Lipid-protein interactions in plasma membranes of fiber cells isolated from the human eye lens.
The protein content in human lens membranes is extremely high, increases with age, and is higher in the nucleus as compared with the cortex, which should strongly affect the organization and properties of the lipid bilayer portion of intact membranes. To assess these effects, the intact cortical and nuclear fiber cell plasma membranes isolated from human lenses from 41- to 60-year-old donors were studied using electron paramagnetic resonance spin-labeling methods. Results were compared with those obtained for lens lipid membranes prepared from total lipid extracts from human eyes of the same age group [Mainali, L., Raguz, M., O'Brien, W. J., and Subczynski, W. K. (2013) Biochim. Biophys. Acta]. Differences were considered to be mainly due to the effect of membrane proteins. The lipid-bilayer portions of intact membranes were significantly less fluid than lipid bilayers of lens lipid membranes, prepared without proteins. The intact membranes were found to contain three distinct lipid environments termed the bulk lipid domain, boundary lipid domain, and trapped lipid domain. However, the cholesterol bilayer domain, which was detected in cortical and nuclear lens lipid membranes, was not detected in intact membranes. The relative amounts of bulk and trapped lipids were evaluated. The amount of lipids in domains uniquely formed due to the presence of membrane proteins was greater in nuclear membranes than in cortical membranes. Thus, it is evident that the rigidity of nuclear membranes is greater than that of cortical membranes. Also the permeability coefficients for oxygen measured in domains of nuclear membranes were significantly lower than appropriate coefficients measured in cortical membranes. Relationships between the organization of lipids into lipid domains in fiber cells plasma membranes and the organization of membrane proteins are discussed.
Department of Biophysics, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee, WI 53226, USA; Department of Medical Physics and Biophysics, School of Medicine, University of Split, Split, Croatia.
Marija
M
Raguz
Department of Biophysics, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee, WI 53226, USA.
Laxman
L
Mainali
Department of Ophthalmology, Medical College of Wisconsin, Milwaukee, WI 53226, USA.
William J
WJ
O'Brien
Department of Biophysics, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee, WI 53226, USA. Electronic address: subczyn@mcw.edu.
Witold K
WK
Subczynski
D000328:Adult; D002462:Cell Membrane / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D006801:Humans; D007908:Lens, Crystalline / Q000166:cytology / Q000378:metabolism*; D008055:Lipids / Q000032:analysis; D008563:Membrane Lipids / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D008875:Middle Aged; D013113:Spin Labels; D014019:Tissue Donors
D008055:Lipids; D008563:Membrane Lipids; D008565:Membrane Proteins; D013113:Spin Labels
cholesterol; fluidity; hydrophobic barrier; membrane domains; oxygen permeation; spin labeling