Abstract
Current hypotheses postulate that the metabolism of glucose within islets results in a transient increase in the ATP:ADP ratio, leading to depolarization and opening of voltage-dependent Ca2+ channels, promoting influx of Ca2+ into the β-cell. The increase in intracellular calcium may activate Ca2+-dependent protein kinases, which in turn phosphorylate key components in the secretory machinery. The nature and identity of these components are at present unclear. In addition, the β-cell contains a high (15–50 μM) concentration of calmodulin (CaM) and it has been shown that inhibitors of CaM block insulin secretion. Possible candidates for Ca2+/calmodulin-dependent protein kinases acting as regulatory enzymes in the exocytotic release process are phosphorylase kinase, myosin light chain kinase and CaM kinases.
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Urquidi, V., Ashcroft, S.J.H. (1997). Molecular Cloning of the cDNA Encoding β-Cell Calcium/Calmodulin-Dependent Protein Kinase II. 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_12
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DOI: https://doi.org/10.1007/978-1-4899-1819-2_12
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