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Wilhelm Stoffel - One of the best experts on this subject based on the ideXlab platform.
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composition and biophysical properties of myelin lipid define the neurological defects in Galactocerebroside and sulfatide deficient mice
Journal of Neurochemistry, 2002Co-Authors: Andreas Bosio, Erika Binczek, W F Haupt, Wilhelm StoffelAbstract:Abstract: Oligodendrocytes and Schwann cell-specific proteins are assembled with a highly ordered membrane lipid bilayer to the myelin sheath of axons, which functions as an insulator and allows rapid saltatory conduction. We approached the question of the function of the CNS and PNS myelin-specific galactospingolipids cerebrosides and sulfatides by generating a ceramide galactosyltransferase null allelic mouse line (cgt−/−). Galactocerebroside- and sulfatide-deficient myelin loses its insulating properties and causes a severe dysmyelinosis that is incompatible with life. Here, we describe the biochemical and biophysical analysis of the myelin lipid bilayer of cgt−/− mice. The lipid composition of CNS and PNS myelin of cgt−/− mice is seriously perturbed and the sphingolipid biosynthetic pathway altered. Nonhydroxy and hydroxy fatty acid-substituted glycosylceramides (GlcC) are synthesized by oligodendrocytes and sulfated GlcC in addition in Schwann cells. The monogalactosyldiglyceride fraction is missing in the cgt−/− mouse. This new lipid composition can be correlated with the biophysical properties of the myelin sheath. The deficiency of Galactocerebrosides and sulfatides leads to an increased fluidity, permeability, and impaired packing of the myelin lipid bilayer of the internodal membrane system. The loss of the two glycosphingolipid classes causes the breakdown of saltatory conductance of myelinated axons in the cgt−/− mouse.
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Composition and Biophysical Properties of Myelin Lipid Define the Neurological Defects in Galactocerebroside‐ and Sulfatide‐Deficient Mice
Journal of neurochemistry, 2002Co-Authors: Andreas Bosio, Erika Binczek, W F Haupt, Wilhelm StoffelAbstract:Abstract: Oligodendrocytes and Schwann cell-specific proteins are assembled with a highly ordered membrane lipid bilayer to the myelin sheath of axons, which functions as an insulator and allows rapid saltatory conduction. We approached the question of the function of the CNS and PNS myelin-specific galactospingolipids cerebrosides and sulfatides by generating a ceramide galactosyltransferase null allelic mouse line (cgt−/−). Galactocerebroside- and sulfatide-deficient myelin loses its insulating properties and causes a severe dysmyelinosis that is incompatible with life. Here, we describe the biochemical and biophysical analysis of the myelin lipid bilayer of cgt−/− mice. The lipid composition of CNS and PNS myelin of cgt−/− mice is seriously perturbed and the sphingolipid biosynthetic pathway altered. Nonhydroxy and hydroxy fatty acid-substituted glycosylceramides (GlcC) are synthesized by oligodendrocytes and sulfated GlcC in addition in Schwann cells. The monogalactosyldiglyceride fraction is missing in the cgt−/− mouse. This new lipid composition can be correlated with the biophysical properties of the myelin sheath. The deficiency of Galactocerebrosides and sulfatides leads to an increased fluidity, permeability, and impaired packing of the myelin lipid bilayer of the internodal membrane system. The loss of the two glycosphingolipid classes causes the breakdown of saltatory conductance of myelinated axons in the cgt−/− mouse.
Andreas Bosio - One of the best experts on this subject based on the ideXlab platform.
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composition and biophysical properties of myelin lipid define the neurological defects in Galactocerebroside and sulfatide deficient mice
Journal of Neurochemistry, 2002Co-Authors: Andreas Bosio, Erika Binczek, W F Haupt, Wilhelm StoffelAbstract:Abstract: Oligodendrocytes and Schwann cell-specific proteins are assembled with a highly ordered membrane lipid bilayer to the myelin sheath of axons, which functions as an insulator and allows rapid saltatory conduction. We approached the question of the function of the CNS and PNS myelin-specific galactospingolipids cerebrosides and sulfatides by generating a ceramide galactosyltransferase null allelic mouse line (cgt−/−). Galactocerebroside- and sulfatide-deficient myelin loses its insulating properties and causes a severe dysmyelinosis that is incompatible with life. Here, we describe the biochemical and biophysical analysis of the myelin lipid bilayer of cgt−/− mice. The lipid composition of CNS and PNS myelin of cgt−/− mice is seriously perturbed and the sphingolipid biosynthetic pathway altered. Nonhydroxy and hydroxy fatty acid-substituted glycosylceramides (GlcC) are synthesized by oligodendrocytes and sulfated GlcC in addition in Schwann cells. The monogalactosyldiglyceride fraction is missing in the cgt−/− mouse. This new lipid composition can be correlated with the biophysical properties of the myelin sheath. The deficiency of Galactocerebrosides and sulfatides leads to an increased fluidity, permeability, and impaired packing of the myelin lipid bilayer of the internodal membrane system. The loss of the two glycosphingolipid classes causes the breakdown of saltatory conductance of myelinated axons in the cgt−/− mouse.
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Composition and Biophysical Properties of Myelin Lipid Define the Neurological Defects in Galactocerebroside‐ and Sulfatide‐Deficient Mice
Journal of neurochemistry, 2002Co-Authors: Andreas Bosio, Erika Binczek, W F Haupt, Wilhelm StoffelAbstract:Abstract: Oligodendrocytes and Schwann cell-specific proteins are assembled with a highly ordered membrane lipid bilayer to the myelin sheath of axons, which functions as an insulator and allows rapid saltatory conduction. We approached the question of the function of the CNS and PNS myelin-specific galactospingolipids cerebrosides and sulfatides by generating a ceramide galactosyltransferase null allelic mouse line (cgt−/−). Galactocerebroside- and sulfatide-deficient myelin loses its insulating properties and causes a severe dysmyelinosis that is incompatible with life. Here, we describe the biochemical and biophysical analysis of the myelin lipid bilayer of cgt−/− mice. The lipid composition of CNS and PNS myelin of cgt−/− mice is seriously perturbed and the sphingolipid biosynthetic pathway altered. Nonhydroxy and hydroxy fatty acid-substituted glycosylceramides (GlcC) are synthesized by oligodendrocytes and sulfated GlcC in addition in Schwann cells. The monogalactosyldiglyceride fraction is missing in the cgt−/− mouse. This new lipid composition can be correlated with the biophysical properties of the myelin sheath. The deficiency of Galactocerebrosides and sulfatides leads to an increased fluidity, permeability, and impaired packing of the myelin lipid bilayer of the internodal membrane system. The loss of the two glycosphingolipid classes causes the breakdown of saltatory conductance of myelinated axons in the cgt−/− mouse.
C. De Michelis - One of the best experts on this subject based on the ideXlab platform.
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anti sulfatide Galactocerebroside antibodies in immunoglobulin m paraproteinemic neuropathies
European Journal of Neurology, 2017Co-Authors: Francesca Boso, S Ruggero, Luana Benedetti, Girolama A Marfia, Marta Campagnolo, Alessandro Salvalaggio, Francesca Gallia, Claudia Giannotta, Mario Ermani, C. De MichelisAbstract:BACKGROUND AND PURPOSE: Anti-sulfatide antibodies have been observed in heterogeneous neuropathies and their clinical relevance is still controversial. Whether the combination of sulfatide with Galactocerebroside would increase sensitivity or specificity of enzyme-linked immunosorbent assay testing compared to sulfatide alone was assessed. METHODS: Immunoglobulin M (IgM) antibodies to sulfatides, Galactocerebroside and combined sulfatide and Galactocerebroside (Sulf/GalC) were measured in 229 neuropathy patients, including 73 with IgM paraproteinemic neuropathy [62 with anti-myelin-associated glycoprotein (anti-MAG) antibody] and 156 with other neuropathies. Results from 27 patients with IgM monoclonal gammopathy without neuropathy and 28 healthy subjects served as control. RESULTS: Thirty-three patients showed increased titers of anti-sulfatide antibodies, 28 of whom had an IgM paraproteinemic neuropathy (P < 0.0001). When evaluating the reactivity for the combination Sulf/GalC, 57/229 patients were found to be positive, including 36/73 (49%) with IgM paraproteinemic neuropathy (P < 0.0001). Patients with known anti-sulfatide antibodies also showed anti-Sulf/GalC reactivity, with increased titers in 48.5% of the cases. Testing for anti-Sulf/GalC antibodies allowed 24 additional patients to be detected (eight with IgM paraproteinemic neuropathies), who had no reactivity to the individual glycolipids. Amongst the 11 subjects with IgM paraproteinemic neuropathy who were negative for anti-MAG antibodies, only two were reactive to sulfatide, whilst six (55%) were found to be positive when tested against the combination of sulfatide and Galactocerebroside. CONCLUSIONS: Testing for both sulfatide and Galactocerebroside in IgM paraproteinemic neuropathies seems to increase the sensitivity compared to anti-sulfatide antibodies alone (49% and 39%, respectively, with a slightly reduced specificity, from 97% to 87%), helping the characterization of otherwise undefined neuropathy that could benefit from immunomodulatory therapy.
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Anti-sulfatide/Galactocerebroside antibodies in immunoglobulin M paraproteinemic neuropathies
European journal of neurology, 2017Co-Authors: Francesca Boso, S Ruggero, Girolama A Marfia, Marta Campagnolo, Alessandro Salvalaggio, Francesca Gallia, Claudia Giannotta, Mario Ermani, Laura Benedetti, C. De MichelisAbstract:BACKGROUND AND PURPOSE: Anti-sulfatide antibodies have been observed in heterogeneous neuropathies and their clinical relevance is still controversial. Whether the combination of sulfatide with Galactocerebroside would increase sensitivity or specificity of enzyme-linked immunosorbent assay testing compared to sulfatide alone was assessed. METHODS: Immunoglobulin M (IgM) antibodies to sulfatides, Galactocerebroside and combined sulfatide and Galactocerebroside (Sulf/GalC) were measured in 229 neuropathy patients, including 73 with IgM paraproteinemic neuropathy [62 with anti-myelin-associated glycoprotein (anti-MAG) antibody] and 156 with other neuropathies. Results from 27 patients with IgM monoclonal gammopathy without neuropathy and 28 healthy subjects served as control. RESULTS: Thirty-three patients showed increased titers of anti-sulfatide antibodies, 28 of whom had an IgM paraproteinemic neuropathy (P < 0.0001). When evaluating the reactivity for the combination Sulf/GalC, 57/229 patients were found to be positive, including 36/73 (49%) with IgM paraproteinemic neuropathy (P < 0.0001). Patients with known anti-sulfatide antibodies also showed anti-Sulf/GalC reactivity, with increased titers in 48.5% of the cases. Testing for anti-Sulf/GalC antibodies allowed 24 additional patients to be detected (eight with IgM paraproteinemic neuropathies), who had no reactivity to the individual glycolipids. Amongst the 11 subjects with IgM paraproteinemic neuropathy who were negative for anti-MAG antibodies, only two were reactive to sulfatide, whilst six (55%) were found to be positive when tested against the combination of sulfatide and Galactocerebroside. CONCLUSIONS: Testing for both sulfatide and Galactocerebroside in IgM paraproteinemic neuropathies seems to increase the sensitivity compared to anti-sulfatide antibodies alone (49% and 39%, respectively, with a slightly reduced specificity, from 97% to 87%), helping the characterization of otherwise undefined neuropathy that could benefit from immunomodulatory therapy.
S. E. Pfeiffer - One of the best experts on this subject based on the ideXlab platform.
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novel stage in the oligodendrocyte lineage defined by reactivity of progenitors with r mab prior to o1 anti Galactocerebroside
Journal of Neuroscience Research, 1992Co-Authors: Rashmi Bansal, S. E. PfeifferAbstract:The developmentally regulated appearance of surface immuno-reactivity of proligodendroblasts [oligodendrocyte progenitors reacting with monoclonal antibodies A007 and O4, but not anti-Galactocerebroside (GalC), i.e., A007/O4+ GalC−] to monoclonal antibodies R-mAb and O1 was studied both in culture and in vivo. In both cases staining with R-mAb shortly preceded that with O1; that is, a transient population of R-mAb+ O1− cells was observed. R-mAb− O1+ cells were not detected. Differential staining with R-mAb and O1 was also noted at the subcellular level. In younger cultures in which R-mAb+ cells were first acquiring O1 immunoreactivity, many of these cells were stained by O1 only on the cell bodies and proximal portions of the processes, whereas in contrast R-mAb stained the whole cell, including the distal portions of the processes. Only in older, more mature R-mAb+ cells did O1 also stain the distal portions of processes. The expression of reactivity to R-mAb and O1 was compared to the proliferative capacity of the cells. Proliferation [assessed by bromodeoxyuridine (BrdU) incorporation] of both R-mAb+ and O1+ cells was negligible both in culture and in vivo. However, treatment of cells in culture with 10 ng/ml basic fibroblast growth factor resulted in an enhancement of proliferation of the R-mAb+ cells. Within the proliferating R-mAb+BrdU+ population, 80% of the cells were O1− (i.e., anti-Galactocerebroside negative). These events occur during a critical period of development when A007/O4+ proligodendroblasts begin to become post-mitotic and express surface Galactocerebroside. The data demonstrate that the use of R-mAb as an “anti-GalC” must be interpreted with caution, and indicate the utility of dual staining with R-mAb and O1 to (1) further subdivide the oligodendrocyte lineage, thus identifying an additional, GalC− developmental compartment, and (2) observe the distribution of R-mAb and O1 immunoreactivity at a subcellular level. © 1992 Wiley-Liss, Inc.
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proligodendroblast antigen poa a developmental antigen expressed by a007 o4 positive oligodendrocyte progenitors prior to the appearance of sulfatide and Galactocerebroside
Journal of Neurochemistry, 1992Co-Authors: Rashmi Bansal, Kari Stefansson, S. E. PfeifferAbstract:: Evidence is presented for the immunological identification of a developmental antigen appearing at a critical point in the oligodendroglial lineage. Specifically, monoclonal antibody A007 recognizes cells in the oligodendrocyte lineage at two distinct stages. Analyses of purified lipid standards and lipid extracts from Galactocerebroside-positive (GalC+) oligodendrocytes by enzyme-linked immunosorbent assay, lipid dot blot, and immuno-TLC demonstrated that A007 recognizes sulfatide (SUL) and seminolipid. However, neither 35SO4 incorporation into SUL nor SUL accumulation could be detected in A007-positive cells lacking Galactocerebroside (i.e., A007+GalC− progenitor cells) present early in development. These data suggest that A007 also recognizes an antigen, named proligodendroblast antigen (POA), that appears during the late stage of oligodendrocyte progenitor development prior to the expression by oligodendrocytes of SUL and GalC. We have previously reported that monoclonal antibody O4 also recognizes not only SUL and seminolipid, but in addition an antigen that appears prior to the expression of SUL and Galactocerebroside. In the present study all A007+ cells were also O4+ (and vice versa), and the developmental patterns of the two antibodies appeared to be identical. We conclude that (1) A007 is similar or identical to O4 with respect to its antigenic specificity, and (2) during oligodendrocyte lineage progression both antibodies react first with antigen POA on the surface of the oligodendrocyte progenitor cell prior to the expression of SUL [i.e., A007+O4+(POA+)SUL−GalC− proligodendroblasts], and only later with SUL as terminally differentiating oligodendrocytes emerge (i.e., A007+-O4+SUL+GalC+ oligodendrocytes).
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proligodendroblast antigen poa a developmental antigen expressed by a007 o4 positive oligodendrocyte progenitors prior to the appearance of sulfatide and Galactocerebroside
Journal of Neurochemistry, 1992Co-Authors: Rashmi Bansal, Kari Stefansson, S. E. PfeifferAbstract:Evidence is presented for the immunological identification of a developmental antigen appearing at a critical point in the oligodendroglial lineage. Specifically, monoclonal antibody A007 recognizes cells in the oligodendrocyte lineage at two distinct stages. Analyses of purified lipid standards and lipid extracts from Galactocerebroside-positive (GalC+) oligodendrocytes by enzyme-linked immunosorbent assay, lipid dot blot, and immuno-TLC demonstrated that A007 recognizes sulfatide (SUL) and seminolipid. However, neither 35SO4 incorporation into SUL nor SUL accumulation could be detected in A007-positive cells lacking Galactocerebroside (i.e., A007+GalC- progenitor cells) present early in development. These data suggest that A007 also recognizes an antigen, named proligodendroblast antigen (POA), that appears during the late stage of oligodendrocyte progenitor development prior to the expression by oligodendrocytes of SUL and GalC. We have previously reported that monoclonal antibody O4 also recognizes not only SUL and seminolipid, but in addition an antigen that appears prior to the expression of SUL and Galactocerebroside. In the present study all A007+ cells were also O4+ (and vice versa), and the developmental patterns of the two antibodies appeared to be identical. We conclude that (1) A007 is similar or identical to O4 with respect to its antigenic specificity, and (2) during oligodendrocyte lineage progression both antibodies react first with antigen POA on the surface of the oligodendrocyte progenitor cell prior to the expression of SUL [i.e., A007+O4+(POA+)SUL-GalC- proligodendroblasts], and only later with SUL as terminally differentiating oligodendrocytes emerge (i.e., A007+O4+SUL+GalC+ oligodendrocytes).
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Proligodendroblast Antigen (POA), a Developmental Antigen Expressed by A007/O4-Positive Oligodendrocyte Progenitors Prior to the Appearance of Sulfatide and Galactocerebroside
Journal of neurochemistry, 1992Co-Authors: Rashmi Bansal, Kari Stefansson, S. E. PfeifferAbstract:Evidence is presented for the immunological identification of a developmental antigen appearing at a critical point in the oligodendroglial lineage. Specifically, monoclonal antibody A007 recognizes cells in the oligodendrocyte lineage at two distinct stages. Analyses of purified lipid standards and lipid extracts from Galactocerebroside-positive (GalC+) oligodendrocytes by enzyme-linked immunosorbent assay, lipid dot blot, and immuno-TLC demonstrated that A007 recognizes sulfatide (SUL) and seminolipid. However, neither 35SO4 incorporation into SUL nor SUL accumulation could be detected in A007-positive cells lacking Galactocerebroside (i.e., A007+GalC- progenitor cells) present early in development. These data suggest that A007 also recognizes an antigen, named proligodendroblast antigen (POA), that appears during the late stage of oligodendrocyte progenitor development prior to the expression by oligodendrocytes of SUL and GalC. We have previously reported that monoclonal antibody O4 also recognizes not only SUL and seminolipid, but in addition an antigen that appears prior to the expression of SUL and Galactocerebroside. In the present study all A007+ cells were also O4+ (and vice versa), and the developmental patterns of the two antibodies appeared to be identical. We conclude that (1) A007 is similar or identical to O4 with respect to its antigenic specificity, and (2) during oligodendrocyte lineage progression both antibodies react first with antigen POA on the surface of the oligodendrocyte progenitor cell prior to the expression of SUL [i.e., A007+O4+(POA+)SUL-GalC- proligodendroblasts], and only later with SUL as terminally differentiating oligodendrocytes emerge (i.e., A007+O4+SUL+GalC+ oligodendrocytes).
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Novel stage in the oligodendrocyte lineage defined by reactivity of progenitors with R‐mAb prior to O1 anti‐Galactocerebroside
Journal of neuroscience research, 1992Co-Authors: Rashmi Bansal, S. E. PfeifferAbstract:The developmentally regulated appearance of surface immuno-reactivity of proligodendroblasts [oligodendrocyte progenitors reacting with monoclonal antibodies A007 and O4, but not anti-Galactocerebroside (GalC), i.e., A007/O4+ GalC−] to monoclonal antibodies R-mAb and O1 was studied both in culture and in vivo. In both cases staining with R-mAb shortly preceded that with O1; that is, a transient population of R-mAb+ O1− cells was observed. R-mAb− O1+ cells were not detected. Differential staining with R-mAb and O1 was also noted at the subcellular level. In younger cultures in which R-mAb+ cells were first acquiring O1 immunoreactivity, many of these cells were stained by O1 only on the cell bodies and proximal portions of the processes, whereas in contrast R-mAb stained the whole cell, including the distal portions of the processes. Only in older, more mature R-mAb+ cells did O1 also stain the distal portions of processes. The expression of reactivity to R-mAb and O1 was compared to the proliferative capacity of the cells. Proliferation [assessed by bromodeoxyuridine (BrdU) incorporation] of both R-mAb+ and O1+ cells was negligible both in culture and in vivo. However, treatment of cells in culture with 10 ng/ml basic fibroblast growth factor resulted in an enhancement of proliferation of the R-mAb+ cells. Within the proliferating R-mAb+BrdU+ population, 80% of the cells were O1− (i.e., anti-Galactocerebroside negative). These events occur during a critical period of development when A007/O4+ proligodendroblasts begin to become post-mitotic and express surface Galactocerebroside. The data demonstrate that the use of R-mAb as an “anti-GalC” must be interpreted with caution, and indicate the utility of dual staining with R-mAb and O1 to (1) further subdivide the oligodendrocyte lineage, thus identifying an additional, GalC− developmental compartment, and (2) observe the distribution of R-mAb and O1 immunoreactivity at a subcellular level. © 1992 Wiley-Liss, Inc.
W F Haupt - One of the best experts on this subject based on the ideXlab platform.
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composition and biophysical properties of myelin lipid define the neurological defects in Galactocerebroside and sulfatide deficient mice
Journal of Neurochemistry, 2002Co-Authors: Andreas Bosio, Erika Binczek, W F Haupt, Wilhelm StoffelAbstract:Abstract: Oligodendrocytes and Schwann cell-specific proteins are assembled with a highly ordered membrane lipid bilayer to the myelin sheath of axons, which functions as an insulator and allows rapid saltatory conduction. We approached the question of the function of the CNS and PNS myelin-specific galactospingolipids cerebrosides and sulfatides by generating a ceramide galactosyltransferase null allelic mouse line (cgt−/−). Galactocerebroside- and sulfatide-deficient myelin loses its insulating properties and causes a severe dysmyelinosis that is incompatible with life. Here, we describe the biochemical and biophysical analysis of the myelin lipid bilayer of cgt−/− mice. The lipid composition of CNS and PNS myelin of cgt−/− mice is seriously perturbed and the sphingolipid biosynthetic pathway altered. Nonhydroxy and hydroxy fatty acid-substituted glycosylceramides (GlcC) are synthesized by oligodendrocytes and sulfated GlcC in addition in Schwann cells. The monogalactosyldiglyceride fraction is missing in the cgt−/− mouse. This new lipid composition can be correlated with the biophysical properties of the myelin sheath. The deficiency of Galactocerebrosides and sulfatides leads to an increased fluidity, permeability, and impaired packing of the myelin lipid bilayer of the internodal membrane system. The loss of the two glycosphingolipid classes causes the breakdown of saltatory conductance of myelinated axons in the cgt−/− mouse.
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Composition and Biophysical Properties of Myelin Lipid Define the Neurological Defects in Galactocerebroside‐ and Sulfatide‐Deficient Mice
Journal of neurochemistry, 2002Co-Authors: Andreas Bosio, Erika Binczek, W F Haupt, Wilhelm StoffelAbstract:Abstract: Oligodendrocytes and Schwann cell-specific proteins are assembled with a highly ordered membrane lipid bilayer to the myelin sheath of axons, which functions as an insulator and allows rapid saltatory conduction. We approached the question of the function of the CNS and PNS myelin-specific galactospingolipids cerebrosides and sulfatides by generating a ceramide galactosyltransferase null allelic mouse line (cgt−/−). Galactocerebroside- and sulfatide-deficient myelin loses its insulating properties and causes a severe dysmyelinosis that is incompatible with life. Here, we describe the biochemical and biophysical analysis of the myelin lipid bilayer of cgt−/− mice. The lipid composition of CNS and PNS myelin of cgt−/− mice is seriously perturbed and the sphingolipid biosynthetic pathway altered. Nonhydroxy and hydroxy fatty acid-substituted glycosylceramides (GlcC) are synthesized by oligodendrocytes and sulfated GlcC in addition in Schwann cells. The monogalactosyldiglyceride fraction is missing in the cgt−/− mouse. This new lipid composition can be correlated with the biophysical properties of the myelin sheath. The deficiency of Galactocerebrosides and sulfatides leads to an increased fluidity, permeability, and impaired packing of the myelin lipid bilayer of the internodal membrane system. The loss of the two glycosphingolipid classes causes the breakdown of saltatory conductance of myelinated axons in the cgt−/− mouse.
