Axotomy Inhibits the Slow Axonal Transport of Tubulin in the Squid Giant Axon

2003 ◽  
Vol 205 (2) ◽  
pp. 187-188
Author(s):  
P. E. Gallant
Keyword(s):  
Axonal Transport ◽  
Giant Axon ◽  
Squid Giant Axon ◽  
Slow Axonal Transport

Fast axonal transport in extruded axoplasm from squid giant axon

Science ◽  
1982 ◽  
Vol 218 (4577) ◽  
pp. 1129-1131 ◽  
Author(s):  
S. Brady ◽  
R. Lasek ◽  
R. Allen
Keyword(s):  
Axonal Transport ◽  
Giant Axon ◽  
Squid Giant Axon ◽  
Fast Axonal Transport

scholarly journals Monomer-polymer equilibria in the axon: direct measurement of tubulin and actin as polymer and monomer in axoplasm.

1984 ◽  
Vol 98 (6) ◽  
pp. 2064-2076 ◽  
Author(s):  
J R Morris ◽  
R J Lasek
Keyword(s):  
Axonal Transport ◽  
Direct Measurement ◽  
Giant Axon ◽  
Squid Giant Axon ◽  
The Other ◽  
Significant Fraction ◽  
Dissociation Reaction ◽  
Basic Principles

The monomer-polymer equilibria for tubulin and actin were analyzed for the cytoskeleton of the squid giant axon. Two methods were evaluated for measuring the concentrations of monomer, soluble (equilibrium) polymer, and stable polymer in extruded axoplasm. One method, the Kinetic Equilibration Paradigm ( KEP ), employs the basic principles of diffusion to distinguish freely diffusible monomer from proteins that are present in the form of polymer. The other method is pharmacological and employs either taxol or phalloidin to stabilize the microtubules and microfilaments, respectively. The results of the two methods agree and demonstrate that 22-36% of the tubulin and 41-47% of the actin are monomeric. The in vivo concentration of monomeric actin and tubulin were two to three times higher than the concentration required to polymerize these proteins in vitro, suggesting that assembly of these proteins is regulated by additional mechanisms in the axon. A significant fraction of the polymerized actin and tubulin in the axoplasm was stable microtubules and microfilaments, which suggests that the dissociation reaction is blocked at both ends of these polymers. These results are discussed in relationship to the axonal transport of the cytoskeleton and with regard to the ability of axons to change their shape in response to environmental stimuli.

Fast axonal transport in squid giant axon

Science ◽  
1982 ◽  
Vol 218 (4577) ◽  
pp. 1127-1129 ◽  
Author(s):  
R. Allen ◽  
J Metuzals ◽  
I Tasaki ◽  
S. Brady ◽  
S. Gilbert
Keyword(s):  
Axonal Transport ◽  
Giant Axon ◽  
Squid Giant Axon ◽  
Fast Axonal Transport

Neurofilaments and Paired Helical Filaments

1985 ◽  
Vol 43 ◽  
pp. 740-743
Author(s):  
J. Metuzals
Keyword(s):  
Animal Model ◽  
Posttranslational Modifications ◽  
Posttranslational Modification ◽  
Giant Axon ◽  
Paired Helical Filaments ◽  
Squid Giant Axon ◽  
In Vitro Experiments ◽  
Thin Sections ◽  
Structural Relationships

It has been demonstrated that the neurofibrillary tangles in biopsies of Alzheimer patients, composed of typical paired helical filaments (PHF), consist also of typical neurofilaments (NF) and 15nm wide filaments. Close structural relationships, and even continuity between NF and PHF, have been observed. In this paper, such relationships are investigated from the standpoint that the PHF are formed through posttranslational modifications of NF. To investigate the validity of the posttranslational modification hypothesis of PHF formation, we have identified in thin sections from frontal lobe biopsies of Alzheimer patients all existing conformations of NF and PHF and ordered these conformations in a hypothetical sequence. However, only experiments with animal model preparations will prove or disprove the validity of the interpretations of static structural observations made on patients. For this purpose, the results of in vitro experiments with the squid giant axon preparations are compared with those obtained from human patients. This approach is essential in discovering etiological factors of Alzheimer's disease and its early diagnosis.

Injury-induced vesiculation and membrane redistribution in squid giant axon

1990 ◽  
Vol 1023 (3) ◽  
pp. 421-435 ◽  
Author(s):  
Harvey M. Fishman ◽  
Kirti P. Tewari ◽  
Philip G. Stein
Keyword(s):  
Giant Axon ◽  
Squid Giant Axon

Anterograde Transport of Peptide-Conjugated Fluorescent Beads in the Squid Giant Axon Identifies a Zip-Code for the Synapse

2004 ◽  
Vol 207 (2) ◽  
pp. 164-164
Author(s):  
Michael P. Conley ◽  
Marcus K. Jang ◽  
Joseph A. DeGiorgis ◽  
Elaine L. Bearer
Keyword(s):  
Giant Axon ◽  
Squid Giant Axon ◽  
Anterograde Transport ◽  
Fluorescent Beads ◽  
Zip Code

scholarly journals Kinesin Mutations Cause Motor Neuron Disease Phenotypes by Disrupting Fast Axonal Transport in Drosophila

Genetics ◽  
1996 ◽  
Vol 144 (3) ◽  
pp. 1075-1085 ◽  
Author(s):  
Daryl D Hurd ◽  
William M Saxton
Keyword(s):  
Motor Neuron ◽  
Axonal Transport ◽  
Action Potentials ◽  
Light And Electron Microscopy ◽  
Synaptic Membrane ◽  
Slow Axonal Transport ◽  
Fast Axonal Transport ◽  
Motor Neuron Diseases ◽  
Transmitter Secretion ◽  
Axon Terminals

Abstract Previous work has shown that mutation of the gene that encodes the microtubule motor subunit kinesin heavy chain (Khc) in Drosophila inhibits neuronal sodium channel activity, action potentials and neurotransmitter secretion. These physiological defects cause progressive distal paralysis in larvae. To identify the cellular defects that cause these phenotypes, larval nerves were studied by light and electron microscopy. The axons of Khc mutants develop dramatic focal swellings along their lengths. The swellings are packed with fast axonal transport cargoes including vesicles, synaptic membrane proteins, mitochondria and prelysosomal organelles, but not with slow axonal transport cargoes such as cytoskeletal elements. Khc mutations also impair the development of larval motor axon terminals, causing dystrophic morphology and marked reductions in synaptic bouton numbers. These observations suggest that as the concentration of maternally provided wild-type KHC decreases, axonal organelles transported by kinesin periodically stall. This causes organelle jams that disrupt retrograde as well as anterograde fast axonal transport, leading to defective action potentials, dystrophic terminals, reduced transmitter secretion and progressive distal paralysis. These phenotypes parallel the pathologies of some vertebrate motor neuron diseases, including some forms of amyotrophic lateral sclerosis (ALS), and suggest that impaired fast axonal transport is a key element in those diseases.

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