Interactions of free and immobilized myelin basic protein with anionic detergents

Burns, Peter F.; Campagnoni, Celia W.; Chaiken, Irwin M.; Campagnoni, Anthony T.

doi:10.1021/bi00512a016

Cited by 24 publications

(6 citation statements)

References 37 publications

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“…Intriguingly, the aggregates were dissolved with increases in the concentration of SDS. A biphasic feature in the aggregation induced by SDS was reported for melittin and myelin basic protein (28)(29)(30), where the dissolution at high SDS concentration was accompanied by global denaturation and R-helix formation. Although the aggregates were dissolved at SDS concentrations less than the CMC, we believe that this phenomenon was due to the global denaturation of β 2 -GPI or domain V by SDS micelles.…”

Section: Sds-induced Aggregation Of β 2 -Gpimentioning

confidence: 82%

Aggregation of β₂-Glycoprotein I Induced by Sodium Lauryl Sulfate and Lysophospholipids

et al. 2001

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beta(2)-Glycoprotein I (beta(2)-GPI) is a plasma protein that binds to negatively charged substances such as DNA, heparin, and anionic phospholipids. The interaction of beta(2)-GPI with anionic phospholipids is intriguing in the context of the autoimmune disease antiphospholipid syndrome. To extend understanding of the binding mechanism to phospholipids, the interactions of beta(2)-GPI with amphiphiles, i.e., sodium lauryl sulfate and lysophospholipids, were examined. These amphiphiles induced the aggregation of beta(2)-GPI below the critical micelle concentration, indicating that the interaction of beta(2)-GPI with monodispersed amphiphiles is unstable, resulting in the formation of large aggregates. However, highly soluble monocaproylphosphatidic acid did not induce aggregation, suggesting that the hydrophobicity of the acyl chain is also an important factor for aggregate formation in addition to negative charges in the headgroup. A series of experiments using deletion mutants and a peptide showed that the fifth domain of beta(2)-GPI (domain V) is responsible for formation of aggregates observed for intact full-length beta(2)-GPI. In addition, the flexible loop (F307-C326) in the C-terminal of domain V, which consists of hydrophobic and positively charged residues, was identified as the important region for aggregation. These results indicate that beta(2)-GPI binds to the amphiphiles through the flexible loop of domain V, resulting in formation of large aggregates where both electrostatic and hydrophobic interactions are involved.

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Section: Sds-induced Aggregation Of β 2 -Gpimentioning

confidence: 82%

Aggregation of β₂-Glycoprotein I Induced by Sodium Lauryl Sulfate and Lysophospholipids

et al. 2001

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“…MBPs are highly cationic, interacting with virtually any molecule with a negative charge, such as anionic lipids (Burns et al, 1981). This property requires a mechanism for targeting MBPs into the oligodendrocyte processes and sequestering them from inappropriate interactions in the process.…”

Section: Introductionmentioning

confidence: 99%

Myelin basic protein mRNA translocation in oligodendrocytes is inhibited by astrocytes in vitro

Amur‐Umarjee

Phan

Campagnoni

1993

J of Neuroscience Research

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Myelin basic protein (MBP) mRNAs are translocated from cell bodies into the slender processes connecting oligodendrocyte somas with the myelin sheath in vivo. This translocation was observed in mixed glial cultures prepared from newborn mouse brains and it occurred in approximately 25% of the cells expressing the gene. However, when "enriched" oligodendrocytes were prepared by shaking them free of other glial cells, MBP mRNA translocation occurred into the processes of essentially all of the cells. When enriched oligodendrocytes were plated back onto astrocytes, MBP mRNA was observed to be confined to the cell bodies of almost all the cells, indicating a marked inhibition of translocation of the mRNA. This inhibition of mRNA translocation did not appear to be mediated through soluble factors secreted by astrocytes or by "astromatrix," but rather through physical contact between the oligodendrocytes and astrocytes. Intact, but not necessarily live, astrocytes were required for the inhibition of mRNA translocation in the oligodendrocytes. Fibroblasts and a neuroblastoma cell line, SKN-SH, did not inhibit MBP mRNA translocation in oligodendrocytes suggesting that astrocyte surface-specific components might be involved in the interaction between astrocytes and oligodendrocytes in culture. These results suggest that contact between these two cell types can influence intramolecular events related to myelinogenesis.

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“…The interaction between MBP and SDS has also been examined in considerable detail. The binding stoichiometry was found to be approximately two detergent micelles per polypeptide over a wide range of ionic strength and pH, which is an unusually high ratio for a water-soluble protein (Smith & McDonald, 1979;Burns et al, 1981;Burns & Campagnoni, 1983).…”

Section: Discussionmentioning

confidence: 93%

Interactions between bovine myelin basic protein and zwitterionic lysophospholipids

Gow¹,

Auton²,

Smith³

1990

Biochemistry

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The binding of myelin basic protein to lysolauroylphosphatidylcholine (lysoLPC) and lysolauroylphosphatidylethanolamine was investigated at neutral pH using gel partition chromatography and equilibrium dialysis at 20 and 37 degrees C. The results show that the protein-lysolipid interactions are highly cooperative and that the free lysolipid concentration at which the binding commences is markedly influenced by both the chemical structure of the lysolipids and the temperature. The binding begins just below the critical micelle concentration for both lysolipids, which suggests that the forces governing micellization and the binding are similar. Circular dichroism (CD) spectroscopy was used to follow changes in the conformation of the protein caused by lysomyristoylphosphatidylcholine and lysoLPC. The CD results indicate that lysolipid association with the protein commences below the critical micelle concentration and continues above this concentration. Mechanisms for the lysolipid-protein interaction, which are consistent with the binding and CD data, are discussed.

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Interactions of free and immobilized myelin basic protein with anionic detergents

Cited by 24 publications

References 37 publications

Aggregation of β₂-Glycoprotein I Induced by Sodium Lauryl Sulfate and Lysophospholipids

Aggregation of β₂-Glycoprotein I Induced by Sodium Lauryl Sulfate and Lysophospholipids

Myelin basic protein mRNA translocation in oligodendrocytes is inhibited by astrocytes in vitro

Interactions between bovine myelin basic protein and zwitterionic lysophospholipids

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Interactions of free and immobilized myelin basic protein with anionic detergents

Cited by 24 publications

References 37 publications

Aggregation of β2-Glycoprotein I Induced by Sodium Lauryl Sulfate and Lysophospholipids

Aggregation of β2-Glycoprotein I Induced by Sodium Lauryl Sulfate and Lysophospholipids

Myelin basic protein mRNA translocation in oligodendrocytes is inhibited by astrocytes in vitro

Interactions between bovine myelin basic protein and zwitterionic lysophospholipids

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Product

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Aggregation of β₂-Glycoprotein I Induced by Sodium Lauryl Sulfate and Lysophospholipids

Aggregation of β₂-Glycoprotein I Induced by Sodium Lauryl Sulfate and Lysophospholipids