Large Scale Preparation of Myelin Basic Protein from Central Nervous Tissue of Several Mammalian Species

Deibler, Gladys E.; Martenson, Russell E.; Kies, Marian W.

doi:10.1080/00327487208061467

Cited by 797 publications

(319 citation statements)

References 15 publications

Supporting

Mentioning

316

Contrasting

Unclassified

Order By: Relevance

“…Chemicals and samples MBP was purified in the water-soluble, lipid-free form from bovine brain according to established procedures (Deibler et al 1972(Deibler et al , 1984. The protein concentration was determined using the Bio-Rad Bradford reagent (Bio-Rad Laboratories, Hercules, CA, USA) and a microassay procedure.…”

Section: Methodsmentioning

confidence: 99%

Microstructural analysis of the effects of incorporation of myelin basic protein in phospholipid layers

et al. 2005

View full text Add to dashboard Cite

We report an X-ray reflectivity study on the effects of adsorption of myelin basic protein (MBP) on Langmuir monolayers and on deposited LangmuirSchaefer multilayers of the phospholipid dipalmitoyl phosphatidylglycerol (DPPG). We provide for the first time, direct microscopic evidence on the destructuring effects of MBP leading to plasticity of the DPPG layers supporting commonly accepted models of the stabilizing role of MBP in the myelin membrane. We also show how protein adsorption onto the layer is determined both by electrostatic and nonspecific hydrophobic interactions.

show abstract

Section: Methodsmentioning

confidence: 99%

Microstructural analysis of the effects of incorporation of myelin basic protein in phospholipid layers

et al. 2005

View full text Add to dashboard Cite

show abstract

“…Myelin basic protein was extracted and purified as described by Deibler et al (1972). The protein was further purified by chromatography on a Sephadex G-75 Superfine column (3 X 90 cm) equilibrated with 10 mM HC1.…”

Section: Methodsmentioning

confidence: 99%

Interaction of two complementary fragments of the bovine spinal cord myelin basic protein with phospholipid bilayers. An ESR spin-label study

Pj²,

Marsh

1989

Biochemistry

View full text Add to dashboard Cite

The myelin basic protein (MBP) from bovine spinal cord was cleaved at the single tryptophan residue to produce an N-terminal fragment ( F l ) of molecular weight 12.6K and a C-terminal fragment (F2) of molecular weight 5.8K. The interactions of the two fragments with bilayers of the acidic lipid dimyristoylphosphatidylglycerol (DMPG) were compared with those of the intact protein, by using both chemical binding assays and spin-label electron spin resonance spectroscopy. The saturation binding stoichiometries of the two fragments were found to sum to that of the MBP, having values of 1 1, 24, and 36 mol of DMPG/mol of protein for F2, F1, and the MBP, respectively. The strength of binding was found to increase in the order F2 < F1 < MBP, which follows that of the net charges on the different fragments.The ionic strength dependence of the protein binding indicated that the interaction is primarily of electrostatic origin. The efficiency of displacement of the proteins by salt was in the order F2 > F1 > MBP, which correlates with both the strength of binding and the net charge on the different protein fragments. Nitroxide derivatives of phosphatidylglycerol (PG) labeled on the sn-2 chain were used to probe the protein-induced changes in the acyl chain dynamics. Both the fragments and the MBP decreased the lipid chain mobility as recorded by the C-5 atom and (2-12 atom position nitroxide-PG spin-labels, in a manner which followed the protein binding curves. At saturation binding, the reduction in mobility recorded by the C-5 atom label was in the order M B P > F1 > F2. An additional population of lipids, whose chain motion was restricted relative to that of the bulk population of fluid lipids, was resolved in the case of the F1 fragment and the MBP, when using the C-12 atom position labeled PG. Approximately nine DMPG molecules per F1 fragment were found in this motionally restricted population, which was assigned to lipids in direct contact with partially penetrant sections of the protein, as opposed to a 18: 1 mol/mol lipid/protein stoichiometry found for the restricted component with the intact MBP. These results suggest that the principal sites of hydrophobic interaction of the protein with lipid bilayers are at least partly located in the 12.6-kDa fragment. The tryptophan residue at position 116 appears also to be important for the structural and functional properties of the intact bovine myelin basic protein.x e water-soluble peripheral myelin basic protein (MBP)' plays an important role in the structural organization of the myelin sheath [see Boggs and Moscarello (1978a,b) and Boggs et al. (1982)l. Induction and maintenance of the multilamellar structure of myelin are thought to be brought about by a bridging of apposing cytoplasmic surfaces. A hairpin structure of the protein caused by a tri-proline sequence approximately in the middle of the molecule is considered to cause interlamellar interactions (Eylar et al., 1971).

show abstract

“…MBP was prepared from guinea pig brains by the method of Deibler et al (1972). MBP in 0.9% saline was emulsified in an equal volume of incomplete Freund's adjuvant containing 4 mg/ml Mycobacterium butyricum.…”

Section: Induction Of Eaementioning

confidence: 99%

Effects of cyclosporin A treatment on clinical course and inflammatory cell apoptosis in experimental autoimmune encephalomyelitis induced in Lewis rats by inoculation with myelin basic protein

McCombe

Harness

Pender

1999

Journal of Neuroimmunology

View full text Add to dashboard Cite

Experimental autoimmune encephalomyelitis (EAE) was induced in Lewis rats by inoculation with myelin basic protein (MBP) and adjuvants. Rats were treated with second daily injections of saline or cyclosporin A (CsA) from the day of inoculation. Saline-treated rats had an acute episode of disease followed by clinical recovery. Rats treated with CsA 16 or 32 mg/kg had minimal signs of EAE at the usual time after inoculation, but developed signs of disease after treatment was ceased. Rats treated with CsA 8 mg/kg had a delayed first episode of disease and then developed a relapsing or a chronic persistent course of disease. CsA 4 mg/kg delayed the onset of disease. To study the effects of CsA on the inflammatory infiltrate, cells were extracted from the spinal cords of rats with EAE, 16 h after a single injection of CsA or saline. Extracted cells were labelled with antibodies to T cells, CD11b/c (macrophages/microglia), CD95 (Fas) and Fas ligand. CsA 4 mg/kg did not alter the composition of the inflammatory infiltrate. Treatment with higher single doses of CsA caused a dose-dependent decline in the percentage of T cell receptor (TCR) + cells in the inflammatory infiltrate. All doses of CsA caused a significant increase in the number and percentage of cells that were apoptotic. CsA treatment caused an increase in the percentages of CD5 + and TCR + cells that were apoptotic. There was a decline in the percentage of apoptotic T cells that were V 8.2 + , compared to the percentage of nonapoptotic T cells that were V 8.2 + , in CsA treated rats compared to saline-treated controls. This suggests that, while CsA treatment caused a non-specific increase in the overall level of T cell apoptosis in the spinal cord, it abrogated the selective apoptosis of V 8.2 + encephalitogenic T cells that normally occurs during spontaneous recovery from acute EAE.

show abstract

Large Scale Preparation of Myelin Basic Protein from Central Nervous Tissue of Several Mammalian Species

Cited by 797 publications

References 15 publications

Microstructural analysis of the effects of incorporation of myelin basic protein in phospholipid layers

Microstructural analysis of the effects of incorporation of myelin basic protein in phospholipid layers

Interaction of two complementary fragments of the bovine spinal cord myelin basic protein with phospholipid bilayers. An ESR spin-label study

Effects of cyclosporin A treatment on clinical course and inflammatory cell apoptosis in experimental autoimmune encephalomyelitis induced in Lewis rats by inoculation with myelin basic protein

Contact Info

Product

Resources

About