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Colocalization of GLUT3 and choline acetyltransferase immunoreactivity in the rat retina.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1999 Mar 24; Vol. 256 (3), pp. 505-11. - Publication Year :
- 1999
-
Abstract
- Toward elucidating the functional aspects ofGLUT3, a primary neuronal glucose transporter isoform in the vertebrate central nervous system, this study examined its expression in cholinergic amacrine cells made identifiable by the presence of acetylcholine-synthesizing enzyme, choline acetyltransferase (ChAT), in the rat retina. Double-immunofluorescence staining of adult rat retinal tissue with anti-GLUT3 and anti-ChAT antibodies revealed characteristic stratified GLUT3 immunoreactivity (GLUT3-IR) in the inner plexiform layer (IPL) that was identical to the arborization pattern of ChAT-positive neuronal processes there. In addition, approximately 30-50% of intensely GLUT3-immunoreactive cell bodies in the inner nuclear layer and ganglion cell layer showed ChAT-IR, while the majority of ChAT-positive cell bodies were also intensely GLUT3 immunoreactive. Analysis at the cellular level using retinal cells in culture revealed similar findings. These results collectively indicate that cholinergic amacrine cells constitute the major component of GLUT3-expressing cells in the rat retina. It is expected that the link demonstrated here between GLUT3 expression and cholinergic amacrine cell population will provide clues for further analyzing GLUT3 function in the retina.<br /> (Copyright 1999 Academic Press.)
- Subjects :
- Animals
Cell Count drug effects
Cells, Cultured
Choline O-Acetyltransferase immunology
Cryoultramicrotomy
Female
Fluorescent Antibody Technique
Glucose Transporter Type 3
Kainic Acid administration & dosage
Kainic Acid pharmacology
Monosaccharide Transport Proteins immunology
Neurons cytology
Neurons drug effects
Neurons metabolism
Rats
Rats, Sprague-Dawley
Retina cytology
Retina drug effects
Retina metabolism
Time Factors
Tissue Fixation
Choline O-Acetyltransferase metabolism
Monosaccharide Transport Proteins metabolism
Nerve Tissue Proteins
Neurons chemistry
Retina chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0006-291X
- Volume :
- 256
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 10080928
- Full Text :
- https://doi.org/10.1006/bbrc.1999.0369