The neuroplasmic network in Loligo and Hermissenda neurons

Hodge, Alan J.; Adelman, William J.

doi:10.1016/s0022-5320(80)80007-4

Cited by 66 publications

(29 citation statements)

References 39 publications

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“…Squid giant axons were treated with saponin. We found cytoskeletal structures, in the extracted axoplasm stained with ruthenium red, that corresponded to structures observed with high voltage electron microscopy and the freeze-etched technique (5,11,16). Some characteristics of the microtubules preserved in our extracted model are described.…”

supporting

confidence: 68%

The fibrillar network in the cytoplasm of squid giant axon extracted with saponin.

Gotoh

Takenaka

Shozushima

1983

Cell Struct. Funct.

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supporting

confidence: 68%

The fibrillar network in the cytoplasm of squid giant axon extracted with saponin.

Gotoh

Takenaka

Shozushima

1983

Cell Struct. Funct.

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“…It is more likely that phosphorylation provides a further compacting or ordering of neurofilament structure, which may involve either neurofilaments alone or a possible association with tubulin (14) or other neurite constituents. The possibility of significance of phosphorylation in the functional complexity of the brain is made likely by the heterogeneity of neurofilaments (6).…”

Section: Discussionmentioning

confidence: 99%

Monoclonal antibodies distinguish phosphorylated and nonphosphorylated forms of neurofilaments in situ.

Sternberger¹,

Sternberger²

1983

Proc. Natl. Acad. Sci. U.S.A.

990

640

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The immunocytochemical staining patterns of 37 neuron-specific monoclonal antibodies previously described fell into four groups: (i) anti-synapse-associated, (ii) anti-neurofibrillar, (iii) anti-perikaryonal-neurofibrillar, and (iv).a single antibody reactive with a widely distributed epitope that covered the patterns of groups ii and iii. Antibodies of groups ii, iii, and iv were shown to be specific to neurofilament triplet subunits, even though there was little overlap in staining patterns between groups ii and iii. We examined nine of these antibodies as to their ability to distinguish functional states of neurofilaments dependent upon phosphorylation. Upon digestion with phosphatase, electroblot staining of neurofilament components was abolished with the five antibodies from group ii, enhanced with the three antibodies from group iii, and unaffected with antibody iv. Immunocytochemical staining of Bouin-fixed paraffin sections of rat brain was unaffected by phosphatase pretreatment. With antibodies of group ii, digestion with trypsin also left staining unaffected, but when followed by digestion with phosphatase, staining was diminished with three out of five antibodies. In contrast, digestion with trypsin abolished all staining with each antibody from group iii. If followed by digestion with phosphatase, staining reappeared, but the group iii pattern was replaced by a group ii pattern. Staining of this pattern was again abolished upon a second treatment with trypsin. The antibody from group iv lost most of its groups ii and iii staining patterns when sections were digested with trypsin. The group ii pattern reappeared and, indeed, was enhanced upon a subsequent phosphatase treatment and was reduced again upon a second trypsin treatment. Staining by four out of five antibodies from group ii was inhibited by inorganic phosphate. The data indicate that certain nerve cell bodies, their dendrites, and at least proximal axons possess nonphosphorylated neurofilaments and that long fibers, including terminal axons, possess phosphorylated neurofilaments. We propose that phosphorylation may be a factor in stabilizing compacted forms of neurofilaments and that heterogeneity of the compacted structures may play a role in a possible multiplicity of function within individual nerve cells.Out of 135 monoclonal antibodies previously obtained upon immunization with hypothalamus, 37 were neuron-specific and delineated heterogeneous antigens (1, 2). Their general staining distribution permitted classification into four groups: (i) an anti-synapse-associated group that stained gray matter to the exclusion of the interior of cell bodies or discernible nerve fibers and reacted with isolated synaptosomes; (ii) an anti-neurofibrillar group that generally stained white and gray matter fibers, basket cell fibers in the cerebellum, and transverse fibers in the cerebral cortex, but never any cell bodies or their proximal axons or dendrites; (iii) an anti-perikaryonal-neurofibrillar group that stained selected perikarya, their...

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“…The cross-bridges between the linear polymers keep these structures aligned so that the polymers form an ordered network (18,29). This network has two important properties : it defines the shape of the axon (44) and it directs the movement of particles so that they move parallel to the long axis (1,13) .…”

Section: Microtubules and Neurofilaments Form A Relatively Stable Netmentioning

confidence: 99%

Axonal transport of the cytoplasmic matrix.

Lasek¹,

Garner²,

Brady³

1984

The Journal of Cell Biology

283

155

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The cytoplasmic matrix is often highly specialized, making it possible to clearly relate particularaspects ofthe cytoplasmic matrix to the specialized functions of cells . For example, in striated muscle cells the contractile components of the cytoplasmic matrix dominate the cell structurally and functionally. Neurons are another example of cells in which specializations of structure and function can be clearly related to particular aspects of the cytoplasmic matrix (36, 37). The primary function of neurons is to convey information from one location in the organism to another. Pathways for information transfer in the nervous system are provided by specialized neuronal extensions, the axons and the dendrites . Axons, in particular, are specialized to convey information over very long distances, meters in some cases. Accordingly, in the axon the cytoplasmic matrix is specialized to generate and support the extremely elongate shape ofthe axon during development, regeneration, and maturity.To generate and maintain the great volume of cytoplasm within the axon, neurons must produce tremendous amounts of protein (32). Essentially all axonal proteins are synthesized in the neuron cell body and then conveyed into the axon by axonal transport, which provides a lifeline for the axon and its terminus (25,36). Axonal transport is a process that is initiated when the axon first develops and that continues throughout the life of the neuron. To meet the needs of large animals, which require long axons, axonal transport has become one of the most highly developed mechanisms for the intracellular transport of materials in metazoan cells .

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The neuroplasmic network in Loligo and Hermissenda neurons

Cited by 66 publications

References 39 publications

The fibrillar network in the cytoplasm of squid giant axon extracted with saponin.

The fibrillar network in the cytoplasm of squid giant axon extracted with saponin.

Monoclonal antibodies distinguish phosphorylated and nonphosphorylated forms of neurofilaments in situ.

Axonal transport of the cytoplasmic matrix.

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