Abstract 9781: A FRET-based Sensor Detects Caveolae as Spatially Distinct Ca2+ Stores in Endothelial Cells

TL;DRAbstract

Objective: Endothelial function is tightly regulated by spatiotemporally organized intracellular Ca 2+ signaling. A variety of Ca 2+ -regulating and Ca 2+ -dependent molecules, such as IP 3 receptor-like protein, Ca 2+ -ATPase and endothelial nitric oxide synthase, are enriched in caveolae, which are mobile and typically shaped as plasmalemmal invaginations or vesicles. As previously reported by us and others, the structure and subcellular distribution of caveolae are critical for Ca 2+ release from endoplasmic reticulum (ER) Ca 2+ stores and for Ca 2+ influx from the extracellular space into the cell. However, the Ca 2+ dynamics inside caveolae have not previously been detected and remain unclear. The aim of this study was to detect and analyze the Ca 2+ changes in subplasmalemmal caveolar vesicles. Methods: To target the FRET-based Ca 2+ -sensing protein D1, a mutant of cameleon, to the intracaveolar space, we created a cDNA construct (LOXD1) encoding a chimeric protein with lectin-l

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