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T.M. Duda, N. Agarwal, R. Ma, V. Venkataraman, R.K. Sharma; Ca2+–Modulated ROS–GC1 Transduction Machinery in Isolated Transformed Retinal Ganglion Cells, RGC–5 . Invest. Ophthalmol. Vis. Sci. 2006;47(13):163.
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© ARVO (1962-2015); The Authors (2016-present)
Biochemical, structural and functional characterization of Ca2+–modulated cyclic GMP signaling pathway in the inner retinal neurons, the ganglion cells.
Immunohistochemical analyses, Western blotting, RT–PCR, Ca2+–imaging, patch clamp recordings and in vitro reconstitution experiments in conjunction with enzyme activity assays were employed.
Ca2+–dependent membrane guanylate cyclase transduction machinery is expressed in RGC–5 cells. Through immunological and functional analyses ROS–GC1 has been identified as the enzyme component of the system. Two Ca2+ sensor proteins, neurocalcin delta and S100B, co–exist with ROS–GC1 and regulate its activity. Staining of RGC–5 cells with specific antibodies against neurocalcin d and ROS–GC1 shows positive reaction in the processes of the cells. Overexpression of ROS–GC1 promotes Ca2+ entry into RGC5 cells as evidenced by the markedly reduced time–to–peak ratio and increased amplitude of the response. Transfection of neurocalcin d into the cells results in membrane depolarization.
Two Ca2+–modulated ROS–GC1 signaling pathways operate in isolated retinal ganglion cells. These pathways employ two Ca2+ sensors, neurocalcin delta and S100B, which via their specific sites on ROS–GC1 regulate Ca2+ traffic in and out of the cell and the membrane polarization. Thus, they may be linked with the visual transduction machinery of the retina.
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