Differences between the two myelin basic proteins of the rat central nervous system

Martenson, Russell E.; Deibler, Gladys E.; Kies, Marian W.; McKneally, S S; Shapira, Raymond; Kibler, Robert F.

doi:10.1016/0005-2795(72)90172-9

Cited by 102 publications

(31 citation statements)

References 25 publications

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“…Rat S basic protein is the smaller of the two basic proteins which occur in rat myelin. It differs from the larger protein in that it lacks approximately 40 amino acids in the carboxy-terminal region after tryptophane (12). This deletion contains none of the rat basic protein encephalitogenic site as tested in rats but does include part of the active site for guinea pigs.…”

Section: Discussionmentioning

confidence: 99%

Linkage of Susceptibility to Experimental Allergic Encephalomyelitis to the Major Histocompatibility Locus in the Rat

Williams

Moore

1973

The Journal of Experimental Medicine

136

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Experimental allergic encephalomyelitis (EAE) was induced in rats of various genotypes by injection of 10 µg guinea pig basic protein in complete Freund's adjuvant containing 100 µg H37 RV M. tuberculosis. Histologically verified EAE was present in 20/20 Lewis, 17/17 (Lewis x BN)F1, 9/9 Lewis backcross, and 21/42 BN backcross rats. Among the BN backcross animals, 25/42 were determined to carry the major histocompatibility type characteristic of the Lewis strain and 21 of these had EAE. Separate groups of Lewis, BN, and (Lewis x BN)F1 rats were immunized as described and skin tested on day 13 with 10 µg guinea pig basic protein and rat S basic protein. Animals of each genotype had Arthus and delayed skin reactivity to both antigens. These data are compatible with the hypothesis that susceptibility to EAE in rats is controlled by an autosomal dominant gene linked to the major histocompatibility locus. It is proposed that this is an immune response gene, designated Ir-EAE, which controls T cell reactivity directed against a highly encephalitogenic portion of the basic protein molecule.

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Section: Discussionmentioning

confidence: 99%

Linkage of Susceptibility to Experimental Allergic Encephalomyelitis to the Major Histocompatibility Locus in the Rat

Williams

Moore

1973

The Journal of Experimental Medicine

136

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“…In the rat, the larger molecule (L, Mr 18,500) is similar in amino acid sequence to MBP from other species. The smaller molecule (S, Mr 14,000) is identical to L except that the region extending from positions 120 to 160 in the sequence is deleted (1,2).…”

mentioning

confidence: 98%

Identification of prelarge and presmall basic proteins in mouse myelin and their structural relationship to large and small basic proteins

Barbarese¹,

Braun²,

Carson³

1977

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

142

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A new technique is described to identify antigenically related proteins by radioimmunoassay after sodium dodecyl sulfate/polyacrylamide gel fractionation. When adult mouse myelin was examined by this technique, four proteins that are anti enically related to the small myelin basic protein were identified. They were designated: prelarge (molecular weight 21,500), large (18,500), presmall (17,000), and small (14,000). The four proteins were isolated by elution from polyacrylamide gels, and each protein migrated as a single band when analyzed by either sodium dodecyl sulfate or acidic polyacrylamide gel electrophoresis. Serial dilutions of the purified proteins were measured by radioimmunoassay. Both the slope of the inhibition curve and the level of maximal inhibition for each protein were the same as for the small myelin basic protein, indicating that each of the four proteins contains all of the antigenic sites present in the small basic protein. Structural relationships among the four proteins were examined by using two-dimensional analysis of tryptic digests. The results showed that: large was similar in amino acid sequence to the major myelin basic protein from other species; small was identical in sequence to large, except for an internal deletion of approximately 40 amino acid residues; prelarge contained the sequence of large plus an additional sequence of 25-35 amino acid residues; and presmall contained the sequence of small plus the same additional sequence as in prelarge. The four proteins were also treated with 2-(2-nitrophenyfsulfenyl)3-methyl-3'-bromoindolienine (BNPS-skatole) which cleaves proteins specifically at tryptophan residues. Analysis of the cleavage products indicated that the additional amino acid sequence in both prelarge and presmall extends from the amino terminus of the molecule. Several implications of these results are discussed.Myelin basic protein (MBP) is a major component of the myelin membrane. It comprises approximately 30% of the total myelin protein and is not present in other cell membranes. Its function in the myelin membrane is not known. In MBP isolated from several different species, the amino acid sequence is highly conserved (1). Much of the sequence, including the single tryptophan residue at position 118, is invariant in every MBP that has been studied (1). Myelin isolated from mouse or rat central nervous system contains two forms of MBP that differ in molecular weight (Mr). In the rat, the larger molecule (L, Mr 18,500) is similar in amino acid sequence to MBP from other species. The smaller molecule (S, Mr 14,000) is identical to L except that the region extending from positions 120 to 160 in the sequence is deleted (1, 2).In this paper, the protein components of mouse myelin were examined by using a new technique combining sodium dodecyl sulfate/polyacrylamide gel electrophoresis with radioimmunoassay for MBP. The results show that, in addition to L and S, mouse myelin contains two minor components, designated prelarge (preL) and presmall (preS), that a...

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“…Therefore, we studied the deposition of MOG during myelinogenesis in normal mice and myelin-deficient (mid) mice, which possess a mutation affecting the posttranscriptional regulation of the myelin basic protein (MBP) gene (Mbp); this results in low concentration of MBP [23], MOG con centrations in whole-brain homogenates were correlated with myelin yield, MBP con centrations and 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNP; EC 3.1.4.37) specific activity. MBP and CNP are specific markers for myelin [24,25] and oligodendro cytes [26][27][28], respectively.…”

Section: Introductionmentioning

confidence: 99%

Myelin/Oligodendrocyte Glycoprotein Expression during Development in Normal and Myelin-Deficient Mice

Matthieu¹,

Amiguet²

1990

Dev Neurosci

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The myelin/oligodendrocyte glycoprotein (MOG) is identified by monoclonal antibody 8–18C5. MOG is localized on the surface of myelin and oligodendrocyte processes. Recently, several studies have shown that MOG plays an important role as a target for antibody-induced demyelination. In the present study, we investigated MOG expression in the brains of normal and myelin-deficient (mld)mutant mice during development. By gel electrophoresis and immunoblotting, we observed the developmental pattern of two closely migrating bands, with apparent molecular masses of 26 and 28 kilodaltons. Their concentrations increased coordinately during the most active phase of myelin and myelin basic protein (MBP) synthesis. Between 20 and 25 days of age, the MOG developmental pattern superimposed that of MBP as well as myelin yields. In mld mutant mice, which are affected by a severe deficit of MBP synthesis, MOG was present at reduced levels (40% of controls at 60 days of age). At 85 days of age, mld mice exhibited increased concentrations of MBP, and myelin was better compacted. At this age, MOG concentrations increased and reached 70% of controls. These results suggest that MOG could play a role in the maintenance or completion of the myelin sheath. Its expression level may be modulated by the presence of compact myelin and/or MBP in the myelin sheath.

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Differences between the two myelin basic proteins of the rat central nervous system

Cited by 102 publications

References 25 publications

Linkage of Susceptibility to Experimental Allergic Encephalomyelitis to the Major Histocompatibility Locus in the Rat

Linkage of Susceptibility to Experimental Allergic Encephalomyelitis to the Major Histocompatibility Locus in the Rat

Identification of prelarge and presmall basic proteins in mouse myelin and their structural relationship to large and small basic proteins

Myelin/Oligodendrocyte Glycoprotein Expression during Development in Normal and Myelin-Deficient Mice

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