In vitro reactive nitrating species toxicity in dissociated spinal motor neurons from NFL (−/−) andhNFL (+/+) transgenic mice

Author(s):  
Michael Strong ◽  
Maggie Sopper ◽  
Bei Ping He
Development ◽  
1996 ◽  
Vol 122 (10) ◽  
pp. 3163-3171 ◽  
Author(s):  
B.J. Fredette ◽  
J. Miller ◽  
B. Ranscht

As spinal motor neurons project to their hindlimb targets, their growth cones avoid particular regions along their pathway. T-cadherin is discretely distributed in the avoided caudal sclerotome and on extrasynaptic muscle surfaces (B. J. Fredette and B. Ranscht (1994) J. Neurosci. 14, 7331–7346), and therefore, the ability of T-cadherin to inhibit neurite growth was tested in vitro. T-cadherin inhibited neurite extension from select neuron populations both as a substratum, and as a soluble recombinant protein. Anti-T-cadherin antibodies neutralized the inhibition. Spinal motor neurons were inhibited only during the stages of axon growth across the sclerotome and muscle innervation. Inhibitory responses corresponded to neuronal T-cadherin expression, suggesting a homophilic binding mechanism. These results suggest that T-cadherin is a negative guidance cue for motor axon projections.


2001 ◽  
Vol 915 (1) ◽  
pp. 104-107 ◽  
Author(s):  
Y. Manabe ◽  
H. Warita ◽  
T. Murakami ◽  
M. Shiote ◽  
T. Hayashi ◽  
...  

2007 ◽  
Vol 1150 ◽  
pp. 182-189 ◽  
Author(s):  
Tetsuro Murakami ◽  
Makiko Nagai ◽  
Kazunori Miyazaki ◽  
Nobutoshi Morimoto ◽  
Yasuyuki Ohta ◽  
...  

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Sebastian Poliak ◽  
Daniel Morales ◽  
Louis-Philippe Croteau ◽  
Dayana Krawchuk ◽  
Elena Palmesino ◽  
...  

During neural circuit assembly, axonal growth cones are exposed to multiple guidance signals at trajectory choice points. While axonal responses to individual guidance cues have been extensively studied, less is known about responses to combination of signals and underlying molecular mechanisms. Here, we studied the convergence of signals directing trajectory selection of spinal motor axons entering the limb. We first demonstrate that Netrin-1 attracts and repels distinct motor axon populations, according to their expression of Netrin receptors. Quantitative in vitro assays demonstrate that motor axons synergistically integrate both attractive or repulsive Netrin-1 signals together with repulsive ephrin signals. Our investigations of the mechanism of ephrin-B2 and Netrin-1 integration demonstrate that the Netrin receptor Unc5c and the ephrin receptor EphB2 can form a complex in a ligand-dependent manner and that Netrin–ephrin synergistic growth cones responses involve the potentiation of Src family kinase signaling, a common effector of both pathways.


1998 ◽  
Vol 140 (5) ◽  
pp. 1167-1176 ◽  
Author(s):  
Jiming Kong ◽  
Vivian W.-Y. Tung ◽  
John Aghajanian ◽  
Zuoshang Xu

Dendrites play important roles in neuronal function. However, the cellular mechanism for the growth and maintenance of dendritic arborization is unclear. Neurofilaments (NFs), a major component of the neuronal cytoskeleton, are composed of three polypeptide subunits, NF-H, NF-M, and NF-L, and are abundant in large dendritic trees. By overexpressing each of the three NF subunits in transgenic mice, we altered subunit composition and found that increasing NF-H and/or NF-M inhibited dendritic arborization, whereas increasing NF-L alleviated this inhibition. Examination of cytoskeletal organization revealed that increasing NF-H and/or NF-M caused NF aggregation and dissociation of the NF network from the microtubule (MT) network. Increasing NF-H or NF-H together with NF-M further reduced NFs from dendrites. However, these changes were reversed by elevating the level of NF-L with either NF-H or NF-M. Thus, NF-L antagonizes NF-H and NF-M in organizing the NF network and maintaining a lower ratio of NF-H and NF-M to NF-L is critical for the growth of complex dendritic trees in motor neurons.


Author(s):  
Ryosuke Fujiki ◽  
Joun Y. Lee ◽  
Julie A. Jurgens ◽  
Mary C. Whitman ◽  
Elizabeth C. Engle

Sign in / Sign up

Export Citation Format

Share Document