Disease relevance of MBP

• In patients with multiple sclerosis low levels of antibody to MBP can be detected in cerebrospinal fluid (CSF) and acid-eluted extracts from brain plaque material; detection of low levels of antibody in human serum has not been possible due to non-specific binding of human serum Ig in this RIA [1].
• Experimental allergic encephalomyelitis (EAE) was induced in chickens by injecting human myelin basic protein (MBP) in Freund's complete adjuvant (CFA) [2].
• The studies concerned the effect of cyclophosphamide on immunological and biochemical indices of MBP-induced encephalomyelitis [3].
• We studied the effects of antiserum against rat peripheral nervous system (PNS) myelin, rat or chicken central nervous system myelin basic protein (BP), or rabbit P2 protein from PNS myelin on myelinated cultures containing only rat dorsal root ganglion neurons and Schwann cells [4].
• Mechanism of demyelination in the guinea pig. Separate sensitization with encephalitogenic myelin basic protein and nonencephalitogenic brain components [5].

High impact information on MBP

• Several regions identified in myelin basic protein and P2 protein can be related to experimental allergic encephalomyelitis or neuritis in laboratory animals [6].
• Utilizing a similar immunological protocol, we evoked a transient alteration of myelin structure in the posthatching (P) chicken spinal cord, characterized by widespread "unravelling" of myelin sheaths and a loss of MBP immunoreactivity (myelin disruption) [7].
• These results suggest that myelin basic protein and histone H1, widely used in biochemical characterization studies of the phosphatase, may not be physiological substrates, and that the cytoplasm, microsomes, and synaptoplasm may prove to be useful sources for the identification of physiological substrates [8].
• Immunoprecipitates from gizzard and aorta cell extracts, generated with the p44mpk antibody, possessed kinase activities toward myelin basic protein as well as caldesmon [9].
• By means of a liquid-phase radioimmunoassay, antibody responses directed toward this determinant in both multi-specific anti-MBP and monospecific anti-peptide antisera were measured [10].

Biological context of MBP

• Nuclease S1 protection experiments revealed further heterogeneity of MBP transcripts, which result from alternative splicing of segments corresponding to the fifth and sixth exon of the homologous murine MBP gene [11].
• To identify functionally important parts of the 18.5-kDa myelin basic protein (MBP), the amino acid sequences from 10 species ranging from shark to human were aligned using the SEQHP computer program [12].
• The neutral binding protein (pI 7.0), which has a high glycine content, is an analog of mammalian liver MBP (F-I) [13].
• In vivo phosphorylation of two myelin basic proteins of developing rabbit brain [14].
• In vivo methylation of an arginine in chicken myelin basic protein [15].

Anatomical context of MBP

• From these data, at least three different forms of MBP are predicted to exist in the chicken central nervous system [11].
• By selective cloning of gene products newly expressed in the developing chick optic tectum, we have isolated cDNA clones encoding myelin basic protein (MBP) [11].
• For control, chick embryo vaccine (CEV) was used and MBP was not detected [16].
• The possibility that ADP-ribosylation of MBP may control stabilization of myelin through regulation of its affinity for phospholipid in vivo would need to be considered [17].
• Identical results were obtained with fresh Concanavalin A activated T cells and T cell hybridomas generated using myelin basic protein or chicken ovalbumin as immunogens [18].

Associations of MBP with chemical compounds

• Two binding proteins which recognize and bind mannose and N-acetylglucosamine (mannan-binding proteins, MBP) have been isolated from chicken liver to near homogeneity mainly by affinity chromatography on a column of Sepharose 4B-mannan [13].
• We found the inhibition of ADP-ribosylation of MBP by hydroxylamine and L-arginine indicating that this modification was likely to be mediated by arginine residues [17].
• 5. The stoichiometry of ADP-ribose incorporation into 21-kD MBP was 3.5 mol of ADP-ribose/mol MBP [17].
• Cycloleucine, an inhibitor of the formation of S-adenosylmethionine, decreased the incorporation of methyl groups into methylarginine in myelin basic protein in vivo [19].
• The intrinsic fluorescence of the native and chemically modified myelin basic proteins upon interacting with liposomes constituted by dipalmitoylphosphatidycholine, glycosphingolipids, egg phosphatidic acid or dipalmitoylphosphatidyl glycerol was studied [20].

Physical interactions of MBP

• In this paper, electrophoretic mobility shift assays (EMSAs) and S1 nuclease treatment are used to demonstrate that the RBF-maltose binding protei (MBP) fusion protein binds to single-stranded DNA of its element [21].

Other interactions of MBP

• 3. In OPIDN, there is also a dose- and time-dependent increase in Ca2+/calmodulin-dependent kinase mediated phosphorylation of the cytoskeletal proteins, alpha- and beta-tubulin, microtubule associated protein-2, neurofilament triplet proteins and myelin basic protein [22].

Analytical, diagnostic and therapeutic context of MBP

• Only the N-terminal domain of RBF binds the RBF DNA element as demonstrated by southwestern blot analyses, and by competition EMSAs between RBF-MBP and the N-terminal domain [21].
• Subsequently, the monomers were further separated, and the purified MBP-BF2, -beta2m, and MBP were analyzed by circular dichroism (CD) spectrum [23].
• Antibodies of IgM, IgA and IgG class to MBP were measured by enzyme-linked immunosorbent assay (ELISA) [2].
• Northern blot analysis indicated that myelin basic protein mRNA was not down-regulated in myelin-suppressed spinal cords, which suggests that oligodendrocytes survived developmental myelin-suppression [24].

References