Solubilization of Myelin Membranes by Detergents

Aveldaño, Marta I.; Díaz, R. S.; Regueiro, Pilar; Monreal, J.

doi:10.1111/j.1471-4159.1991.tb02122.x

Cited by 20 publications

(6 citation statements)

References 29 publications

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“…To characterize the myelin rafts further, the myelin CHAPS lysis included 500 mM NaCl to diminish possible protein–protein and/or protein–lipid electrostatic interactions, or the myelin membranes were pretreated with mβCD prior to CHAPS extraction to deplete the cholesterol. In general, the presence of salts increased the solubilization of myelin proteins by detergents including CHAPS (Aveldano et al, 1991). With the addition of NaCl, there was no disruption of the integrity of myelin rafts, and the peripheral membrane proteins MBP and CNP remained raft associated (results not shown).…”

Section: Resultsmentioning

confidence: 99%

Developmental partitioning of myelin basic protein into membrane microdomains

et al. 2005

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Specific membrane microdomains (including lipid rafts) exist in myelin but have not been fully characterized. Myelin basic protein (MBP) maintains the compactness of the myelin sheath and is highly posttranslationally modified. Thus, it has been suggested that MBP might also have other functions, e.g., in signal transduction. Here, the distribution of MBP and its modified forms was studied, spatially and temporally, by detailed characterization of membrane microdomains from developing and mature bovine myelin. Myelin membranes were extracted with three different detergents (Brij 96V, CHAPS, or Triton X-100) at 4 degrees C. The detergent-resistant membranes (DRMs), representing coalesced lipid rafts, were isolated as low-buoyant-density fractions on a sucrose density gradient. These myelin rafts were disrupted when cholesterol was depleted with methyl-beta-cyclodextrin. The use of CHAPS detergent led to enrichment of several myelin proteins, including phospho-Thr97-MBP, in the DRMs from mature myelin. Citrullinated and methylated MBP remained in "nonraft" microdomains. In contrast, the DRMs from early myelin were enriched in Golli-MBP, Fyn, Lyn, and CNP. The localization of various proteins in DRMs was further supported by the colocalization of these lipid raft components in cultured mouse oligodendrocytes. Thus, there is a developmental regulation of posttranslationally modified forms of MBP into specific membrane microdomains.

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Section: Resultsmentioning

confidence: 99%

Developmental partitioning of myelin basic protein into membrane microdomains

et al. 2005

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“…VLC-PUFAs with more than 28 carbon atoms are also detected in retina and brain. However, in retina and brain these VLC-PUFAs are part of phosphoglycerolipids like phosphatidylcholine [12][13][14][15][16], for a detailed review see [8].…”

Section: Spermatozoa/testes and Fertilitymentioning

confidence: 99%

Very long chain sphingolipids: Tissue expression, function and synthesis

Sandhoff

2009

FEBS Letters

110

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a b s t r a c tForecort membranes of all mammalian cells contain, in addition to phosphoglycerolipids and cholesterol, substantial amounts of sphingolipids. In most cells the acyl moieties of these sphingolipids are of long chain type (C16-24) and often saturated. However, epidermal keratinocytes and male germ cells largely express sphingolipids with very long chain-acyl moieties (C26-C36) during their differentiation and maturation. This expression seems to depend on CerS3, one of six ceramide synthases. However, the complex biosynthetic sequence for both epidermal and testicular sphingolipids has not been elucidated completely. Whereas it is established that omega-hydroxylated very long chain-sphingolipids are essential for proper skin barrier function, the role of polyunsaturated very long chain-sphingolipids (ceramides, sphingomyelins and glycosphingolipids) in differentiating spermatocytes/spermatids is just beginning to be revealed.

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“…Following ultracentrifugation (100,000 ϫ G, 18˚C, 30 minutes), the supernatant was collected and stored at -20˚C until further use. 1 …”

Section: Preparation Of Myelin Membrane Substrates and Mpesmentioning

confidence: 99%

Inhibition of oligodendrocyte precursor cell differentiation by myelin-associated proteins

Syed¹,

Baer²,

Lubec³

et al. 2008

FOC

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Object Promoting repair of central nervous system (CNS) white matter represents an important approach to easing the course of a number of tragic neurological diseases. For this purpose, strategies are currently being evaluated for transplanting cells capable of generating new oligodendrocytes into areas of demyelination and/or enhancing the potential of endogenous stem/precursor cells to give rise to new oligodendrocytes. Emerging evidence, however, indicates that increasing the presence of cells capable of forming new myelin sheaths is not sufficient to promote repair because of unknown inhibitors that accumulate in lesions as a consequence of myelin degeneration and impair the generation of new oligodendrocytes. The aim of the present study was to characterize the nature of the inhibitory molecules present in myelin. Methods Differentiation of primary rat oligodendrocyte precursor cells (OPCs) in the presence of CNS and peripheral nervous system myelin was assessed by immunocytochemical methods. The authors further characterized the nature of the inhibitors by submitting myelin membrane preparations to biochemical precipitation and digestion. Finally, OPCs were grown on purified Nogo-A, oligodendrocyte myelin glycoprotein, and myelin-associated glycoprotein, the most prominent inhibitors of axon regeneration. Results Myelin membrane preparations induced a differentiation block in OPCs that was associated with down-regulation of expression of the transcription factor Nkx2.2. The inhibitory activity in myelin was restricted to the CNS and was predominantly associated with white matter. Furthermore, the results demonstrate that myelin proteins that are distinct from the most prominent inhibitors of axon outgrowth are specific inhibitors of OPC differentiation. Conclusions The inhibitory effect of unknown myelin-associated proteins should be considered in future treatment strategies aimed at enhancing CNS repair.

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Solubilization of Myelin Membranes by Detergents

Cited by 20 publications

References 29 publications

Developmental partitioning of myelin basic protein into membrane microdomains

Developmental partitioning of myelin basic protein into membrane microdomains

Very long chain sphingolipids: Tissue expression, function and synthesis

Inhibition of oligodendrocyte precursor cell differentiation by myelin-associated proteins

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