Myelin basic protein: Wikis


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Myelin basic protein
Symbols MBP; MGC99675
External IDs OMIM159430 MGI96925 HomoloGene1788 GeneCards: MBP Gene
RNA expression pattern
PBB GE MBP 207323 s at tn.png
PBB GE MBP 209072 at tn.png
More reference expression data
Species Human Mouse
Entrez 4155 17196
Ensembl ENSG00000197971 ENSMUSG00000041607
UniProt P02686 P04370
RefSeq (mRNA) NM_001025081 NM_001025245
RefSeq (protein) NP_001020252 NP_001020416
Location (UCSC) Chr 18:
72.82 - 72.97 Mb
Chr 18:
82.61 - 82.72 Mb
PubMed search [1] [2]

Myelin basic protein (MBP) is a protein believed to be important in the process of myelination of nerves in the central nervous system (CNS).

MBP was initially sequenced in 1979 after isolation from myelin membranes a. Since that time, knockout mice deficient in MBP have been developed which showed decreased amounts of CNS myelination and a progressive disorder characterized by tremors, seizures, and early death. The gene for MBP is on chromosome 18; the protein localizes to the CNS and to various cells of the hematopoietic system.

The pool of MBP in the central nervous system is very diverse, with several splice variants being expressed and a large number of post-translational modifications on the protein, which include phosphorylation, methylation, deamidation and citrullination.

In melanocytic cell types MBP gene expression may be regulated by MITF a.


Role in disease

Interest in MBP has centered on its role in demyelinating diseases, particularly multiple sclerosis (MS). Several studies have shown a role for antibodies against MBP in the pathogenesis of MS a. Some studies have linked a genetic predisposition to MS to the MBP gene, though a majority have not.

Some recent works have shown that administration of MBP artificially increases blood-brain barrier permeability.

MBP is currently being researched as a possible treatment for lethal rabies infection. The administration of MBP increases the permeability of the blood-brain barrier (BBB) allowing immune cells to enter the brain, the primary site of rabies virus replication. In a study of mice infected with Silver-haired bat rabies virus (SHBRV) the mortality rate of mice treated with MBP improved 20%-30% over the untreated control group. It is significant to note that healthy uninfected mice treated with MBP showed an increase in mortality rate between 0% and 40%a.


Myelin basic protein has been shown to interact with Proteolipid protein 1.[1][2]


  1. ^ Wood, D D; Vella G J, Moscarello M A (Oct. 1984). "Interaction between human myelin basic protein and lipophilin". Neurochem. Res. (UNITED STATES) 9 (10): 1523–31. ISSN 0364-3190. PMID 6083474. 
  2. ^ Edwards, A M; Ross N W, Ulmer J B, Braun P E (Jan. 1989). "Interaction of myelin basic protein and proteolipid protein". J. Neurosci. Res. (UNITED STATES) 22 (1): 97–102. doi:10.1002/jnr.490220113. ISSN 0360-4012. PMID 2467009. 
  1. ^a  Free text.png Basic A1 protein of the myelin membrane: the complete amino acid sequence. J Biol Chem. 1971 Sep 25;246(18):5770-84; PubMed Free text - PDF (1.9MB)
  2. ^a  Free text.png Antimyelin antibodies as a predictor of clinically definite multiple sclerosis after a first demyelinating event. N Engl J Med. 2003 Jul 10;349(2):139-45; PubMed Free text after free registration
  3. ^a  Roy A, Hooper DC (2007). "Lethal silver-haired bat rabies virus infection can be prevented by opening the blood-brain barrier". J. Virol. 81 (15): 7993–8. doi:10.1128/JVI.00710-07. PMID 17507463. 
  4. ^a  Hoek KS, Schlegel NC, Eichhoff OM, et al. (2008). "Novel MITF targets identified using a two-step DNA microarray strategy". Pigment Cell Melanoma Res. 21 (6): 665–76. doi:10.1111/j.1755-148X.2008.00505.x. PMID 19067971. 

Further reading

  • Boylan KB, Ayres TM, Popko B, et al. (1990). "Repetitive DNA (TGGA)n 5' to the human myelin basic protein gene: a new form of oligonucleotide repetitive sequence showing length polymorphism.". Genomics 6 (1): 16–22. doi:10.1016/0888-7543(90)90443-X. PMID 1689270. 
  • Kishimoto A, Nishiyama K, Nakanishi H, et al. (1985). "Studies on the phosphorylation of myelin basic protein by protein kinase C and adenosine 3':5'-monophosphate-dependent protein kinase.". J. Biol. Chem. 260 (23): 12492–9. PMID 2413024. 
  • Saxe DF, Takahashi N, Hood L, Simon MI (1985). "Localization of the human myelin basic protein gene (MBP) to region 18q22----qter by in situ hybridization.". Cytogenet. Cell Genet. 39 (4): 246–9. doi:10.1159/000132152. PMID 2414074. 
  • Kamholz J, de Ferra F, Puckett C, Lazzarini R (1986). "Identification of three forms of human myelin basic protein by cDNA cloning.". Proc. Natl. Acad. Sci. U.S.A. 83 (13): 4962–6. doi:10.1073/pnas.83.13.4962. PMID 2425357. 
  • Scoble HA, Whitaker JN, Biemann K (1986). "Analysis of the primary sequence of human myelin basic protein peptides 1-44 and 90-170 by fast atom bombardment mass spectrometry.". J. Neurochem. 47 (2): 614–6. PMID 2426402. 
  • Roth HJ, Kronquist K, Pretorius PJ, et al. (1986). "Isolation and characterization of a cDNA coding for a novel human 17.3K myelin basic protein (MBP) variant.". J. Neurosci. Res. 16 (1): 227–38. doi:10.1002/jnr.490160120. PMID 2427738. 
  • Popko B, Puckett C, Lai E, et al. (1987). "Myelin deficient mice: expression of myelin basic protein and generation of mice with varying levels of myelin.". Cell 48 (4): 713–21. doi:10.1016/0092-8674(87)90249-2. PMID 2434243. 
  • Kamholz J, Spielman R, Gogolin K, et al. (1987). "The human myelin-basic-protein gene: chromosomal localization and RFLP analysis.". Am. J. Hum. Genet. 40 (4): 365–73. PMID 2437795. 
  • Roth HJ, Kronquist KE, Kerlero de Rosbo N, et al. (1987). "Evidence for the expression of four myelin basic protein variants in the developing human spinal cord through cDNA cloning.". J. Neurosci. Res. 17 (4): 321–8. doi:10.1002/jnr.490170402. PMID 2442403. 
  • Shoji S, Ohnishi J, Funakoshi T, et al. (1988). "Phosphorylation sites of bovine brain myelin basic protein phosphorylated with Ca2+-calmodulin-dependent protein kinase from rat brain.". J. Biochem. 102 (5): 1113–20. PMID 2449425. 
  • Wood DD, Moscarello MA (1989). "The isolation, characterization, and lipid-aggregating properties of a citrulline containing myelin basic protein.". J. Biol. Chem. 264 (9): 5121–7. PMID 2466844. 
  • Edwards AM, Ross NW, Ulmer JB, Braun PE (1989). "Interaction of myelin basic protein and proteolipid protein.". J. Neurosci. Res. 22 (1): 97–102. doi:10.1002/jnr.490220113. PMID 2467009. 
  • Streicher R, Stoffel W (1989). "The organization of the human myelin basic protein gene. Comparison with the mouse gene.". Biol. Chem. Hoppe-Seyler 370 (5): 503–10. PMID 2472816. 
  • Lennon VA, Wilks AV, Carnegie PR (1971). "Immunologic properties of the main encephalitogenic peptide from the basic protein of human myelin.". J. Immunol. 105 (5): 1223–30. PMID 4099924. 
  • Carnegie PR (1972). "Amino acid sequence of the encephalitogenic basic protein from human myelin.". Biochem. J. 123 (1): 57–67. PMID 4108501. 
  • Baldwin GS, Carnegie PR (1971). "Specific enzymic methylation of an arginine in the experimental allergic encephalomyelitis protein from human myelin.". Science 171 (971): 579–81. doi:10.1126/science.171.3971.579. PMID 4924231. 
  • Baldwin GS, Carnegie PR (1972). "Isolation and partial characterization of methylated arginines from the encephalitogenic basic protein of myelin.". Biochem. J. 123 (1): 69–74. PMID 5128665. 
  • Wood DD, Vella GJ, Moscarello MA (1985). "Interaction between human myelin basic protein and lipophilin.". Neurochem. Res. 9 (10): 1523–31. doi:10.1007/BF00964678. PMID 6083474. 
  • Gibson BW, Gilliom RD, Whitaker JN, Biemann K (1984). "Amino acid sequence of human myelin basic protein peptide 45-89 as determined by mass spectrometry.". J. Biol. Chem. 259 (8): 5028–31. PMID 6201481. 
  • Pribyl TM, Campagnoni CW, Kampf K, et al. (1993). "The human myelin basic protein gene is included within a 179-kilobase transcription unit: expression in the immune and central nervous systems.". Proc. Natl. Acad. Sci. U.S.A. 90 (22): 10695–9. doi:10.1073/pnas.90.22.10695. PMID 7504278. 


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