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Prevention of amyloid fibril formation of amyloidogenic chicken cystatin by site‐specific glycosylation in yeast
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| Zeitschriftentitel: | Protein Science |
|---|---|
| Personen und Körperschaften: | , , , , , |
| In: | Protein Science, 15, 2006, 2, S. 213-222 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
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| Schlagwörter: |
| author_facet |
He, Jianwei Song, Youtao Ueyama, Nobuhiro Saito, Akira Azakami, Hiroyuki Kato, Akio He, Jianwei Song, Youtao Ueyama, Nobuhiro Saito, Akira Azakami, Hiroyuki Kato, Akio |
|---|---|
| author |
He, Jianwei Song, Youtao Ueyama, Nobuhiro Saito, Akira Azakami, Hiroyuki Kato, Akio |
| spellingShingle |
He, Jianwei Song, Youtao Ueyama, Nobuhiro Saito, Akira Azakami, Hiroyuki Kato, Akio Protein Science Prevention of amyloid fibril formation of amyloidogenic chicken cystatin by site‐specific glycosylation in yeast Molecular Biology Biochemistry |
| author_sort |
he, jianwei |
| spelling |
He, Jianwei Song, Youtao Ueyama, Nobuhiro Saito, Akira Azakami, Hiroyuki Kato, Akio 0961-8368 1469-896X Wiley Molecular Biology Biochemistry http://dx.doi.org/10.1110/ps.051753306 <jats:title>Abstract</jats:title><jats:p>To address the role of glycosylation on fibrillogenicity of amyloidogenic chicken cystatin, the consensus sequence for <jats:italic>N</jats:italic>‐linked glycosylation (Asn<jats:sub>106</jats:sub>‐Ile<jats:sub>108</jats:sub> → Asn<jats:sub>106</jats:sub>‐Thr<jats:sub>108</jats:sub>) was introduced by site‐directed mutagenesis into the wild‐type and amyloidogenic chicken cystatins to construct the glycosylated form of chicken cystatins. Both the glycosylated and unglycosylated forms of wild‐type and amyloidogenic mutant I66Q cystatin were expressed and secreted in a culture medium of yeast <jats:italic>Pichia pastoris</jats:italic> transformants. Comparison of the amount of insoluble aggregate, the secondary structure, and fibrillogenicity has shown that the <jats:italic>N</jats:italic>‐linked glycosylation could prevent amyloid fibril formation of amyloidogenic chicken cystatin secreted in yeast cells without affecting its inhibitory activities. Further study showed this glycosylation could inhibit the formation of cystatin dimers. Therefore, our data strongly suggested that the mechanism causing the prevention of amyloidogenic cystation fibril formation may be realized through suppression of the formation of three‐dimensional domain‐swapped dimers and oligomers of amyloidogenic cystatin by the glycosylated chains at position 106.</jats:p> Prevention of amyloid fibril formation of amyloidogenic chicken cystatin by site‐specific glycosylation in yeast Protein Science |
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10.1110/ps.051753306 |
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| title |
Prevention of amyloid fibril formation of amyloidogenic chicken cystatin by site‐specific glycosylation in yeast |
| title_unstemmed |
Prevention of amyloid fibril formation of amyloidogenic chicken cystatin by site‐specific glycosylation in yeast |
| title_full |
Prevention of amyloid fibril formation of amyloidogenic chicken cystatin by site‐specific glycosylation in yeast |
| title_fullStr |
Prevention of amyloid fibril formation of amyloidogenic chicken cystatin by site‐specific glycosylation in yeast |
| title_full_unstemmed |
Prevention of amyloid fibril formation of amyloidogenic chicken cystatin by site‐specific glycosylation in yeast |
| title_short |
Prevention of amyloid fibril formation of amyloidogenic chicken cystatin by site‐specific glycosylation in yeast |
| title_sort |
prevention of amyloid fibril formation of amyloidogenic chicken cystatin by site‐specific glycosylation in yeast |
| topic |
Molecular Biology Biochemistry |
| url |
http://dx.doi.org/10.1110/ps.051753306 |
| publishDate |
2006 |
| physical |
213-222 |
| description |
<jats:title>Abstract</jats:title><jats:p>To address the role of glycosylation on fibrillogenicity of amyloidogenic chicken cystatin, the consensus sequence for <jats:italic>N</jats:italic>‐linked glycosylation (Asn<jats:sub>106</jats:sub>‐Ile<jats:sub>108</jats:sub> → Asn<jats:sub>106</jats:sub>‐Thr<jats:sub>108</jats:sub>) was introduced by site‐directed mutagenesis into the wild‐type and amyloidogenic chicken cystatins to construct the glycosylated form of chicken cystatins. Both the glycosylated and unglycosylated forms of wild‐type and amyloidogenic mutant I66Q cystatin were expressed and secreted in a culture medium of yeast <jats:italic>Pichia pastoris</jats:italic> transformants. Comparison of the amount of insoluble aggregate, the secondary structure, and fibrillogenicity has shown that the <jats:italic>N</jats:italic>‐linked glycosylation could prevent amyloid fibril formation of amyloidogenic chicken cystatin secreted in yeast cells without affecting its inhibitory activities. Further study showed this glycosylation could inhibit the formation of cystatin dimers. Therefore, our data strongly suggested that the mechanism causing the prevention of amyloidogenic cystation fibril formation may be realized through suppression of the formation of three‐dimensional domain‐swapped dimers and oligomers of amyloidogenic cystatin by the glycosylated chains at position 106.</jats:p> |
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| author | He, Jianwei, Song, Youtao, Ueyama, Nobuhiro, Saito, Akira, Azakami, Hiroyuki, Kato, Akio |
| author_facet | He, Jianwei, Song, Youtao, Ueyama, Nobuhiro, Saito, Akira, Azakami, Hiroyuki, Kato, Akio, He, Jianwei, Song, Youtao, Ueyama, Nobuhiro, Saito, Akira, Azakami, Hiroyuki, Kato, Akio |
| author_sort | he, jianwei |
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| description | <jats:title>Abstract</jats:title><jats:p>To address the role of glycosylation on fibrillogenicity of amyloidogenic chicken cystatin, the consensus sequence for <jats:italic>N</jats:italic>‐linked glycosylation (Asn<jats:sub>106</jats:sub>‐Ile<jats:sub>108</jats:sub> → Asn<jats:sub>106</jats:sub>‐Thr<jats:sub>108</jats:sub>) was introduced by site‐directed mutagenesis into the wild‐type and amyloidogenic chicken cystatins to construct the glycosylated form of chicken cystatins. Both the glycosylated and unglycosylated forms of wild‐type and amyloidogenic mutant I66Q cystatin were expressed and secreted in a culture medium of yeast <jats:italic>Pichia pastoris</jats:italic> transformants. Comparison of the amount of insoluble aggregate, the secondary structure, and fibrillogenicity has shown that the <jats:italic>N</jats:italic>‐linked glycosylation could prevent amyloid fibril formation of amyloidogenic chicken cystatin secreted in yeast cells without affecting its inhibitory activities. Further study showed this glycosylation could inhibit the formation of cystatin dimers. Therefore, our data strongly suggested that the mechanism causing the prevention of amyloidogenic cystation fibril formation may be realized through suppression of the formation of three‐dimensional domain‐swapped dimers and oligomers of amyloidogenic cystatin by the glycosylated chains at position 106.</jats:p> |
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| imprint | Wiley, 2006 |
| imprint_str_mv | Wiley, 2006 |
| institution | DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229 |
| issn | 1469-896X, 0961-8368 |
| issn_str_mv | 1469-896X, 0961-8368 |
| language | English |
| last_indexed | 2024-03-01T14:32:40.494Z |
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| physical | 213-222 |
| publishDate | 2006 |
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| spelling | He, Jianwei Song, Youtao Ueyama, Nobuhiro Saito, Akira Azakami, Hiroyuki Kato, Akio 0961-8368 1469-896X Wiley Molecular Biology Biochemistry http://dx.doi.org/10.1110/ps.051753306 <jats:title>Abstract</jats:title><jats:p>To address the role of glycosylation on fibrillogenicity of amyloidogenic chicken cystatin, the consensus sequence for <jats:italic>N</jats:italic>‐linked glycosylation (Asn<jats:sub>106</jats:sub>‐Ile<jats:sub>108</jats:sub> → Asn<jats:sub>106</jats:sub>‐Thr<jats:sub>108</jats:sub>) was introduced by site‐directed mutagenesis into the wild‐type and amyloidogenic chicken cystatins to construct the glycosylated form of chicken cystatins. Both the glycosylated and unglycosylated forms of wild‐type and amyloidogenic mutant I66Q cystatin were expressed and secreted in a culture medium of yeast <jats:italic>Pichia pastoris</jats:italic> transformants. Comparison of the amount of insoluble aggregate, the secondary structure, and fibrillogenicity has shown that the <jats:italic>N</jats:italic>‐linked glycosylation could prevent amyloid fibril formation of amyloidogenic chicken cystatin secreted in yeast cells without affecting its inhibitory activities. Further study showed this glycosylation could inhibit the formation of cystatin dimers. Therefore, our data strongly suggested that the mechanism causing the prevention of amyloidogenic cystation fibril formation may be realized through suppression of the formation of three‐dimensional domain‐swapped dimers and oligomers of amyloidogenic cystatin by the glycosylated chains at position 106.</jats:p> Prevention of amyloid fibril formation of amyloidogenic chicken cystatin by site‐specific glycosylation in yeast Protein Science |
| spellingShingle | He, Jianwei, Song, Youtao, Ueyama, Nobuhiro, Saito, Akira, Azakami, Hiroyuki, Kato, Akio, Protein Science, Prevention of amyloid fibril formation of amyloidogenic chicken cystatin by site‐specific glycosylation in yeast, Molecular Biology, Biochemistry |
| title | Prevention of amyloid fibril formation of amyloidogenic chicken cystatin by site‐specific glycosylation in yeast |
| title_full | Prevention of amyloid fibril formation of amyloidogenic chicken cystatin by site‐specific glycosylation in yeast |
| title_fullStr | Prevention of amyloid fibril formation of amyloidogenic chicken cystatin by site‐specific glycosylation in yeast |
| title_full_unstemmed | Prevention of amyloid fibril formation of amyloidogenic chicken cystatin by site‐specific glycosylation in yeast |
| title_short | Prevention of amyloid fibril formation of amyloidogenic chicken cystatin by site‐specific glycosylation in yeast |
| title_sort | prevention of amyloid fibril formation of amyloidogenic chicken cystatin by site‐specific glycosylation in yeast |
| title_unstemmed | Prevention of amyloid fibril formation of amyloidogenic chicken cystatin by site‐specific glycosylation in yeast |
| topic | Molecular Biology, Biochemistry |
| url | http://dx.doi.org/10.1110/ps.051753306 |