Zinc transporter 3 and zinc ions in the rodent superior cervical ganglion neurons.
Previous studies have revealed that zinc-enriched (ZEN) terminals are present in all parts of the CNS though with great differences in intensity. The densest populations of both ZEN terminals and ZEN somata are found in telencephalic structures, but also structures like the spinal cord demonstrate impressive ZEN systems spreading terminals several segments around the respective ZEN somata. The present study evaluates whether sympathetic neurons in the superior cervical ganglia (SCG) are ZEN neurons, i.e. contain vesicles that have zinc transporter 3 (ZnT3) proteins in their membranes and contain zinc ions. ZnT3 immunoreactivity (IR) was found in the somata and processes in the postganglionic neurons of mouse SCG. Only a small fraction of neurons (less than 5%), expressed varying degrees of ZnT3. Colchicine treatment, however, increased the number of ZnT3-positive neurons three-fold, suggesting an accumulation of ZnT3 protein in the somata. A small proportion of the postganglionic axons revealed dotted accumulations of ZnT3 IR along their courses. Double labeling showed that all ZnT3-positive neurons and axons were also tyrosine hydroxylase-positive with strong immunofluorescence, while no colocalization was found between ZnT3 and the vesicular acetylcholine transporter (VAChT) or neuropeptide Y IR. VAChT-positive preganglionic neurons were found to terminate on ZnT3 neuronal somata. 6-Methoxy 8-para toluene sulfonamide quinoline fluorescence and zinc selenium autometallography (ZnSe(AMG)) revealed that a subgroup of SCG cells contained free or loosely bound zinc ions. It is therefore concluded that ZnT3 and zinc ions are present in a subpopulation of TH-positive, NPY-negative neurons in the rodent SCG, supporting the notion that vesicular zinc ions may play a special role in the peripheral sympathetic adrenergic system.
Wang
Z Y
ZY
Department of Histology and Embryology, China Medical University, Shenyang 110001, China.
Danscher
G
G
Dahlström
A
A
Li
J Y
JY
D000818:Animals; D001369:Axons / Q000737:chemistry; D002352:Carrier Proteins / Q000032:analysis*; D027682:Cation Transport Proteins; D005455:Fluorescent Antibody Technique; D008297:Male; D008565:Membrane Proteins / Q000032:analysis*; D026901:Membrane Transport Proteins; D051379:Mice; D008807:Mice, Inbred BALB C; D018613:Microscopy, Confocal; D008856:Microscopy, Fluorescence; D009478:Neuropeptide Y / Q000032:analysis; D051381:Rats; D017208:Rats, Wistar; D017783:Superior Cervical Ganglion / Q000737:chemistry*; D014446:Tyrosine 3-Monooxygenase / Q000032:analysis; D050494:Vesicular Acetylcholine Transport Proteins; D033921:Vesicular Transport Proteins; D015032:Zinc / Q000032:analysis*
D002352:Carrier Proteins; D027682:Cation Transport Proteins; D008565:Membrane Proteins; D026901:Membrane Transport Proteins; D009478:Neuropeptide Y; C493460:Slc18a3 protein, mouse; C493461:Slc18a3 protein, rat; C491177:Slc30a3 protein, mouse; D050494:Vesicular Acetylcholine Transport Proteins; D033921:Vesicular Transport Proteins; D014446:Tyrosine 3-Monooxygenase; D015032:Zinc