scholarly journals Proportion of N-Type Calcium Current Activated by Action Potential Stimuli

2005 ◽  
Vol 94 (6) ◽  
pp. 3762-3770 ◽  
Author(s):  
J. Darwin King ◽  
Stephen D. Meriney

N-type calcium currents are important in many neuronal functions, including cellular signaling, regulation of gene expression, and triggering of neurotransmitter release. Often the control of these diverse cellular functions is governed by the spatial and temporal patterns of calcium entry in subcellular compartments. Underlying this issue is the effectiveness of action potentials at triggering calcium channel opening. Chick ciliary ganglion neurons were used as model cells to study the activation of N-type calcium current during action potential depolarization. Several different action potential shapes were recorded, used as voltage command templates, and altered such that control action potential–evoked currents could be compared with those elicited by broadened action potential commands. Depending on the action potential shape used to activate calcium currents in chick ciliary ganglion neurons, and the temperature at which recordings were performed, varying proportions ( I/ Imax) of N-type calcium current could be activated. The largest proportion measured occurred using a broad ciliary ganglion cell soma action potential to activate calcium current at 37°C (100%). The smallest proportion measured occurred using a fast, high-temperature–adjusted frog motoneuron nerve terminal action potential to activate calcium current at room temperature (10%). These data are discussed with respect to the impact on cellular signaling and the regulation of transmitter release.

1985 ◽  
Vol 33 (8) ◽  
pp. 837-839 ◽  
Author(s):  
A Messing ◽  
A Stieber ◽  
N K Gonatas

The resolution of indirect immunoperoxidase methods for localizing antigens on the surface of plasma membranes of cultured cells was tested using dissociated monolayer cultures of ciliary ganglion neurons prelabeled with cationic ferritin. Clusters of ferritin were produced on the cell surface by warming the cells to 37 degrees C after the ferritin, rabbit anti-ferritin, and goat anti-rabbit immunoglobulin coupled to horseradish peroxidase had all been applied. Intense 3,3'-diaminobenzidine tetrahydrochloride (DAB) staining was limited to the regions immediately surrounding the ferritin clusters. The lateral spread of the DAB reaction product beyond the outer ferritin particles in each cluster averaged 54-81 nm in four experiments. A second type of increased density, coinciding with the thickness of the plasma membrane, was also seen. These stained plasma membranes extended 161-339 nm from the ferritin clusters.


1995 ◽  
Vol 168 (2) ◽  
pp. 662-669 ◽  
Author(s):  
Wendy S. Thomas ◽  
Michele H. Jacob ◽  
Diane K. O'Dowd ◽  
Martin A. Smith

Development ◽  
2001 ◽  
Vol 128 (19) ◽  
pp. 3773-3782 ◽  
Author(s):  
Eri Hashino ◽  
Marlene Shero ◽  
Dirk Junghans ◽  
Hermann Rohrer ◽  
Jeffrey Milbrandt ◽  
...  

During development, parasympathetic ciliary ganglion neurons arise from the neural crest and establish synaptic contacts on smooth and striate muscle in the eye. The factors that promote the ciliary ganglion pioneer axons to grow toward their targets have yet to be determined. Here, we show that glial cell line-derived neurotrophic factor (GDNF) and neurturin (NRTN) constitute target-derived factors for developing ciliary ganglion neurons. Both GDNF and NRTN are secreted from eye muscle located in the target and trajectory pathway of ciliary ganglion pioneer axons during the period of target innervation. After this period, however, the synthesis of GDNF declines markedly, while that of NRTN is maintained throughout the cell death period. Furthermore, both in vitro and in vivo function-blocking of GDNF at early embryonic ages almost entirely suppresses ciliary axon outgrowth. These results demonstrate that target-derived GDNF is necessary for ciliary ganglion neurons to innervate ciliary muscle in the eye. Since the down-regulation of GDNF in the eye is accompanied by down-regulation of GFRα1 and Ret, but not of GFRα2, in innervating ciliary ganglion neurons, the results also suggest that target-derived GDNF regulates the expression of its high-affinity coreceptors.


1987 ◽  
Vol 105 (4) ◽  
pp. 1847-1854 ◽  
Author(s):  
M H Jacob ◽  
D K Berg

The regulation of nicotinic acetylcholine receptors (AChRs) in chick ciliary ganglia was examined by using a radiolabeled anti-AChR mAb to quantitate the amount of receptor in ganglion detergent extracts after preganglionic denervation or postganglionic axotomy. Surgical transection of the preganglionic input to the ciliary ganglion in newly hatched chicks caused a threefold reduction in the total number of AChRs within 10 d compared with that present in unoperated contralateral control ganglia. Surgical transection of both the choroid and ciliary nerves emerging from the ciliary ganglion in newly hatched chicks to establish postganglionic axotomy led to a nearly 10-fold reduction in AChRs within 5 d compared with unoperated contralateral ganglia. The declines were specific since they could not be accounted for by changes in ganglionic protein or by decreases in neuronal survival or size. Light microscopy revealed no gross morphological differences between neurons in operated and control ganglia. A second membrane component of cholinergic relevance on chick ciliary ganglion neurons is the alpha-bungarotoxin (alpha-Bgt)-binding component. The alpha-Bgt-binding component also declined in number after either postganglionic axotomy or preganglionic denervation, but appeared to do so with a more rapid time course than did ganglionic AChRs. The results imply that cell-cell interactions in vivo specifically regulate both the number of AChRs and the number of alpha-Bgt-binding components in the ganglion. Regulation of these neuronal cholinergic membrane components clearly differs from that previously described for muscle AChRs.


2002 ◽  
Vol 64 (3) ◽  
pp. 1169-1174 ◽  
Author(s):  
Masaru Sorimachi ◽  
Yumiko Abe ◽  
Katsutoshi Furukawa ◽  
Norio Akaike

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