title: Lysenin-sphingomyelin binding at the surface of oligodendrocyte lineage cells increases during differentiation in vitro.
abstract: We have investigated the relationship between the developmental expression of sphingomyelin, a major component of myelin, and oligodendrocyte lineage. Using lysenin as a cytochemical probe for membrane sphingomyelin, we have now determined the distribution pattern of sphingomyelin on the plasma membrane of rat cultured oligodendrocytes. Although lysenin does not bind to A2B5(+)/NG2(+) bipolar oligodendrocyte progenitors, lysenin recognizes sphingomyelin on the cell bodies of multipolar A2B5(+) cells, but not on their processes. O4(+) and O1(+) immature and MBP(+) mature oligodendrocytes are strongly labeled by lysenin from cell bodies to the tips of processes. The content of sphingomyelin in immature and mature oligodendrocytes is approximately 2-fold higher than that in oligodendrocyte progenitors. These findings show that sphingomyelin increases during differentiation of cells in the oligodendrocyte lineage. In multipolar oligodendrocyte progenitors exposed to Triton X-100 at 4 degrees C, lysenin labels cell processes in addition to cell bodies. In contrast, Triton X-100 extraction does not alter the distribution of lysenin binding on O4(+), O1(+) and MBP(+) cells, although the immunocytochemical intensities of the lysenin bindings increase. Our data suggest that the alteration in sphingomyelin content and distribution in the oligodendrocyte lineage cells could have important consequences for cell recognition and downstream signaling events through sphingomyelin-rich domains.
authors.affiliation: Department of Physiology, Keio University, Tokyo, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Nakai
authors.forename: Y
authors.initials: Y
authors.lastname: Sakurai
authors.forename: A
authors.initials: A
authors.lastname: Yamaji
authors.forename: H
authors.initials: H
authors.lastname: Asou
authors.forename: M
authors.initials: M
authors.lastname: Umeda
authors.forename: K
authors.initials: K
authors.lastname: Uyemura
authors.forename: K
authors.initials: K
authors.lastname: Itoh
mesh_terms: D000818:Animals; D001665:Binding Sites / Q000187:drug effects / Q000502:physiology; D001921:Brain / Q000166:cytology / Q000196:embryology* / Q000378:metabolism; D002450:Cell Communication / Q000187:drug effects / Q000502:physiology; D002451:Cell Compartmentation / Q000187:drug effects / Q000502:physiology; D002454:Cell Differentiation / Q000187:drug effects / Q000502:physiology*; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism; D002784:Cholesterol / Q000378:metabolism; D005260:Female; D005333:Fetus; D005372:Filipin / Q000494:pharmacology; D018507:Gene Expression Regulation, Developmental / Q000187:drug effects / Q000502:physiology; D006026:Glycoside Hydrolases / Q000494:pharmacology; D008049:Lipase / Q000494:pharmacology; D017830:Octoxynol / Q000494:pharmacology; D009836:Oligodendroglia / Q000166:cytology / Q000187:drug effects / Q000378:metabolism*; D010641:Phenotype; D011247:Pregnancy; D011506:Proteins / Q000494:pharmacology*; D051381:Rats; D015398:Signal Transduction / Q000187:drug effects / Q000502:physiology; D013109:Sphingomyelins / Q000096:biosynthesis*; D013234:Stem Cells / Q000166:cytology / Q000187:drug effects / Q000378:metabolism*; D014118:Toxins, Biological; D014662:Vasoconstrictor Agents / Q000494:pharmacology*
chemical_list: D011506:Proteins; D013109:Sphingomyelins; D014118:Toxins, Biological; D014662:Vasoconstrictor Agents; C107040:lysenin; D005372:Filipin; D017830:Octoxynol; D002784:Cholesterol; D008049:Lipase; D006026:Glycoside Hydrolases