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Manganese treatments decrease immunofluorescence emissions of post‐synaptic dopamine D2 receptors
Author(s) -
Opoku Rachael,
Chekayev Yelena,
Carroll Margaret A.,
Catapane Edward J.
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.662.15
Subject(s) - receptor , dopamine receptor d2 , dopamine , immunofluorescence , biology , dopamine receptor , neurotoxin , biophysics , chemistry , antibody , medicine , microbiology and biotechnology , endocrinology , biochemistry , immunology
Manganese (Mn) a neurotoxin causing Manganism, a Parkinsons‐like disease, disrupts dopamine (DA) neurotransmission. Gill lateral cell cilia of Crassostrea virginica are controlled by DA innervations. DA is cilio‐inhibition. Our lab showed post‐synaptic DA receptors in gill cells are D2 type and Mn blocks cilio‐inhibitory effects of DA. Questions exist in the literature if Mn decreases the number of D2 receptors in brain. To test this we used histoimmunofluorescence techniques to visualize DA D2 receptors in gill and ganglia of C. virginica. Animals were treated with 500 FM of Mn for 5 days. Paraffin embedded sections were viewed with a phase contrast fluorescence microscope with a ProgRes C3 Peltier cooled camera. Antibody treated sections showed bright FITC fluorescence in lateral ciliated cells and other areas of gill and ganglia. Sections lacking 1E antibody treatment did not display similar fluorescence. We analyzed fluorescence intensity of the cells using ImageJ software. Intensity of Mn treated cells was 70% less than controls. The study identifies DA D2 receptors in gill cells and cerebral and visceral ganglia and shows a negative correlation between fluorescence intensity of the receptors in Mn treated animals. The question if the decrease in intensity is due to decrease in actual number of receptors or if Mn alters protein conformation of D2 receptor and D2‐ligand binding sites needs to be further explored.