Neurofilament Transport

2010 ◽  
pp. 249-260
Author(s):  
Andrew J. Grierson ◽  
Christopher C.J. Miller
Keyword(s):  
Neurofilament Transport

Carbon disulfide axonopathy. Another experimental model characterized by acceleration of neurofilament transport and distinct changes of axonal size

1987 ◽  
Vol 424 (2) ◽  
pp. 272-280 ◽  
Author(s):  
Miguel Pappolla ◽  
Roxanne Penton ◽  
Harold S. Weiss ◽  
Carl H. Miller ◽  
Zarife Sahenk ◽  
...  
Keyword(s):  
Experimental Model ◽  
Carbon Disulfide ◽  
Neurofilament Transport

scholarly journals Slowing of neurofilament transport and the radial growth of developing nerve fibers

1985 ◽  
Vol 5 (11) ◽  
pp. 2920-2929 ◽  
Author(s):  
PN Hoffman ◽  
JW Griffin ◽  
BG Gold ◽  
DL Price
Keyword(s):  
Radial Growth ◽  
Nerve Fibers ◽  
Neurofilament Transport

scholarly journals Glutamate Slows Axonal Transport of Neurofilaments in Transfected Neurons

2000 ◽  
Vol 150 (1) ◽  
pp. 165-176 ◽  
Author(s):  
Steven Ackerley ◽  
Andrew J. Grierson ◽  
Janet Brownlees ◽  
Paul Thornhill ◽  
Brian H. Anderton ◽  
...  
Keyword(s):  
Neurodegenerative Diseases ◽  
Axonal Transport ◽  
Fluorescent Protein ◽  
Mitogen Activated Protein Kinase ◽  
Glutamate Excitotoxicity ◽  
Slow Axonal Transport ◽  
Mitogen Activated Protein ◽  
Green Fluorescent ◽  
Pathogenic Process ◽  
Neurofilament Transport

Neurofilaments are transported through axons by slow axonal transport. Abnormal accumulations of neurofilaments are seen in several neurodegenerative diseases, and this suggests that neurofilament transport is defective. Excitotoxic mechanisms involving glutamate are believed to be part of the pathogenic process in some neurodegenerative diseases, but there is currently little evidence to link glutamate with neurofilament transport. We have used a novel technique involving transfection of the green fluorescent protein–tagged neurofilament middle chain to measure neurofilament transport in cultured neurons. Treatment of the cells with glutamate induces a slowing of neurofilament transport. Phosphorylation of the side-arm domains of neurofilaments has been associated with a slowing of neurofilament transport, and we show that glutamate causes increased phosphorylation of these domains in cell bodies. We also show that glutamate activates members of the mitogen-activated protein kinase family, and that these kinases will phosphorylate neurofilament side-arm domains. These results provide a molecular framework to link glutamate excitotoxicity with neurofilament accumulation seen in some neurodegenerative diseases.

scholarly journals Local Regulation of Neurofilament Transport by Myelinating Cells

2014 ◽  
Vol 34 (8) ◽  
pp. 2979-2988 ◽  
Author(s):  
P. C. Monsma ◽  
Y. Li ◽  
J. D. Fenn ◽  
P. Jung ◽  
A. Brown
Keyword(s):  
Local Regulation ◽  
Neurofilament Transport

Neurofilament Transport in Axonal Regeneration

1984 ◽  
pp. 243-260 ◽  
Author(s):  
Paul N. Hoffman ◽  
John W. Griffin ◽  
Donald L. Price
Keyword(s):  
Axonal Regeneration ◽  
Neurofilament Transport

Aluminum intoxication: a disorder of neurofilament transport in motor neurons

1985 ◽  
Vol 342 (1) ◽  
pp. 172-175 ◽  
Author(s):  
Juan C. Troncoso ◽  
Paul N. Hoffman ◽  
John W. Griffin ◽  
Kathryn M. Hess-Kozlow ◽  
Donald L. Price
Keyword(s):  
Motor Neurons ◽  
Aluminum Intoxication ◽  
Neurofilament Transport

scholarly journals Neurofilament heavy chain side arm phosphorylation regulates axonal transport of neurofilaments

2003 ◽  
Vol 161 (3) ◽  
pp. 489-495 ◽  
Author(s):  
Steven Ackerley ◽  
Paul Thornhill ◽  
Andrew J. Grierson ◽  
Janet Brownlees ◽  
Brian H. Anderton ◽  
...  
Keyword(s):  
Axonal Transport ◽  
Heavy Chain ◽  
Phosphorylation Sites ◽  
Heavy Chains ◽  
Transport Assay ◽  
Living Neurons ◽  
Carboxy Terminal ◽  
Bulk Transport ◽  
Neurofilament Transport ◽  
Terminal Domains

Neurofilaments possess side arms that comprise the carboxy-terminal domains of neurofilament middle and heavy chains (NFM and NFH); that of NFH is heavily phosphorylated in axons. Here, we demonstrate that phosphorylation of NFH side arms is a mechanism for regulating transport of neurofilaments through axons. Mutants in which known NFH phosphorylation sites were mutated to preclude phosphorylation or mimic permanent phosphorylation display altered rates of transport in a bulk transport assay. Similarly, application of roscovitine, an inhibitor of the NFH side arm kinase Cdk5/p35, accelerates neurofilament transport. Analyses of neurofilament movement in transfected living neurons demonstrated that a mutant mimicking permanent phosphorylation spent a higher proportion of time pausing than one that could not be phosphorylated. Thus, phosphorylation of NFH slows neurofilament transport, and this is due to increased pausing in neurofilament movement.

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