical University School of Dentistry
  • Tsumura Maki
    Oral Health Science Center, hrc7, Tokyo Dental College Department of Physiology, Tokyo Dental College Department of Clinical Pharmacy, Faculty of Pharmaceutical Sciences, Toho University
  • Qi Bing
    Department of Physiology, Nihon University School of Dentistry at Matsudo
  • Satoh Keitaro
    Department of Regulatory Physiology, Dokkyo Medical University, School of Medicine
  • Narita Takanori
    Department of Physiology, Nihon University School of Dentistry at Matsudo
  • Hashimoto Sadamitsu
    Oral Health Science Center, hrc7, Tokyo Dental College Department of Pathology, Tokyo Dental College
  • Momose Yasunori
    Department of Clinical Pharmacy, Faculty of Pharmaceutical Sciences, Toho University
  • Tazaki Masakazu
    Oral Health Science Center, hrc7, Tokyo Dental College Department of Physiology, Tokyo Dental College
  • Shimono Masaki
    Department of Pathology, Tokyo Dental College
  • Sugiya Hiroshi
    Department of Physiology, Nihon University School of Dentistry at Matsudo

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Abstract

Salivary gland acinar cells secrete large amounts of water and electrolytes, where aquaporins (AQPs) are thought to be involved in the secretion. In the present study, we investigated expression/localization of AQP6, and the anion transporting properties of AQP6 in mouse parotid acinar cells. RT-PCR, western blotting and immunohistochemical analyses revealed expression of AQP6 in acinar cells, localized in apical membrane. Voltage ramp from -100 mV to +100 mV at a holding potential of -60 mV elicited outwardly-rectifying currents, in the presence of extracellular Cl- channel blockers and intracellular solution with 150 mM Cs+. These outward currents were increased when extracellular Cl- was replaced by Br-, NO3-, I-, or SCN-, accompanying a negative shift of reversal potentials. The outward current was enhanced by extracellular Hg2+. These results were consistent with the biophysical properties of transfected AQP6 oocytes or HEK cells, which indicate that the AQP6 channel is functionally expressed in parotid acinar cells, and suggest that AQP6 contributes to secretion of anions in parotid acinar cells. J. Med. Invest. 56 Suppl.: 347-349, December, 2009

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