scholarly journals GABAA, GABACand glycine receptor-mediated inhibition differentially affects light-evoked signalling from mouse retinal rod bipolar cells

2006 ◽  
Vol 572 (1) ◽  
pp. 215-225 ◽  
Author(s):  
Erika D. Eggers ◽  
Peter D. Lukasiewicz
Keyword(s):  
Glycine Receptor ◽  
Bipolar Cells ◽  
Retinal Rod ◽  
Rod Bipolar Cells

Expression of glycine receptor subunits and gephyrin in single bipolar cells of the rat retina

1995 ◽  
Vol 12 (3) ◽  
pp. 501-507 ◽  
Author(s):  
Ralf Enz ◽  
Joachim Bormann
Keyword(s):  
Glycine Receptor ◽  
Bipolar Cells ◽  
Β Subunit ◽  
Rt Pcr ◽  
Patch Clamp Recording ◽  
Chain Reaction ◽  
Rat Retina ◽  
Adult Rat ◽  
Polymerase Chain ◽  
Rod Bipolar Cells

AbstractWe studied the expression of glycine receptor (GlyR) subunits and gephyrin in the adult rat retina. Reverse transcribed RNA was amplified by polymerase chain reaction (RT-PCR) with primers designed to recognize GlyR α1, α2, α3, β subunits, and gephyrin. Using RNA isolated from the whole retina, signals for all four GlyR subunits and gephyrin could be observed. In rod bipolar cells, in contrast, we detected a subset of GlyR subunits, α1 and β, and no gephyrin. Patch-clamp recording employing two subtype-specific blockers of the GlyR, picrotoxinin and cyanotriphenylborate (CTB), indicated that the GlyR in rod bipolar cells is a heteromeric protein composed of the α1 and β subunit. Moreover, the absence of detectable amounts of gephyrin mRNA suggests that the anchor protein is not required for the function of GlyRs in rod bipolar cells.

scholarly journals Glycine Receptors and Glycinergic Synaptic Input at the Axon Terminals of Mammalian Retinal Rod Bipolar Cells

2003 ◽  
Vol 553 (3) ◽  
pp. 895-909 ◽  
Author(s):  
Jinjuan Cui ◽  
Yu‐Ping Ma ◽  
Stuart A. Lipton ◽  
Zhuo‐Hua Pan
Keyword(s):  
Synaptic Input ◽  
Bipolar Cells ◽  
Glycine Receptors ◽  
Axon Terminals ◽  
Retinal Rod ◽  
Rod Bipolar Cells

scholarly journals LIM-Homeodomain Transcription Factor LHX4 Is Required for the Differentiation of Retinal Rod Bipolar Cells and OFF-Cone Bipolar Subtypes

Cell Reports ◽  
2020 ◽  
Vol 32 (11) ◽  
pp. 108144
Author(s):  
Xuhui Dong ◽  
Hua Yang ◽  
Xiangtian Zhou ◽  
Xiaoling Xie ◽  
Dongliang Yu ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Bipolar Cells ◽  
Homeodomain Transcription Factor ◽  
Retinal Rod ◽  
Rod Bipolar Cells ◽  
Lim Homeodomain

scholarly journals Functional ectopic neuritogenesis by retinal rod bipolar cells is regulated by miR-125b-5p during retinal remodeling in RCS rats

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Yan Fu ◽  
Baoke Hou ◽  
Chuanhuang Weng ◽  
Weiping Liu ◽  
Jiaman Dai ◽  
...  
Keyword(s):  
Bipolar Cells ◽  
Retinal Rod ◽  
Rcs Rats ◽  
Retinal Remodeling ◽  
Rod Bipolar Cells

Response of retinal rod bipolar cells in chronically hypoglycemic mice

2010 ◽  
Vol 68 ◽  
pp. e268
Author(s):  
Fuminobu Tamalu ◽  
Yumiko Umino ◽  
Yuning Sun ◽  
Eduardo Solessio ◽  
Shu-Ichi Watanabe ◽  
...  
Keyword(s):  
Bipolar Cells ◽  
Retinal Rod ◽  
Rod Bipolar Cells

scholarly journals Cone synapses in mammalian retinal rod bipolar cells

2018 ◽  
Vol 526 (12) ◽  
pp. 1896-1909 ◽  
Author(s):  
Ji-Jie Pang ◽  
Zhuo Yang ◽  
Roy A. Jacoby ◽  
Samuel M. Wu
Keyword(s):  
Bipolar Cells ◽  
Retinal Rod ◽  
Rod Bipolar Cells

scholarly journals Identification of PKCα-dependent phosphoproteins in mouse retina

2019 ◽  
Author(s):  
Colin M. Wakeham ◽  
Phillip A. Wilmarth ◽  
Jennifer M. Cunliffe ◽  
John E. Klimek ◽  
Gaoying Ren ◽  
...  
Keyword(s):  
Transcriptional Regulation ◽  
Functional Groups ◽  
Phorbol Ester ◽  
Bipolar Cells ◽  
Mouse Retina ◽  
Wild Type ◽  
Light Intensities ◽  
Retinal Rod ◽  
Wide Range ◽  
Rod Bipolar Cells

AbstractAdjusting to a wide range of light intensities is an essential feature of retinal rod bipolar cell (RBC) function. While persuasive evidence suggests this modulation involves phosphorylation by protein kinase C-alpha (PKCα), the targets of PKCα phosphorylation in the retina have not been identified. PKCα activity and phosphorylation in RBCs was examined by immunofluorescence confocal microscopy using a conformation-specific PKCα antibody and antibodies to phosphorylated PKC motifs. PKCα activity was dependent on light and expression of TRPM1, and RBC dendrites were the primary sites of light-dependent phosphorylation. PKCα-dependent retinal phosphoproteins were identified using a phosphoproteomics approach to compare total protein and phosphopeptide abundance between phorbol ester-treated wild type and PKCα knockout (PKCα-KO) mouse retinas. Phosphopeptide mass spectrometry identified over 1100 phosphopeptides in mouse retina, with 12 displaying significantly greater phosphorylation in WT compared to PKCα-KO samples. The differentially phosphorylated proteins fall into the following functional groups: cytoskeleton/trafficking (4 proteins), ECM/adhesion (2 proteins), signaling (2 proteins), transcriptional regulation (3 proteins), and homeostasis/metabolism (1 protein). Two strongly differentially expressed phosphoproteins, BORG4 and TPBG, were localized to the synaptic layers of the retina, and may play a role in PKCα-dependent modulation of RBC physiology. Data are available via ProteomeXchange with identifier PXD012906.SignificanceRetinal rod bipolar cells (RBCs), the second-order neurons of the mammalian rod visual pathway, are able to modulate their sensitivity to remain functional across a wide range of light intensities, from starlight to daylight. Evidence suggests that this modulation requires the serine/threonine kinase, PKCα, though the specific mechanism by which PKCα modulates RBC physiology is unknown. This study examined PKCα phosophorylation patterns in mouse rod bipolar cells and then used a phosphoproteomics approach to identify PKCα-dependent phosphoproteins in the mouse retina. A small number of retinal proteins showed significant PKCα-dependent phosphorylation, including BORG4 and TPBG, suggesting a potential contribution to PKCα-dependent modulation of RBC physiology.HighlightsPKCα is a major source of phosphorylation in retinal RBC dendrites and its activity in RBCs is light dependent.Proteins showing differential phosphorylation between phorbol ester-treated wild type and PKCα-KO retinas belong to the following major functional groups: cytoskeleton/trafficking (4 proteins), ECM/adhesion (2 proteins), signaling (2 proteins), transcriptional regulation (3 proteins), and homeostasis/metabolism (1 protein).The PKCα-dependent phosphoproteins, BORG4 and TPBG, are present in the synaptic layers of the retina and may be involved in PKCα-dependent modulation of RBC physiology.

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