Immunochemical evidence for the light-regulated modulation of phosphatidylinositol-4,5-bisphosphate in rat photoreceptor cells.
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Immunocytochemical localization of phosphatidylinositol-4, 5-bisphosphate (PIP<SUB>2</SUB>) in the rat rod photoreceptor outer segments (OS) was investigated with rabbit antiPIP<SUB>2</SUB> antibodies. The OS of the light-adapted rat eye showed little or no staining, whereas the OS of the dark-adapted eye were intensely stained for PIP<SUB>2</SUB>. The immunoreactivity of photoreceptor PIP<SUB>2</SUB> in the eye exposed to a brief flash of light was markedly reduced. However, subsequent dark-adaptation of the flash-bleached eye resulted in a rapid recovery of PIP<SUB>2</SUB> immunoreactivity; dark-adaptation for 5 min was sufficient for recovery to the fully dark-adapted level. In dark-adapted eyes exposed to graded light intensities, the PIP<SUB>2</SUB> immunostaining varied with light levels and was correlated with unbleached rhodopsin concentrations. These results suggest that PIP<SUB>2</SUB> in the rat photoreceptor cells is rapidly hydrolyzed upon light exposure and rapidly synthesized in the dark and that the decrease of PIP<SUB>2</SUB> level is triggered by photic bleaching of rhodopsin.
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