Cysteine 144 Is a Key Residue in the Copper Reduction by the β-Amyloid Precursor Protein
Abstract : The β-amyloid precursor protein (β-APP) contains a copper-binding site localized between amino acids 135 and 156 (β-APP135-156). We have employed synthetic β-APP peptides to characterize their capacities to reduce Cu(II) to Cu(I). Analogues of the wild-type β-APP135-156 peptide, containin...
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| Autor*in: |
Ruiz, Francisca H. [verfasserIn] González, Mauricio [verfasserIn] Bodini, Mario [verfasserIn] |
|---|
| Format: |
E-Artikel |
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| Erschienen: |
Oxford UK: Blackwell Science Ltd ; 1999 |
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Online-Ressource |
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2001 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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In: Journal of neurochemistry - Oxford : Wiley-Blackwell, 1956, 73(1999), 3, Seite 0 |
| Übergeordnetes Werk: |
volume:73 ; year:1999 ; number:3 ; pages:0 |
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| DOI / URN: |
10.1046/j.1471-4159.1999.0731288.x |
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| 520 | |a Abstract : The β-amyloid precursor protein (β-APP) contains a copper-binding site localized between amino acids 135 and 156 (β-APP135-156). We have employed synthetic β-APP peptides to characterize their capacities to reduce Cu(II) to Cu(I). Analogues of the wild-type β-APP135-156 peptide, containing specific amino acid substitutions, were used to establish which residues are specifically involved in the reduction of copper by β-APP135-156. We report here that β-APP’s copper-binding domain reduced Cu(II) to Cu(I). The single-mutant β-APPHis147→Ala and the double-mutant β-APPHis147→Ala/His149→Ala showed a small decrease in copper reduction in relation to the wild-type peptide and the β-APPSys144→Ser mutation abolished it, suggesting that Cys144 is the key amino acid in the oxidoreduction reaction. Our results confirm that soluble β-APP is involved in the reduction of Cu(II) to Cu(I). | ||
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10.1046/j.1471-4159.1999.0731288.x doi (DE-627)NLEJ243154445 DE-627 ger DE-627 rakwb Ruiz, Francisca H. verfasserin aut Cysteine 144 Is a Key Residue in the Copper Reduction by the β-Amyloid Precursor Protein Oxford UK Blackwell Science Ltd 1999 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract : The β-amyloid precursor protein (β-APP) contains a copper-binding site localized between amino acids 135 and 156 (β-APP135-156). We have employed synthetic β-APP peptides to characterize their capacities to reduce Cu(II) to Cu(I). Analogues of the wild-type β-APP135-156 peptide, containing specific amino acid substitutions, were used to establish which residues are specifically involved in the reduction of copper by β-APP135-156. We report here that β-APP’s copper-binding domain reduced Cu(II) to Cu(I). The single-mutant β-APPHis147→Ala and the double-mutant β-APPHis147→Ala/His149→Ala showed a small decrease in copper reduction in relation to the wild-type peptide and the β-APPSys144→Ser mutation abolished it, suggesting that Cys144 is the key amino acid in the oxidoreduction reaction. Our results confirm that soluble β-APP is involved in the reduction of Cu(II) to Cu(I). 2001 Blackwell Publishing Journal Backfiles 1879-2005 |2001|||||||||| β-Amyloid precursor protein González, Mauricio verfasserin aut Bodini, Mario verfasserin aut Opazo, Carlos oth Inestrosa, Nibaldo C. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 73(1999), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:73 year:1999 number:3 pages:0 http://dx.doi.org/10.1046/j.1471-4159.1999.0731288.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 73 1999 3 0 |
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10.1046/j.1471-4159.1999.0731288.x doi (DE-627)NLEJ243154445 DE-627 ger DE-627 rakwb Ruiz, Francisca H. verfasserin aut Cysteine 144 Is a Key Residue in the Copper Reduction by the β-Amyloid Precursor Protein Oxford UK Blackwell Science Ltd 1999 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract : The β-amyloid precursor protein (β-APP) contains a copper-binding site localized between amino acids 135 and 156 (β-APP135-156). We have employed synthetic β-APP peptides to characterize their capacities to reduce Cu(II) to Cu(I). Analogues of the wild-type β-APP135-156 peptide, containing specific amino acid substitutions, were used to establish which residues are specifically involved in the reduction of copper by β-APP135-156. We report here that β-APP’s copper-binding domain reduced Cu(II) to Cu(I). The single-mutant β-APPHis147→Ala and the double-mutant β-APPHis147→Ala/His149→Ala showed a small decrease in copper reduction in relation to the wild-type peptide and the β-APPSys144→Ser mutation abolished it, suggesting that Cys144 is the key amino acid in the oxidoreduction reaction. Our results confirm that soluble β-APP is involved in the reduction of Cu(II) to Cu(I). 2001 Blackwell Publishing Journal Backfiles 1879-2005 |2001|||||||||| β-Amyloid precursor protein González, Mauricio verfasserin aut Bodini, Mario verfasserin aut Opazo, Carlos oth Inestrosa, Nibaldo C. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 73(1999), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:73 year:1999 number:3 pages:0 http://dx.doi.org/10.1046/j.1471-4159.1999.0731288.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 73 1999 3 0 |
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10.1046/j.1471-4159.1999.0731288.x doi (DE-627)NLEJ243154445 DE-627 ger DE-627 rakwb Ruiz, Francisca H. verfasserin aut Cysteine 144 Is a Key Residue in the Copper Reduction by the β-Amyloid Precursor Protein Oxford UK Blackwell Science Ltd 1999 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract : The β-amyloid precursor protein (β-APP) contains a copper-binding site localized between amino acids 135 and 156 (β-APP135-156). We have employed synthetic β-APP peptides to characterize their capacities to reduce Cu(II) to Cu(I). Analogues of the wild-type β-APP135-156 peptide, containing specific amino acid substitutions, were used to establish which residues are specifically involved in the reduction of copper by β-APP135-156. We report here that β-APP’s copper-binding domain reduced Cu(II) to Cu(I). The single-mutant β-APPHis147→Ala and the double-mutant β-APPHis147→Ala/His149→Ala showed a small decrease in copper reduction in relation to the wild-type peptide and the β-APPSys144→Ser mutation abolished it, suggesting that Cys144 is the key amino acid in the oxidoreduction reaction. Our results confirm that soluble β-APP is involved in the reduction of Cu(II) to Cu(I). 2001 Blackwell Publishing Journal Backfiles 1879-2005 |2001|||||||||| β-Amyloid precursor protein González, Mauricio verfasserin aut Bodini, Mario verfasserin aut Opazo, Carlos oth Inestrosa, Nibaldo C. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 73(1999), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:73 year:1999 number:3 pages:0 http://dx.doi.org/10.1046/j.1471-4159.1999.0731288.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 73 1999 3 0 |
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10.1046/j.1471-4159.1999.0731288.x doi (DE-627)NLEJ243154445 DE-627 ger DE-627 rakwb Ruiz, Francisca H. verfasserin aut Cysteine 144 Is a Key Residue in the Copper Reduction by the β-Amyloid Precursor Protein Oxford UK Blackwell Science Ltd 1999 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract : The β-amyloid precursor protein (β-APP) contains a copper-binding site localized between amino acids 135 and 156 (β-APP135-156). We have employed synthetic β-APP peptides to characterize their capacities to reduce Cu(II) to Cu(I). Analogues of the wild-type β-APP135-156 peptide, containing specific amino acid substitutions, were used to establish which residues are specifically involved in the reduction of copper by β-APP135-156. We report here that β-APP’s copper-binding domain reduced Cu(II) to Cu(I). The single-mutant β-APPHis147→Ala and the double-mutant β-APPHis147→Ala/His149→Ala showed a small decrease in copper reduction in relation to the wild-type peptide and the β-APPSys144→Ser mutation abolished it, suggesting that Cys144 is the key amino acid in the oxidoreduction reaction. Our results confirm that soluble β-APP is involved in the reduction of Cu(II) to Cu(I). 2001 Blackwell Publishing Journal Backfiles 1879-2005 |2001|||||||||| β-Amyloid precursor protein González, Mauricio verfasserin aut Bodini, Mario verfasserin aut Opazo, Carlos oth Inestrosa, Nibaldo C. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 73(1999), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:73 year:1999 number:3 pages:0 http://dx.doi.org/10.1046/j.1471-4159.1999.0731288.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 73 1999 3 0 |
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10.1046/j.1471-4159.1999.0731288.x doi (DE-627)NLEJ243154445 DE-627 ger DE-627 rakwb Ruiz, Francisca H. verfasserin aut Cysteine 144 Is a Key Residue in the Copper Reduction by the β-Amyloid Precursor Protein Oxford UK Blackwell Science Ltd 1999 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract : The β-amyloid precursor protein (β-APP) contains a copper-binding site localized between amino acids 135 and 156 (β-APP135-156). We have employed synthetic β-APP peptides to characterize their capacities to reduce Cu(II) to Cu(I). Analogues of the wild-type β-APP135-156 peptide, containing specific amino acid substitutions, were used to establish which residues are specifically involved in the reduction of copper by β-APP135-156. We report here that β-APP’s copper-binding domain reduced Cu(II) to Cu(I). The single-mutant β-APPHis147→Ala and the double-mutant β-APPHis147→Ala/His149→Ala showed a small decrease in copper reduction in relation to the wild-type peptide and the β-APPSys144→Ser mutation abolished it, suggesting that Cys144 is the key amino acid in the oxidoreduction reaction. Our results confirm that soluble β-APP is involved in the reduction of Cu(II) to Cu(I). 2001 Blackwell Publishing Journal Backfiles 1879-2005 |2001|||||||||| β-Amyloid precursor protein González, Mauricio verfasserin aut Bodini, Mario verfasserin aut Opazo, Carlos oth Inestrosa, Nibaldo C. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 73(1999), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:73 year:1999 number:3 pages:0 http://dx.doi.org/10.1046/j.1471-4159.1999.0731288.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 73 1999 3 0 |
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Cysteine 144 Is a Key Residue in the Copper Reduction by the β-Amyloid Precursor Protein |
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Abstract : The β-amyloid precursor protein (β-APP) contains a copper-binding site localized between amino acids 135 and 156 (β-APP135-156). We have employed synthetic β-APP peptides to characterize their capacities to reduce Cu(II) to Cu(I). Analogues of the wild-type β-APP135-156 peptide, containing specific amino acid substitutions, were used to establish which residues are specifically involved in the reduction of copper by β-APP135-156. We report here that β-APP’s copper-binding domain reduced Cu(II) to Cu(I). The single-mutant β-APPHis147→Ala and the double-mutant β-APPHis147→Ala/His149→Ala showed a small decrease in copper reduction in relation to the wild-type peptide and the β-APPSys144→Ser mutation abolished it, suggesting that Cys144 is the key amino acid in the oxidoreduction reaction. Our results confirm that soluble β-APP is involved in the reduction of Cu(II) to Cu(I). |
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Abstract : The β-amyloid precursor protein (β-APP) contains a copper-binding site localized between amino acids 135 and 156 (β-APP135-156). We have employed synthetic β-APP peptides to characterize their capacities to reduce Cu(II) to Cu(I). Analogues of the wild-type β-APP135-156 peptide, containing specific amino acid substitutions, were used to establish which residues are specifically involved in the reduction of copper by β-APP135-156. We report here that β-APP’s copper-binding domain reduced Cu(II) to Cu(I). The single-mutant β-APPHis147→Ala and the double-mutant β-APPHis147→Ala/His149→Ala showed a small decrease in copper reduction in relation to the wild-type peptide and the β-APPSys144→Ser mutation abolished it, suggesting that Cys144 is the key amino acid in the oxidoreduction reaction. Our results confirm that soluble β-APP is involved in the reduction of Cu(II) to Cu(I). |
| abstract_unstemmed |
Abstract : The β-amyloid precursor protein (β-APP) contains a copper-binding site localized between amino acids 135 and 156 (β-APP135-156). We have employed synthetic β-APP peptides to characterize their capacities to reduce Cu(II) to Cu(I). Analogues of the wild-type β-APP135-156 peptide, containing specific amino acid substitutions, were used to establish which residues are specifically involved in the reduction of copper by β-APP135-156. We report here that β-APP’s copper-binding domain reduced Cu(II) to Cu(I). The single-mutant β-APPHis147→Ala and the double-mutant β-APPHis147→Ala/His149→Ala showed a small decrease in copper reduction in relation to the wild-type peptide and the β-APPSys144→Ser mutation abolished it, suggesting that Cys144 is the key amino acid in the oxidoreduction reaction. Our results confirm that soluble β-APP is involved in the reduction of Cu(II) to Cu(I). |
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González, Mauricio Bodini, Mario Opazo, Carlos Inestrosa, Nibaldo C. |
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González, Mauricio Bodini, Mario Opazo, Carlos Inestrosa, Nibaldo C. |
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NLEJ243927584 |
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| doi_str |
10.1046/j.1471-4159.1999.0731288.x |
| up_date |
2024-07-06T04:29:49.303Z |
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7.398178 |