The Folch-Lees proteolipid induces phase coexistence and transverse reorganization of lateral domains in myelin monolayers.
Solvent solubilized myelin membranes spread as monomolecular layers at the air-water interface show a heterogeneous pattern at all surface pressures. In order to asses the role of myelin protein and lipid components in the surface structuring we compared the topography, as seen by Brewster angle microscopy (BAM) and epifluorescence microscopy, of monolayers made from mixtures containing all myelin lipids (except gangliosides) and variable proportions of Folch-Lees proteolipid protein (PLP, the major protein component of myelin). The presence of the single PLP, in the absence of the other myelin proteins, can reproduce the surface pattern of the whole myelin extract films in a concentration-dependant manner. Moreover, a threshold mole fraction of PLP is necessary to induce the lipid-protein component reorganization leading to the appearance of a rigid (gray) phase, acting as a surface skeleton, at low surface pressures and of fractal clusters at high surface pressures. The average size of those clusters is also dependent on the PLP content in the monolayer and on the time elapsed from the moment of film spreading, as they apparently result from an irreversible lateral aggregation process. The transverse rearrangement of the monolayer occurring under compression was different in films with the highest and lowest PLP mole fractions tested.
Rosetti
C M
CM
Departamento de Química Biológica-CIQUIBIC, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Ciudad Universitaria, 5000 Córdoba, Argentina.
Oliveira
R G
RG
Maggio
B
B
D000818:Animals; D002417:Cattle; D005453:Fluorescence; D008853:Microscopy; D018991:Myelin Proteolipid Protein / Q000737:chemistry* / Q000378:metabolism*; D009186:Myelin Sheath / Q000737:chemistry* / Q000378:metabolism*
D018991:Myelin Proteolipid Protein