Isolation and characterization of a cDNA coding for a novel human 17.3k myelin basic protein (MBP) variant

@article{Roth1986IsolationAC,
  title={Isolation and characterization of a cDNA coding for a novel human 17.3k myelin basic protein (MBP) variant},
  author={H. John Roth and Kathryn E. Kronquist and Piet J. Pretorius and Barbara F. Crandall and Anthony T. Campagnoni},
  journal={Journal of Neuroscience Research},
  year={1986},
  volume={16}
}
Human fetal spinal cord poly A (+) mRNA was found to direct the synthesis of three major myelin basic protein (MBP) variants with molecular weights of 17K, 18.5K, and 21.5K when translated in reticulocyte lysates. In order to investigate the structural relationships between these MBP variants and their corresponding mouse variants, human fetal spinal cord and mouse brain cDNA libraries were constructed and screened for MBP cDNAs. A number of MBP cDNA clones were isolated and characterized. One… 
Evidence for the expression of four myelin basic protein variants in the developing human spinal cord through cDNA cloning
TLDR
All four human MBP variants were identical except for the insertion or deletion of two peptide fragments corresponding to those encoded by exons 2 and 5 of the MBP gene, which indicates that the predominant MBP splicing pathways in human and mouse are different.
Expression of myelin proteins in the developing human spinal cord: Cloning and sequencing of human proteolipid protein cDNA
TLDR
A full‐length clone for the human proteolipid protein (PLP) was isolated from a cDNA library constructed from poly (A)+ RNA isolated from fetal spinal cords obtained at 15–24 weeks of conceptional age, and the deduced amino acid sequence was found to be identical with that of rat PLP.
Expression of a Novel Transcript of the Myelin Basic Protein Gene
TLDR
The results suggest that the structure of the MBP gene is more complex than originally thought, containing at least two more exons and there appears to be at least one moreMBP gene promoter that directs the synthesis of a subset of MBP mRNAs with a unique 5′‐untranslated region.
Protein factors and 5' flanking sequences involved in the expression of the mouse myelin basic protein gene
TLDR
This project was initiated by the isolation of the putative promoter region of the mouse myelin basic protein (MBP) gene and the presence of protein factors specifically binding to the region -609 to -577 was demonstrated by electrophoretic mobility shift assay (EMSA).
A 39-kD DNA-binding protein from mouse brain stimulates transcription of myelin basic protein gene in oligodendrocytic cells
TLDR
Purification of a 39-kD protein from mouse brain tissue at the peak of myelination and MBP production that binds to the MB1 regulatory motif is reported, and a complementary DNA encoding a 39 -kD DNA-binding protein called pur alpha is identified.
Isolation and sequence determination of cDNA encoding the major structural protein of human peripheral myelin.
Isolation and sequence determination of cDNA encoding P2 protein of human peripheral myelin.
Nuclear proteins in mouse brain cells bind specifically to the myelin basic protein regulatory region.
TLDR
Using synthetic DNA fragments spanning the MBP control region, nuclear proteins obtained from newborn, young adult, and adult animals are analyzed and the observation that the minor 37-kD protein became more abundant in the extract derived from adult brain, whereas the major 39-k D protein became less abundant is observed.
Molecular Biology of Myelin Proteins from the Central Nervous System
TLDR
Most of the dysmyelinating mutants, including those in which the genetic defect is established, appear to exhibit pleiotropy with respect to the expression of other myelin protein genes, and their structures have been established through an analysis of the cDNA clones encoding them.
Structural Features of Myelin Basic Protein mRNAs Influence Their Translational Efficiencies
TLDR
The 8 and 3’UTRs of MBP mRNAs appear to influence the translation of these m RNAs, and such factors may be involved in the translational regulation of MBp gene expression.
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References

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In Vitro Synthesis of the Four Mouse Myelin Basic Proteins: Evidence for the Lack of a Metabolic Relationship
TLDR
It is proposed that the four MBPs are the primary translation products of independent brain mRNAs and are not metabolically related.
Expression of Myelin Basic Protein Genes in Several Dysmyelinating Mouse Mutants During Early Postnatal Brain Development
TLDR
It appears that jimpy and quaking mice exhibit developmental patterns of MBP expression different from each other and from C57BL/6J control mice.
Partial characterization of 21.5K myelin basic protein from sheep brain.
TLDR
The 21,500 molecular weight variant of myelin basic protein (MBP) was isolated from sheep brain and partially characterized and showed that approximately 30 additional amino acids were inserted at the equivalent of the amino acid at position 57 in the bovine 18.5K MBP sequence.
Expression of Myelin Proteolipid Protein and Basic Protein in Normal and Dysmyelinating Mutant Mice
TLDR
expression of myelin proteins was studied in the brains of 21‐day‐old normal mice and three dysmyelinating mutants and the mutation appears to affect the expression of the MBPs and PLP independently, regardless of their absolute levels of synthesis.
Cell‐Free Synthesis of Myelin Basic Proteins in Normal and Dysmyelinating Mutant Mice
TLDR
The data indicate that shi/shi and mld/mld mutants either produce altered BPs not recognized by the authors' antibody or synthesize very low levels of BP, and provide additional support for the notion that the qk/qk mutant synthesizes much higher levels of MBP than are incorporated into myelin.
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