scholarly journals AXONAL TRANSPORT OF NEWLY SYNTHESIZED GLYCOPROTEINS IN A SINGLE IDENTIFIED NEURON OF APLYSIA CALIFORNICA

1974 ◽  
Vol 61 (3) ◽  
pp. 665-675 ◽  
Author(s):  
Richard T. Ambron ◽  
James E. Goldman ◽  
James H. Schwartz

Increasing amounts of glycoprotein synthesized from L-[3H]fucose injected into the cell body of R2, an identified Aplysia neuron, were found in the right pleuro-abdominal connective. Autoradiography revealed that the glycoproteins were localized in the axon of R2. Glycoproteins appearing in the axon presumably were synthesized in the cell body, since no significant incorporation was observed when [3H]fucose was injected directly into the axon. [3H]glycoproteins were detected in the connective after a delay of 1 h after intrasomatic injection. Thereafter, transport from the cell body was rapid, and by 10 h after injection, 45% of the total neuronal [3H]glycoprotein had appeared in the axon. By analysing the radioactivity in cell body and connective 4, 10, and 15 h after injection, we found that [3H]glycoproteins were transported selectively compared to nonmacromolecular material. Sequential sectioning of the connective revealed that [3H]glycoproteins were transported in discrete waves. The population of membrane-associated [3H]glycoproteins in the axon differed from that in the cell body. Two of the five somatic components appeared to be transported preferentially. In addition a new component appeared in the axon 10 h after injection.

2010 ◽  
Vol 133 (1) ◽  
Author(s):  
A. V. Kuznetsov

This paper develops a model for simulating transport of newly synthesized material from the neuron body toward the synapse of the axon as well as transport of misfolded and aggregated proteins back to the neuron body for recycling. The model demonstrates that motor-assisted transport, much similar to diffusion, can occur due to a simple concentration difference between the cell body and the synapse; organelles heading to the synapse do not need to attach preferably to plus-end-directed molecular motors, same as organelles heading to the neuron body for recycling do not need to attach preferably to minus-end-directed molecular motors. The underlying mechanics of molecular-motor-assisted transport is such that organelles would be transported to the right place even if new and used organelles had the same probability of attachment to plus-end-directed (and minus-end-directed) motors. It is also demonstrated that the axon with organelle traps and a region with a reversed microtubule polarity would support much smaller organelle fluxes of both new and used organelles than a healthy axon. The flux of organelles is shown to decrease as the width of organelle traps increases.


2020 ◽  
Vol 202 (8) ◽  
Author(s):  
Daisuke Nakane ◽  
Tatsuro Ito ◽  
Takayuki Nishizaka

ABSTRACT The mechanism underlying Spiroplasma swimming is an enigma. This small bacterium possesses two helical shapes with opposite-handedness at a time, and the boundary between them, called a kink, travels down, possibly accompanying the dual rotations of these physically connected helical structures, without any rotary motors such as flagella. Although the outline of dynamics and structural basis has been proposed, the underlying cause to explain the kink translation is missing. We here demonstrated that the cell morphology of Spiroplasma eriocheiris was fixed at the right-handed helix after motility was stopped by the addition of carbonyl cyanide 3-chlorophenylhydrazone (CCCP), and the preferential state was transformed to the other-handedness by the trigger of light irradiation. This process coupled with the generation and propagation of the artificial kink, presumably without any energy input through biological motors. These findings indicate that the coexistence of two chiral helices is sufficient to propagate the kink and thus to propel the cell body. IMPORTANCE Many swimming bacteria generate a propulsion force by rotating helical filaments like a propeller. However, the nonflagellated bacteria Spiroplasma spp. swim without the use of the appendages. The tiny wall-less bacteria possess two chiral helices at a time, and the boundary called a kink travels down, possibly accompanying the dual rotations of the helices. To solve this enigma, we developed an assay to determine the handedness of the body helices at the single-wind level, and demonstrated that the coexistence of body helices triggers the translation of the kink and that the cell body moves by the resultant cell bend propagation. This finding provides us a totally new aspect of bacterial motility, where the body functions as a transformable screw to propel itself forward.


Recent studies of axonal transport indicate that cytoskeletal proteins are assembled into polymers in the neuron cell body and that these polymers move from the cell body toward the end of the axon. On the other hand, membranous elements appear to be inserted into the axonal plasma membrane preferentially at the end of the axon. These new observations are explored in relation to our current understanding of axonal elongation.


1976 ◽  
Vol 40 (0) ◽  
pp. 83-92 ◽  
Author(s):  
J. H. Schwartz ◽  
J. E. Goldman ◽  
R. T. Ambron ◽  
D. J. Goldberg

Sign in / Sign up

Export Citation Format

Share Document