A new procedure for the isolation of the brain myelin basic protein in a lipid‐bound form

Riccio, P.; Rosenbusch, J P; Quagliariello, E

doi:10.1016/0014-5793(84)81290-9

Cited by 39 publications

(18 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In our hands, after freeze-drying and HC104-H2S04 hydrolysis, phosphate in myelin incubation media, if present at all, was less than 0.1 pmol Pi/mg protein (data not shown). This contrasts strongly with MBP extracted from myelin membranes with nonionic detergent which contained 1.2 pmol Pi/mg protein (Riccio et al, 1985). Nonetheless, the presence of one or two phosphate groups per mole of dissociated MBP peptides cannot as yet be ruled out; such phosphates might be involved in interactions with zinc and this possibility merits further investigation.…”

Section: Discussionmentioning

confidence: 73%

Zinc Ions Stabilise the Association of Basic Protein with Brain Myelin Membranes

Earl

Chantry

Mohammad

et al. 1988

Journal of Neurochemistry

View full text Add to dashboard Cite

Myelin basic protein (MBP) dissociated from brain myelin membranes when they were incubated (37 degrees C; pH 7.4) at physiological ionic strength. Zinc ions inhibited, and calcium promoted, this process. Protease activity in the membrane preparations cleaved the dissociated MBP into both small (less than 4 kilodaltons) and large (greater than 8 kilodaltons) fragments. The latter were detected, together with intact MBP, by gel electrophoresis of incubation media. Zinc ions appeared to act in two distinct processes. In the presence or absence of added CaCl2, zinc ions in the range 0.1-1 mM inhibited MBP-membrane dissociation. This process was relatively insensitive to heat and Zn2+ could be substituted by either copper (II) or cobalt (II) ions. A second effect was evident only in the presence of added calcium ions, when lower concentrations of Zn2+ (less than 0.1 mM) inhibited MBP-membrane dissociation and the accumulation of intact MBP in incubation media. This process was heat sensitive and only copper (II), but not cobalt (II), ions could replace Zn2+. To determine whether endogenous zinc in myelin membranes is bound to MBP, preparations were solubilised in buffers containing Triton X-100/2 mM CaCl2 and subjected to gel filtration. Endogenous zinc, as indicated by a dithizone-binding method, eluted with fractions containing both MBP and proteolipid protein (PLP). Thus, one means whereby zinc stabilises association of MBP with brain myelin membranes may be by promoting its binding to PLP.

show abstract

Section: Discussionmentioning

confidence: 73%

Zinc Ions Stabilise the Association of Basic Protein with Brain Myelin Membranes

Earl

Chantry

Mohammad

et al. 1988

Journal of Neurochemistry

View full text Add to dashboard Cite

show abstract

“…The classic 18.5 kDa MBP isoform is primarily disordered in aqueous solution, but gains ordered secondary structure (a-helix, b-sheet) in the presence of lipids and detergents, a phenomenon that has been demonstrated countless times (Braun and Radin, 1969;Anthony and Moscarello, 1971;Moscarello et al, 1974;Epand et al, 1974;Liebes et al, 1975;Krigbaum and Hsu, 1975;Chapman and Moore, 1976;Smith, 1977bSmith, , 1985Smith, , 1992Chapman et al, 1978;Martenson, 1978;Littlemore and Ledeen, 1979;Smith, 1979, 1981;Hughes et al, 1982;Mendz et al, 1982Mendz et al, , 1984Mendz et al, , 1988Mendz et al, , 1991Mendz et al, , 1995bMoore, 1982;Moore, 1983, 1985;Smith et al, 1983;Cheifetz et al, 1984;Fraser and Deber, 1984;Ong and Yu, 1984;Riccio et al, 1984Riccio et al, , 1985Stone et al, 1985;Randall and Zand, 1985;Martenson et al, 1985a,b;Boggs et al, 1985a;Gow et al, 1987;Surewicz et al, 1987;Riccio et al, 1990Riccio et al, , 1994Zehetbauer et al, 1991;Hayer-Hartl et al, 1993;Reinl...…”

Section: Mbp Binds Detergents and Lipidsmentioning

confidence: 97%

Myelin basic protein—diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis

Harauz

Ishiyama

Hill

et al. 2004

Micron

233

209

View full text Add to dashboard Cite

“…Here we report that removal of the detergent from the MBP-lipid complex by long-term dialysis promoted the formation of membrane-like multilamellar assemblies whose morphology and period, as determined by electron microscopy and x-ray diffraction, resembled stacks of single myelin membranes separated by "cytoplasmic" appositions. The lipid-bound form of MBP, which is enriched in certain of the myelin lipids (Riccio et al, 1984(Riccio et al, , 1990, could correspond more closely to native MBP as it actually resides in the membrane, and thus might be a more appropriate form of the protein for studies on its role as an adhesion molecule in myelin membrane compaction and structure.…”

mentioning

confidence: 97%

Multilamellar packing of myelin modeled by lipid-bound MBP

Riccio¹,

Fasano²,

Borenshtein³

et al. 2000

J. Neurosci. Res.

Self Cite

View full text Add to dashboard Cite

Membrane compaction and adhesion at the major dense line (cytoplasmic apposition) of myelin, particularly in the central nervous system (CNS), is typically attributed to myelin basic protein (MBP). To explore the role of MBP in myelin membrane adhesion, we attempted to reconstitute the major dense line of myelin from purified lipid-bound MBP, which is a detergent-soluble form of MBP that retains the binding of all the myelin lipids. Removal of detergent by long-term dialysis yielded a precipitate, which, when analyzed by sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE) and thin-layer chromatography, contained MBP that was still associated with myelin lipids, but in different proportions than in the native membrane. Comparison of lipid composition among isolated myelin, MBP-free myelin lipids, and lipid-bound MBP aggregates showed that the lipid-bound form of the protein was specifically enriched in phosphatidylethanolamine, phosphatidylcholine, sphingomyelin, phosphatidylinositol, and phosphatidylserine. Electron microscopy and x-ray diffraction demonstrated that the lipid-MBP complexes formed multilayers having periods of 70-85 A, which correspond in width to individual myelin membranes. By contrast, the lipids alone assembled as multilayers having a period of approximately 40 A. Thus, the detergent-soluble form of MBP, which is bound to lipids, might serve as a simple model for the cytoplasmic apposition of myelin.

show abstract

A new procedure for the isolation of the brain myelin basic protein in a lipid‐bound form

Abstract: Myelin Basic protein Protein purification Lipid Protein structure Multiple sclerosis

Cited by 39 publications

References 29 publications

Zinc Ions Stabilise the Association of Basic Protein with Brain Myelin Membranes

Zinc Ions Stabilise the Association of Basic Protein with Brain Myelin Membranes

Myelin basic protein—diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis

Multilamellar packing of myelin modeled by lipid-bound MBP

Contact Info

Product

Resources

About