Distribution of Ankyrin Isoforms and Their Proteolysis After Ischemia and Reperfusion in Rat Brain
Abstract: The distribution of brain-type ankyrin (ankyrinB, 212 kDa) and erythrocyte-type ankyrin (ankyrinR, 239 kDa) was investigated in the subcellular fractions of rat forebrain (P1, 1,000 g pellet; P2, 15,000 g pellet; P3, 100,000 g pellet; S, 100,000 g supernatant) by immunoblotting using speci...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Harada, Kazuki [verfasserIn] Fukuda, Shiro [verfasserIn] Kunimoto, Manabu [verfasserIn] |
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| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Science Ltd ; 1997 |
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| Schlagwörter: |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2002 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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| Übergeordnetes Werk: |
In: Journal of neurochemistry - Oxford : Wiley-Blackwell, 1956, 69(1997), 1, Seite 0 |
| Übergeordnetes Werk: |
volume:69 ; year:1997 ; number:1 ; pages:0 |
| Links: |
|---|
| DOI / URN: |
10.1046/j.1471-4159.1997.69010371.x |
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NLEJ243167660 |
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| 520 | |a Abstract: The distribution of brain-type ankyrin (ankyrinB, 212 kDa) and erythrocyte-type ankyrin (ankyrinR, 239 kDa) was investigated in the subcellular fractions of rat forebrain (P1, 1,000 g pellet; P2, 15,000 g pellet; P3, 100,000 g pellet; S, 100,000 g supernatant) by immunoblotting using specific antibodies. The P2 fraction contained ∼40% of the 212- and 163-kDa isoforms of ankyrinB and the 239-kDa isoform of ankyrinR. Further subfractionation of the P2 by Percoll gradient centrifugation followed by separation of myelin showed association of the three ankyrin isoforms with the synaptosome-rich fraction but not with the myelin-rich fraction. The plasma membrane-rich P3 fraction contained a concentration of ankyrin isoforms similar to that in the P2 fraction. In vitro proteolysis of ankyrin in the P2 fraction with calpain showed that the 212-kDa ankyrinB was more susceptible to calpain than was ankyrinR. In the two-vessel occlusion model, ischemia for 30 min generated the 160-kDa fragment of ankyrinR, and reperfusion for 60 min after 30 min of ischemia remarkably increased the 160-kDa fragment. The reperfusion also significantly decreased the 212-kDa isoform of ankyrinB. Both ischemia-reperfusion and in vitro proteolysis with calpain generated the 160-kDa fragment of ankyrinR, suggesting the involvement of calpain. | ||
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10.1046/j.1471-4159.1997.69010371.x doi (DE-627)NLEJ243167660 DE-627 ger DE-627 rakwb Harada, Kazuki verfasserin aut Distribution of Ankyrin Isoforms and Their Proteolysis After Ischemia and Reperfusion in Rat Brain Oxford, UK Blackwell Science Ltd 1997 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: The distribution of brain-type ankyrin (ankyrinB, 212 kDa) and erythrocyte-type ankyrin (ankyrinR, 239 kDa) was investigated in the subcellular fractions of rat forebrain (P1, 1,000 g pellet; P2, 15,000 g pellet; P3, 100,000 g pellet; S, 100,000 g supernatant) by immunoblotting using specific antibodies. The P2 fraction contained ∼40% of the 212- and 163-kDa isoforms of ankyrinB and the 239-kDa isoform of ankyrinR. Further subfractionation of the P2 by Percoll gradient centrifugation followed by separation of myelin showed association of the three ankyrin isoforms with the synaptosome-rich fraction but not with the myelin-rich fraction. The plasma membrane-rich P3 fraction contained a concentration of ankyrin isoforms similar to that in the P2 fraction. In vitro proteolysis of ankyrin in the P2 fraction with calpain showed that the 212-kDa ankyrinB was more susceptible to calpain than was ankyrinR. In the two-vessel occlusion model, ischemia for 30 min generated the 160-kDa fragment of ankyrinR, and reperfusion for 60 min after 30 min of ischemia remarkably increased the 160-kDa fragment. The reperfusion also significantly decreased the 212-kDa isoform of ankyrinB. Both ischemia-reperfusion and in vitro proteolysis with calpain generated the 160-kDa fragment of ankyrinR, suggesting the involvement of calpain. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Ankyrin Fukuda, Shiro verfasserin aut Kunimoto, Manabu verfasserin aut Yoshida, Ken-ichi oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 69(1997), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:69 year:1997 number:1 pages:0 http://dx.doi.org/10.1046/j.1471-4159.1997.69010371.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 69 1997 1 0 |
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10.1046/j.1471-4159.1997.69010371.x doi (DE-627)NLEJ243167660 DE-627 ger DE-627 rakwb Harada, Kazuki verfasserin aut Distribution of Ankyrin Isoforms and Their Proteolysis After Ischemia and Reperfusion in Rat Brain Oxford, UK Blackwell Science Ltd 1997 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: The distribution of brain-type ankyrin (ankyrinB, 212 kDa) and erythrocyte-type ankyrin (ankyrinR, 239 kDa) was investigated in the subcellular fractions of rat forebrain (P1, 1,000 g pellet; P2, 15,000 g pellet; P3, 100,000 g pellet; S, 100,000 g supernatant) by immunoblotting using specific antibodies. The P2 fraction contained ∼40% of the 212- and 163-kDa isoforms of ankyrinB and the 239-kDa isoform of ankyrinR. Further subfractionation of the P2 by Percoll gradient centrifugation followed by separation of myelin showed association of the three ankyrin isoforms with the synaptosome-rich fraction but not with the myelin-rich fraction. The plasma membrane-rich P3 fraction contained a concentration of ankyrin isoforms similar to that in the P2 fraction. In vitro proteolysis of ankyrin in the P2 fraction with calpain showed that the 212-kDa ankyrinB was more susceptible to calpain than was ankyrinR. In the two-vessel occlusion model, ischemia for 30 min generated the 160-kDa fragment of ankyrinR, and reperfusion for 60 min after 30 min of ischemia remarkably increased the 160-kDa fragment. The reperfusion also significantly decreased the 212-kDa isoform of ankyrinB. Both ischemia-reperfusion and in vitro proteolysis with calpain generated the 160-kDa fragment of ankyrinR, suggesting the involvement of calpain. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Ankyrin Fukuda, Shiro verfasserin aut Kunimoto, Manabu verfasserin aut Yoshida, Ken-ichi oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 69(1997), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:69 year:1997 number:1 pages:0 http://dx.doi.org/10.1046/j.1471-4159.1997.69010371.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 69 1997 1 0 |
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10.1046/j.1471-4159.1997.69010371.x doi (DE-627)NLEJ243167660 DE-627 ger DE-627 rakwb Harada, Kazuki verfasserin aut Distribution of Ankyrin Isoforms and Their Proteolysis After Ischemia and Reperfusion in Rat Brain Oxford, UK Blackwell Science Ltd 1997 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: The distribution of brain-type ankyrin (ankyrinB, 212 kDa) and erythrocyte-type ankyrin (ankyrinR, 239 kDa) was investigated in the subcellular fractions of rat forebrain (P1, 1,000 g pellet; P2, 15,000 g pellet; P3, 100,000 g pellet; S, 100,000 g supernatant) by immunoblotting using specific antibodies. The P2 fraction contained ∼40% of the 212- and 163-kDa isoforms of ankyrinB and the 239-kDa isoform of ankyrinR. Further subfractionation of the P2 by Percoll gradient centrifugation followed by separation of myelin showed association of the three ankyrin isoforms with the synaptosome-rich fraction but not with the myelin-rich fraction. The plasma membrane-rich P3 fraction contained a concentration of ankyrin isoforms similar to that in the P2 fraction. In vitro proteolysis of ankyrin in the P2 fraction with calpain showed that the 212-kDa ankyrinB was more susceptible to calpain than was ankyrinR. In the two-vessel occlusion model, ischemia for 30 min generated the 160-kDa fragment of ankyrinR, and reperfusion for 60 min after 30 min of ischemia remarkably increased the 160-kDa fragment. The reperfusion also significantly decreased the 212-kDa isoform of ankyrinB. Both ischemia-reperfusion and in vitro proteolysis with calpain generated the 160-kDa fragment of ankyrinR, suggesting the involvement of calpain. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Ankyrin Fukuda, Shiro verfasserin aut Kunimoto, Manabu verfasserin aut Yoshida, Ken-ichi oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 69(1997), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:69 year:1997 number:1 pages:0 http://dx.doi.org/10.1046/j.1471-4159.1997.69010371.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 69 1997 1 0 |
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10.1046/j.1471-4159.1997.69010371.x doi (DE-627)NLEJ243167660 DE-627 ger DE-627 rakwb Harada, Kazuki verfasserin aut Distribution of Ankyrin Isoforms and Their Proteolysis After Ischemia and Reperfusion in Rat Brain Oxford, UK Blackwell Science Ltd 1997 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: The distribution of brain-type ankyrin (ankyrinB, 212 kDa) and erythrocyte-type ankyrin (ankyrinR, 239 kDa) was investigated in the subcellular fractions of rat forebrain (P1, 1,000 g pellet; P2, 15,000 g pellet; P3, 100,000 g pellet; S, 100,000 g supernatant) by immunoblotting using specific antibodies. The P2 fraction contained ∼40% of the 212- and 163-kDa isoforms of ankyrinB and the 239-kDa isoform of ankyrinR. Further subfractionation of the P2 by Percoll gradient centrifugation followed by separation of myelin showed association of the three ankyrin isoforms with the synaptosome-rich fraction but not with the myelin-rich fraction. The plasma membrane-rich P3 fraction contained a concentration of ankyrin isoforms similar to that in the P2 fraction. In vitro proteolysis of ankyrin in the P2 fraction with calpain showed that the 212-kDa ankyrinB was more susceptible to calpain than was ankyrinR. In the two-vessel occlusion model, ischemia for 30 min generated the 160-kDa fragment of ankyrinR, and reperfusion for 60 min after 30 min of ischemia remarkably increased the 160-kDa fragment. The reperfusion also significantly decreased the 212-kDa isoform of ankyrinB. Both ischemia-reperfusion and in vitro proteolysis with calpain generated the 160-kDa fragment of ankyrinR, suggesting the involvement of calpain. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Ankyrin Fukuda, Shiro verfasserin aut Kunimoto, Manabu verfasserin aut Yoshida, Ken-ichi oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 69(1997), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:69 year:1997 number:1 pages:0 http://dx.doi.org/10.1046/j.1471-4159.1997.69010371.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 69 1997 1 0 |
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10.1046/j.1471-4159.1997.69010371.x doi (DE-627)NLEJ243167660 DE-627 ger DE-627 rakwb Harada, Kazuki verfasserin aut Distribution of Ankyrin Isoforms and Their Proteolysis After Ischemia and Reperfusion in Rat Brain Oxford, UK Blackwell Science Ltd 1997 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: The distribution of brain-type ankyrin (ankyrinB, 212 kDa) and erythrocyte-type ankyrin (ankyrinR, 239 kDa) was investigated in the subcellular fractions of rat forebrain (P1, 1,000 g pellet; P2, 15,000 g pellet; P3, 100,000 g pellet; S, 100,000 g supernatant) by immunoblotting using specific antibodies. The P2 fraction contained ∼40% of the 212- and 163-kDa isoforms of ankyrinB and the 239-kDa isoform of ankyrinR. Further subfractionation of the P2 by Percoll gradient centrifugation followed by separation of myelin showed association of the three ankyrin isoforms with the synaptosome-rich fraction but not with the myelin-rich fraction. The plasma membrane-rich P3 fraction contained a concentration of ankyrin isoforms similar to that in the P2 fraction. In vitro proteolysis of ankyrin in the P2 fraction with calpain showed that the 212-kDa ankyrinB was more susceptible to calpain than was ankyrinR. In the two-vessel occlusion model, ischemia for 30 min generated the 160-kDa fragment of ankyrinR, and reperfusion for 60 min after 30 min of ischemia remarkably increased the 160-kDa fragment. The reperfusion also significantly decreased the 212-kDa isoform of ankyrinB. Both ischemia-reperfusion and in vitro proteolysis with calpain generated the 160-kDa fragment of ankyrinR, suggesting the involvement of calpain. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Ankyrin Fukuda, Shiro verfasserin aut Kunimoto, Manabu verfasserin aut Yoshida, Ken-ichi oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 69(1997), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:69 year:1997 number:1 pages:0 http://dx.doi.org/10.1046/j.1471-4159.1997.69010371.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 69 1997 1 0 |
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distribution of ankyrin isoforms and their proteolysis after ischemia and reperfusion in rat brain |
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Distribution of Ankyrin Isoforms and Their Proteolysis After Ischemia and Reperfusion in Rat Brain |
| abstract |
Abstract: The distribution of brain-type ankyrin (ankyrinB, 212 kDa) and erythrocyte-type ankyrin (ankyrinR, 239 kDa) was investigated in the subcellular fractions of rat forebrain (P1, 1,000 g pellet; P2, 15,000 g pellet; P3, 100,000 g pellet; S, 100,000 g supernatant) by immunoblotting using specific antibodies. The P2 fraction contained ∼40% of the 212- and 163-kDa isoforms of ankyrinB and the 239-kDa isoform of ankyrinR. Further subfractionation of the P2 by Percoll gradient centrifugation followed by separation of myelin showed association of the three ankyrin isoforms with the synaptosome-rich fraction but not with the myelin-rich fraction. The plasma membrane-rich P3 fraction contained a concentration of ankyrin isoforms similar to that in the P2 fraction. In vitro proteolysis of ankyrin in the P2 fraction with calpain showed that the 212-kDa ankyrinB was more susceptible to calpain than was ankyrinR. In the two-vessel occlusion model, ischemia for 30 min generated the 160-kDa fragment of ankyrinR, and reperfusion for 60 min after 30 min of ischemia remarkably increased the 160-kDa fragment. The reperfusion also significantly decreased the 212-kDa isoform of ankyrinB. Both ischemia-reperfusion and in vitro proteolysis with calpain generated the 160-kDa fragment of ankyrinR, suggesting the involvement of calpain. |
| abstractGer |
Abstract: The distribution of brain-type ankyrin (ankyrinB, 212 kDa) and erythrocyte-type ankyrin (ankyrinR, 239 kDa) was investigated in the subcellular fractions of rat forebrain (P1, 1,000 g pellet; P2, 15,000 g pellet; P3, 100,000 g pellet; S, 100,000 g supernatant) by immunoblotting using specific antibodies. The P2 fraction contained ∼40% of the 212- and 163-kDa isoforms of ankyrinB and the 239-kDa isoform of ankyrinR. Further subfractionation of the P2 by Percoll gradient centrifugation followed by separation of myelin showed association of the three ankyrin isoforms with the synaptosome-rich fraction but not with the myelin-rich fraction. The plasma membrane-rich P3 fraction contained a concentration of ankyrin isoforms similar to that in the P2 fraction. In vitro proteolysis of ankyrin in the P2 fraction with calpain showed that the 212-kDa ankyrinB was more susceptible to calpain than was ankyrinR. In the two-vessel occlusion model, ischemia for 30 min generated the 160-kDa fragment of ankyrinR, and reperfusion for 60 min after 30 min of ischemia remarkably increased the 160-kDa fragment. The reperfusion also significantly decreased the 212-kDa isoform of ankyrinB. Both ischemia-reperfusion and in vitro proteolysis with calpain generated the 160-kDa fragment of ankyrinR, suggesting the involvement of calpain. |
| abstract_unstemmed |
Abstract: The distribution of brain-type ankyrin (ankyrinB, 212 kDa) and erythrocyte-type ankyrin (ankyrinR, 239 kDa) was investigated in the subcellular fractions of rat forebrain (P1, 1,000 g pellet; P2, 15,000 g pellet; P3, 100,000 g pellet; S, 100,000 g supernatant) by immunoblotting using specific antibodies. The P2 fraction contained ∼40% of the 212- and 163-kDa isoforms of ankyrinB and the 239-kDa isoform of ankyrinR. Further subfractionation of the P2 by Percoll gradient centrifugation followed by separation of myelin showed association of the three ankyrin isoforms with the synaptosome-rich fraction but not with the myelin-rich fraction. The plasma membrane-rich P3 fraction contained a concentration of ankyrin isoforms similar to that in the P2 fraction. In vitro proteolysis of ankyrin in the P2 fraction with calpain showed that the 212-kDa ankyrinB was more susceptible to calpain than was ankyrinR. In the two-vessel occlusion model, ischemia for 30 min generated the 160-kDa fragment of ankyrinR, and reperfusion for 60 min after 30 min of ischemia remarkably increased the 160-kDa fragment. The reperfusion also significantly decreased the 212-kDa isoform of ankyrinB. Both ischemia-reperfusion and in vitro proteolysis with calpain generated the 160-kDa fragment of ankyrinR, suggesting the involvement of calpain. |
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Distribution of Ankyrin Isoforms and Their Proteolysis After Ischemia and Reperfusion in Rat Brain |
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Fukuda, Shiro Kunimoto, Manabu Yoshida, Ken-ichi |
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