BETA CELL CALCIUM INDEPENDENT GROUP VIA PHOSPHOLIPASE A2

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Evidence that the Group VIA cytosolic calcium-independent phospholipase A2 (iPLA2B) appears to participate in B-cell signal transduction includes the observations that inhibition of iPLA2B with the bromoenol lactone suicide substrate (BEL) suppresses glucose-stimulated insulin secretion and that over expression of iPLA2B amplifies insulin secretory responses in INS-1 insulinoma cell. Arachidonic acid produced by iPLA2B-catalyzed hydrolysis of their substrates induces release of Ca2+ from ER stores, an event thought to participate in glucose-stimulated insulin secretion.