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Freshly enzymatically isolated cells from the aorta of a rat model of vascular hypertrophy were used to investigate the role of protein kinase C (PKC) isoforms during a physiologically relevant growth response. With the combination of immunofluorescence with digital imaging microscopy, PKC isoforms alpha, delta, and zeta were found to be present in single cells from control and hypertrophied rat aortas. The alpha- and zeta-isoforms were distributed in the cytoplasm of control cells; however, in hypertrophied cells, sustained translocations of alpha-PKC to the surface membrane and zeta-PKC to the intranuclear area were seen. delta-PKC was concentrated in the perinuclear area in control cells but appeared to translocate to a more diffuse localization in the cytosol of hypertrophied cells. Staining of mitochondria with rhodamine 123 indicated some similarity in the spatial distribution compared with that of delta-PKC. In control cells, translocation of isoforms alpha and delta was activated by phenylephrine or 12-deoxyphorbol 13-isobutyrate 20-acetate. Agonist stimulation produced translocation of no isoforms in the hypertrophied cells. These results indicate that isoform-specific spatial distribution and translocation of PKC occur in association with the growth response of vascular hypertrophy.
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Liou et al. (1994) studied this question.
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