N-Glycans on the receptor for advanced glycation end products influence amphoterin binding and neurite outgrowth
In this study we show that embryonic neurite growth-promoting protein amphoterin binds to carboxylated N-glycans previously identified on mammalian endothelial cells. Since amphoterin is a ligand for the receptor for advanced glycation end products (RAGE), and the ligand-binding V-domain of the rece...
Ausführliche Beschreibung
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| Autor*in: |
Srikrishna, Geetha [verfasserIn] Huttunen, Henri J. [verfasserIn] Johansson, Lena [verfasserIn] |
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| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Science, Ltd ; 2002 |
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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, 80(2002), 6, Seite 0 |
| Übergeordnetes Werk: |
volume:80 ; year:2002 ; number:6 ; pages:0 |
| Links: |
|---|
| DOI / URN: |
10.1046/j.0022-3042.2002.00796.x |
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| 520 | |a In this study we show that embryonic neurite growth-promoting protein amphoterin binds to carboxylated N-glycans previously identified on mammalian endothelial cells. Since amphoterin is a ligand for the receptor for advanced glycation end products (RAGE), and the ligand-binding V-domain of the receptor contains two potential N-glycosylation sites, we hypothesized that N-glycans on RAGE may mediate its interactions with amphoterin. In support of this, anti-carboxylate antibody mAbGB3.1 immunoprecipitates bovine RAGE, and PNGase F treatment reduces its molecular mass by 4.5 kDa, suggesting that the native receptor is a glycoprotein. The binding potential of amphoterin to RAGE decreases significantly in presence of soluble carboxylated glycans or when the receptor is deglycosylated. Oligosaccharide analysis shows that RAGE contains complex type anionic N-glycans with non-sialic acid carboxylate groups, but not the HNK-1 (3-sulfoglucuronyl β1–3 galactoside) epitope. Consistent with the functional localization of RAGE and amphoterin at the leading edges of developing neurons, mAbGB3.1 stains axons and growth cones of mouse embryonic cortical neurons, and inhibits neurite outgrowth on amphoterin matrix. The carboxylated glycans themselves promote neurite outgrowth in embryonic neurons and RAGE-transfected neuroblastoma cells. This outgrowth requires full-length, signalling-competent RAGE, as cells expressing cytoplasmic domain-deleted RAGE are unresponsive. These results indicate that carboxylated N-glycans on RAGE play an important functional role in amphoterin-RAGE-mediated signalling. | ||
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10.1046/j.0022-3042.2002.00796.x doi (DE-627)NLEJ243138814 DE-627 ger DE-627 rakwb Srikrishna, Geetha verfasserin aut N-Glycans on the receptor for advanced glycation end products influence amphoterin binding and neurite outgrowth Oxford, UK Blackwell Science, Ltd 2002 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier In this study we show that embryonic neurite growth-promoting protein amphoterin binds to carboxylated N-glycans previously identified on mammalian endothelial cells. Since amphoterin is a ligand for the receptor for advanced glycation end products (RAGE), and the ligand-binding V-domain of the receptor contains two potential N-glycosylation sites, we hypothesized that N-glycans on RAGE may mediate its interactions with amphoterin. In support of this, anti-carboxylate antibody mAbGB3.1 immunoprecipitates bovine RAGE, and PNGase F treatment reduces its molecular mass by 4.5 kDa, suggesting that the native receptor is a glycoprotein. The binding potential of amphoterin to RAGE decreases significantly in presence of soluble carboxylated glycans or when the receptor is deglycosylated. Oligosaccharide analysis shows that RAGE contains complex type anionic N-glycans with non-sialic acid carboxylate groups, but not the HNK-1 (3-sulfoglucuronyl β1–3 galactoside) epitope. Consistent with the functional localization of RAGE and amphoterin at the leading edges of developing neurons, mAbGB3.1 stains axons and growth cones of mouse embryonic cortical neurons, and inhibits neurite outgrowth on amphoterin matrix. The carboxylated glycans themselves promote neurite outgrowth in embryonic neurons and RAGE-transfected neuroblastoma cells. This outgrowth requires full-length, signalling-competent RAGE, as cells expressing cytoplasmic domain-deleted RAGE are unresponsive. These results indicate that carboxylated N-glycans on RAGE play an important functional role in amphoterin-RAGE-mediated signalling. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| amphoterin Huttunen, Henri J. verfasserin aut Johansson, Lena verfasserin aut Weigle, Bernd oth Yamaguchi, Yu oth Rauvala, Heikki oth Freeze, Hudson H. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 80(2002), 6, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:80 year:2002 number:6 pages:0 http://dx.doi.org/10.1046/j.0022-3042.2002.00796.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 80 2002 6 0 |
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10.1046/j.0022-3042.2002.00796.x doi (DE-627)NLEJ243138814 DE-627 ger DE-627 rakwb Srikrishna, Geetha verfasserin aut N-Glycans on the receptor for advanced glycation end products influence amphoterin binding and neurite outgrowth Oxford, UK Blackwell Science, Ltd 2002 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier In this study we show that embryonic neurite growth-promoting protein amphoterin binds to carboxylated N-glycans previously identified on mammalian endothelial cells. Since amphoterin is a ligand for the receptor for advanced glycation end products (RAGE), and the ligand-binding V-domain of the receptor contains two potential N-glycosylation sites, we hypothesized that N-glycans on RAGE may mediate its interactions with amphoterin. In support of this, anti-carboxylate antibody mAbGB3.1 immunoprecipitates bovine RAGE, and PNGase F treatment reduces its molecular mass by 4.5 kDa, suggesting that the native receptor is a glycoprotein. The binding potential of amphoterin to RAGE decreases significantly in presence of soluble carboxylated glycans or when the receptor is deglycosylated. Oligosaccharide analysis shows that RAGE contains complex type anionic N-glycans with non-sialic acid carboxylate groups, but not the HNK-1 (3-sulfoglucuronyl β1–3 galactoside) epitope. Consistent with the functional localization of RAGE and amphoterin at the leading edges of developing neurons, mAbGB3.1 stains axons and growth cones of mouse embryonic cortical neurons, and inhibits neurite outgrowth on amphoterin matrix. The carboxylated glycans themselves promote neurite outgrowth in embryonic neurons and RAGE-transfected neuroblastoma cells. This outgrowth requires full-length, signalling-competent RAGE, as cells expressing cytoplasmic domain-deleted RAGE are unresponsive. These results indicate that carboxylated N-glycans on RAGE play an important functional role in amphoterin-RAGE-mediated signalling. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| amphoterin Huttunen, Henri J. verfasserin aut Johansson, Lena verfasserin aut Weigle, Bernd oth Yamaguchi, Yu oth Rauvala, Heikki oth Freeze, Hudson H. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 80(2002), 6, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:80 year:2002 number:6 pages:0 http://dx.doi.org/10.1046/j.0022-3042.2002.00796.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 80 2002 6 0 |
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10.1046/j.0022-3042.2002.00796.x doi (DE-627)NLEJ243138814 DE-627 ger DE-627 rakwb Srikrishna, Geetha verfasserin aut N-Glycans on the receptor for advanced glycation end products influence amphoterin binding and neurite outgrowth Oxford, UK Blackwell Science, Ltd 2002 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier In this study we show that embryonic neurite growth-promoting protein amphoterin binds to carboxylated N-glycans previously identified on mammalian endothelial cells. Since amphoterin is a ligand for the receptor for advanced glycation end products (RAGE), and the ligand-binding V-domain of the receptor contains two potential N-glycosylation sites, we hypothesized that N-glycans on RAGE may mediate its interactions with amphoterin. In support of this, anti-carboxylate antibody mAbGB3.1 immunoprecipitates bovine RAGE, and PNGase F treatment reduces its molecular mass by 4.5 kDa, suggesting that the native receptor is a glycoprotein. The binding potential of amphoterin to RAGE decreases significantly in presence of soluble carboxylated glycans or when the receptor is deglycosylated. Oligosaccharide analysis shows that RAGE contains complex type anionic N-glycans with non-sialic acid carboxylate groups, but not the HNK-1 (3-sulfoglucuronyl β1–3 galactoside) epitope. Consistent with the functional localization of RAGE and amphoterin at the leading edges of developing neurons, mAbGB3.1 stains axons and growth cones of mouse embryonic cortical neurons, and inhibits neurite outgrowth on amphoterin matrix. The carboxylated glycans themselves promote neurite outgrowth in embryonic neurons and RAGE-transfected neuroblastoma cells. This outgrowth requires full-length, signalling-competent RAGE, as cells expressing cytoplasmic domain-deleted RAGE are unresponsive. These results indicate that carboxylated N-glycans on RAGE play an important functional role in amphoterin-RAGE-mediated signalling. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| amphoterin Huttunen, Henri J. verfasserin aut Johansson, Lena verfasserin aut Weigle, Bernd oth Yamaguchi, Yu oth Rauvala, Heikki oth Freeze, Hudson H. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 80(2002), 6, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:80 year:2002 number:6 pages:0 http://dx.doi.org/10.1046/j.0022-3042.2002.00796.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 80 2002 6 0 |
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10.1046/j.0022-3042.2002.00796.x doi (DE-627)NLEJ243138814 DE-627 ger DE-627 rakwb Srikrishna, Geetha verfasserin aut N-Glycans on the receptor for advanced glycation end products influence amphoterin binding and neurite outgrowth Oxford, UK Blackwell Science, Ltd 2002 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier In this study we show that embryonic neurite growth-promoting protein amphoterin binds to carboxylated N-glycans previously identified on mammalian endothelial cells. Since amphoterin is a ligand for the receptor for advanced glycation end products (RAGE), and the ligand-binding V-domain of the receptor contains two potential N-glycosylation sites, we hypothesized that N-glycans on RAGE may mediate its interactions with amphoterin. In support of this, anti-carboxylate antibody mAbGB3.1 immunoprecipitates bovine RAGE, and PNGase F treatment reduces its molecular mass by 4.5 kDa, suggesting that the native receptor is a glycoprotein. The binding potential of amphoterin to RAGE decreases significantly in presence of soluble carboxylated glycans or when the receptor is deglycosylated. Oligosaccharide analysis shows that RAGE contains complex type anionic N-glycans with non-sialic acid carboxylate groups, but not the HNK-1 (3-sulfoglucuronyl β1–3 galactoside) epitope. Consistent with the functional localization of RAGE and amphoterin at the leading edges of developing neurons, mAbGB3.1 stains axons and growth cones of mouse embryonic cortical neurons, and inhibits neurite outgrowth on amphoterin matrix. The carboxylated glycans themselves promote neurite outgrowth in embryonic neurons and RAGE-transfected neuroblastoma cells. This outgrowth requires full-length, signalling-competent RAGE, as cells expressing cytoplasmic domain-deleted RAGE are unresponsive. These results indicate that carboxylated N-glycans on RAGE play an important functional role in amphoterin-RAGE-mediated signalling. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| amphoterin Huttunen, Henri J. verfasserin aut Johansson, Lena verfasserin aut Weigle, Bernd oth Yamaguchi, Yu oth Rauvala, Heikki oth Freeze, Hudson H. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 80(2002), 6, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:80 year:2002 number:6 pages:0 http://dx.doi.org/10.1046/j.0022-3042.2002.00796.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 80 2002 6 0 |
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10.1046/j.0022-3042.2002.00796.x doi (DE-627)NLEJ243138814 DE-627 ger DE-627 rakwb Srikrishna, Geetha verfasserin aut N-Glycans on the receptor for advanced glycation end products influence amphoterin binding and neurite outgrowth Oxford, UK Blackwell Science, Ltd 2002 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier In this study we show that embryonic neurite growth-promoting protein amphoterin binds to carboxylated N-glycans previously identified on mammalian endothelial cells. Since amphoterin is a ligand for the receptor for advanced glycation end products (RAGE), and the ligand-binding V-domain of the receptor contains two potential N-glycosylation sites, we hypothesized that N-glycans on RAGE may mediate its interactions with amphoterin. In support of this, anti-carboxylate antibody mAbGB3.1 immunoprecipitates bovine RAGE, and PNGase F treatment reduces its molecular mass by 4.5 kDa, suggesting that the native receptor is a glycoprotein. The binding potential of amphoterin to RAGE decreases significantly in presence of soluble carboxylated glycans or when the receptor is deglycosylated. Oligosaccharide analysis shows that RAGE contains complex type anionic N-glycans with non-sialic acid carboxylate groups, but not the HNK-1 (3-sulfoglucuronyl β1–3 galactoside) epitope. Consistent with the functional localization of RAGE and amphoterin at the leading edges of developing neurons, mAbGB3.1 stains axons and growth cones of mouse embryonic cortical neurons, and inhibits neurite outgrowth on amphoterin matrix. The carboxylated glycans themselves promote neurite outgrowth in embryonic neurons and RAGE-transfected neuroblastoma cells. This outgrowth requires full-length, signalling-competent RAGE, as cells expressing cytoplasmic domain-deleted RAGE are unresponsive. These results indicate that carboxylated N-glycans on RAGE play an important functional role in amphoterin-RAGE-mediated signalling. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| amphoterin Huttunen, Henri J. verfasserin aut Johansson, Lena verfasserin aut Weigle, Bernd oth Yamaguchi, Yu oth Rauvala, Heikki oth Freeze, Hudson H. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 80(2002), 6, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:80 year:2002 number:6 pages:0 http://dx.doi.org/10.1046/j.0022-3042.2002.00796.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 80 2002 6 0 |
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N-Glycans on the receptor for advanced glycation end products influence amphoterin binding and neurite outgrowth |
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Srikrishna, Geetha |
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Journal of neurochemistry |
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Journal of neurochemistry |
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2002 |
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Srikrishna, Geetha Huttunen, Henri J. Johansson, Lena |
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Elektronische Aufsätze |
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Srikrishna, Geetha |
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10.1046/j.0022-3042.2002.00796.x |
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verfasserin |
| title_sort |
n-glycans on the receptor for advanced glycation end products influence amphoterin binding and neurite outgrowth |
| title_auth |
N-Glycans on the receptor for advanced glycation end products influence amphoterin binding and neurite outgrowth |
| abstract |
In this study we show that embryonic neurite growth-promoting protein amphoterin binds to carboxylated N-glycans previously identified on mammalian endothelial cells. Since amphoterin is a ligand for the receptor for advanced glycation end products (RAGE), and the ligand-binding V-domain of the receptor contains two potential N-glycosylation sites, we hypothesized that N-glycans on RAGE may mediate its interactions with amphoterin. In support of this, anti-carboxylate antibody mAbGB3.1 immunoprecipitates bovine RAGE, and PNGase F treatment reduces its molecular mass by 4.5 kDa, suggesting that the native receptor is a glycoprotein. The binding potential of amphoterin to RAGE decreases significantly in presence of soluble carboxylated glycans or when the receptor is deglycosylated. Oligosaccharide analysis shows that RAGE contains complex type anionic N-glycans with non-sialic acid carboxylate groups, but not the HNK-1 (3-sulfoglucuronyl β1–3 galactoside) epitope. Consistent with the functional localization of RAGE and amphoterin at the leading edges of developing neurons, mAbGB3.1 stains axons and growth cones of mouse embryonic cortical neurons, and inhibits neurite outgrowth on amphoterin matrix. The carboxylated glycans themselves promote neurite outgrowth in embryonic neurons and RAGE-transfected neuroblastoma cells. This outgrowth requires full-length, signalling-competent RAGE, as cells expressing cytoplasmic domain-deleted RAGE are unresponsive. These results indicate that carboxylated N-glycans on RAGE play an important functional role in amphoterin-RAGE-mediated signalling. |
| abstractGer |
In this study we show that embryonic neurite growth-promoting protein amphoterin binds to carboxylated N-glycans previously identified on mammalian endothelial cells. Since amphoterin is a ligand for the receptor for advanced glycation end products (RAGE), and the ligand-binding V-domain of the receptor contains two potential N-glycosylation sites, we hypothesized that N-glycans on RAGE may mediate its interactions with amphoterin. In support of this, anti-carboxylate antibody mAbGB3.1 immunoprecipitates bovine RAGE, and PNGase F treatment reduces its molecular mass by 4.5 kDa, suggesting that the native receptor is a glycoprotein. The binding potential of amphoterin to RAGE decreases significantly in presence of soluble carboxylated glycans or when the receptor is deglycosylated. Oligosaccharide analysis shows that RAGE contains complex type anionic N-glycans with non-sialic acid carboxylate groups, but not the HNK-1 (3-sulfoglucuronyl β1–3 galactoside) epitope. Consistent with the functional localization of RAGE and amphoterin at the leading edges of developing neurons, mAbGB3.1 stains axons and growth cones of mouse embryonic cortical neurons, and inhibits neurite outgrowth on amphoterin matrix. The carboxylated glycans themselves promote neurite outgrowth in embryonic neurons and RAGE-transfected neuroblastoma cells. This outgrowth requires full-length, signalling-competent RAGE, as cells expressing cytoplasmic domain-deleted RAGE are unresponsive. These results indicate that carboxylated N-glycans on RAGE play an important functional role in amphoterin-RAGE-mediated signalling. |
| abstract_unstemmed |
In this study we show that embryonic neurite growth-promoting protein amphoterin binds to carboxylated N-glycans previously identified on mammalian endothelial cells. Since amphoterin is a ligand for the receptor for advanced glycation end products (RAGE), and the ligand-binding V-domain of the receptor contains two potential N-glycosylation sites, we hypothesized that N-glycans on RAGE may mediate its interactions with amphoterin. In support of this, anti-carboxylate antibody mAbGB3.1 immunoprecipitates bovine RAGE, and PNGase F treatment reduces its molecular mass by 4.5 kDa, suggesting that the native receptor is a glycoprotein. The binding potential of amphoterin to RAGE decreases significantly in presence of soluble carboxylated glycans or when the receptor is deglycosylated. Oligosaccharide analysis shows that RAGE contains complex type anionic N-glycans with non-sialic acid carboxylate groups, but not the HNK-1 (3-sulfoglucuronyl β1–3 galactoside) epitope. Consistent with the functional localization of RAGE and amphoterin at the leading edges of developing neurons, mAbGB3.1 stains axons and growth cones of mouse embryonic cortical neurons, and inhibits neurite outgrowth on amphoterin matrix. The carboxylated glycans themselves promote neurite outgrowth in embryonic neurons and RAGE-transfected neuroblastoma cells. This outgrowth requires full-length, signalling-competent RAGE, as cells expressing cytoplasmic domain-deleted RAGE are unresponsive. These results indicate that carboxylated N-glycans on RAGE play an important functional role in amphoterin-RAGE-mediated signalling. |
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N-Glycans on the receptor for advanced glycation end products influence amphoterin binding and neurite outgrowth |
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Huttunen, Henri J. Johansson, Lena Weigle, Bernd Yamaguchi, Yu Rauvala, Heikki Freeze, Hudson H. |
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Huttunen, Henri J. Johansson, Lena Weigle, Bernd Yamaguchi, Yu Rauvala, Heikki Freeze, Hudson H. |
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