Axonal Transport of Complex Carbohydrates

Elam, John S.

doi:10.1007/978-1-4613-2925-1_12

Cited by 20 publications

(19 citation statements)

References 110 publications

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“…However, the methods used in this study would not detect many of the structural changes that might occur in chains subsequent to transport. Peripheral modification of glycoproteins has been demonstrated in single axons ofAplysia (Ambron and Treistman, 1977) and has been widely speculated in vertebrate studies (Elam, 1979). The significantly lower specific radioactivity of some glycopeptides of the soluble fraction may reflect the presence of molecules that are modified subsequent to transport and are not yet labeled.…”

Section: Discussionmentioning

confidence: 95%

“…Previous studies in our laboratory provided evidence for r a p i d a x o n a l t r a n s p o r t of "SO, or [3H]glucosamine-labeled glycoconjugates in t h e garfish olfactory nerve (Elam andPeterson, 1976, 1979). Limit protease digestion of the molecules in transit showed the presence of the GAGs heparan sulfate and chondroitin sulfate as well as varioussized glycopeptide chains.…”

Section: Studies On a Variety Of Experimental Preparationsmentioning

confidence: 88%

“…have documented the axonal transport of glycoproteins (for review see Elam, 1979; see also Lavoie et al, 1978;Giulian et al, 1980;Griffin et al, 1981;Karlsson, 1980;Padilla and Morell, 1980;Tessler et al, 1980;Tytell et al, 1980) while a more limited number of studies have provided evidence for the transport of glycosaminoglycans (GAGS) (Elam et al, 1970;Elam and Peterson, 1976;Karlsson and Linde, 1977;Goodrum e t al., 1979;Elam, 1979). A number of these investigations have examined the subaxonal distribution of transported glycoconjugates in both nerve (Forrnan, 1971;Edstrom and Mattson, 1972;Frizell and Sjostrand, 1974;Ambron et al, 1974;Thompson et al, 1976;Griffin et al, 1981;Tessler et al, 1980) and nerve terminals (Karlsson and Sjostrand, 1971;Elam and Agranoff, 1971;McEwen et al, 1971;Bennett et al, 1973;Marko and Cuenod, 1973;DiGiamberardino et al, 1973;Goodrum et al, 1979).…”

Section: Studies On a Variety Of Experimental Preparationsmentioning

confidence: 99%

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Composition and Subcellular Distribution of Glycoproteins and Glycosaminoglycans Undergoing Axonal Transport in Garfish Olfactory Nerves

Elam

1982

Journal of Neurochemistry

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The study examined the subcellular distribution of [3H]glucosamine-labeled glycoconjugates undergoing axonal transport in 100,000 x g soluble and two membranous subfractions of the garfish olfactory nerve. Analysis was made of intact glycoconjugates and of glycopeptides and glycosaminoglycans derived from these molecules by limit protease digestion. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed labeling of a variety of high-molecular-weight molecules with a lower molecular weight distribution in the soluble fraction than in the membranous fractions. Following protease digestion, nearly two-thirds of transported radioactivity in glycopeptides was recovered in the plasma membrane-enriched subfraction, with the remainder equally divided between soluble and higher density membrane fraction. Comparison of the distribution of glycopeptide radioactivity and chemically assayed hexosamine revealed transport labeling of a large variety of different-sized neutral and acidic glycopeptides in all subfractions. Transport labeling of most glycoprotein carbohydrate chains was in proportion of their hexosamine content. Transported glycosaminoglycan label was most heavily concentrated in the plasma membrane fraction, whereas hexosamine was most concentrated in the higher density membrane fraction. The labeling pattern suggested both transported and nontransported pools of these molecules. The specific glycosaminoglycans chondroitin sulfate and heparan sulfate were recovered in all subfractions, whereas hyaluronic acid was confined to the soluble fraction.

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Section: Discussionmentioning

confidence: 95%

Section: Studies On a Variety Of Experimental Preparationsmentioning

confidence: 88%

Section: Studies On a Variety Of Experimental Preparationsmentioning

confidence: 99%

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Composition and Subcellular Distribution of Glycoproteins and Glycosaminoglycans Undergoing Axonal Transport in Garfish Olfactory Nerves

Elam

1982

Journal of Neurochemistry

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“…Association between the transmitter-synthesizing enzymes, dopamine-, 8- nocytochemical techniques (3,27). Finally, at least one group of fast-transported proteins, the glycoproteins, must pass through the GA (8,16), since this intracellular site contains the glycosyltransferases for completing carbohydrate side chains (23,31) .…”

mentioning

confidence: 99%

Evidence that all newly synthesized proteins destined for fast axonal transport pass through the Golgi apparatus.

Hammerschlag¹,

Stone²,

Bolen³

et al. 1982

The Journal of Cell Biology

124

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Effects of the sodium ionophore, monensin, were examined on the passage from neuronal cell body to axon of materials undergoing fast intracellular transport. In vitro exposure of bullfrog dorsal root ganglia to concentrations of drug <1 .0 UM led to a dose-dependent depression in the amount of fast-transported [3H]leucine-or [3H]glycerol-labeled material appearing in the nerve trunk. Incorporation of either precursor was unaffected . Exposure of a desheathed nerve trunk to similar concentrations of monensin, while ganglia were incubated in drug-free medium, had no effect on transport. With [3H]fucose as precursor, fast transport of labeled glycoproteins was depressed to the same extent as with [3H]leucine; synthesis, again, was unaffected . By contrast, with [3 H]galactose as precursor, an apparent reduction in transport of labeled glycoproteins was accounted for by a marked depression in incorporation . The inference from these findings, that monensin acts to block fast transport at the level of the Golgi apparatus, was supported by ultrastructural examination of the drug-treated neurons. An extensive and selective disruption of Golgi saccules was observed, accompanied by an accumulation of clumped smooth membranous cisternae.Quantitative analyses of 48 individual fast-transported protein species, after separation by two-dimensional gel electrophoresis, revealed that monensin depresses all proteins to a similar extent . These results indicate that passage through the Golgi apparatus is an obligatory step in the intracellular routing of materials destined for fast axonal transport.

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“…Studies specifically of glycoprotein transport have been conducted primarily in the visual system (for example, Karlsson and Sjostrand, 1971;Specht and Grafstein, 1977;Goodrum et al, 1979;Goodrum and Morell, 1982) and in other cranial nerves DiGiamberardino et al, 1973;Frizell and Sjostrand, 1974;Elam and Peterson, 1979;Tytell et al, 1980), although several other tracts located entirely within the CNS have also been investigated (Levin, 1977;Padilla and Morell, 1980;Roger et al, 1980). Fucosylated glycoproteins are rapidly transported, primarily as particulate material, and are destined primarily for nerve endings (for reviews, see Elam, 1979;Grafstein and Forman, 1980). However, autoradiographic studies have indicated that some transported glycoproteins are deposited in axolemma (Griffin et al, 1981), and we have recently demonstrated that two trans-ported fucosylated glycoproteins are preferentially deposited in the axons of the rat optic pathway (Goodrum and Morell, 1982).…”

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confidence: 99%

Axonal Transport and Metabolism of Glycoproteins in Rat Sciatic Nerve

Toews

Saunders

Morell

1982

Journal of Neurochemistry

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The axonal transport and metabolism of glycoproteins in sciatic nerve sensory axons were examined from 2 h to 7 weeks following injection of [3H]fucose into the 5th lumbar dorsal root ganglion of adult rats. Incorporation of fucose into glycoproteins was prolonged; only half of the 3H label in the ganglion was acid‐insoluble after 4 h, and maximal labeling did not occur until approximately 24 h after injection. [3H]Glycoproteins were transported distally at a rate of approximately 310 mm per day after a synthesis and/or processing lag of approximately 40 min. Gel electrophoresis demonstrated that many glycoproteins were transported, including prominent labeled species having apparent M.W. of approximately 49,000, 90,000, 118,000, and 132,000. With increasing time after injection, a peak with an apparent M.W. of 49,000 accounted for an increasing proportion of the total label in the nerve. The accumulation of this glycoprotein (possibly a subunit of Na+,K+‐ATPase, an enzyme known to be present in axolemma) was due in part to its preferential deposition in the axons, while other glycoproteins passed through the axons directly to the nerve terminals. Radioactivity in another labeled glycoprotein, with an apparent M.W. of 30,000, also increased preferentially in the nerve relative to other labeled glycoproteins. This was shown to be the myelin P0 protein. This protein was not transported from the ganglion; rather, its increased prominence with time in the nerve was due both to a decrease in amounts of other labeled species and to an absolute increase in labeling of the P0 protein, possibly due to reutilization by the Schwann cells of fucose released during turnover of labeled glycoproteins delivered to the axons by axonal transport.

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Axonal Transport of Complex Carbohydrates

Cited by 20 publications

References 110 publications

Composition and Subcellular Distribution of Glycoproteins and Glycosaminoglycans Undergoing Axonal Transport in Garfish Olfactory Nerves

Composition and Subcellular Distribution of Glycoproteins and Glycosaminoglycans Undergoing Axonal Transport in Garfish Olfactory Nerves

Evidence that all newly synthesized proteins destined for fast axonal transport pass through the Golgi apparatus.

Axonal Transport and Metabolism of Glycoproteins in Rat Sciatic Nerve

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