Sites of action potential generation in cultured vertebrate neurons

1983 ◽  
Vol 288 (1-2) ◽  
pp. 381-383 ◽  
Author(s):  
T.G. Smith

1988 ◽  
Vol 20 (1) ◽  
pp. 73-79
Author(s):  
V. N. Ierusalimskii ◽  
P. M. Balaban


2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Benjamin Grieb ◽  
Sivaranjan Uppala ◽  
Gal Sapir ◽  
David Shaul ◽  
J. Moshe Gomori ◽  
...  

AbstractDirect and real-time monitoring of cerebral metabolism exploiting the drastic increase in sensitivity of hyperpolarized 13C-labeled metabolites holds the potential to report on neural activity via in-cell metabolic indicators. Here, we followed the metabolic consequences of curbing action potential generation and ATP-synthase in rat cerebrum slices, induced by tetrodotoxin and oligomycin, respectively. The results suggest that pyruvate dehydrogenase (PDH) activity in the cerebrum is 4.4-fold higher when neuronal firing is unperturbed. The PDH activity was 7.4-fold reduced in the presence of oligomycin, and served as a pharmacological control for testing the ability to determine changes to PDH activity in viable cerebrum slices. These findings may open a path towards utilization of PDH activity, observed by magnetic resonance of hyperpolarized 13C-labeled pyruvate, as a reporter of neural activity.



Author(s):  
Xuanyuan Wu ◽  
Haixiang Li ◽  
Jiechang Huang ◽  
Mengqi Xu ◽  
Cheng Xiao ◽  
...  


2018 ◽  
Vol 165 (5) ◽  
pp. 610-612 ◽  
Author(s):  
A. A. Zverev ◽  
T. A. Anikina ◽  
N. G. Iskakov ◽  
A. L. Zefirov ◽  
T. L. Zefirov




2007 ◽  
Vol 177 (5) ◽  
pp. 857-870 ◽  
Author(s):  
Yulia Dzhashiashvili ◽  
Yanqing Zhang ◽  
Jolanta Galinska ◽  
Isabel Lam ◽  
Martin Grumet ◽  
...  

Axon initial segments (AISs) and nodes of Ranvier are sites of action potential generation and propagation, respectively. Both domains are enriched in sodium channels complexed with adhesion molecules (neurofascin [NF] 186 and NrCAM) and cytoskeletal proteins (ankyrin G and βIV spectrin). We show that the AIS and peripheral nervous system (PNS) nodes both require ankyrin G but assemble by distinct mechanisms. The AIS is intrinsically specified; it forms independent of NF186, which is targeted to this site via intracellular interactions that require ankyrin G. In contrast, NF186 is targeted to the node, and independently cleared from the internode, by interactions of its ectodomain with myelinating Schwann cells. NF186 is critical for and initiates PNS node assembly by recruiting ankyrin G, which is required for the localization of sodium channels and the entire nodal complex. Thus, initial segments assemble from the inside out driven by the intrinsic accumulation of ankyrin G, whereas PNS nodes assemble from the outside in, specified by Schwann cells, which direct the NF186-dependent recruitment of ankyrin G.



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