Characterization of aldehyde dehydrogenase-positive amacrine cells restricted in distribution to the dorsal retina

Visual Neuroscience
A H MilamJ C Saari

Abstract

A class 1 aldehyde dehydrogenase (ALDH) catalyzes oxidation of retinaldehyde to retinoic acid in bovine retina. We used immunocytochemistry and in situ hybridization to localize this enzyme in adult and fetal bovine retinas. Specific ALDH immunoreactivity was present in the cytoplasm of wide-field amacrine cells restricted in distribution to the dorsal part of the adult retina. The somata diameters ranged from approximately 8 microns to approximately 15 microns, and the cells increased in density from approximately 125 cells/mm2 near the horizontal meridian to approximately 425 cells/mm2 in the superior far periphery. The ALDH-positive cells had somata on both sides of the inner plexiform layer (IPL) and processes in two IPL strata. The majority of ALDH-positive cells were unreactive with antibodies against known amacrine cell enzymes and neurotransmitters, including GABA and glycine. The ALDH-positive amacrine cells also did not react with anti-cellular retinoic acid-binding protein, which was present in a subset of GABA-positive amacrine cells. In flat-mounted retinas processed by in situ hybridization, the larger ALDH-positive amacrine cells tended to be more heavily labeled. In addition to amacrine cells, Müller cell proces...Continue Reading

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Citations

Aug 15, 1998·The Journal of Biological Chemistry·F HaeseleerK Palczewski
Jun 17, 1998·Proceedings of the National Academy of Sciences of the United States of America·R WeilerU Janssen-Bienhold
Sep 21, 2004·Journal of Neuroscience Research·Petra DirksReto Weiler
Mar 28, 1998·The Journal of Biological Chemistry·X ZhaoK Palczewski
Oct 6, 1999·The European Journal of Neuroscience·R WeilerD I Vaney
Mar 11, 2000·The European Journal of Neuroscience·M Pottek, R Weiler

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