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Plasma membrane of cultured oligodendrocytes: II. Possible structural and functional domains
Author(s) -
Szuchet Sara,
Polak Paul E.,
Yim Sung Hye,
Lange Yvonne
Publication year - 1988
Publication title -
glia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.954
H-Index - 164
eISSN - 1098-1136
pISSN - 0894-1491
DOI - 10.1002/glia.440010107
Subject(s) - vesicle , biology , membrane , golgi apparatus , membrane protein , membrane glycoproteins , golgi membrane , biochemistry , oligodendrocyte , membrane structure , density gradient , differential centrifugation , glycoprotein , polyacrylamide gel electrophoresis , centrifugation , myelin , chromatography , chemistry , endoplasmic reticulum , physics , quantum mechanics , neuroscience , enzyme , central nervous system
An oligodendrocyte plasma membrane‐rich fraction, F2.2, was resolved by equilibrium density centrifugation on a linear sucrose gradient from 0.5 M to 1.3 M into three fractions, F2.2a, F.2.2b, F2.2c, and a pellet F2.2p. F2.2a and F.2.2b were enriched 1.5‐fold relative to F2.2 in plasma membrane markers at the expense of F2.2c and F2.2p, which became correspondingly impoverished. This gave F2.2a and F2.2b a 42‐fold and 37‐fold enrichment, respectively, in plasma membrane markers relative to the initial cell homogenate. F2.2c had a sevenfold enrichment in a Golgi marker; together with F2.2p, they contained all the Golgi marker initially present in F2.2. Preliminary data indicated that the F2.2‐subfractions differed from one another in their molar ratios of cholesterol to phospholipids and protein to lipids but had similar protein profiles when examined by sodium dodecylsulfate‐polyacrylamide gel electrophoresis. Their content of fucosylated glycoproteins appeared also to be different. Morphologically, F2.2a and F2.2b were very similar: they contained large membrane vesicles, membrane sheets, and vesicles entrapped within other vesicles. Membrane‐membrane interaction was apparent in these fractions. F2.2c had many of the same elements, but most of the membrane structures contained amorphous material. F2.2p differed morphologically from the other fractions in that it had principally electron‐dense structures. It is postulated that F2.2a, F2.2b, and perhaps F2.2c represent different domains of oligodendrocyte plasma membrane. Alternatively, these fractions might correspond to the plasma membrane of oligodendrocyte subtypes.