Decreased Fatty Acylation of Myelin Proteolipid Protein in the Twitcher Mouse
Abstract: We examined chronological changes of myelin proteins of the brainstem and spinal cord of the twitcher mouse (15, 20, and 30 days old), a murine model of human globoid cell leukodystrophy caused by a genetic deficiency of galactosylceramidase I activity. The yield of myelin was normal until...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Yoshimura, Takeo [verfasserIn] Kobayashi, Takuro [verfasserIn] Mitsuo, Kunihiko [verfasserIn] |
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| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1989 |
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| Schlagwörter: |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2006 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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| Übergeordnetes Werk: |
In: Journal of neurochemistry - Oxford : Wiley-Blackwell, 1956, 52(1989), 3, Seite 0 |
| Übergeordnetes Werk: |
volume:52 ; year:1989 ; number:3 ; pages:0 |
| Links: |
|---|
| DOI / URN: |
10.1111/j.1471-4159.1989.tb02529.x |
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| 520 | |a Abstract: We examined chronological changes of myelin proteins of the brainstem and spinal cord of the twitcher mouse (15, 20, and 30 days old), a murine model of human globoid cell leukodystrophy caused by a genetic deficiency of galactosylceramidase I activity. The yield of myelin was normal until postnatal day 20, whereas galactosylsphingosine (psychosine) accumulated with age in myelin. The protein profiles of myelin and the activity of 2′,3′-cyclic nucleotide 3′-phosphodiesterase in the myelin remained normal throughout the experimental period. Fatty acylation of proteolipid protein (PLP) was examined in a cell-free system by incubation of myelin with [3H]palmitic acid, CoA, and ATP, and was normal at postnatal day 15, but decreased after postnatal day 20. Decreased fatty acylation of PLP was also observed in the twitcher mouse at postnatal day 20 when the isolated myelin was incubated with [14C]palmitoyl-CoA in the absence of ATP and CoA, or the slices of brainstem and spinal cord were incubated with [3H]palmitic acid. The activity of fatty acid: CoA ligase was reduced in myelin. These data suggest that decreased acylation of PLP in twitcher mouse myelin is probably due to reduced activities for both activation and transfer of fatty acid into PLP and that metabolic disturbance is present in myelin because acylation of PLP has been shown to occur in myelin membrane. Although psychosine (200 μM) inhibited only 17% of the acylation in vitro, it may be responsible for the reduced acylation of PLP in vivo. | ||
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10.1111/j.1471-4159.1989.tb02529.x doi (DE-627)NLEJ240276809 DE-627 ger DE-627 rakwb Yoshimura, Takeo verfasserin aut Decreased Fatty Acylation of Myelin Proteolipid Protein in the Twitcher Mouse Oxford, UK Blackwell Publishing Ltd 1989 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: We examined chronological changes of myelin proteins of the brainstem and spinal cord of the twitcher mouse (15, 20, and 30 days old), a murine model of human globoid cell leukodystrophy caused by a genetic deficiency of galactosylceramidase I activity. The yield of myelin was normal until postnatal day 20, whereas galactosylsphingosine (psychosine) accumulated with age in myelin. The protein profiles of myelin and the activity of 2′,3′-cyclic nucleotide 3′-phosphodiesterase in the myelin remained normal throughout the experimental period. Fatty acylation of proteolipid protein (PLP) was examined in a cell-free system by incubation of myelin with [3H]palmitic acid, CoA, and ATP, and was normal at postnatal day 15, but decreased after postnatal day 20. Decreased fatty acylation of PLP was also observed in the twitcher mouse at postnatal day 20 when the isolated myelin was incubated with [14C]palmitoyl-CoA in the absence of ATP and CoA, or the slices of brainstem and spinal cord were incubated with [3H]palmitic acid. The activity of fatty acid: CoA ligase was reduced in myelin. These data suggest that decreased acylation of PLP in twitcher mouse myelin is probably due to reduced activities for both activation and transfer of fatty acid into PLP and that metabolic disturbance is present in myelin because acylation of PLP has been shown to occur in myelin membrane. Although psychosine (200 μM) inhibited only 17% of the acylation in vitro, it may be responsible for the reduced acylation of PLP in vivo. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Acylation Kobayashi, Takuro verfasserin aut Mitsuo, Kunihiko verfasserin aut Goto, Ikuo oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 52(1989), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:52 year:1989 number:3 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1989.tb02529.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 52 1989 3 0 |
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10.1111/j.1471-4159.1989.tb02529.x doi (DE-627)NLEJ240276809 DE-627 ger DE-627 rakwb Yoshimura, Takeo verfasserin aut Decreased Fatty Acylation of Myelin Proteolipid Protein in the Twitcher Mouse Oxford, UK Blackwell Publishing Ltd 1989 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: We examined chronological changes of myelin proteins of the brainstem and spinal cord of the twitcher mouse (15, 20, and 30 days old), a murine model of human globoid cell leukodystrophy caused by a genetic deficiency of galactosylceramidase I activity. The yield of myelin was normal until postnatal day 20, whereas galactosylsphingosine (psychosine) accumulated with age in myelin. The protein profiles of myelin and the activity of 2′,3′-cyclic nucleotide 3′-phosphodiesterase in the myelin remained normal throughout the experimental period. Fatty acylation of proteolipid protein (PLP) was examined in a cell-free system by incubation of myelin with [3H]palmitic acid, CoA, and ATP, and was normal at postnatal day 15, but decreased after postnatal day 20. Decreased fatty acylation of PLP was also observed in the twitcher mouse at postnatal day 20 when the isolated myelin was incubated with [14C]palmitoyl-CoA in the absence of ATP and CoA, or the slices of brainstem and spinal cord were incubated with [3H]palmitic acid. The activity of fatty acid: CoA ligase was reduced in myelin. These data suggest that decreased acylation of PLP in twitcher mouse myelin is probably due to reduced activities for both activation and transfer of fatty acid into PLP and that metabolic disturbance is present in myelin because acylation of PLP has been shown to occur in myelin membrane. Although psychosine (200 μM) inhibited only 17% of the acylation in vitro, it may be responsible for the reduced acylation of PLP in vivo. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Acylation Kobayashi, Takuro verfasserin aut Mitsuo, Kunihiko verfasserin aut Goto, Ikuo oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 52(1989), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:52 year:1989 number:3 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1989.tb02529.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 52 1989 3 0 |
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10.1111/j.1471-4159.1989.tb02529.x doi (DE-627)NLEJ240276809 DE-627 ger DE-627 rakwb Yoshimura, Takeo verfasserin aut Decreased Fatty Acylation of Myelin Proteolipid Protein in the Twitcher Mouse Oxford, UK Blackwell Publishing Ltd 1989 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: We examined chronological changes of myelin proteins of the brainstem and spinal cord of the twitcher mouse (15, 20, and 30 days old), a murine model of human globoid cell leukodystrophy caused by a genetic deficiency of galactosylceramidase I activity. The yield of myelin was normal until postnatal day 20, whereas galactosylsphingosine (psychosine) accumulated with age in myelin. The protein profiles of myelin and the activity of 2′,3′-cyclic nucleotide 3′-phosphodiesterase in the myelin remained normal throughout the experimental period. Fatty acylation of proteolipid protein (PLP) was examined in a cell-free system by incubation of myelin with [3H]palmitic acid, CoA, and ATP, and was normal at postnatal day 15, but decreased after postnatal day 20. Decreased fatty acylation of PLP was also observed in the twitcher mouse at postnatal day 20 when the isolated myelin was incubated with [14C]palmitoyl-CoA in the absence of ATP and CoA, or the slices of brainstem and spinal cord were incubated with [3H]palmitic acid. The activity of fatty acid: CoA ligase was reduced in myelin. These data suggest that decreased acylation of PLP in twitcher mouse myelin is probably due to reduced activities for both activation and transfer of fatty acid into PLP and that metabolic disturbance is present in myelin because acylation of PLP has been shown to occur in myelin membrane. Although psychosine (200 μM) inhibited only 17% of the acylation in vitro, it may be responsible for the reduced acylation of PLP in vivo. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Acylation Kobayashi, Takuro verfasserin aut Mitsuo, Kunihiko verfasserin aut Goto, Ikuo oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 52(1989), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:52 year:1989 number:3 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1989.tb02529.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 52 1989 3 0 |
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10.1111/j.1471-4159.1989.tb02529.x doi (DE-627)NLEJ240276809 DE-627 ger DE-627 rakwb Yoshimura, Takeo verfasserin aut Decreased Fatty Acylation of Myelin Proteolipid Protein in the Twitcher Mouse Oxford, UK Blackwell Publishing Ltd 1989 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: We examined chronological changes of myelin proteins of the brainstem and spinal cord of the twitcher mouse (15, 20, and 30 days old), a murine model of human globoid cell leukodystrophy caused by a genetic deficiency of galactosylceramidase I activity. The yield of myelin was normal until postnatal day 20, whereas galactosylsphingosine (psychosine) accumulated with age in myelin. The protein profiles of myelin and the activity of 2′,3′-cyclic nucleotide 3′-phosphodiesterase in the myelin remained normal throughout the experimental period. Fatty acylation of proteolipid protein (PLP) was examined in a cell-free system by incubation of myelin with [3H]palmitic acid, CoA, and ATP, and was normal at postnatal day 15, but decreased after postnatal day 20. Decreased fatty acylation of PLP was also observed in the twitcher mouse at postnatal day 20 when the isolated myelin was incubated with [14C]palmitoyl-CoA in the absence of ATP and CoA, or the slices of brainstem and spinal cord were incubated with [3H]palmitic acid. The activity of fatty acid: CoA ligase was reduced in myelin. These data suggest that decreased acylation of PLP in twitcher mouse myelin is probably due to reduced activities for both activation and transfer of fatty acid into PLP and that metabolic disturbance is present in myelin because acylation of PLP has been shown to occur in myelin membrane. Although psychosine (200 μM) inhibited only 17% of the acylation in vitro, it may be responsible for the reduced acylation of PLP in vivo. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Acylation Kobayashi, Takuro verfasserin aut Mitsuo, Kunihiko verfasserin aut Goto, Ikuo oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 52(1989), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:52 year:1989 number:3 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1989.tb02529.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 52 1989 3 0 |
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10.1111/j.1471-4159.1989.tb02529.x doi (DE-627)NLEJ240276809 DE-627 ger DE-627 rakwb Yoshimura, Takeo verfasserin aut Decreased Fatty Acylation of Myelin Proteolipid Protein in the Twitcher Mouse Oxford, UK Blackwell Publishing Ltd 1989 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: We examined chronological changes of myelin proteins of the brainstem and spinal cord of the twitcher mouse (15, 20, and 30 days old), a murine model of human globoid cell leukodystrophy caused by a genetic deficiency of galactosylceramidase I activity. The yield of myelin was normal until postnatal day 20, whereas galactosylsphingosine (psychosine) accumulated with age in myelin. The protein profiles of myelin and the activity of 2′,3′-cyclic nucleotide 3′-phosphodiesterase in the myelin remained normal throughout the experimental period. Fatty acylation of proteolipid protein (PLP) was examined in a cell-free system by incubation of myelin with [3H]palmitic acid, CoA, and ATP, and was normal at postnatal day 15, but decreased after postnatal day 20. Decreased fatty acylation of PLP was also observed in the twitcher mouse at postnatal day 20 when the isolated myelin was incubated with [14C]palmitoyl-CoA in the absence of ATP and CoA, or the slices of brainstem and spinal cord were incubated with [3H]palmitic acid. The activity of fatty acid: CoA ligase was reduced in myelin. These data suggest that decreased acylation of PLP in twitcher mouse myelin is probably due to reduced activities for both activation and transfer of fatty acid into PLP and that metabolic disturbance is present in myelin because acylation of PLP has been shown to occur in myelin membrane. Although psychosine (200 μM) inhibited only 17% of the acylation in vitro, it may be responsible for the reduced acylation of PLP in vivo. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Acylation Kobayashi, Takuro verfasserin aut Mitsuo, Kunihiko verfasserin aut Goto, Ikuo oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 52(1989), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:52 year:1989 number:3 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1989.tb02529.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 52 1989 3 0 |
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Decreased Fatty Acylation of Myelin Proteolipid Protein in the Twitcher Mouse |
| abstract |
Abstract: We examined chronological changes of myelin proteins of the brainstem and spinal cord of the twitcher mouse (15, 20, and 30 days old), a murine model of human globoid cell leukodystrophy caused by a genetic deficiency of galactosylceramidase I activity. The yield of myelin was normal until postnatal day 20, whereas galactosylsphingosine (psychosine) accumulated with age in myelin. The protein profiles of myelin and the activity of 2′,3′-cyclic nucleotide 3′-phosphodiesterase in the myelin remained normal throughout the experimental period. Fatty acylation of proteolipid protein (PLP) was examined in a cell-free system by incubation of myelin with [3H]palmitic acid, CoA, and ATP, and was normal at postnatal day 15, but decreased after postnatal day 20. Decreased fatty acylation of PLP was also observed in the twitcher mouse at postnatal day 20 when the isolated myelin was incubated with [14C]palmitoyl-CoA in the absence of ATP and CoA, or the slices of brainstem and spinal cord were incubated with [3H]palmitic acid. The activity of fatty acid: CoA ligase was reduced in myelin. These data suggest that decreased acylation of PLP in twitcher mouse myelin is probably due to reduced activities for both activation and transfer of fatty acid into PLP and that metabolic disturbance is present in myelin because acylation of PLP has been shown to occur in myelin membrane. Although psychosine (200 μM) inhibited only 17% of the acylation in vitro, it may be responsible for the reduced acylation of PLP in vivo. |
| abstractGer |
Abstract: We examined chronological changes of myelin proteins of the brainstem and spinal cord of the twitcher mouse (15, 20, and 30 days old), a murine model of human globoid cell leukodystrophy caused by a genetic deficiency of galactosylceramidase I activity. The yield of myelin was normal until postnatal day 20, whereas galactosylsphingosine (psychosine) accumulated with age in myelin. The protein profiles of myelin and the activity of 2′,3′-cyclic nucleotide 3′-phosphodiesterase in the myelin remained normal throughout the experimental period. Fatty acylation of proteolipid protein (PLP) was examined in a cell-free system by incubation of myelin with [3H]palmitic acid, CoA, and ATP, and was normal at postnatal day 15, but decreased after postnatal day 20. Decreased fatty acylation of PLP was also observed in the twitcher mouse at postnatal day 20 when the isolated myelin was incubated with [14C]palmitoyl-CoA in the absence of ATP and CoA, or the slices of brainstem and spinal cord were incubated with [3H]palmitic acid. The activity of fatty acid: CoA ligase was reduced in myelin. These data suggest that decreased acylation of PLP in twitcher mouse myelin is probably due to reduced activities for both activation and transfer of fatty acid into PLP and that metabolic disturbance is present in myelin because acylation of PLP has been shown to occur in myelin membrane. Although psychosine (200 μM) inhibited only 17% of the acylation in vitro, it may be responsible for the reduced acylation of PLP in vivo. |
| abstract_unstemmed |
Abstract: We examined chronological changes of myelin proteins of the brainstem and spinal cord of the twitcher mouse (15, 20, and 30 days old), a murine model of human globoid cell leukodystrophy caused by a genetic deficiency of galactosylceramidase I activity. The yield of myelin was normal until postnatal day 20, whereas galactosylsphingosine (psychosine) accumulated with age in myelin. The protein profiles of myelin and the activity of 2′,3′-cyclic nucleotide 3′-phosphodiesterase in the myelin remained normal throughout the experimental period. Fatty acylation of proteolipid protein (PLP) was examined in a cell-free system by incubation of myelin with [3H]palmitic acid, CoA, and ATP, and was normal at postnatal day 15, but decreased after postnatal day 20. Decreased fatty acylation of PLP was also observed in the twitcher mouse at postnatal day 20 when the isolated myelin was incubated with [14C]palmitoyl-CoA in the absence of ATP and CoA, or the slices of brainstem and spinal cord were incubated with [3H]palmitic acid. The activity of fatty acid: CoA ligase was reduced in myelin. These data suggest that decreased acylation of PLP in twitcher mouse myelin is probably due to reduced activities for both activation and transfer of fatty acid into PLP and that metabolic disturbance is present in myelin because acylation of PLP has been shown to occur in myelin membrane. Although psychosine (200 μM) inhibited only 17% of the acylation in vitro, it may be responsible for the reduced acylation of PLP in vivo. |
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| title_short |
Decreased Fatty Acylation of Myelin Proteolipid Protein in the Twitcher Mouse |
| url |
http://dx.doi.org/10.1111/j.1471-4159.1989.tb02529.x |
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| author2 |
Kobayashi, Takuro Mitsuo, Kunihiko Goto, Ikuo |
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Kobayashi, Takuro Mitsuo, Kunihiko Goto, Ikuo |
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| doi_str |
10.1111/j.1471-4159.1989.tb02529.x |
| up_date |
2024-07-06T09:33:39.522Z |
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