Literature DB >> 6174152

The effects of bovine myelin basic protein on the phase transition properties of sphingomyelin.

R M Epand, M A Moscarello.   

Abstract

The basic protein of myelin can spontaneously associate with the synthetic phospholipid N-palmitoyl-sphingosinephosphatidylcholine. The protein alters the phase transition properties of the lipid from a single transition at 41.5 degrees C to two overlapping transitions, one being slightly above and the other slightly below the transition temperature of the pure lipid. The effect was not seen upon the addition of poly(L-lysine) to this lipid nor does the myelin basic protein alter the phase transition properties of dimyristoylphosphatidylcholine. The results thus demonstrate that the myelin basic protein can interact with a major zwitterionic lipid component of myelin in addition to acidic phospholipids.

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Year:  1982        PMID: 6174152     DOI: 10.1016/0005-2736(82)90105-5

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  4 in total

1.  Effect of chemical modifications of myelin basic protein on its interaction with lipid interfaces and cell fusion ability.

Authors:  C G Monferran; B Maggio; F A Cumar
Journal:  Mol Cell Biochem       Date:  1986-05       Impact factor: 3.396

2.  Cardiolipin remodeling enables protein crowding in the inner mitochondrial membrane.

Authors:  Yang Xu; Hediye Erdjument-Bromage; Colin K L Phoon; Thomas A Neubert; Mindong Ren; Michael Schlame
Journal:  EMBO J       Date:  2021-10-18       Impact factor: 11.598

3.  Sphingomyelin/phosphatidylcholine/cholesterol phase diagram: boundaries and composition of lipid rafts.

Authors:  Rodrigo F M de Almeida; Aleksandre Fedorov; Manuel Prieto
Journal:  Biophys J       Date:  2003-10       Impact factor: 4.033

4.  Phospholipid vesicle aggregation induced by human myelin basic protein.

Authors:  S I Sridhara; R M Epand; M A Moscarello
Journal:  Neurochem Res       Date:  1984-02       Impact factor: 3.996

  4 in total

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