Sprouty4 levels are increased under hypoxic conditions by enhanced mRNA stability and transcription
Sprouty (Spry) proteins are well-known negative regulators of receptor tyrosine kinase-mediated signalling. Their expression is controlled by mitogens, implying a negative feedback loop. Correspondingly, the different members of the family fulfil important roles during organogenesis by adjustment of...
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Walter de Gruyter ; 2010 |
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©2010 by Walter de Gruyter Berlin New York |
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9 |
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Walter de Gruyter Online Zeitschriften |
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Enthalten in: Biological chemistry - Berlin [u.a.] : de Gruyter, 1996, 391(2010), 7 vom: 19. Mai, Seite 813-821 |
| Übergeordnetes Werk: |
volume:391 ; year:2010 ; number:7 ; day:19 ; month:05 ; pages:813-821 ; extent:9 |
| Links: |
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| DOI / URN: |
10.1515/bc.2010.082 |
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NLEJ24652815X |
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| 520 | |a Sprouty (Spry) proteins are well-known negative regulators of receptor tyrosine kinase-mediated signalling. Their expression is controlled by mitogens, implying a negative feedback loop. Correspondingly, the different members of the family fulfil important roles during organogenesis by adjustment of growth factor-induced processes. In addition, Spry4, one member of this protein family, has been shown to regulate angiogenesis by inhibiting vascular endothelial cell growth factor-induced extracellular signalling-regulated kinase (ERK) activation. Because oxygen is an important regulator of angiogenesis, we investigated Spry4 expression patterns under hypoxic conditions. Our data demonstrate that both hypoxia and desferrioxamine (DFO) treatment increased Spry4 expression. Following iron depletion, elevated Spry4 levels were detected in several cell types independent of tissue origin, presence of mitogens, cell differentiation and malignancy. Evaluation of the underlying regulative mechanisms revealed that augmented transcription and increased mRNA stability enhance mRNA levels of Spry4 in response to DFO. This study unveils a growth factor-independent regulation mechanism of Spry4 expression. Because increased Spry4 levels are accompanied by disappearing ERK phosphorylation, Spry4 might be involved in the timely restriction of MAPK signals under hypoxic conditions, similar to its role in mitogen-regulated processes. However, the functional significance of the observed upregulation of Spry4 during iron depletion remains to be clarified. | ||
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10.1515/bc.2010.082 doi artikel_Grundlieferung.pp (DE-627)NLEJ24652815X DE-627 ger DE-627 rakwb Sprouty4 levels are increased under hypoxic conditions by enhanced mRNA stability and transcription Walter de Gruyter 2010 9 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ©2010 by Walter de Gruyter Berlin New York Sprouty (Spry) proteins are well-known negative regulators of receptor tyrosine kinase-mediated signalling. Their expression is controlled by mitogens, implying a negative feedback loop. Correspondingly, the different members of the family fulfil important roles during organogenesis by adjustment of growth factor-induced processes. In addition, Spry4, one member of this protein family, has been shown to regulate angiogenesis by inhibiting vascular endothelial cell growth factor-induced extracellular signalling-regulated kinase (ERK) activation. Because oxygen is an important regulator of angiogenesis, we investigated Spry4 expression patterns under hypoxic conditions. Our data demonstrate that both hypoxia and desferrioxamine (DFO) treatment increased Spry4 expression. Following iron depletion, elevated Spry4 levels were detected in several cell types independent of tissue origin, presence of mitogens, cell differentiation and malignancy. Evaluation of the underlying regulative mechanisms revealed that augmented transcription and increased mRNA stability enhance mRNA levels of Spry4 in response to DFO. This study unveils a growth factor-independent regulation mechanism of Spry4 expression. Because increased Spry4 levels are accompanied by disappearing ERK phosphorylation, Spry4 might be involved in the timely restriction of MAPK signals under hypoxic conditions, similar to its role in mitogen-regulated processes. However, the functional significance of the observed upregulation of Spry4 during iron depletion remains to be clarified. Walter de Gruyter Online Zeitschriften desferrioxamine (DFO) extracellular signalling-regulated kinase (ERK) hypoxia Sprouty Haigl, Barbara oth Mayer, Christoph-Erik oth Siegwart, Gerald oth Sutterlüty, Hedwig oth Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 391(2010), 7 vom: 19. Mai, Seite 813-821 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:391 year:2010 number:7 day:19 month:05 pages:813-821 extent:9 https://doi.org/10.1515/bc.2010.082 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 391 2010 7 19 05 813-821 9 |
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10.1515/bc.2010.082 doi artikel_Grundlieferung.pp (DE-627)NLEJ24652815X DE-627 ger DE-627 rakwb Sprouty4 levels are increased under hypoxic conditions by enhanced mRNA stability and transcription Walter de Gruyter 2010 9 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ©2010 by Walter de Gruyter Berlin New York Sprouty (Spry) proteins are well-known negative regulators of receptor tyrosine kinase-mediated signalling. Their expression is controlled by mitogens, implying a negative feedback loop. Correspondingly, the different members of the family fulfil important roles during organogenesis by adjustment of growth factor-induced processes. In addition, Spry4, one member of this protein family, has been shown to regulate angiogenesis by inhibiting vascular endothelial cell growth factor-induced extracellular signalling-regulated kinase (ERK) activation. Because oxygen is an important regulator of angiogenesis, we investigated Spry4 expression patterns under hypoxic conditions. Our data demonstrate that both hypoxia and desferrioxamine (DFO) treatment increased Spry4 expression. Following iron depletion, elevated Spry4 levels were detected in several cell types independent of tissue origin, presence of mitogens, cell differentiation and malignancy. Evaluation of the underlying regulative mechanisms revealed that augmented transcription and increased mRNA stability enhance mRNA levels of Spry4 in response to DFO. This study unveils a growth factor-independent regulation mechanism of Spry4 expression. Because increased Spry4 levels are accompanied by disappearing ERK phosphorylation, Spry4 might be involved in the timely restriction of MAPK signals under hypoxic conditions, similar to its role in mitogen-regulated processes. However, the functional significance of the observed upregulation of Spry4 during iron depletion remains to be clarified. Walter de Gruyter Online Zeitschriften desferrioxamine (DFO) extracellular signalling-regulated kinase (ERK) hypoxia Sprouty Haigl, Barbara oth Mayer, Christoph-Erik oth Siegwart, Gerald oth Sutterlüty, Hedwig oth Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 391(2010), 7 vom: 19. Mai, Seite 813-821 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:391 year:2010 number:7 day:19 month:05 pages:813-821 extent:9 https://doi.org/10.1515/bc.2010.082 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 391 2010 7 19 05 813-821 9 |
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10.1515/bc.2010.082 doi artikel_Grundlieferung.pp (DE-627)NLEJ24652815X DE-627 ger DE-627 rakwb Sprouty4 levels are increased under hypoxic conditions by enhanced mRNA stability and transcription Walter de Gruyter 2010 9 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ©2010 by Walter de Gruyter Berlin New York Sprouty (Spry) proteins are well-known negative regulators of receptor tyrosine kinase-mediated signalling. Their expression is controlled by mitogens, implying a negative feedback loop. Correspondingly, the different members of the family fulfil important roles during organogenesis by adjustment of growth factor-induced processes. In addition, Spry4, one member of this protein family, has been shown to regulate angiogenesis by inhibiting vascular endothelial cell growth factor-induced extracellular signalling-regulated kinase (ERK) activation. Because oxygen is an important regulator of angiogenesis, we investigated Spry4 expression patterns under hypoxic conditions. Our data demonstrate that both hypoxia and desferrioxamine (DFO) treatment increased Spry4 expression. Following iron depletion, elevated Spry4 levels were detected in several cell types independent of tissue origin, presence of mitogens, cell differentiation and malignancy. Evaluation of the underlying regulative mechanisms revealed that augmented transcription and increased mRNA stability enhance mRNA levels of Spry4 in response to DFO. This study unveils a growth factor-independent regulation mechanism of Spry4 expression. Because increased Spry4 levels are accompanied by disappearing ERK phosphorylation, Spry4 might be involved in the timely restriction of MAPK signals under hypoxic conditions, similar to its role in mitogen-regulated processes. However, the functional significance of the observed upregulation of Spry4 during iron depletion remains to be clarified. Walter de Gruyter Online Zeitschriften desferrioxamine (DFO) extracellular signalling-regulated kinase (ERK) hypoxia Sprouty Haigl, Barbara oth Mayer, Christoph-Erik oth Siegwart, Gerald oth Sutterlüty, Hedwig oth Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 391(2010), 7 vom: 19. Mai, Seite 813-821 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:391 year:2010 number:7 day:19 month:05 pages:813-821 extent:9 https://doi.org/10.1515/bc.2010.082 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 391 2010 7 19 05 813-821 9 |
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10.1515/bc.2010.082 doi artikel_Grundlieferung.pp (DE-627)NLEJ24652815X DE-627 ger DE-627 rakwb Sprouty4 levels are increased under hypoxic conditions by enhanced mRNA stability and transcription Walter de Gruyter 2010 9 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ©2010 by Walter de Gruyter Berlin New York Sprouty (Spry) proteins are well-known negative regulators of receptor tyrosine kinase-mediated signalling. Their expression is controlled by mitogens, implying a negative feedback loop. Correspondingly, the different members of the family fulfil important roles during organogenesis by adjustment of growth factor-induced processes. In addition, Spry4, one member of this protein family, has been shown to regulate angiogenesis by inhibiting vascular endothelial cell growth factor-induced extracellular signalling-regulated kinase (ERK) activation. Because oxygen is an important regulator of angiogenesis, we investigated Spry4 expression patterns under hypoxic conditions. Our data demonstrate that both hypoxia and desferrioxamine (DFO) treatment increased Spry4 expression. Following iron depletion, elevated Spry4 levels were detected in several cell types independent of tissue origin, presence of mitogens, cell differentiation and malignancy. Evaluation of the underlying regulative mechanisms revealed that augmented transcription and increased mRNA stability enhance mRNA levels of Spry4 in response to DFO. This study unveils a growth factor-independent regulation mechanism of Spry4 expression. Because increased Spry4 levels are accompanied by disappearing ERK phosphorylation, Spry4 might be involved in the timely restriction of MAPK signals under hypoxic conditions, similar to its role in mitogen-regulated processes. However, the functional significance of the observed upregulation of Spry4 during iron depletion remains to be clarified. Walter de Gruyter Online Zeitschriften desferrioxamine (DFO) extracellular signalling-regulated kinase (ERK) hypoxia Sprouty Haigl, Barbara oth Mayer, Christoph-Erik oth Siegwart, Gerald oth Sutterlüty, Hedwig oth Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 391(2010), 7 vom: 19. Mai, Seite 813-821 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:391 year:2010 number:7 day:19 month:05 pages:813-821 extent:9 https://doi.org/10.1515/bc.2010.082 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 391 2010 7 19 05 813-821 9 |
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10.1515/bc.2010.082 doi artikel_Grundlieferung.pp (DE-627)NLEJ24652815X DE-627 ger DE-627 rakwb Sprouty4 levels are increased under hypoxic conditions by enhanced mRNA stability and transcription Walter de Gruyter 2010 9 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ©2010 by Walter de Gruyter Berlin New York Sprouty (Spry) proteins are well-known negative regulators of receptor tyrosine kinase-mediated signalling. Their expression is controlled by mitogens, implying a negative feedback loop. Correspondingly, the different members of the family fulfil important roles during organogenesis by adjustment of growth factor-induced processes. In addition, Spry4, one member of this protein family, has been shown to regulate angiogenesis by inhibiting vascular endothelial cell growth factor-induced extracellular signalling-regulated kinase (ERK) activation. Because oxygen is an important regulator of angiogenesis, we investigated Spry4 expression patterns under hypoxic conditions. Our data demonstrate that both hypoxia and desferrioxamine (DFO) treatment increased Spry4 expression. Following iron depletion, elevated Spry4 levels were detected in several cell types independent of tissue origin, presence of mitogens, cell differentiation and malignancy. Evaluation of the underlying regulative mechanisms revealed that augmented transcription and increased mRNA stability enhance mRNA levels of Spry4 in response to DFO. This study unveils a growth factor-independent regulation mechanism of Spry4 expression. Because increased Spry4 levels are accompanied by disappearing ERK phosphorylation, Spry4 might be involved in the timely restriction of MAPK signals under hypoxic conditions, similar to its role in mitogen-regulated processes. However, the functional significance of the observed upregulation of Spry4 during iron depletion remains to be clarified. Walter de Gruyter Online Zeitschriften desferrioxamine (DFO) extracellular signalling-regulated kinase (ERK) hypoxia Sprouty Haigl, Barbara oth Mayer, Christoph-Erik oth Siegwart, Gerald oth Sutterlüty, Hedwig oth Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 391(2010), 7 vom: 19. Mai, Seite 813-821 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:391 year:2010 number:7 day:19 month:05 pages:813-821 extent:9 https://doi.org/10.1515/bc.2010.082 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 391 2010 7 19 05 813-821 9 |
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sprouty4 levels are increased under hypoxic conditions by enhanced mrna stability and transcription |
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Sprouty4 levels are increased under hypoxic conditions by enhanced mRNA stability and transcription |
| abstract |
Sprouty (Spry) proteins are well-known negative regulators of receptor tyrosine kinase-mediated signalling. Their expression is controlled by mitogens, implying a negative feedback loop. Correspondingly, the different members of the family fulfil important roles during organogenesis by adjustment of growth factor-induced processes. In addition, Spry4, one member of this protein family, has been shown to regulate angiogenesis by inhibiting vascular endothelial cell growth factor-induced extracellular signalling-regulated kinase (ERK) activation. Because oxygen is an important regulator of angiogenesis, we investigated Spry4 expression patterns under hypoxic conditions. Our data demonstrate that both hypoxia and desferrioxamine (DFO) treatment increased Spry4 expression. Following iron depletion, elevated Spry4 levels were detected in several cell types independent of tissue origin, presence of mitogens, cell differentiation and malignancy. Evaluation of the underlying regulative mechanisms revealed that augmented transcription and increased mRNA stability enhance mRNA levels of Spry4 in response to DFO. This study unveils a growth factor-independent regulation mechanism of Spry4 expression. Because increased Spry4 levels are accompanied by disappearing ERK phosphorylation, Spry4 might be involved in the timely restriction of MAPK signals under hypoxic conditions, similar to its role in mitogen-regulated processes. However, the functional significance of the observed upregulation of Spry4 during iron depletion remains to be clarified. ©2010 by Walter de Gruyter Berlin New York |
| abstractGer |
Sprouty (Spry) proteins are well-known negative regulators of receptor tyrosine kinase-mediated signalling. Their expression is controlled by mitogens, implying a negative feedback loop. Correspondingly, the different members of the family fulfil important roles during organogenesis by adjustment of growth factor-induced processes. In addition, Spry4, one member of this protein family, has been shown to regulate angiogenesis by inhibiting vascular endothelial cell growth factor-induced extracellular signalling-regulated kinase (ERK) activation. Because oxygen is an important regulator of angiogenesis, we investigated Spry4 expression patterns under hypoxic conditions. Our data demonstrate that both hypoxia and desferrioxamine (DFO) treatment increased Spry4 expression. Following iron depletion, elevated Spry4 levels were detected in several cell types independent of tissue origin, presence of mitogens, cell differentiation and malignancy. Evaluation of the underlying regulative mechanisms revealed that augmented transcription and increased mRNA stability enhance mRNA levels of Spry4 in response to DFO. This study unveils a growth factor-independent regulation mechanism of Spry4 expression. Because increased Spry4 levels are accompanied by disappearing ERK phosphorylation, Spry4 might be involved in the timely restriction of MAPK signals under hypoxic conditions, similar to its role in mitogen-regulated processes. However, the functional significance of the observed upregulation of Spry4 during iron depletion remains to be clarified. ©2010 by Walter de Gruyter Berlin New York |
| abstract_unstemmed |
Sprouty (Spry) proteins are well-known negative regulators of receptor tyrosine kinase-mediated signalling. Their expression is controlled by mitogens, implying a negative feedback loop. Correspondingly, the different members of the family fulfil important roles during organogenesis by adjustment of growth factor-induced processes. In addition, Spry4, one member of this protein family, has been shown to regulate angiogenesis by inhibiting vascular endothelial cell growth factor-induced extracellular signalling-regulated kinase (ERK) activation. Because oxygen is an important regulator of angiogenesis, we investigated Spry4 expression patterns under hypoxic conditions. Our data demonstrate that both hypoxia and desferrioxamine (DFO) treatment increased Spry4 expression. Following iron depletion, elevated Spry4 levels were detected in several cell types independent of tissue origin, presence of mitogens, cell differentiation and malignancy. Evaluation of the underlying regulative mechanisms revealed that augmented transcription and increased mRNA stability enhance mRNA levels of Spry4 in response to DFO. This study unveils a growth factor-independent regulation mechanism of Spry4 expression. Because increased Spry4 levels are accompanied by disappearing ERK phosphorylation, Spry4 might be involved in the timely restriction of MAPK signals under hypoxic conditions, similar to its role in mitogen-regulated processes. However, the functional significance of the observed upregulation of Spry4 during iron depletion remains to be clarified. ©2010 by Walter de Gruyter Berlin New York |
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Sprouty4 levels are increased under hypoxic conditions by enhanced mRNA stability and transcription |
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https://doi.org/10.1515/bc.2010.082 |
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Haigl, Barbara Mayer, Christoph-Erik Siegwart, Gerald Sutterlüty, Hedwig |
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