Variable interaction of spin-labeled human myelin basic protein with different acidic lipids

Stollery, John G.; Boggs, Joan M.; Moscarello, Mario A.

doi:10.1021/bi00547a028

Cited by 40 publications

(16 citation statements)

References 38 publications

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“…In a recent study Lampe et al (1983) suggest that the mechanism of the promotion of vesicle aggregation by MBP is through protein-protein interactions. The interaction with zwitterionic PC is much weaker than that with acid phospholipids (Palmer and Dawson, 1969;Boggs and Moscarello, 1978;Stollery et al, 1980) and no aggregation of PC vesicles by MBP was observed by Young et al (1982) or under the conditions of the present study. This is Tabulated values are the measured absorbance changes at 400 nm due 10 increased turbidity occurring as a result of the addition of the given amount of MBP, PLL, or PLA to 3 ml of sonicated vesicles (lipid concentration = 0.5 mdml) in 0.01 M HEPES, 0.1 M NaCl, 0.02% NaN,, pH 7.4, at 37°C.…”

Section: Discussioncontrasting

confidence: 61%

“…In all of our studies we compared the effects of MBP with nonspecific effects induced by PLL. We compared the properties of vesicles made solely of PC with those admixed with sphingomyelin (SM), a phospholipid thought to interact more strongly with MBP (Epand and Moscarello, 1982); or admixed with phosphatidylethanolamine (PE), a phospholipid that interacts with MBP (Stollery and Vail, 1977) and that more readily forms a hexagonal phase (Cullis and DeKruijff, 1978); or admixed with phosphatidylglycerol (PG), a negatively charged phospholipid that interacts strongly with MBP (Boggs and Moscarello, 1978;Stollery et al, 1980). In the course of this work it was observed that vesicles containing PE extracted from bovine brain were much more readily aggregated by MBP than were vesicles containing equivalent amounts of PE made from egg PC.…”

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confidence: 99%

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Effect of Lipid Structure on the Capacity of Myelin Basic Protein to Alter Vesicle Properties: Potent Effects of Aliphatic Aldehydes in Promoting Basic Protein‐Induced Vesicle Aggregation

Epand

Dell

Surewicz

et al. 1984

Journal of Neurochemistry

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The capacity of myelin basic protein or of poly-L-lysine to promote leakage of carboxyfluorescein from vesicles or the aggregation of vesicles was studied. The vesicles were composed of phosphatidylcholine as the sole or major lipid component. Addition of 10% sphingomyelin, 10% phosphatidylglycerol, 10% egg or bovine brain phosphatidylethanolamine, or 30% dodecanal had relatively little effect on the extent of carboxyfluorescein release in the presence of either myelin basic protein or poly-L-lysine. In contrast with these results, the extent of vesicle aggregation was very sensitive to lipid composition. Addition of 10% phosphatidylglycerol induced more aggregation than the other phospholipids tested. Admixing 10% of a partially degraded sample of bovine brain phosphatidylethanolamine also led to a large amount of aggregation induced by the myelin basic protein. This latter aggregation appeared more specific for the basic protein, as it occurred to a much smaller extent with poly-L-lysine. In general, the effects of the myelin basic protein on either carboxyfluorescein release or vesicle aggregation were similar to, although somewhat greater than, that of poly-L-lysine. The aggregation of vesicles containing degradation products of phosphatidylethanolamine can be ascribed largely to the presence of aliphatic aldehydes. The effect of aliphatic aldehydes was specific in that the aliphatic alcohol, hexadecanol, or the short-chain aldehydes, acetaldehyde or butyraldehyde, did not promote myelin basic protein-induced vesicle aggregation. In addition, poly-L-lysine was less effective than the basic protein in aggregating vesicles containing aliphatic aldehydes. (ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Discussioncontrasting

confidence: 61%

mentioning

confidence: 99%

Effect of Lipid Structure on the Capacity of Myelin Basic Protein to Alter Vesicle Properties: Potent Effects of Aliphatic Aldehydes in Promoting Basic Protein‐Induced Vesicle Aggregation

Epand

Dell

Surewicz

et al. 1984

Journal of Neurochemistry

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“…Light and X-ray scattering have provided information on global features such as size and shape of MBP and MBP -lipid complexes under various conditions (Liebes et al, 1975(Liebes et al, , 1976Murthy et al, 1984;Mendz et al, 1988Mendz et al, , 1991Mendz et al, , 1995bRiccio et al, 1995;Boggs et al, 1999;Mac Millan et al, 2000;Haas et al, 2004;Libich et al, 2003a). Electron paramagnetic (or spin) resonance (EPR or ESR) (Boggs and Moscarello, 1978;Boggs et al, 1980Boggs et al, , 1981aBoggs et al, ,b, 1985bStollery et al, 1980a;Mendz et al, 1988Mendz et al, , 1991Mendz et al, , 1995bBates et al, , 2004, and nuclear magnetic resonance (NMR) spectrometry (Liebes et al, 1975(Liebes et al, , 1976Chapman and Moore, 1976;Chapman et al, 1978;Keniry and Smith, 1980;Stollery et al, 1980b;Hughes et al, 1982;Mendz et al, 1982Mendz et al, , 1983aMendz et al, , b, 1984Mendz et al, , 1986Mendz et al, , 1988Mendz et al, , 1990Mendz et al, , 1991Mendz et al, , 1992Mendz et al, , 1995aMoore, 1983, 1985;Deber et al, 1983Deber et al, , 1986Smith et al, 1983;…”

Section: Spectroscopic and Spectrometric Studies Of Mbpmentioning

confidence: 99%

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

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“…In this sense, it has been described that myelin basic protein exhibits both electrostatic and hydrophobic components on its interaction with PG vesicles. This last has been attributed to the existence of some segments of hydrophobic and/or uncharged residues, despite the fact that the protein is highly basic (Boggs et al, 1980;Stollery et al, 1980). This also occurs for aL-sarcin.…”

Section: Aggregation Of Phospholipid Vesicles Induced By O-sarcinmentioning

confidence: 99%

Study of the interaction between the antitumour protein α-sarcin and phospholipid vesicles

Gasset

Martínez‐del‐Pozo

Oñaderra

et al. 1989

Biochemical Journal

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alpha-Sarcin is a single polypeptide chain protein which exhibits antitumour activity by degrading the larger ribosomal RNA of tumour cells. We describe the interaction of a alpha-sarcin with lipid model systems. The protein specifically interacts with negatively-charged phospholipid vesicles, resulting in protein-lipid complexes which can be isolated by ultracentrifugation in a sucrose gradient. alpha-Sarcin causes aggregation of such vesicles. The extent of this interaction progressively decreases when the molar ratio of phosphatidylcholine increases in acidic vesicles. The kinetics of the vesicle aggregation induced by the protein have been measured. This process is dependent on the ratio of alpha-sarcin present in the protein-lipid system. A saturation plot is observed from phospholipid vesicles-protein titrations. The saturating protein/lipid molar ratio is 1:50. The effect produced by the antitumour protein on the lipid vesicles is dependent on neither the length nor the degree of unsaturation of the phospholipid acyl chain. However, the aggregation is dependent on temperature, being many times higher above the phase transition temperature of the corresponding phospholipid than below it. The effects of pH and ionic strength have also been considered. An increase in the ionic strength does not abolish the protein-lipid interaction. The effect of pH may be related to conformational changes of the protein. Binding experiments reveal a strong interaction between alpha-sarcin and acidic vesicles, with Kd = 0.06 microM. The peptide bonds of the protein are protected against trypsin hydrolysis upon binding to acidic vesicles. The interaction of the protein with phosphatidylglycerol vesicles does not modify the phase transition temperature of the lipid, although it decreases the amplitude of the change of fluorescence anisotropy associated to the co-operative melting of 1,6-diphenyl-1,3,5-hexatriene (DPH)-labelled vesicles. The results are interpreted in terms of the existence of both electrostatic and hydrophobic components for the interaction between phospholipid vesicles and the antitumour protein.

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Variable interaction of spin-labeled human myelin basic protein with different acidic lipids

Cited by 40 publications

References 38 publications

Effect of Lipid Structure on the Capacity of Myelin Basic Protein to Alter Vesicle Properties: Potent Effects of Aliphatic Aldehydes in Promoting Basic Protein‐Induced Vesicle Aggregation

Effect of Lipid Structure on the Capacity of Myelin Basic Protein to Alter Vesicle Properties: Potent Effects of Aliphatic Aldehydes in Promoting Basic Protein‐Induced Vesicle Aggregation

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

Study of the interaction between the antitumour protein α-sarcin and phospholipid vesicles

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