The flow of mitochondria in chicken sciatic nerve

Jeffrey, Peter L.; James, K. A. C.; Kidman, Antony D.; Richards, Alison; Austin, L.

doi:10.1002/neu.480030303

Cited by 37 publications

(18 citation statements)

References 21 publications

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“…The intra-axonal transport of mitochondria has previously been demonstrated in a number of systems (12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23)(24). Although a few of these previous studies have suggested a relatively rapid movement of mitochondria (e.g., refs.…”

Section: Discussionmentioning

confidence: 99%

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Subcellular fractionation of intra-axonally transport polypeptides in the rabbit visual system.

Lorenz¹,

Willard²

1978

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

114

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We analyzed the subcellular distributions of proteins that are transported down the axons of rabbit retinal ganglion cells and compared these distributions to those of enzyme markers for endoplasmic reticulum, plasma membrane, and mitochondria. The proteins of each of five previously identified transport groups were uniquely distributed through the subcellular fractions, suggesting that each transport group is associated with different subcellular organelles. In particular, all of the observed group I polypeptides (the most rapidly moving group, maximum velocity > 240 mm/day) were associated with material of hydrodynamic properties similar to those of the plasma membrane. The proteins of group II (maximum velocity = 34-68 mm/day) were heterogeneous in their subcellular distributions but included mitochondrial proteins. Groups III and IV (maximum velocity = 4-8 and 2-4 mm/day, respectively) included materials that may be involved in motile processes; group V (maximum velocity = 0.7-1.1 mm/day) contained material of very high density which may be associated with neurofilaments. Many of the proteins required by the axons and synaptic terminals of neurons are synthesized in the neuronal cell bodies and conveyed to their destinations by the process of intra-axonal transport. The identities and organization of the transported proteins are of interest not only because of the importance of these proteins in axonal and synaptic functions but also because their transport may represent a modification of transport processes used to convey proteins over less dramatic distances in other cell types.In the retinal ganglion cells of the rabbit, the intra-axonal transport of proteins appears to be a complex but highly organized process. Proteins synthesized in the cell bodies of these neurons can be labeled with radioactive amino acids injected into the vitreous of the eye, and the labeled transported proteins can be subsequently monitored as they move down the axons.[The axons of the retinal ganglion cells pass through the optic nerve (ON) and contralateral optic tract (OT), a total distance of about 3 cm, to form synapses in the lateral geniculate nucleus (LGN) and superior colliculus (SC)]. We previously used sodium dodecyl sulfate/polyacrylamide gel electrophoresis followed by autoradiography of the gels to resolve more than 40 of the transported polypeptides; these polypeptides can be assigned to at least five groups, according to the time at which they first appear in labeled form in segments of the ON and OT-i.e., according to their maximum transport velocities (1, 2). The significance of this organization is not understood; however, the principles governing this grouping could be reflected in the subcellular associations of the polypeptides within each group.We have therefore begun to analyze the subcellular distributions of the transported polypeptides in homogenates of the ON and OT (which contain the axons of the retinal ganglion cells) as well as of the LGN and SC (which contain nerve endings in addition to t...

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Section: Discussionmentioning

confidence: 99%

“…5 shows the arrival of group V polypeptides (those transported at a maximum velocity of 0.7-1.1 mm/day) [e.g., H(9),] 45, and 46 (2) in ON + OT by 16 days after the retina was labeled. Group V included material that was denser than mitochondria.…”

Section: Methodsmentioning

confidence: 99%

Subcellular fractionation of intra-axonally transport polypeptides in the rabbit visual system.

Lorenz¹,

Willard²

1978

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

114

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“…Verification of these issues needs quantitative analysis of in situ hybridization at the EM level. It is also possible that different levels of mitochondrial-encoded proteins may be caused by posttranslationally regulatory mechanisms, such as mitochondrial redistribution (Banks et al, 1969;Jeffrey et al, 1972;Morris and Hollenbeck, 1993). The greater consumption of energy in functionally active regions could lead to a local increase in ADP/ATP ratio, which can signal mitochondria to cease movement, resulting in clustering of mitochondria in regions of high ATP demand (Bereiter-Hahn and Voth, 1983).…”

Section: Factors Attributing To the Local Differential Levels Of Co Smentioning

confidence: 97%

Mitochondrial- and nuclear-encoded subunits of cytochrome oxidase in neurons: Differences in compartmental distribution, correlation with enzyme activity, and regulation by neuronal activity

Nie

Wong‐Riley

1996

J. Comp. Neurol.

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Cytochrome oxidase (CO), a mitochondrial energy-generating enzyme, contains both mitochondrial- and nuclear-encoded subunits. In neurons, local levels of CO activity vary among different neuronal compartments, reflecting local demands for energy. The goals of the present study were to determine if compartmental distribution of CO subunit proteins from the two genomes was correlated with local CO activity, and if their expression was regulated proportionately in neurons. The subcellular distributions of mitochondrial-encoded CO III and nuclear-encoded CO Vb proteins were quantitatively analyzed in mouse cerebellar sections subjected to postembedding immunocytochemistry. Local levels of subunit proteins were also compared to local CO activity, as revealed by CO cytochemistry. In order to study the regulation of subunit protein expression, we assessed changes in immunoreactivity of the two CO subunits as well as changes in CO activity in mouse superior colliculus after 1 to 7 days of monocular enucleation. We found that immunoreaction product for both CO III and CO Vb existed almost exclusively in mitochondria, but their compartmental distributions were different. CO III was nonhomogeneously distributed among different neuronal compartments, where its local level was positively correlated with that of CO activity. In contrast, the subcellular distribution of CO Vb was relatively uniform and did not bear a direct relationship with that of CO activity. Moreover, the two subunit proteins were disproportionately regulated by neuronal activity. CO III and CO activity exhibited parallel decreases after the deprivation of afferent input, and their changes were earlier and to a greater degree than that of CO Vb proteins. Thus, the present findings indicate that the local expression and/or distribution of CO subunit proteins from the two genomes may involve different regulatory mechanisms in neurons. Our data also suggest that the activity-dependent regulation of mitochondrial-encoded CO subunits is likely to play a major role in controlling the local levels of CO content and its activity.

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“…Certain oxidative enzymes may be used as mitochondrial markers (Banks et al 1969;Partlow et al 1972), but the mitochondria of Schwann cells constitute by far the largest share of the total mitochondrial population of the nerve and they may, in addition, be altered by experimental techniques of ligature or of injury to the nerve. Isotopic tracers (Jeffery, James, Kidman, Richards & Austin 1972;Elam & Agranoff 1971), on the other hand, possess low specificity and may be subject to redistribution among other axoplasmic organelles upon release from mitochondria.…”

Section: Discussionmentioning

confidence: 99%

The relation of axonal transport of mitochondria with microtubules and other axoplasmic organelles.

Friede¹,

Ho²

1977

The Journal of Physiology

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SUMMARYAxonal transport of mitochondria was studied in frog sciatic nerves incubated in agents selected for their known or alleged effect on microtubules or axonal flow.Quantitative data on mitochondria, microtubules, neurofilaments, endoplasmic reticulum, and cross-sectional area of the axon indicate that axonal transport of mitochondria is dependent on microtubules. When more than half of the microtubules are destroyed, the axonal transport of mitochondria is diminished in proportion to the destruction of microtubules.Axonal transport of mitochondria is not related to neurofilaments and endoplasmic reticulum.Changes in the cross-sectional area of axons, even upon reduction to half the normal size, do not noticeably affect mitochondrial transport.Cyanide which blocks oxidative metabolism also blocks axonal transport of mitochondria, but analysis of fine structure indicates that cyanide is destructive to microtubules as well.

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The flow of mitochondria in chicken sciatic nerve

Cited by 37 publications

References 21 publications

Subcellular fractionation of intra-axonally transport polypeptides in the rabbit visual system.

Subcellular fractionation of intra-axonally transport polypeptides in the rabbit visual system.

Mitochondrial- and nuclear-encoded subunits of cytochrome oxidase in neurons: Differences in compartmental distribution, correlation with enzyme activity, and regulation by neuronal activity

The relation of axonal transport of mitochondria with microtubules and other axoplasmic organelles.

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