Lipid-protein interactions with native and modified myelin basic protein

Steck, Andreas; Siegrist, H P; Zahler, Peter; Herschkowitz, N

doi:10.1016/0005-2736(76)90310-2

Cited by 30 publications

(12 citation statements)

References 25 publications

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“…Our results using CD spectroscopy indicated a conformational change in rmMBP-Cit 0 induced by PI (Fig. 5), consistent with expectations from the literature (e.g., Bates et al, 2000;Polverini et al, 1999;Steck et al, 1976). For rmMBP-Cit 0 , a lipid-induced increase in ␤ sheet could have assisted in the formation of an extensive and regular quaternary organization (i.e., the polymers).…”

Section: Interactions Of Mbp With Pi-containing Monolayerssupporting

confidence: 90%

“…MBP also interacts with the acidic phospholipid PI noncovalently, but by hydrogen bonding as well as electrostatic interactions Jo and Boggs, 1995;McLaurin et al, 1990). Steck et al (1976) estimated that 15 PI molecules bound to one MBP molecule (6 PI per MBP when the lysyl residues were acetylated). The carboxyl-terminal third of the protein is the domain that interacts with acidic lipids such as PS and PI (Jones and FIG.…”

Section: Interactions Of Mbp With Pi-containing Monolayersmentioning

confidence: 98%

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The Effects of Deimination of Myelin Basic Protein on Structures Formed by Its Interaction with Phosphoinositide- Containing Lipid Monolayers

Ishiyama

Bates

Hill

et al. 2001

Journal of Structural Biology

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Section: Interactions Of Mbp With Pi-containing Monolayerssupporting

confidence: 90%

Section: Interactions Of Mbp With Pi-containing Monolayersmentioning

confidence: 98%

The Effects of Deimination of Myelin Basic Protein on Structures Formed by Its Interaction with Phosphoinositide- Containing Lipid Monolayers

Ishiyama

Bates

Hill

et al. 2001

Journal of Structural Biology

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“…It has been shown that PI induces ␤-sheet structure in the amyloid-␤ peptide (A␤), with subsequent fibril formation (103). It is also known that MBP interacts relatively strongly with PI via a combination of electrostatic, hydrogen bonding, and hydrophobic interactions (76,104,105), but not via a glycosylphosphatidylinositol (GPI) anchor (106). Riccio et al (100) have shown that lipid-bound MBP preparations are specifically enriched in certain lipids, including PI.…”

Section: Transmission Electron Microscopy Of Rmmbpmentioning

confidence: 97%

Characterization of a Recombinant Murine 18.5-kDa Myelin Basic Protein

Bates

Matharu

Ishiyama

et al. 2000

Protein Expression and Purification

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“…It appears to interact with lipid primarily through electrostatic interactions since it binds only to acid lipids (Palmer & Dawson, 1969;Demel et al, 1973;Steck et al, 1976), has 25 ~o basic amino acids distributed throughout the molecule and its binding can be inhibited by high salt concentrations. However, studies with bovine basic protein indicate that part of the molecule penetrates into the hydrocarbon region to interact hydrophobically with the lipid fatty acid chains, since it increases the permeability of lipid vesicles to glucose (Gould & London, 1972) and Na § (Papahadjopoulos et al, 1975a) and expands monolayers (Demel et al, 1973 ;Papahadjopoulos, 1975).…”

mentioning

confidence: 99%

Effect of basic protein from human central nervous system myelin on lipid bilayer structure

1978

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The effect of myelin basic protein from normal human central nervous system on lipid organization has been investigated by studying model membranes containing the protein by differential scanning calorimetry or electron spin resonance spectroscopy. Basic protein was found to decrease the phase transition temperature of dipalmitoyl phosphatidylglycerol, phosphatidic acid, and phosphatidylserine. The protein had a greater effect on the freezing temperature, measured from the cooling scan, than on the melting temperature, measured from the heating scan. These results are consistent with partial penetration of parts of the protein into the hydrocarbon region of the bilayer in the liquid crystalline state and partial freezing out when the lipid has been cooled below its phase transition temperature. The effect of the protein on fatty acid chain packing was investigated by using a series of fatty acid spin labels with the nitroxide group located at different positions along the chain. If the protein has not yet penetrated, it increases the order throughout the bilayer in the gel phase, probably by decreasing the repulsion between the lipid polar head groups. Above the phase transition temperature, when parts of it are able to pentrate, it decreases the motion of the lipid fatty acid chains greatly near the polar head group region, but has little or no effect near the interior of the bilayer. Upon cooling again the protein still decreases the motion near the polar head group region but increases it greatly in the interior. Thus, the protein penetrates partway into the bilayer, distorts the packing of the lipid fatty acid chains, and prevents recrystallization, thus decreasing the phase transition temperature. The magnitude of the effect varied with the lipid and was greatest for phosphatidic acid and phosphatidylglycerol. It could be reversed upon cooling for phosphatidylglycerol but not phosphatidic acid. The protein was only observed to decrease the phase transition temperature of phosphatidylserine upon cooling. It had only a small effect on phosphatidylethanolamine and no effect on phosphatidylcholine. Thus, the protein may penetrate to a different extent into different lipids even if it binds to the polar head group region by electrostatic interactions.

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Lipid-protein interactions with native and modified myelin basic protein

Cited by 30 publications

References 25 publications

The Effects of Deimination of Myelin Basic Protein on Structures Formed by Its Interaction with Phosphoinositide- Containing Lipid Monolayers

The Effects of Deimination of Myelin Basic Protein on Structures Formed by Its Interaction with Phosphoinositide- Containing Lipid Monolayers

Characterization of a Recombinant Murine 18.5-kDa Myelin Basic Protein

Effect of basic protein from human central nervous system myelin on lipid bilayer structure

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