Cleavage of β-dystroglycan occurs in sarcoglycan-deficient skeletal muscle without MMP-2 and MMP-9
The dystroglycan complex consists of two subunits: extracellular α-dystroglycan and membrane-spanning β-dystroglycan, which provide a tight link between the extracellular matrix and the intracellular cytoskeleton. Previous studies showed that 43 kDa β-dystroglycan is proteolytically cleaved into the...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Fukai, Yuta [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2017transfer abstract |
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| Schlagwörter: |
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| Umfang: |
7 |
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| Übergeordnetes Werk: |
Enthalten in: Preparation and characterization of glass-ceramics via co-sintering of coal fly ash and oil shale ash-derived amorphous slag - Zhang, Zhikun ELSEVIER, 2019, BBRC, Orlando, Fla |
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| Übergeordnetes Werk: |
volume:492 ; year:2017 ; number:2 ; day:14 ; month:10 ; pages:199-205 ; extent:7 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.bbrc.2017.08.048 |
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ELV020497679 |
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| 520 | |a The dystroglycan complex consists of two subunits: extracellular α-dystroglycan and membrane-spanning β-dystroglycan, which provide a tight link between the extracellular matrix and the intracellular cytoskeleton. Previous studies showed that 43 kDa β-dystroglycan is proteolytically cleaved into the 30 kDa fragment by matrix metalloproteinases (MMPs) in various non-muscle tissues, whereas it is protected from cleavage in muscles by the sarcoglycan complex which resides close to the dystroglycan complex. It is noteworthy that cleaved β-dystroglycan is detected in muscles from patients with sarcoglycanopathy, sarcoglycan-deficient muscular dystrophy. In vitro assays using protease inhibitors suggest that both MMP-2 and MMP-9 contribute to the cleavage of β-dystroglycan. However, this has remained uninvestigated in vivo. | ||
| 520 | |a The dystroglycan complex consists of two subunits: extracellular α-dystroglycan and membrane-spanning β-dystroglycan, which provide a tight link between the extracellular matrix and the intracellular cytoskeleton. Previous studies showed that 43 kDa β-dystroglycan is proteolytically cleaved into the 30 kDa fragment by matrix metalloproteinases (MMPs) in various non-muscle tissues, whereas it is protected from cleavage in muscles by the sarcoglycan complex which resides close to the dystroglycan complex. It is noteworthy that cleaved β-dystroglycan is detected in muscles from patients with sarcoglycanopathy, sarcoglycan-deficient muscular dystrophy. In vitro assays using protease inhibitors suggest that both MMP-2 and MMP-9 contribute to the cleavage of β-dystroglycan. However, this has remained uninvestigated in vivo. | ||
| 650 | 7 | |a Matrix metalloproteinase (MMP)-2 |2 Elsevier | |
| 650 | 7 | |a β-dystroglycan |2 Elsevier | |
| 650 | 7 | |a MMP-14 |2 Elsevier | |
| 650 | 7 | |a Sarcoglycanopathy |2 Elsevier | |
| 650 | 7 | |a γ-sarcoglycan |2 Elsevier | |
| 650 | 7 | |a MMP-9 |2 Elsevier | |
| 700 | 1 | |a Ohsawa, Yutaka |4 oth | |
| 700 | 1 | |a Ohtsubo, Hideaki |4 oth | |
| 700 | 1 | |a Nishimatsu, Shin-ichiro |4 oth | |
| 700 | 1 | |a Hagiwara, Hiroki |4 oth | |
| 700 | 1 | |a Noda, Makoto |4 oth | |
| 700 | 1 | |a Sasaoka, Toshikuni |4 oth | |
| 700 | 1 | |a Murakami, Tatsufumi |4 oth | |
| 700 | 1 | |a Sunada, Yoshihide |4 oth | |
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10.1016/j.bbrc.2017.08.048 doi GBVA2017019000001.pica (DE-627)ELV020497679 (ELSEVIER)S0006-291X(17)31601-7 DE-627 ger DE-627 rakwb eng 570 570 DE-600 670 VZ 51.60 bkl 58.45 bkl Fukai, Yuta verfasserin aut Cleavage of β-dystroglycan occurs in sarcoglycan-deficient skeletal muscle without MMP-2 and MMP-9 2017transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The dystroglycan complex consists of two subunits: extracellular α-dystroglycan and membrane-spanning β-dystroglycan, which provide a tight link between the extracellular matrix and the intracellular cytoskeleton. Previous studies showed that 43 kDa β-dystroglycan is proteolytically cleaved into the 30 kDa fragment by matrix metalloproteinases (MMPs) in various non-muscle tissues, whereas it is protected from cleavage in muscles by the sarcoglycan complex which resides close to the dystroglycan complex. It is noteworthy that cleaved β-dystroglycan is detected in muscles from patients with sarcoglycanopathy, sarcoglycan-deficient muscular dystrophy. In vitro assays using protease inhibitors suggest that both MMP-2 and MMP-9 contribute to the cleavage of β-dystroglycan. However, this has remained uninvestigated in vivo. The dystroglycan complex consists of two subunits: extracellular α-dystroglycan and membrane-spanning β-dystroglycan, which provide a tight link between the extracellular matrix and the intracellular cytoskeleton. Previous studies showed that 43 kDa β-dystroglycan is proteolytically cleaved into the 30 kDa fragment by matrix metalloproteinases (MMPs) in various non-muscle tissues, whereas it is protected from cleavage in muscles by the sarcoglycan complex which resides close to the dystroglycan complex. It is noteworthy that cleaved β-dystroglycan is detected in muscles from patients with sarcoglycanopathy, sarcoglycan-deficient muscular dystrophy. In vitro assays using protease inhibitors suggest that both MMP-2 and MMP-9 contribute to the cleavage of β-dystroglycan. However, this has remained uninvestigated in vivo. Matrix metalloproteinase (MMP)-2 Elsevier β-dystroglycan Elsevier MMP-14 Elsevier Sarcoglycanopathy Elsevier γ-sarcoglycan Elsevier MMP-9 Elsevier Ohsawa, Yutaka oth Ohtsubo, Hideaki oth Nishimatsu, Shin-ichiro oth Hagiwara, Hiroki oth Noda, Makoto oth Sasaoka, Toshikuni oth Murakami, Tatsufumi oth Sunada, Yoshihide oth Enthalten in Academic Press Zhang, Zhikun ELSEVIER Preparation and characterization of glass-ceramics via co-sintering of coal fly ash and oil shale ash-derived amorphous slag 2019 BBRC Orlando, Fla (DE-627)ELV002811154 volume:492 year:2017 number:2 day:14 month:10 pages:199-205 extent:7 https://doi.org/10.1016/j.bbrc.2017.08.048 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 51.60 Keramische Werkstoffe Hartstoffe Werkstoffkunde VZ 58.45 Gesteinshüttenkunde VZ AR 492 2017 2 14 1014 199-205 7 045F 570 |
| spelling |
10.1016/j.bbrc.2017.08.048 doi GBVA2017019000001.pica (DE-627)ELV020497679 (ELSEVIER)S0006-291X(17)31601-7 DE-627 ger DE-627 rakwb eng 570 570 DE-600 670 VZ 51.60 bkl 58.45 bkl Fukai, Yuta verfasserin aut Cleavage of β-dystroglycan occurs in sarcoglycan-deficient skeletal muscle without MMP-2 and MMP-9 2017transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The dystroglycan complex consists of two subunits: extracellular α-dystroglycan and membrane-spanning β-dystroglycan, which provide a tight link between the extracellular matrix and the intracellular cytoskeleton. Previous studies showed that 43 kDa β-dystroglycan is proteolytically cleaved into the 30 kDa fragment by matrix metalloproteinases (MMPs) in various non-muscle tissues, whereas it is protected from cleavage in muscles by the sarcoglycan complex which resides close to the dystroglycan complex. It is noteworthy that cleaved β-dystroglycan is detected in muscles from patients with sarcoglycanopathy, sarcoglycan-deficient muscular dystrophy. In vitro assays using protease inhibitors suggest that both MMP-2 and MMP-9 contribute to the cleavage of β-dystroglycan. However, this has remained uninvestigated in vivo. The dystroglycan complex consists of two subunits: extracellular α-dystroglycan and membrane-spanning β-dystroglycan, which provide a tight link between the extracellular matrix and the intracellular cytoskeleton. Previous studies showed that 43 kDa β-dystroglycan is proteolytically cleaved into the 30 kDa fragment by matrix metalloproteinases (MMPs) in various non-muscle tissues, whereas it is protected from cleavage in muscles by the sarcoglycan complex which resides close to the dystroglycan complex. It is noteworthy that cleaved β-dystroglycan is detected in muscles from patients with sarcoglycanopathy, sarcoglycan-deficient muscular dystrophy. In vitro assays using protease inhibitors suggest that both MMP-2 and MMP-9 contribute to the cleavage of β-dystroglycan. However, this has remained uninvestigated in vivo. Matrix metalloproteinase (MMP)-2 Elsevier β-dystroglycan Elsevier MMP-14 Elsevier Sarcoglycanopathy Elsevier γ-sarcoglycan Elsevier MMP-9 Elsevier Ohsawa, Yutaka oth Ohtsubo, Hideaki oth Nishimatsu, Shin-ichiro oth Hagiwara, Hiroki oth Noda, Makoto oth Sasaoka, Toshikuni oth Murakami, Tatsufumi oth Sunada, Yoshihide oth Enthalten in Academic Press Zhang, Zhikun ELSEVIER Preparation and characterization of glass-ceramics via co-sintering of coal fly ash and oil shale ash-derived amorphous slag 2019 BBRC Orlando, Fla (DE-627)ELV002811154 volume:492 year:2017 number:2 day:14 month:10 pages:199-205 extent:7 https://doi.org/10.1016/j.bbrc.2017.08.048 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 51.60 Keramische Werkstoffe Hartstoffe Werkstoffkunde VZ 58.45 Gesteinshüttenkunde VZ AR 492 2017 2 14 1014 199-205 7 045F 570 |
| allfields_unstemmed |
10.1016/j.bbrc.2017.08.048 doi GBVA2017019000001.pica (DE-627)ELV020497679 (ELSEVIER)S0006-291X(17)31601-7 DE-627 ger DE-627 rakwb eng 570 570 DE-600 670 VZ 51.60 bkl 58.45 bkl Fukai, Yuta verfasserin aut Cleavage of β-dystroglycan occurs in sarcoglycan-deficient skeletal muscle without MMP-2 and MMP-9 2017transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The dystroglycan complex consists of two subunits: extracellular α-dystroglycan and membrane-spanning β-dystroglycan, which provide a tight link between the extracellular matrix and the intracellular cytoskeleton. Previous studies showed that 43 kDa β-dystroglycan is proteolytically cleaved into the 30 kDa fragment by matrix metalloproteinases (MMPs) in various non-muscle tissues, whereas it is protected from cleavage in muscles by the sarcoglycan complex which resides close to the dystroglycan complex. It is noteworthy that cleaved β-dystroglycan is detected in muscles from patients with sarcoglycanopathy, sarcoglycan-deficient muscular dystrophy. In vitro assays using protease inhibitors suggest that both MMP-2 and MMP-9 contribute to the cleavage of β-dystroglycan. However, this has remained uninvestigated in vivo. The dystroglycan complex consists of two subunits: extracellular α-dystroglycan and membrane-spanning β-dystroglycan, which provide a tight link between the extracellular matrix and the intracellular cytoskeleton. Previous studies showed that 43 kDa β-dystroglycan is proteolytically cleaved into the 30 kDa fragment by matrix metalloproteinases (MMPs) in various non-muscle tissues, whereas it is protected from cleavage in muscles by the sarcoglycan complex which resides close to the dystroglycan complex. It is noteworthy that cleaved β-dystroglycan is detected in muscles from patients with sarcoglycanopathy, sarcoglycan-deficient muscular dystrophy. In vitro assays using protease inhibitors suggest that both MMP-2 and MMP-9 contribute to the cleavage of β-dystroglycan. However, this has remained uninvestigated in vivo. Matrix metalloproteinase (MMP)-2 Elsevier β-dystroglycan Elsevier MMP-14 Elsevier Sarcoglycanopathy Elsevier γ-sarcoglycan Elsevier MMP-9 Elsevier Ohsawa, Yutaka oth Ohtsubo, Hideaki oth Nishimatsu, Shin-ichiro oth Hagiwara, Hiroki oth Noda, Makoto oth Sasaoka, Toshikuni oth Murakami, Tatsufumi oth Sunada, Yoshihide oth Enthalten in Academic Press Zhang, Zhikun ELSEVIER Preparation and characterization of glass-ceramics via co-sintering of coal fly ash and oil shale ash-derived amorphous slag 2019 BBRC Orlando, Fla (DE-627)ELV002811154 volume:492 year:2017 number:2 day:14 month:10 pages:199-205 extent:7 https://doi.org/10.1016/j.bbrc.2017.08.048 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 51.60 Keramische Werkstoffe Hartstoffe Werkstoffkunde VZ 58.45 Gesteinshüttenkunde VZ AR 492 2017 2 14 1014 199-205 7 045F 570 |
| allfieldsGer |
10.1016/j.bbrc.2017.08.048 doi GBVA2017019000001.pica (DE-627)ELV020497679 (ELSEVIER)S0006-291X(17)31601-7 DE-627 ger DE-627 rakwb eng 570 570 DE-600 670 VZ 51.60 bkl 58.45 bkl Fukai, Yuta verfasserin aut Cleavage of β-dystroglycan occurs in sarcoglycan-deficient skeletal muscle without MMP-2 and MMP-9 2017transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The dystroglycan complex consists of two subunits: extracellular α-dystroglycan and membrane-spanning β-dystroglycan, which provide a tight link between the extracellular matrix and the intracellular cytoskeleton. Previous studies showed that 43 kDa β-dystroglycan is proteolytically cleaved into the 30 kDa fragment by matrix metalloproteinases (MMPs) in various non-muscle tissues, whereas it is protected from cleavage in muscles by the sarcoglycan complex which resides close to the dystroglycan complex. It is noteworthy that cleaved β-dystroglycan is detected in muscles from patients with sarcoglycanopathy, sarcoglycan-deficient muscular dystrophy. In vitro assays using protease inhibitors suggest that both MMP-2 and MMP-9 contribute to the cleavage of β-dystroglycan. However, this has remained uninvestigated in vivo. The dystroglycan complex consists of two subunits: extracellular α-dystroglycan and membrane-spanning β-dystroglycan, which provide a tight link between the extracellular matrix and the intracellular cytoskeleton. Previous studies showed that 43 kDa β-dystroglycan is proteolytically cleaved into the 30 kDa fragment by matrix metalloproteinases (MMPs) in various non-muscle tissues, whereas it is protected from cleavage in muscles by the sarcoglycan complex which resides close to the dystroglycan complex. It is noteworthy that cleaved β-dystroglycan is detected in muscles from patients with sarcoglycanopathy, sarcoglycan-deficient muscular dystrophy. In vitro assays using protease inhibitors suggest that both MMP-2 and MMP-9 contribute to the cleavage of β-dystroglycan. However, this has remained uninvestigated in vivo. Matrix metalloproteinase (MMP)-2 Elsevier β-dystroglycan Elsevier MMP-14 Elsevier Sarcoglycanopathy Elsevier γ-sarcoglycan Elsevier MMP-9 Elsevier Ohsawa, Yutaka oth Ohtsubo, Hideaki oth Nishimatsu, Shin-ichiro oth Hagiwara, Hiroki oth Noda, Makoto oth Sasaoka, Toshikuni oth Murakami, Tatsufumi oth Sunada, Yoshihide oth Enthalten in Academic Press Zhang, Zhikun ELSEVIER Preparation and characterization of glass-ceramics via co-sintering of coal fly ash and oil shale ash-derived amorphous slag 2019 BBRC Orlando, Fla (DE-627)ELV002811154 volume:492 year:2017 number:2 day:14 month:10 pages:199-205 extent:7 https://doi.org/10.1016/j.bbrc.2017.08.048 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 51.60 Keramische Werkstoffe Hartstoffe Werkstoffkunde VZ 58.45 Gesteinshüttenkunde VZ AR 492 2017 2 14 1014 199-205 7 045F 570 |
| allfieldsSound |
10.1016/j.bbrc.2017.08.048 doi GBVA2017019000001.pica (DE-627)ELV020497679 (ELSEVIER)S0006-291X(17)31601-7 DE-627 ger DE-627 rakwb eng 570 570 DE-600 670 VZ 51.60 bkl 58.45 bkl Fukai, Yuta verfasserin aut Cleavage of β-dystroglycan occurs in sarcoglycan-deficient skeletal muscle without MMP-2 and MMP-9 2017transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The dystroglycan complex consists of two subunits: extracellular α-dystroglycan and membrane-spanning β-dystroglycan, which provide a tight link between the extracellular matrix and the intracellular cytoskeleton. Previous studies showed that 43 kDa β-dystroglycan is proteolytically cleaved into the 30 kDa fragment by matrix metalloproteinases (MMPs) in various non-muscle tissues, whereas it is protected from cleavage in muscles by the sarcoglycan complex which resides close to the dystroglycan complex. It is noteworthy that cleaved β-dystroglycan is detected in muscles from patients with sarcoglycanopathy, sarcoglycan-deficient muscular dystrophy. In vitro assays using protease inhibitors suggest that both MMP-2 and MMP-9 contribute to the cleavage of β-dystroglycan. However, this has remained uninvestigated in vivo. The dystroglycan complex consists of two subunits: extracellular α-dystroglycan and membrane-spanning β-dystroglycan, which provide a tight link between the extracellular matrix and the intracellular cytoskeleton. Previous studies showed that 43 kDa β-dystroglycan is proteolytically cleaved into the 30 kDa fragment by matrix metalloproteinases (MMPs) in various non-muscle tissues, whereas it is protected from cleavage in muscles by the sarcoglycan complex which resides close to the dystroglycan complex. It is noteworthy that cleaved β-dystroglycan is detected in muscles from patients with sarcoglycanopathy, sarcoglycan-deficient muscular dystrophy. In vitro assays using protease inhibitors suggest that both MMP-2 and MMP-9 contribute to the cleavage of β-dystroglycan. However, this has remained uninvestigated in vivo. Matrix metalloproteinase (MMP)-2 Elsevier β-dystroglycan Elsevier MMP-14 Elsevier Sarcoglycanopathy Elsevier γ-sarcoglycan Elsevier MMP-9 Elsevier Ohsawa, Yutaka oth Ohtsubo, Hideaki oth Nishimatsu, Shin-ichiro oth Hagiwara, Hiroki oth Noda, Makoto oth Sasaoka, Toshikuni oth Murakami, Tatsufumi oth Sunada, Yoshihide oth Enthalten in Academic Press Zhang, Zhikun ELSEVIER Preparation and characterization of glass-ceramics via co-sintering of coal fly ash and oil shale ash-derived amorphous slag 2019 BBRC Orlando, Fla (DE-627)ELV002811154 volume:492 year:2017 number:2 day:14 month:10 pages:199-205 extent:7 https://doi.org/10.1016/j.bbrc.2017.08.048 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 51.60 Keramische Werkstoffe Hartstoffe Werkstoffkunde VZ 58.45 Gesteinshüttenkunde VZ AR 492 2017 2 14 1014 199-205 7 045F 570 |
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Enthalten in Preparation and characterization of glass-ceramics via co-sintering of coal fly ash and oil shale ash-derived amorphous slag Orlando, Fla volume:492 year:2017 number:2 day:14 month:10 pages:199-205 extent:7 |
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Enthalten in Preparation and characterization of glass-ceramics via co-sintering of coal fly ash and oil shale ash-derived amorphous slag Orlando, Fla volume:492 year:2017 number:2 day:14 month:10 pages:199-205 extent:7 |
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Preparation and characterization of glass-ceramics via co-sintering of coal fly ash and oil shale ash-derived amorphous slag |
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Cleavage of β-dystroglycan occurs in sarcoglycan-deficient skeletal muscle without MMP-2 and MMP-9 |
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The dystroglycan complex consists of two subunits: extracellular α-dystroglycan and membrane-spanning β-dystroglycan, which provide a tight link between the extracellular matrix and the intracellular cytoskeleton. Previous studies showed that 43 kDa β-dystroglycan is proteolytically cleaved into the 30 kDa fragment by matrix metalloproteinases (MMPs) in various non-muscle tissues, whereas it is protected from cleavage in muscles by the sarcoglycan complex which resides close to the dystroglycan complex. It is noteworthy that cleaved β-dystroglycan is detected in muscles from patients with sarcoglycanopathy, sarcoglycan-deficient muscular dystrophy. In vitro assays using protease inhibitors suggest that both MMP-2 and MMP-9 contribute to the cleavage of β-dystroglycan. However, this has remained uninvestigated in vivo. |
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The dystroglycan complex consists of two subunits: extracellular α-dystroglycan and membrane-spanning β-dystroglycan, which provide a tight link between the extracellular matrix and the intracellular cytoskeleton. Previous studies showed that 43 kDa β-dystroglycan is proteolytically cleaved into the 30 kDa fragment by matrix metalloproteinases (MMPs) in various non-muscle tissues, whereas it is protected from cleavage in muscles by the sarcoglycan complex which resides close to the dystroglycan complex. It is noteworthy that cleaved β-dystroglycan is detected in muscles from patients with sarcoglycanopathy, sarcoglycan-deficient muscular dystrophy. In vitro assays using protease inhibitors suggest that both MMP-2 and MMP-9 contribute to the cleavage of β-dystroglycan. However, this has remained uninvestigated in vivo. |
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The dystroglycan complex consists of two subunits: extracellular α-dystroglycan and membrane-spanning β-dystroglycan, which provide a tight link between the extracellular matrix and the intracellular cytoskeleton. Previous studies showed that 43 kDa β-dystroglycan is proteolytically cleaved into the 30 kDa fragment by matrix metalloproteinases (MMPs) in various non-muscle tissues, whereas it is protected from cleavage in muscles by the sarcoglycan complex which resides close to the dystroglycan complex. It is noteworthy that cleaved β-dystroglycan is detected in muscles from patients with sarcoglycanopathy, sarcoglycan-deficient muscular dystrophy. In vitro assays using protease inhibitors suggest that both MMP-2 and MMP-9 contribute to the cleavage of β-dystroglycan. However, this has remained uninvestigated in vivo. |
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