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- Title
Expression and modulation of connexin30.2, a novel gap junction protein in the mouse retina.
- Authors
De Sevilla Müller, Luis Pérez; Dedek, Karin; Janssen-Bienhold, Ulrike; Meyer, Arndt; Kreuzberg, Maria M.; Lorenz, Susanne; Willecke, Klaus; Weiler, Reto
- Abstract
Mammalian retinae express multiple connexins that mediate the metabolic and electrical coupling of various cell types. In retinal neurons, only connexin36, connexin45, connexin50, and connexin57 have been described so far. Here, we present an analysis of a novel retinal connexin, connexin30.2 (Cx30.2), and its regulation in the mouse retina. To analyze the expression of Cx30.2, we used a transgenic mouse line in which the coding region of Cx30.2 was replaced by lacZ reporter DNA. We detected the lacZ signal in the nuclei of neurons located in the inner nuclear layer and the ganglion cell layer (GCL). In this study, we focused on the GCL and characterized the morphology of the Cx30.2- expressing cells. Using immunocytochemistry and intracellular dye injections, we found six different types of Cx30.2-expressing ganglion cells: one type of ON-OFF, three types of OFF, and two types of ON ganglion cells; among the latter was the RGA1 type. We show that RGA1 cells were heterologously coupled to numerous displaced amacrine cells. Our results suggest that these gap junction channels may be heterotypic, involving Cx30.2 and a connexin yet unidentified in the mouse retina. Gap junction coupling can be modulated by protein kinases, a process that plays a major role in retinal adaptation. Therefore, we studied the protein kinase-induced modulation of coupling between RGA1 and displaced amacrine cells. Our data provide evidence that coupling of RGA1 cells to displaced amacrine cells is mediated by Cx30.2 and that the extent of this coupling is modulated by protein kinase C.
- Subjects
NEURONS; RETINA; CONNEXINS; IMMUNOCYTOCHEMISTRY; PROTEIN kinases
- Publication
Visual Neuroscience, 2010, Vol 27, Issue 3/4, p91
- ISSN
0952-5238
- Publication type
Article
- DOI
10.1017/S0952523810000131