Pelizaeus-Merzbacher Disease: Biochemical Analysis of Isolated Myelin (Electron-Microscopy;Protein, Lipid and Unsubstituted Fatty Acids Analysis)

Bourre, Jean‐Marie; Jacque, C.; Nguyen‐Legros, Jeanine; Bornhofen, John H.; Araoz, C.; O, Daudu; Baumann, Nicole

doi:10.1159/000114969

Cited by 19 publications

(9 citation statements)

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“…Lipids and fatty acids were extracted, identified and measured as previously described (12). Eventually, brains were homogenized in water, and the 100,000 g supernatant was put on a sucrose gradient in a zonal rotor (0.4 M-l. 2.M).…”

Section: Methodsmentioning

confidence: 99%

Influence of Intrauterine Malnutrition on Brain Development: Alteration of Myelination

Bourre¹,

Morand²,

Chanez³

et al. 1981

Neonatology

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As compared to other organs, in intrauterine growth retardation brain is less affected; however, forebrain weight and total lipids are reduced. Myelin quantity is reduced by 27, 17, 9 and 6% at 15, 18, 30 and 60 days after birth, respectively. Thus, intrauterine undernutrition followed by normal diet after birth affects myelination, a postnatal event. Prenatal growth retardation moderately but irreversibly impairs brain maturation, whereas the composition of myelin during maturation is close to normal (when density profile, lipid amount and the fatty acid pattern are considered).

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Section: Methodsmentioning

confidence: 99%

Influence of Intrauterine Malnutrition on Brain Development: Alteration of Myelination

Bourre¹,

Morand²,

Chanez³

et al. 1981

Neonatology

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mentioning

confidence: 89%

“…PLP and DM20 may have a relationship similar to that found among the four MBPs, since they have identical amino-and carboxyl-terminal sequences (46), and they are very closely related by amino acid composition and by antigenic characteristics. The expression of these myelin proteins correlates closely with the formation of myelin in the developing rat brain, and mouse mutants that are defective in myelin formation show lowered levels of these myelin proteins (4,14,20,25 expression and the genetic deficiency in the shiverer mouse myelination mutant (12,34,44). Several groups have recently isolated cDNA clones for the other major myelin protein, PLP, and have studied PLP mRNAs in bovine and rat tissue (11,13,27, 29).…”

mentioning

confidence: 99%

Characterization of myelin proteolipid mRNAs in normal and jimpy mice.

Gardinier¹,

Macklin²,

Diniak³

et al. 1986

Mol. Cell. Biol.

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A clone specific for the rat myelin proteolipid protein (PLP) was isolated from a cDNA library made in pUC18 from 17-day-old rat brain stem mRNA. This clone corresponded to the carboxyl-terminal third of the PLP-coding region. The clone was used to identify PLP-specific mRNAs in mouse brain and to establish the time course of PLP mRNA expression during mouse brain development. Three PLP-specific mRNAs were seen, approximately 1,500, 2,400, and 3,200 bases in length, of which the largest was the most abundant. During brain development, the maximal period of PLP mRNA expression was from 14 to 25 days of age, and this was a similar time course to that for myelin basic protein mRNA expression. When the jimpy mouse, an X-linked dysmyelination mutant, was studied for PLP mRNA expression, low levels of PLP mRNA were seen which were approximately 5% of wild-type levels at 20 days of age. When jimpy brain RNA was analyzed by Northern blotting, the PLP-specific mRNA was shown to be 100 to 200 bases shorter than the wild-type PLP-specific mRNA. This size difference was seen in the two major PLP mRNAs, and it did not result from a loss of polyadenylation of these mRNAs.The biosynthesis of the myelin sheath is a crucial part of nervous system development, and as a result, the developmental expression of the myelin protein genes is highly regulated. The normal pattern of myelin protein expression in rodents indicates that little myelin protein expression occurs prenatally or in neonatal animals (2,5,6,8,23,26,28) and that myelin protein synthesis and accumulation increase significantly in the brain at about 10 days after birth, reaching a peak between 15 and 22 days after birth (2,5,6,8,23).Central nervous system myelin contains two major classes of proteins, myelin basic protein (MBP) and proteolipid protein (PLP), which together constitute as much as 80% of the total myelin protein (15,30). The four MBPs that are present in rodent myelin have homologous amino acid sequences, including identical amino-and carboxyl-terminal sequences but internal segments of unique amino acid sequence (3). They are translated from four different mRNAs (50), and the four MBP mRNAs can be produced from a single MBP gene by alternative mRNA splicing (12,44). Two PLPs are present in myelin, the major PLP, which has an apparent molecular weight of 25,000, and the closely related proteolipid DM20 (1), which has an apparent molecular weight of 20,000. PLP and DM20 may have a relationship similar to that found among the four MBPs, since they have identical amino-and carboxyl-terminal sequences (46), and they are very closely related by amino acid composition and by antigenic characteristics. The expression of these myelin proteins correlates closely with the formation of myelin in the developing rat brain, and mouse mutants that are defective in myelin formation show lowered levels of these myelin proteins (4,14,20,25 expression and the genetic deficiency in the shiverer mouse myelination mutant (12,34,44). Several groups have recently isolated cDNA ...

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“…Myelin was prepared according to the method of Norton and Poduslo (1973). It was routinely prepared in the laboratory (Bourre et al, 1978); the purity was checked by electron microscopy (Baumann et al, 1973) lipid analysis (Baumann et al, 1973;Bourre et al, 1977) and protein electrophoresis (Jacque et al, 1972).…”

Section: Tissue Fractionationmentioning

confidence: 99%

Alteration of 5′‐Nucleotidase and Na⁺, K⁺‐ATPase in Central and Peripheral Nervous Tissue from Dysmyelinating Mutants (jimpy, quaking, Trembler, shiverer, and mld). Comparison with CNPase in the Developing Sciatic Nerve from Trembler

Bourre

Chanez

Dumont

et al. 1982

Journal of Neurochemistry

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5′Nucleotidase and Na+,K+‐ATPase are very probably myelin‐associated enzymes, although not specific for this membrane. Thus, it is important to determine their activity in dysmyelinating mutants in either CNS (quaking, jimpy, shiverer, and mld) or PNS (Trembler). CNS: The activity of 5′nucleotidase was lower in mouse than in rat (10.5 and 28.0 nmol/min/mg protein in brain, respectively). In mouse myelin, the activity was 30 nmol/min/mg protein (and 72 in rat myelin). In mutants, the brain activity was very close to normal. In contrast, ATPase, the activity of which was higher in myelin as compared with forebrain homogenate, presented a reduced activity in various 21‐day‐old and adult mutants, except Trembler. It was normal in 8‐day‐old quaking and in cerebella from mutants. PNS: ATPase was lower than in brain and reduced in most mutants, this being expected for Trembler and quaking but not for shiverer and mld. 5′‐Nucleotidase activity was higher compared with that in brain homogenate (relatively stable between 10‐day postnatal and adult). It was affected in the mutants; in Trembler it was nearly normal in young animals but increased during development. Thus in Trembler, two different myelin‐related enzymes and a myelin‐specific enzyme (CNPase) presented different developmental patterns: ATPase was always reduced, 5′‐nucleotidase was normal, and CNPase was slightly below normal in young (68% of the control value); CNPase activity declined during development but 5′‐nucleotidase increased (42% and 190% of the control in 60‐day‐old animals). It is necessary to consider these results in parallel with alterations in the PNS because of Schwann cell abnormalities. Thus, determination of these two enzymes will provide a useful tool to study myelination and myelin assembly under both normal and pathological conditions.

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Pelizaeus-Merzbacher Disease: Biochemical Analysis of Isolated Myelin (Electron-Microscopy;Protein, Lipid and Unsubstituted Fatty Acids Analysis)

Cited by 19 publications

References 0 publications

Influence of Intrauterine Malnutrition on Brain Development: Alteration of Myelination

Influence of Intrauterine Malnutrition on Brain Development: Alteration of Myelination

Characterization of myelin proteolipid mRNAs in normal and jimpy mice.

Alteration of 5′‐Nucleotidase and Na⁺, K⁺‐ATPase in Central and Peripheral Nervous Tissue from Dysmyelinating Mutants (jimpy, quaking, Trembler, shiverer, and mld). Comparison with CNPase in the Developing Sciatic Nerve from Trembler

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Pelizaeus-Merzbacher Disease: Biochemical Analysis of Isolated Myelin (Electron-Microscopy;Protein, Lipid and Unsubstituted Fatty Acids Analysis)

Cited by 19 publications

References 0 publications

Influence of Intrauterine Malnutrition on Brain Development: Alteration of Myelination

Influence of Intrauterine Malnutrition on Brain Development: Alteration of Myelination

Characterization of myelin proteolipid mRNAs in normal and jimpy mice.

Alteration of 5′‐Nucleotidase and Na+, K+‐ATPase in Central and Peripheral Nervous Tissue from Dysmyelinating Mutants (jimpy, quaking, Trembler, shiverer, and mld). Comparison with CNPase in the Developing Sciatic Nerve from Trembler

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Alteration of 5′‐Nucleotidase and Na⁺, K⁺‐ATPase in Central and Peripheral Nervous Tissue from Dysmyelinating Mutants (jimpy, quaking, Trembler, shiverer, and mld). Comparison with CNPase in the Developing Sciatic Nerve from Trembler