The thiol-oxidizing agent diamide reduces isoproterenol-stimulated amylase release in rat parotid acinar cells

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  • Guo Ming-Yu
    Department of Physiology, Nihon University School of Dentistry at Matsudo
  • Narita Takanori
    Department of Physiology, Nihon University School of Dentistry at Matsudo Research Institute of Oral Science, Nihon University School of Dentistry at Matsudo
  • Qi Bing
    Department of Physiology, Nihon University School of Dentistry at Matsudo
  • Satoh Keitaro
    Department of Physiology, Nihon University School of Dentistry at Matsudo
  • Katsumata-Kato Osamu
    Department of Physiology, Nihon University School of Dentistry at Matsudo
  • Matsuki-Fukushima Miwako
    Department of Physiology, Nihon University School of Dentistry at Matsudo
  • Fujita-Yoshigaki Junko
    Department of Physiology, Nihon University School of Dentistry at Matsudo Research Institute of Oral Science, Nihon University School of Dentistry at Matsudo
  • Sugiya Hiroshi
    Department of Physiology, Nihon University School of Dentistry at Matsudo Research Institute of Oral Science, Nihon University School of Dentistry at Matsudo

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Abstract

In parotid acinar cells, activation of β-adrenergic receptors provokes exocytotic amylase release via the accumulation of intracellular cAMP. Cellular redox status plays a pivotal role in the regulation of various cellular functions. Cellular redox imbalance caused by the oxidation of cellular antioxidants, as a result of oxidative stress, induces significant biological damages. In this study, we examined effect of diamide, a thiol-oxidizing reagent, on amylase release in rat parotid acinar cells. In the presence of diamide, isoproterenol (IPR)-induced cAMP formation and amylase release were partially reduced. Diamide had no effect on amylase release induced by forskolin and mastoparan, an adenylate cyclase activator and heterotrimeric GTP binding protein activator, respectively. In the cells pretreated with diamide, the binding affinity of [3H]dihydroalprenolol to β-receptors was reduced. These results suggest that oxidative stress results in reduction of binding affinity of ligand on β-receptor and consequently reduces protein secretory function in rat parotid acinar cells. J. Med. Invest. 56 Suppl.: 284-286, December, 2009

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