Axonal transport of phospholipid in goldfish optic system

Grafstein, Bernice; Miller, James A.; Ledeen, Robert W.; Haley, James E.; Specht, Susan C.

doi:10.1016/0014-4886(75)90134-x

Cited by 83 publications

(35 citation statements)

References 50 publications

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“…Present findings also strengthen the emerging view of fast axonal transport as a movement of assembled membrane (1, 9,12,17,25,32). That monensin blocks transport of glycerollabeled material in a manner similar to that of leucine-labeled protein can be added to observed similarities in rates, Q1o values and subcellular distribution (e .g., reference 1) to indicate that fast-transport of lipid and protein are closely interrelated.…”

Section: Discussionsupporting

confidence: 88%

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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Section: Discussionsupporting

confidence: 88%

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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“…This method has been used in the work reported here to investigate the effects of the interruption of protein synthesis on the axonal transport of proteins and lipids. Our objectives were: first, to confirm for our amphibian preparations the reports of Abe et al (1973) and Grafstein et al (1975) that lipid export is dependent on protein synthesis. Secondly, we have investigated whether the interruption of protein synthesis following labelling causes the transport of labelled protein or lipid to cease abruptly or whether axonal transport continues until a labelled pool of these materials is depleted.…”

Section: Introductionmentioning

confidence: 99%

“…Materials which undergo rapid axonal transport are believed to be associated with membranous structures which are possibly in the form of vesicles (Grafstein, 1977; port: protein (Grafstein, 1977), lipid (Abe, Haga & Kurokawa, 1973; Grafstein, Miller, Ledeen, Haley & Specht, 1975), glycoprotein (Edstr6m & Mattsson, 1972b;Forman, Grafstein & McEwen, 1972;Ambron, Goldman, Shkolnik & Schwartz, 1980), and glycolipid (Ambron et al 1975;Sherbany, Ambron & Schwartz, 1979). These studies have provided evidence that the protein and lipid components of rapid axonal transport occur in the same subcellular fractions; proteins and lipids show very similar transport velocities over a range of temperatures and their transport is blocked by mitotic inhibitors.…”

Section: Introductionmentioning

confidence: 99%

“…Mitotic inhibitors are also known to block the rapid anterograde transport of membrane-bound organelles and vesicles (Hammond & Smith, 1977;Smith, 1980). Inhibitors of protein synthesis interrupt the export from the cell body of proteins and glycoproteins (Ochs, Sabri & Ranish, 1970;Grafstein et al 1975; Hines & Garwood, 1977;Forman, McEwen & Grafstein, 1971;Edstrom & Mattsson, 1972b;Ambron et al 1975) and also interrupt the rapid transport of phospholipid (Grafstein et al 1975), glycolipid (Forman et al 1971;Edstrom & Mattsson, 1972b;Sherbany et al 1979), and sulphate-labelled materials (Edstrom & Mattsson, 1972b). Conversely, inhibitors of the synthesis of phospholipids interrupt the export of proteins (Longo & Hammerschlag, 1980).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

The action of puromycin and cycloheximide on the initiation of rapid axonal transport in amphibian dorsal root neurones

Nichols

Smith

Snyder

1982

The Journal of Physiology

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“…Evidence has accumulated for myelin-associated enzyme activity and for interactions between myelin and the axon in the course of myelin development and maintenance. For example, movement of specific lipids between the axon and -myelin has been demonstrated, and this phenomenon may be important for the turnover of myelin components (17)(18)(19). Several enzymes in myelin are concerned with the transport of small molecules (5)(6)(7), suggesting that these enzymes may participate in the removal of metabolites from the axon.…”

mentioning

confidence: 99%

Interactions of dicyclohexylcarbodiimide with myelin proteolipid.

Lin¹,

Lees²

1982

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

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Dicyclohexylcarbodiimide (DCCD) is known to bind preferentially to a proteolipid subunit ofproton-translocating systems and thereby to inhibit proton transport. In the present study we show that, in an aqueous medium, DCCD binds to the bovine white matter proteolipid apoprotein, the major protein of central nervous system myelin. The binding is dependent on time, temperature, and concentration and is not inhibited by the hydrophilic carbodiimide 1-ethyl-3-(3-dimethylaminopropyl)' carbodiimide. By contrast, when the incubation is carried out in chloroform/methanol no labeling by DCCD is demonstrable. In isolated rat myelin, DCCD binds specifically to the proteolipid and not to the myelin basic proteins. Liposomes reconstituted with the myelin proteolipid apoprotein transport protons, as assayed by quenching of the fluorescence of 9-aminoacridine. Preincubation of proteolipid-containing liposomes with DCCD results in an inhibition of transport. These studies have important implications for a possible ionophoric function ofthe myelin proteolipid and for the occurrence of transport processes within myelin.Proteolipids are a class of intrinsic membrane proteins that are characterized by their solubility in chloroform/methanol (1,2). In prokaryotic cells and in the mitochondria of eukaryotic cells, proteolipids associated with the ATPase complex have been shown to be involved in the mechanism of proton translocation (see ref. 3 for review). This proton translocation can be inhibited by dicyclohexylcarbodiimide (DCCD), a lipid-soluble probe that binds to a specific site on proteolipids (4). In the mammalian central nervous system half of the protein of the myelin sheath is a proteolipid protein that is chemically distinct from the DCCD-binding proteolipids identified thus far. Although myelin was for many years considered a metabolically inert membrane that acts only as an insulator around the nerve axon, a reassessment ofthe evidence suggests an involvement ofmyelin in active processes. Several enzymes known to participate in ion transport have been identified in myelin (5-7). In addition, voltage-dependent channels are formed upon incorporation of the myelin proteolipid apoprotein into planar lipid bilayers (8), suggesting participation of this protein in ion transport. The amphipathic properties, conformational flexibility (2), and subunit structure (9) of the myelin proteolipid protein are consistent with this concept. In the present communication the specific binding of DCCD to the proteolipid protein has been demonstrated in isolated myelin. Furthermore, we have shown the occurrence ofproton transport in reconstituted vesicles containing the apoprotein and the inhibition of this transport by DCCD. These data provide additional support for a functional role for the myelin proteolipid.MATERIALS AND METHODS DCCD was obtained from Aldrich and was added to the incubation medium (see below) in 0.05 vol of absolute ethanol. '4C-Labeled DCCD (50 mCi/mmol; 1 Ci = 3.7 x 1010 becquerels) was obtained from Research ...

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Axonal transport of phospholipid in goldfish optic system

Cited by 83 publications

References 50 publications

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

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

The action of puromycin and cycloheximide on the initiation of rapid axonal transport in amphibian dorsal root neurones

Interactions of dicyclohexylcarbodiimide with myelin proteolipid.

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