Myelin Basic Protein (68-82) Guinea Pig

GWB-549F64

{TYR} {GLY} {SER} {LEU} {PRO} {GLN} {LYS} {SER} {GLN} {ARG} {SER} {GLN} {ASP} {GLU} {ASN}

The classic group of MBP isoforms (isoform 4-isoform 14) are with PLP the most abundant protein components of the myelin membrane in the CNS. They have a role in both its formation and stabilization. The smaller isoforms might have an important role in remyelination of denuded axons in multiple sclerosis. The non-classic group of MBP isoforms (isoform 1-isoform 3/Golli-MBPs) may preferentially have a role in the early developing brain long before myelination maybe as components of transcriptional complexes and may also be involved in signaling pathways in T-cells and neural cells. Differential splicing events combined to optional posttranslational modifications give a wide spectrum of isomers each of them having maybe a specialized function.

Myelin membrane; peripheral membrane protein; cytoplasmic side. Cytoplasmic side of myelin.

Several charge isomers of MBP; C1 (the most cationic least modified and most abundant form) C2 C3 C4 C5 C6 C7 C8-A and C8-B (the least cationic form); are produced as a result of optional PTM such as phosphorylation deamidation of glutamine or asparagine arginine citrullination and methylation. C8-A and C8-B contain each two mass isoforms termed C8-A(H) C8-A(L) C8-B(H) and C8-B(L) (H) standing for higher and (L) for lower molecular weight. C3 C4 and C5 are phosphorylated. The ratio of methylated arginine residues decreases in aging making the protein more cationic.

Arg-241 was found to be 6% monomethylated and 60% symmetrically dimethylated.

Belongs to the myelin basic protein family. [1] Carnegie P. R. Amino acid sequence of the encephalitogenic basic protein from human myelin. [2] Roth H. J. Kronquist K. E. Pretorius P. J. Crandall B. F. Campagnoni A. T. Isolation and characterization of a cDNA coding for a novel human 17. 3K myelin basic protein (MBP) variant. [3] Kamholz J. de Ferra F. Puckett C. Lazzarini R. A. Identification of three forms of human myelin basic protein by cDNA cloning. [4] Roth H. J. Kronquist K. E. de Rosbo N. Crandall B. F. Campagnoni A. T. Evidence for the expression of four myelin basic protein variants in the developing human spinal cord through cDNA cloning. [5] Streicher R. Stoffel W. The organization of the human myelin basic protein gene. Comparison with the mouse gene. [6] Pribyl T. M. Campagnoni C. W. Kampf K. Kashima T. Handley V. W. McMahon J. Campagnoni A. T. The human myelin basic protein gene is included within a 179-kilobase transcription unit: expression in the immune and central nervous systems. [7] Ebert L. Schick M. Neubert P. Schatten R. Henze S. Korn B. Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201). [8] Boylan K. B. Ayres T. M. Popko B. Takahashi N. Hood L. E. Prusiner S. B. Repetitive DNA (TGGA)n 5\' to the human myelin basic protein gene: a new form of oligonucleotide repetitive sequence showing length polymorphism. [9] Scoble H. A. Whitaker J. N. Biemann K. Analysis of the primary sequence of human myelin basic protein peptides 1-44 and 90-170 by fast atom bombardment mass spectrometry. [10] Wood D. D. Moscarello M. A. The isolation characterization and lipid-aggregating properties of a citrulline containing myelin basic protein.