Calcyclin, a Calcium-Binding Protein, which Regulates Insulin Secretion from the Permeabilized Pancreatic β-Cell

  • Ichiro Niki
  • Katsuo Okazaki
  • Satoshi Iino
  • Sigeru Kobayashi
  • Hiroyoshi Hidaka
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 426)


Although it is widely accepted that an increase in intracellular Ca2+ is a crucial event in the stimulus-secretion coupling in the pancreatic β-cell [1], we have limited knowledge on the later steps in the signal transduction pathway. Calcium binding proteins are considered to be involved in the control of Ca2+-dependent cellular functions including hormone release [2]. Various types of calcium-binding proteins such as calmodulin, calbindin and S-100b protein are identified in the islet cells biochemically or immunohistochemically [3,4]. Calmodulin, the best characterized calcium binding protein, was demonstrated to exist in the pancreatic islet cells by Sugden et al [5]. The pancreatic β-cell possesses the kinase activity which is dependent on Ca2+/calmodulin [6]. Involvement of calmodulin and calmodulin-dependent protein kinases in insulin release has been suggested mainly based on the inhibitory effect of calmodulin antagonists on the release [7,8,9], albeit there is the argument against this idea [10].


Pancreatic Islet Insulin Release Calcium Binding Protein Pancreatic Islet Cell Rabbit Lung 
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Copyright information

© Springer Science+Business Media New York 1997

Authors and Affiliations

  • Ichiro Niki
    • 1
  • Katsuo Okazaki
    • 1
  • Satoshi Iino
    • 1
  • Sigeru Kobayashi
    • 1
  • Hiroyoshi Hidaka
    • 1
  1. 1.Departments of Pharmacology and AnatomyNagoya University School of MedicineShowa-ku, 466, NagoyaJapan

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