Abstract
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].
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Niki, I., Okazaki, K., Iino, S., Kobayashi, S., Hidaka, H. (1997). Calcyclin, a Calcium-Binding Protein, which Regulates Insulin Secretion from the Permeabilized Pancreatic β-Cell. In: Soria, B. (eds) Physiology and Pathophysiology of the Islets of Langerhans. Advances in Experimental Medicine and Biology, vol 426. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1819-2_11
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DOI: https://doi.org/10.1007/978-1-4899-1819-2_11
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