Triton X-100 extractions of central nervous system myelin indicate a possible role for the minor myelin proteins in the stability of lamellae

Pereyra, Pedro M.; Horvath, E.; Braun, Peter E.

doi:10.1007/bf00973301

Cited by 60 publications

(54 citation statements)

References 43 publications

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“…However, there were significant differences in their contents: OLG plasmalemma was enriched in actin relative to the tubulins; the opposite was the case for myelin. Analysis of purified CNS myelin further indicated that its cytoskeletal matrix includes MBPs and 2',3'-cyclic nucleotide 3'-phosphohydrolases I and 11 (50,51). Whereas these findings do not suggest a function for cytoskeletal elements in myelination, they underscore the likely importance of the codistribution of tau and MBP observed in our studies.…”

Section: Discussioncontrasting

confidence: 48%

Functional implications for the microtubule-associated protein tau: localization in oligodendrocytes.

LoPresti¹,

Szuchet

Papasozomenos³

et al. 1995

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

343

260

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We present evidence that the microtubuleassociated protein tau is present in oligodendrocytes (OLGs), the central nervous system cells that make myelin. By showing that tau is distributed in a pattern similar to that of myelin basic protein, our results suggest a possible involvement of tau in some aspect of myelination. Tau protein has been identified in OLGs in situ and in vitro. In interfascicular OLGs, tau localization, revealed by monoclonal antibody Tau-5, was confined to the cell somata. However, in cultured ovine OLGs with an exuberant network of processes, tau was detected in cell somata, cellular processes, and membrane expansions at the tips of these processes. Moreover, in such cultures, tau appeared localized adjacent to or coincident with myelin basic protein in membrane expansions along and at the ends of the cellular processes. The presence of tau mRNA was documented using fluorescence in situ hybridization. The distribution of the tau mRNA was similar to that of the tau protein.Western blot analysis of cultured OLGs showed the presence of many tau isoforms. Together, these results demonstrate that tau is a genuine oligodendrocyte protein and pave the way for determining its functional role in these cells.

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Section: Discussioncontrasting

confidence: 48%

Functional implications for the microtubule-associated protein tau: localization in oligodendrocytes.

LoPresti¹,

Szuchet

Papasozomenos³

et al. 1995

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

343

260

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“…The combination of biochemical studies with these photophysical, microfluorimetric methods will yield a better insight in the biological relevance of rafts in OLGs and help to come to a consensus on lipid rafts concerning their existence, size, lifetime and molecular organization. Pereyra et al 1988 4 to 6-weeks-old rat TX-100 0.5% 3 min RT Gillespie et al 1989 35-days-old mice TX-102 1% 30 min 4°C Taylor et al 2002 4-months-old mice: WT and MAL KO CHAPS na 30 min 4°C Schaeren-Wiemers et al 2004 Purified myelin Bovine brain E29 -E40 CHAPS 1.5% 30 min 4°C Debruin et al 2005 …”

Section: Perspectivesmentioning

confidence: 99%

“…Mouse OLG 5 DIV CHAPS 20 mM 30 min 4°C 30-days-old rat TX-100 1% 30 min 4°C Kim and Pfeiffer 1999 4-6 weeks old rat TX-100 0.5% 3 min RT Gillespie et al 1989 35-days-old mice TX-100 / CHAPS / Brij 96V / TX-102 1% 30 min 4°C/37°C Taylor et al 2002 2-year-old mice TX-100 2% 30 min 4°C Saravanan et al 2004 TX-100 1% na 4°C Mouse CHAPS 30 mM na 4°C Boyanapalli et al 2005 Rabbit TX-100 1% 16h + 24h 4°C Pereyra et al 1988 Purified myelin Bovine brain E11 -E40 CHAPS 1.5% 30 min 4°C Debruin et al 2005 Primary OLGs 1-2 day old rat brain OLGs 12 DIV TX-100 0.5% 3 min RT Wilson and Brophy 1989 CNP Optic nerve p13, p18, p24 and 2 months old rat TX-100 1% 1h 4°C Maier et al 2005 Primary OLGs premyelinating mouse OLGs TX-100 1% 1h 4°C Schafer et al 2004 TX-100 1% 30 min 4°C Spinal cord Rat (WT or EAE) Lubrol WX 0.5% 30 min 4°C Maier et al 2005 Optic nerve p13, p18, p24 and 2 months old rat TX-100 1% 1h 4°C Schafer et al 2004 35-days-old mice TX-100 / CHAPS / Brij 96V / TX-102 1% 30 min 4°C Taylor et al 2002 Adult mouse brain TX-100 2% 30 min 4°C Krämer et al 1997Krämer et al , 1999 Purified myelin 2-year-old mice TX-100 2% 30 min 4°C Saravanan et al 2004 Mouse OLGs 5/8 DIV TX-100 2% 30 min 4°C Krämer et al 1997Krämer et al , 1999 Primary OLGs Mouse OLG 5 DIV CHAPS 20 mM 30 min 4°C NCAM 120…”

Section: Primary Olgsmentioning

confidence: 99%

Rafts in oligodendrocytes: Evidence and structure–function relationship

Gielen

Baron

vandeVen

et al. 2006

Glia

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“…In addition MBP and 2' ,3 '-cyclic nucleotide 3 '-phosphohydrolase (CNPase) associate with a cytoskeletal fraction that includes actin and microtubule proteins but not intermediate filaments (Gillespie et al, 1989;Pereyra et al, 1988;Wilson and Brophy, 1989;Dyer and Benjamins 1989 (Hirokawa et al, 1982;Shiomura et al, 1987a,b;SatoYoshitake, et al, 1989). In addition.…”

Section: Introductionmentioning

confidence: 95%

Microtubule associated protein (MAP1B) is present in cultured oligodendrocytes and co‐localizes with tubulin

Fischer

Konola

Cochary

1990

J of Neuroscience Research

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Differentiation of oligodendrocytes is accompanied by the extension of processes and the assembly of the myelin membrane. It is likely that the cytoskeleton plays an important role in this process in terms of changes in cell shape, transport of myelin components, and organization of the myelin membrane. Oligodendrocytes contain microtubules (MT) which associate with other components of the cytoskeleton, and microtubule associated proteins (MAPs) may mediate some of these interactions. In this study we have shown the presence of MAP1B in oligodendrocytes grown in primary glial cultures by double-label immunofluorescence using antibodies to galactocerebroside (GC) and MAP1B. The staining of the cultures showed that GC-positive oligodendrocytes were also stained with MAP1B antibodies. However, MAP1B stain was limited to cell bodies and processes, whereas GC stain was also seen in flattened membrane sheets and punctate staining in processes. MAP1B staining was also compared with that of myelin proteolipid (PLP), myelin basic protein (MBP) and beta-tubulin in secondary glial cultures that were enriched for oligodendrocytes. The results showed a typical staining of cell bodies and membranous profiles using PLP antibodies, and the staining of cell bodies and flattened regions of membranous sheets by MBP antibodies. In contrast, both polyclonal and monoclonal antibodies to MAP1B showed a uniform diffuse staining of cell bodies, major processes, and fine interconnected processes. Double-labeling of the cells showed that MAP1B was co-localized with tubulin, but was not present in glial fibrillary acidic protein (GFAP)-positive astrocytes. Western and Northern blot analyses of primary glial cultures showed that MAP1B had a molecular mass of 320 kDa and a mRNA of 10 kb. These values are identical to those previously reported for brain MAP1B (Safaei and Fischer, 1989) and demonstrate the presence of MAP1B in oligodendrocytes.

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Triton X-100 extractions of central nervous system myelin indicate a possible role for the minor myelin proteins in the stability of lamellae

Cited by 60 publications

References 43 publications

Functional implications for the microtubule-associated protein tau: localization in oligodendrocytes.

Functional implications for the microtubule-associated protein tau: localization in oligodendrocytes.

Rafts in oligodendrocytes: Evidence and structure–function relationship

Microtubule associated protein (MAP1B) is present in cultured oligodendrocytes and co‐localizes with tubulin

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