## Abstract Calcium calmodulin‐dependent cyclic nucleotide phosphodiesterase (PDE1) was identified in crude extract and immunolabeled sections of rat retina. Both cAMP and cGMP PDE activities were stimulated by calcium‐calmodulin (4.7‐fold and 2.3‐fold, respectively). To characterize PDE1 isoforms
Differential localization and expression of α and β isoenzymes of protein kinase c in the rat retina
✍ Scribed by Jun Kosaka; Akira Suzuki; Eiichi Morii; Shintaro Nomura
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 582 KB
- Volume
- 54
- Category
- Article
- ISSN
- 0360-4012
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✦ Synopsis
Expression and cellular localization of three isoenzymes of Ca 2ϩ -dependent protein kinase C (PKC␣, PKC, and PKC␥) in the adult rat retina were revealed by immunohistochemistry and in situ hybridization histochemistry with isoenzyme-specific antibodies and cRNA probes. Immunoreactivities and mRNA signals for PKC␣ were conspicuous in rod bipolar cells. A subgroup of amacrine cells expressed PKC␣. The cells in the ganglion cell layer also displayed PKC␣ gene products. Positive immunoreactivities for PKC were localized as stripe patterns in the inner plexiform layer, corresponding to the stratification levels of axon terminals of cone bipolar cells. The somata of cone bipolar cells expressed PKC. Amacrine cells and retinal ganglion cells also displayed PKC gene products. The results obtained by immunohistochemistry were confirmed with colocalization of mRNA signals for PKC␣ and PKC on the somata. The cell membranes showed stronger immunoreactivities than did the cytoplasms for both PKC␣ and PKC. Neither immunoreactivities nor mRNA signals for PKC␥ were detected in all retinal regions. The differential roles of Ca 2ϩ -dependent PKC isoenzymes could be revealed in physiological defined retinal neurons.
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