Vesicular transport of sulfatide in the myelinating mouse brain. Functional association with lysosomes?

Burkart, Thomas; Caimi, Luigi; Siegrist, H P; Herschkowitz, N; Wiesmann, Ulrich

doi:10.1016/s0021-9258(19)81088-8

Cited by 37 publications

(1 citation statement)

References 27 publications

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“…Other insights into intracellular ganglioside transport have been provided by experiments on neuroblastoma and glial cells in culture (Miller-Podraza & Fishman, 1982. The actual mecha-nism^) of glycolipid movement in cells remain(s) poorly elucidated although both vesicular and protein-associated glycolipid transport have been suggested (Burkart et al, 1982;Sonnino et al, 1979;Tettamanti, 1984).…”

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confidence: 99%

Spontaneous transfer of ganglioside GM1 between phospholipid vesicles

Brown¹,

Thompson²

1987

Biochemistry

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The transfer kinetics of the negatively charged glycosphingolipid II3-N-acetylneuraminosyl-gangliotetraosylceramide (GM1) were investigated by monitoring tritiated GM1 movement between donor and acceptor vesicles. After appropriate incubation times at 45 degrees C, donor and acceptor vesicles were separated by molecular sieve chromatography. Donors were small unilamellar vesicles produced by sonication, whereas acceptors were large unilamellar vesicles produced by either fusion or ethanol injection. Initial GM1 transfer to acceptors followed first-order kinetics with a half-time of about 40 h assuming that GM1 is present in equal mole fractions in the exterior and interior surfaces of the donor vesicle bilayer and that no glycolipid flip-flop occurs. GM1 net transfer was calculated relative to that of [14C]cholesteryl oleate, which served as a nontransferable marker in the donor vesicles. Factors affecting the GM1 interbilayer transfer rate included phospholipid matrix composition, initial GM1 concentration in donor vesicles, and the GM1 distribution in donor vesicles with respect to total lipid symmetry. The findings provide evidence that GM1 is molecularly dispersed at low concentrations within liquid-crystalline phospholipid bilayers.

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confidence: 99%

Spontaneous transfer of ganglioside GM1 between phospholipid vesicles

Brown¹,

Thompson²

1987

Biochemistry

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Temporal and spatial profiles of ABCA2‐expressing oligodendrocytes in the developing rat brain

Tanaka

Yamada

Zhou

et al. 2002

J of Comparative Neurology

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ABCA2 protein belongs to the ABCA subclass of ATP-binding cassette (ABC) transporters proposed to exert critical functions in transmembrane transport of endogenous lipids. In this study, we found by immunoblot analyses that approximately 260 kDa of ABCA2 protein is expressed predominantly in oligodendrocytes, and that the expression of the protein is upregulated in the brain during maturation, especially between postnatal days 6 and 19. Parallel to the changes in expression of ABCA2, immunohistochemical analyses showed rapid spatial spread of ABCA2-immunolabeled oligodendrocytes in the brain during this period. These temporal and spatial changes in ABCA2 expression were in good agreement with findings in myeloarchitectonics reported previously. Further, double immunolabeling with ABCA2 and a major structural protein of myelin, myelin basic protein, demonstrated that onset of ABCA2 expression in oligodendrocytes coincides with the appearance of thick myelin segments immunolabeled with myelin basic protein. Because ABCA2 was abundantly expressed in adult cortex in white matter and gray matter, coexpression of ABCA2 and a marker for the oligodendroglial progenitors NG2 or platelet-derived growth factor alpha receptor was investigated. No cells coexpressing ABCA2 and the marker were observed, suggesting that ABCA2 is expressed predominantly in myelin-forming oligodendrocytes distinct from the adult oligodendroglial progenitors tested. These results suggested a role for ABCA2 in membrane transport of substrates such as the lipids that are closely linked to myelination processes.

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Membrane traffic in myelinating oligodendrocytes

Krämer

Schardt

Nave

2001

Microscopy Res & Technique

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In the central nervous system (CNS), the myelin sheath is synthesised by oligodendrocytes as a specialised subdomain of an extended plasma membrane, reminiscent of the segregated membrane domains of polarised cells. Myelination takes place within a relatively short period of time and oligodendrocytes must have adapted membrane sorting and transport mechanisms to achieve such a high rate of myelin synthesis and to maintain the unique organisation of the myelin membrane. In adult life, maintenance of the functional myelin sheath requires a carefully orchestrated balance of myelin synthesis and turnover. Imbalance in these processes may cause dys- or demyelination and disease. This review summarises what is currently known about myelin protein trafficking and mistrafficking in oligodendrocytes. We also present data demonstrating distinct transport pathways for myelin structural proteins and the expression of SNARE proteins in differentiating oligodendrocytes. Myelinating glial cells may well serve as a model system for studying general aspects of membrane trafficking and organisation of membrane domains.

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Vesicular transport of sulfatide in the myelinating mouse brain. Functional association with lysosomes?

Cited by 37 publications

References 27 publications

Spontaneous transfer of ganglioside GM1 between phospholipid vesicles

Spontaneous transfer of ganglioside GM1 between phospholipid vesicles

Temporal and spatial profiles of ABCA2‐expressing oligodendrocytes in the developing rat brain

Membrane traffic in myelinating oligodendrocytes

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