The Mouse Brown (b) Locus Protein Functions as a Dopachrome Tautomerase
The mouse b locus controls black/brown coat coloration. Its product, the b-protein or TRP-1, has significant homology to tyrosinase, and this has led to suggestions that the b-protein is itself a melanogenic enzyme. In order to investigate its function, we have used lines of mouse fibroblasts stably...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
WINDER, ALISON J. [verfasserIn] WITTBJER, ANNA [verfasserIn] ODH, GERD [verfasserIn] |
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| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1994 |
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| Schlagwörter: |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2006 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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| Übergeordnetes Werk: |
In: Periodontology 2000 - Oxford [u.a.] : Wiley-Blackwell, 1993, 7(1994), 5, Seite 0 |
| Übergeordnetes Werk: |
volume:7 ; year:1994 ; number:5 ; pages:0 |
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| DOI / URN: |
10.1111/j.1600-0749.1994.tb00632.x |
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| 520 | |a The mouse b locus controls black/brown coat coloration. Its product, the b-protein or TRP-1, has significant homology to tyrosinase, and this has led to suggestions that the b-protein is itself a melanogenic enzyme. In order to investigate its function, we have used lines of mouse fibroblasts stably expressing the b-protein. We were unable to con-firm previous reports that the b-protein has tyrosinase or catalase activity, but detected stereospecific dopachrome tautomerase activity in b-protein-expressing fibroblasts. This dopachrome tautomerase binds to Concanavalin A-Sepharose, and the major product of its action on L-dopachrome is 5,6-dihydroxyindole-2-carboxylic acid, as expected for the mammalian enzyme. Since this activity is not present in untransfected fibroblasts we conclude that the b-protein has dopachrome tautomerase activity. Further supporting evidence comes from the analysis of melanin metabolites produced by fibroblasts expressing tyrosinase alone, or in combination with the b-protein. Culture medium from the line expressing both proteins contains significant amounts of methylated carboxylated indoles, such as 6-hydroxy-5-methoxyindole-2-carboxylic acid, which would be expected in cells with an active dopachrome tautomerase. The levels of these compounds in medium from cells expressing tyrosinase alone are approximately 20-fold lower, and not significantly above background. Hence, it appears that the b-protein acts as a dopachrome tautomerase in vivo as well as in vitro. | ||
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10.1111/j.1600-0749.1994.tb00632.x doi (DE-627)NLEJ241157358 DE-627 ger DE-627 rakwb WINDER, ALISON J. verfasserin aut The Mouse Brown (b) Locus Protein Functions as a Dopachrome Tautomerase Oxford, UK Blackwell Publishing Ltd 1994 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The mouse b locus controls black/brown coat coloration. Its product, the b-protein or TRP-1, has significant homology to tyrosinase, and this has led to suggestions that the b-protein is itself a melanogenic enzyme. In order to investigate its function, we have used lines of mouse fibroblasts stably expressing the b-protein. We were unable to con-firm previous reports that the b-protein has tyrosinase or catalase activity, but detected stereospecific dopachrome tautomerase activity in b-protein-expressing fibroblasts. This dopachrome tautomerase binds to Concanavalin A-Sepharose, and the major product of its action on L-dopachrome is 5,6-dihydroxyindole-2-carboxylic acid, as expected for the mammalian enzyme. Since this activity is not present in untransfected fibroblasts we conclude that the b-protein has dopachrome tautomerase activity. Further supporting evidence comes from the analysis of melanin metabolites produced by fibroblasts expressing tyrosinase alone, or in combination with the b-protein. Culture medium from the line expressing both proteins contains significant amounts of methylated carboxylated indoles, such as 6-hydroxy-5-methoxyindole-2-carboxylic acid, which would be expected in cells with an active dopachrome tautomerase. The levels of these compounds in medium from cells expressing tyrosinase alone are approximately 20-fold lower, and not significantly above background. Hence, it appears that the b-protein acts as a dopachrome tautomerase in vivo as well as in vitro. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Melanin synthesis WITTBJER, ANNA verfasserin aut ODH, GERD verfasserin aut ROSENGREN, EVALD oth RORSMAN, HANS oth In Periodontology 2000 Oxford [u.a.] : Wiley-Blackwell, 1993 7(1994), 5, Seite 0 Online-Ressource (DE-627)NLEJ243925956 (DE-600)2027098-7 1600-0757 nnns volume:7 year:1994 number:5 pages:0 http://dx.doi.org/10.1111/j.1600-0749.1994.tb00632.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 7 1994 5 0 |
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10.1111/j.1600-0749.1994.tb00632.x doi (DE-627)NLEJ241157358 DE-627 ger DE-627 rakwb WINDER, ALISON J. verfasserin aut The Mouse Brown (b) Locus Protein Functions as a Dopachrome Tautomerase Oxford, UK Blackwell Publishing Ltd 1994 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The mouse b locus controls black/brown coat coloration. Its product, the b-protein or TRP-1, has significant homology to tyrosinase, and this has led to suggestions that the b-protein is itself a melanogenic enzyme. In order to investigate its function, we have used lines of mouse fibroblasts stably expressing the b-protein. We were unable to con-firm previous reports that the b-protein has tyrosinase or catalase activity, but detected stereospecific dopachrome tautomerase activity in b-protein-expressing fibroblasts. This dopachrome tautomerase binds to Concanavalin A-Sepharose, and the major product of its action on L-dopachrome is 5,6-dihydroxyindole-2-carboxylic acid, as expected for the mammalian enzyme. Since this activity is not present in untransfected fibroblasts we conclude that the b-protein has dopachrome tautomerase activity. Further supporting evidence comes from the analysis of melanin metabolites produced by fibroblasts expressing tyrosinase alone, or in combination with the b-protein. Culture medium from the line expressing both proteins contains significant amounts of methylated carboxylated indoles, such as 6-hydroxy-5-methoxyindole-2-carboxylic acid, which would be expected in cells with an active dopachrome tautomerase. The levels of these compounds in medium from cells expressing tyrosinase alone are approximately 20-fold lower, and not significantly above background. Hence, it appears that the b-protein acts as a dopachrome tautomerase in vivo as well as in vitro. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Melanin synthesis WITTBJER, ANNA verfasserin aut ODH, GERD verfasserin aut ROSENGREN, EVALD oth RORSMAN, HANS oth In Periodontology 2000 Oxford [u.a.] : Wiley-Blackwell, 1993 7(1994), 5, Seite 0 Online-Ressource (DE-627)NLEJ243925956 (DE-600)2027098-7 1600-0757 nnns volume:7 year:1994 number:5 pages:0 http://dx.doi.org/10.1111/j.1600-0749.1994.tb00632.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 7 1994 5 0 |
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10.1111/j.1600-0749.1994.tb00632.x doi (DE-627)NLEJ241157358 DE-627 ger DE-627 rakwb WINDER, ALISON J. verfasserin aut The Mouse Brown (b) Locus Protein Functions as a Dopachrome Tautomerase Oxford, UK Blackwell Publishing Ltd 1994 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The mouse b locus controls black/brown coat coloration. Its product, the b-protein or TRP-1, has significant homology to tyrosinase, and this has led to suggestions that the b-protein is itself a melanogenic enzyme. In order to investigate its function, we have used lines of mouse fibroblasts stably expressing the b-protein. We were unable to con-firm previous reports that the b-protein has tyrosinase or catalase activity, but detected stereospecific dopachrome tautomerase activity in b-protein-expressing fibroblasts. This dopachrome tautomerase binds to Concanavalin A-Sepharose, and the major product of its action on L-dopachrome is 5,6-dihydroxyindole-2-carboxylic acid, as expected for the mammalian enzyme. Since this activity is not present in untransfected fibroblasts we conclude that the b-protein has dopachrome tautomerase activity. Further supporting evidence comes from the analysis of melanin metabolites produced by fibroblasts expressing tyrosinase alone, or in combination with the b-protein. Culture medium from the line expressing both proteins contains significant amounts of methylated carboxylated indoles, such as 6-hydroxy-5-methoxyindole-2-carboxylic acid, which would be expected in cells with an active dopachrome tautomerase. The levels of these compounds in medium from cells expressing tyrosinase alone are approximately 20-fold lower, and not significantly above background. Hence, it appears that the b-protein acts as a dopachrome tautomerase in vivo as well as in vitro. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Melanin synthesis WITTBJER, ANNA verfasserin aut ODH, GERD verfasserin aut ROSENGREN, EVALD oth RORSMAN, HANS oth In Periodontology 2000 Oxford [u.a.] : Wiley-Blackwell, 1993 7(1994), 5, Seite 0 Online-Ressource (DE-627)NLEJ243925956 (DE-600)2027098-7 1600-0757 nnns volume:7 year:1994 number:5 pages:0 http://dx.doi.org/10.1111/j.1600-0749.1994.tb00632.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 7 1994 5 0 |
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10.1111/j.1600-0749.1994.tb00632.x doi (DE-627)NLEJ241157358 DE-627 ger DE-627 rakwb WINDER, ALISON J. verfasserin aut The Mouse Brown (b) Locus Protein Functions as a Dopachrome Tautomerase Oxford, UK Blackwell Publishing Ltd 1994 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The mouse b locus controls black/brown coat coloration. Its product, the b-protein or TRP-1, has significant homology to tyrosinase, and this has led to suggestions that the b-protein is itself a melanogenic enzyme. In order to investigate its function, we have used lines of mouse fibroblasts stably expressing the b-protein. We were unable to con-firm previous reports that the b-protein has tyrosinase or catalase activity, but detected stereospecific dopachrome tautomerase activity in b-protein-expressing fibroblasts. This dopachrome tautomerase binds to Concanavalin A-Sepharose, and the major product of its action on L-dopachrome is 5,6-dihydroxyindole-2-carboxylic acid, as expected for the mammalian enzyme. Since this activity is not present in untransfected fibroblasts we conclude that the b-protein has dopachrome tautomerase activity. Further supporting evidence comes from the analysis of melanin metabolites produced by fibroblasts expressing tyrosinase alone, or in combination with the b-protein. Culture medium from the line expressing both proteins contains significant amounts of methylated carboxylated indoles, such as 6-hydroxy-5-methoxyindole-2-carboxylic acid, which would be expected in cells with an active dopachrome tautomerase. The levels of these compounds in medium from cells expressing tyrosinase alone are approximately 20-fold lower, and not significantly above background. Hence, it appears that the b-protein acts as a dopachrome tautomerase in vivo as well as in vitro. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Melanin synthesis WITTBJER, ANNA verfasserin aut ODH, GERD verfasserin aut ROSENGREN, EVALD oth RORSMAN, HANS oth In Periodontology 2000 Oxford [u.a.] : Wiley-Blackwell, 1993 7(1994), 5, Seite 0 Online-Ressource (DE-627)NLEJ243925956 (DE-600)2027098-7 1600-0757 nnns volume:7 year:1994 number:5 pages:0 http://dx.doi.org/10.1111/j.1600-0749.1994.tb00632.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 7 1994 5 0 |
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10.1111/j.1600-0749.1994.tb00632.x doi (DE-627)NLEJ241157358 DE-627 ger DE-627 rakwb WINDER, ALISON J. verfasserin aut The Mouse Brown (b) Locus Protein Functions as a Dopachrome Tautomerase Oxford, UK Blackwell Publishing Ltd 1994 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The mouse b locus controls black/brown coat coloration. Its product, the b-protein or TRP-1, has significant homology to tyrosinase, and this has led to suggestions that the b-protein is itself a melanogenic enzyme. In order to investigate its function, we have used lines of mouse fibroblasts stably expressing the b-protein. We were unable to con-firm previous reports that the b-protein has tyrosinase or catalase activity, but detected stereospecific dopachrome tautomerase activity in b-protein-expressing fibroblasts. This dopachrome tautomerase binds to Concanavalin A-Sepharose, and the major product of its action on L-dopachrome is 5,6-dihydroxyindole-2-carboxylic acid, as expected for the mammalian enzyme. Since this activity is not present in untransfected fibroblasts we conclude that the b-protein has dopachrome tautomerase activity. Further supporting evidence comes from the analysis of melanin metabolites produced by fibroblasts expressing tyrosinase alone, or in combination with the b-protein. Culture medium from the line expressing both proteins contains significant amounts of methylated carboxylated indoles, such as 6-hydroxy-5-methoxyindole-2-carboxylic acid, which would be expected in cells with an active dopachrome tautomerase. The levels of these compounds in medium from cells expressing tyrosinase alone are approximately 20-fold lower, and not significantly above background. Hence, it appears that the b-protein acts as a dopachrome tautomerase in vivo as well as in vitro. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Melanin synthesis WITTBJER, ANNA verfasserin aut ODH, GERD verfasserin aut ROSENGREN, EVALD oth RORSMAN, HANS oth In Periodontology 2000 Oxford [u.a.] : Wiley-Blackwell, 1993 7(1994), 5, Seite 0 Online-Ressource (DE-627)NLEJ243925956 (DE-600)2027098-7 1600-0757 nnns volume:7 year:1994 number:5 pages:0 http://dx.doi.org/10.1111/j.1600-0749.1994.tb00632.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 7 1994 5 0 |
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The Mouse Brown (b) Locus Protein Functions as a Dopachrome Tautomerase |
| abstract |
The mouse b locus controls black/brown coat coloration. Its product, the b-protein or TRP-1, has significant homology to tyrosinase, and this has led to suggestions that the b-protein is itself a melanogenic enzyme. In order to investigate its function, we have used lines of mouse fibroblasts stably expressing the b-protein. We were unable to con-firm previous reports that the b-protein has tyrosinase or catalase activity, but detected stereospecific dopachrome tautomerase activity in b-protein-expressing fibroblasts. This dopachrome tautomerase binds to Concanavalin A-Sepharose, and the major product of its action on L-dopachrome is 5,6-dihydroxyindole-2-carboxylic acid, as expected for the mammalian enzyme. Since this activity is not present in untransfected fibroblasts we conclude that the b-protein has dopachrome tautomerase activity. Further supporting evidence comes from the analysis of melanin metabolites produced by fibroblasts expressing tyrosinase alone, or in combination with the b-protein. Culture medium from the line expressing both proteins contains significant amounts of methylated carboxylated indoles, such as 6-hydroxy-5-methoxyindole-2-carboxylic acid, which would be expected in cells with an active dopachrome tautomerase. The levels of these compounds in medium from cells expressing tyrosinase alone are approximately 20-fold lower, and not significantly above background. Hence, it appears that the b-protein acts as a dopachrome tautomerase in vivo as well as in vitro. |
| abstractGer |
The mouse b locus controls black/brown coat coloration. Its product, the b-protein or TRP-1, has significant homology to tyrosinase, and this has led to suggestions that the b-protein is itself a melanogenic enzyme. In order to investigate its function, we have used lines of mouse fibroblasts stably expressing the b-protein. We were unable to con-firm previous reports that the b-protein has tyrosinase or catalase activity, but detected stereospecific dopachrome tautomerase activity in b-protein-expressing fibroblasts. This dopachrome tautomerase binds to Concanavalin A-Sepharose, and the major product of its action on L-dopachrome is 5,6-dihydroxyindole-2-carboxylic acid, as expected for the mammalian enzyme. Since this activity is not present in untransfected fibroblasts we conclude that the b-protein has dopachrome tautomerase activity. Further supporting evidence comes from the analysis of melanin metabolites produced by fibroblasts expressing tyrosinase alone, or in combination with the b-protein. Culture medium from the line expressing both proteins contains significant amounts of methylated carboxylated indoles, such as 6-hydroxy-5-methoxyindole-2-carboxylic acid, which would be expected in cells with an active dopachrome tautomerase. The levels of these compounds in medium from cells expressing tyrosinase alone are approximately 20-fold lower, and not significantly above background. Hence, it appears that the b-protein acts as a dopachrome tautomerase in vivo as well as in vitro. |
| abstract_unstemmed |
The mouse b locus controls black/brown coat coloration. Its product, the b-protein or TRP-1, has significant homology to tyrosinase, and this has led to suggestions that the b-protein is itself a melanogenic enzyme. In order to investigate its function, we have used lines of mouse fibroblasts stably expressing the b-protein. We were unable to con-firm previous reports that the b-protein has tyrosinase or catalase activity, but detected stereospecific dopachrome tautomerase activity in b-protein-expressing fibroblasts. This dopachrome tautomerase binds to Concanavalin A-Sepharose, and the major product of its action on L-dopachrome is 5,6-dihydroxyindole-2-carboxylic acid, as expected for the mammalian enzyme. Since this activity is not present in untransfected fibroblasts we conclude that the b-protein has dopachrome tautomerase activity. Further supporting evidence comes from the analysis of melanin metabolites produced by fibroblasts expressing tyrosinase alone, or in combination with the b-protein. Culture medium from the line expressing both proteins contains significant amounts of methylated carboxylated indoles, such as 6-hydroxy-5-methoxyindole-2-carboxylic acid, which would be expected in cells with an active dopachrome tautomerase. The levels of these compounds in medium from cells expressing tyrosinase alone are approximately 20-fold lower, and not significantly above background. Hence, it appears that the b-protein acts as a dopachrome tautomerase in vivo as well as in vitro. |
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| title_short |
The Mouse Brown (b) Locus Protein Functions as a Dopachrome Tautomerase |
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WITTBJER, ANNA ODH, GERD ROSENGREN, EVALD RORSMAN, HANS |
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10.1111/j.1600-0749.1994.tb00632.x |
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2024-07-05T22:01:47.701Z |
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