Regulation of Rat Pineal Hydroxyindole-O-Methyltransferase: Evidence of S-Adenosylmethionine-Mediated Glucocorticoid Control
: Rat pineal hydroxyindole-O-methyltransferase is controlled similarly to adrenal medullary phenylethanolamine N-methyltransferase. S-adenosylmethionine (SAM), the in vivo cofactor utilized by the enzyme to convert N-acetylserotonin to melatonin, protects this methyltransferase against tryptic prote...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Sandrock, Alfred W. [verfasserIn] Leblanc, Gabrielle G. [verfasserIn] Wong, Dona L. [verfasserIn] |
|---|
| Format: |
E-Artikel |
|---|
| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1980 |
|---|
| Umfang: |
Online-Ressource |
|---|
| Reproduktion: |
2006 ; Blackwell Publishing Journal Backfiles 1879-2005 |
|---|---|
| Übergeordnetes Werk: |
In: Journal of neurochemistry - Oxford : Wiley-Blackwell, 1956, 35(1980), 3, Seite 0 |
| Übergeordnetes Werk: |
volume:35 ; year:1980 ; number:3 ; pages:0 |
| Links: |
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| DOI / URN: |
10.1111/j.1471-4159.1980.tb03688.x |
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| 520 | |a : Rat pineal hydroxyindole-O-methyltransferase is controlled similarly to adrenal medullary phenylethanolamine N-methyltransferase. S-adenosylmethionine (SAM), the in vivo cofactor utilized by the enzyme to convert N-acetylserotonin to melatonin, protects this methyltransferase against tryptic proteolysis in vitro. Furthermore, in vivo studies suggest that the nucleoside itself is controlled by glucocorticoids. Hypophysectomy decreases hydroxyindole-O-methyltransferase levels as compared with control animals, while dexamethasone and SAM administration restore enzyme levels toward control values. In vitro proteolytic studies further demonstrate that, although N-acetylserotonin does not stabilize the enzyme against trypsinization, this substrate acts synergistically with SAM to confer greater stabilization than observed with SAM alone. | ||
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10.1111/j.1471-4159.1980.tb03688.x doi (DE-627)NLEJ240324846 DE-627 ger DE-627 rakwb Sandrock, Alfred W. verfasserin aut Regulation of Rat Pineal Hydroxyindole-O-Methyltransferase: Evidence of S-Adenosylmethionine-Mediated Glucocorticoid Control Oxford, UK Blackwell Publishing Ltd 1980 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier : Rat pineal hydroxyindole-O-methyltransferase is controlled similarly to adrenal medullary phenylethanolamine N-methyltransferase. S-adenosylmethionine (SAM), the in vivo cofactor utilized by the enzyme to convert N-acetylserotonin to melatonin, protects this methyltransferase against tryptic proteolysis in vitro. Furthermore, in vivo studies suggest that the nucleoside itself is controlled by glucocorticoids. Hypophysectomy decreases hydroxyindole-O-methyltransferase levels as compared with control animals, while dexamethasone and SAM administration restore enzyme levels toward control values. In vitro proteolytic studies further demonstrate that, although N-acetylserotonin does not stabilize the enzyme against trypsinization, this substrate acts synergistically with SAM to confer greater stabilization than observed with SAM alone. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Leblanc, Gabrielle G. verfasserin aut Wong, Dona L. verfasserin aut Ciaranello, Roland D. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 35(1980), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:35 year:1980 number:3 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1980.tb03688.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 35 1980 3 0 |
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10.1111/j.1471-4159.1980.tb03688.x doi (DE-627)NLEJ240324846 DE-627 ger DE-627 rakwb Sandrock, Alfred W. verfasserin aut Regulation of Rat Pineal Hydroxyindole-O-Methyltransferase: Evidence of S-Adenosylmethionine-Mediated Glucocorticoid Control Oxford, UK Blackwell Publishing Ltd 1980 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier : Rat pineal hydroxyindole-O-methyltransferase is controlled similarly to adrenal medullary phenylethanolamine N-methyltransferase. S-adenosylmethionine (SAM), the in vivo cofactor utilized by the enzyme to convert N-acetylserotonin to melatonin, protects this methyltransferase against tryptic proteolysis in vitro. Furthermore, in vivo studies suggest that the nucleoside itself is controlled by glucocorticoids. Hypophysectomy decreases hydroxyindole-O-methyltransferase levels as compared with control animals, while dexamethasone and SAM administration restore enzyme levels toward control values. In vitro proteolytic studies further demonstrate that, although N-acetylserotonin does not stabilize the enzyme against trypsinization, this substrate acts synergistically with SAM to confer greater stabilization than observed with SAM alone. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Leblanc, Gabrielle G. verfasserin aut Wong, Dona L. verfasserin aut Ciaranello, Roland D. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 35(1980), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:35 year:1980 number:3 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1980.tb03688.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 35 1980 3 0 |
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10.1111/j.1471-4159.1980.tb03688.x doi (DE-627)NLEJ240324846 DE-627 ger DE-627 rakwb Sandrock, Alfred W. verfasserin aut Regulation of Rat Pineal Hydroxyindole-O-Methyltransferase: Evidence of S-Adenosylmethionine-Mediated Glucocorticoid Control Oxford, UK Blackwell Publishing Ltd 1980 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier : Rat pineal hydroxyindole-O-methyltransferase is controlled similarly to adrenal medullary phenylethanolamine N-methyltransferase. S-adenosylmethionine (SAM), the in vivo cofactor utilized by the enzyme to convert N-acetylserotonin to melatonin, protects this methyltransferase against tryptic proteolysis in vitro. Furthermore, in vivo studies suggest that the nucleoside itself is controlled by glucocorticoids. Hypophysectomy decreases hydroxyindole-O-methyltransferase levels as compared with control animals, while dexamethasone and SAM administration restore enzyme levels toward control values. In vitro proteolytic studies further demonstrate that, although N-acetylserotonin does not stabilize the enzyme against trypsinization, this substrate acts synergistically with SAM to confer greater stabilization than observed with SAM alone. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Leblanc, Gabrielle G. verfasserin aut Wong, Dona L. verfasserin aut Ciaranello, Roland D. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 35(1980), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:35 year:1980 number:3 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1980.tb03688.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 35 1980 3 0 |
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10.1111/j.1471-4159.1980.tb03688.x doi (DE-627)NLEJ240324846 DE-627 ger DE-627 rakwb Sandrock, Alfred W. verfasserin aut Regulation of Rat Pineal Hydroxyindole-O-Methyltransferase: Evidence of S-Adenosylmethionine-Mediated Glucocorticoid Control Oxford, UK Blackwell Publishing Ltd 1980 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier : Rat pineal hydroxyindole-O-methyltransferase is controlled similarly to adrenal medullary phenylethanolamine N-methyltransferase. S-adenosylmethionine (SAM), the in vivo cofactor utilized by the enzyme to convert N-acetylserotonin to melatonin, protects this methyltransferase against tryptic proteolysis in vitro. Furthermore, in vivo studies suggest that the nucleoside itself is controlled by glucocorticoids. Hypophysectomy decreases hydroxyindole-O-methyltransferase levels as compared with control animals, while dexamethasone and SAM administration restore enzyme levels toward control values. In vitro proteolytic studies further demonstrate that, although N-acetylserotonin does not stabilize the enzyme against trypsinization, this substrate acts synergistically with SAM to confer greater stabilization than observed with SAM alone. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Leblanc, Gabrielle G. verfasserin aut Wong, Dona L. verfasserin aut Ciaranello, Roland D. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 35(1980), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:35 year:1980 number:3 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1980.tb03688.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 35 1980 3 0 |
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10.1111/j.1471-4159.1980.tb03688.x doi (DE-627)NLEJ240324846 DE-627 ger DE-627 rakwb Sandrock, Alfred W. verfasserin aut Regulation of Rat Pineal Hydroxyindole-O-Methyltransferase: Evidence of S-Adenosylmethionine-Mediated Glucocorticoid Control Oxford, UK Blackwell Publishing Ltd 1980 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier : Rat pineal hydroxyindole-O-methyltransferase is controlled similarly to adrenal medullary phenylethanolamine N-methyltransferase. S-adenosylmethionine (SAM), the in vivo cofactor utilized by the enzyme to convert N-acetylserotonin to melatonin, protects this methyltransferase against tryptic proteolysis in vitro. Furthermore, in vivo studies suggest that the nucleoside itself is controlled by glucocorticoids. Hypophysectomy decreases hydroxyindole-O-methyltransferase levels as compared with control animals, while dexamethasone and SAM administration restore enzyme levels toward control values. In vitro proteolytic studies further demonstrate that, although N-acetylserotonin does not stabilize the enzyme against trypsinization, this substrate acts synergistically with SAM to confer greater stabilization than observed with SAM alone. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Leblanc, Gabrielle G. verfasserin aut Wong, Dona L. verfasserin aut Ciaranello, Roland D. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 35(1980), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:35 year:1980 number:3 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1980.tb03688.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 35 1980 3 0 |
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Regulation of Rat Pineal Hydroxyindole-O-Methyltransferase: Evidence of S-Adenosylmethionine-Mediated Glucocorticoid Control |
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: Rat pineal hydroxyindole-O-methyltransferase is controlled similarly to adrenal medullary phenylethanolamine N-methyltransferase. S-adenosylmethionine (SAM), the in vivo cofactor utilized by the enzyme to convert N-acetylserotonin to melatonin, protects this methyltransferase against tryptic proteolysis in vitro. Furthermore, in vivo studies suggest that the nucleoside itself is controlled by glucocorticoids. Hypophysectomy decreases hydroxyindole-O-methyltransferase levels as compared with control animals, while dexamethasone and SAM administration restore enzyme levels toward control values. In vitro proteolytic studies further demonstrate that, although N-acetylserotonin does not stabilize the enzyme against trypsinization, this substrate acts synergistically with SAM to confer greater stabilization than observed with SAM alone. |
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: Rat pineal hydroxyindole-O-methyltransferase is controlled similarly to adrenal medullary phenylethanolamine N-methyltransferase. S-adenosylmethionine (SAM), the in vivo cofactor utilized by the enzyme to convert N-acetylserotonin to melatonin, protects this methyltransferase against tryptic proteolysis in vitro. Furthermore, in vivo studies suggest that the nucleoside itself is controlled by glucocorticoids. Hypophysectomy decreases hydroxyindole-O-methyltransferase levels as compared with control animals, while dexamethasone and SAM administration restore enzyme levels toward control values. In vitro proteolytic studies further demonstrate that, although N-acetylserotonin does not stabilize the enzyme against trypsinization, this substrate acts synergistically with SAM to confer greater stabilization than observed with SAM alone. |
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: Rat pineal hydroxyindole-O-methyltransferase is controlled similarly to adrenal medullary phenylethanolamine N-methyltransferase. S-adenosylmethionine (SAM), the in vivo cofactor utilized by the enzyme to convert N-acetylserotonin to melatonin, protects this methyltransferase against tryptic proteolysis in vitro. Furthermore, in vivo studies suggest that the nucleoside itself is controlled by glucocorticoids. Hypophysectomy decreases hydroxyindole-O-methyltransferase levels as compared with control animals, while dexamethasone and SAM administration restore enzyme levels toward control values. In vitro proteolytic studies further demonstrate that, although N-acetylserotonin does not stabilize the enzyme against trypsinization, this substrate acts synergistically with SAM to confer greater stabilization than observed with SAM alone. |
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