Pleiotrophin expression and role in physiological angiogenesis in vivo: potential involvement of nucleolin
Background Pleiotrophin (PTN) is a heparin-binding growth factor with significant role(s) in tumour growth and angiogenesis. Although implication of endogenous PTN has been studied in several in vivo models of tumour angiogenesis, its role in physiological angiogenesis has not been addressed. In the...
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| Autor*in: |
Koutsioumpa, Marina [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2012 |
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| Anmerkung: |
© Koutsioumpa et al; licensee BioMed Central Ltd. 2012. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( |
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| Übergeordnetes Werk: |
Enthalten in: Journal of angiogenesis research - London : BioMed Central, 2009, 4(2012), 1 vom: 16. März |
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| Übergeordnetes Werk: |
volume:4 ; year:2012 ; number:1 ; day:16 ; month:03 |
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| DOI / URN: |
10.1186/2045-824X-4-4 |
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SPR030901421 |
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| 245 | 1 | 0 | |a Pleiotrophin expression and role in physiological angiogenesis in vivo: potential involvement of nucleolin |
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| 520 | |a Background Pleiotrophin (PTN) is a heparin-binding growth factor with significant role(s) in tumour growth and angiogenesis. Although implication of endogenous PTN has been studied in several in vivo models of tumour angiogenesis, its role in physiological angiogenesis has not been addressed. In the present work, we studied expression and functional significance of endogenous PTN during angiogenesis in the chicken embryo chorioallantoic membrane (CAM). Methods Using molecular, cellular and biochemical assays, we studied the expression pattern of PTN in CAM and human endothelial cells and its possible interaction with nucleolin (NCL). CAM cells were transfected with a pCDNA3.1 vector, empty (PC) or containing full length cDNA for PTN in antisense orientation (AS-PTN). Angiogenesis was estimated by measuring total vessel length. In vitro, human endothelial cells migration was studied by using a transwell assay, and down-regulation of NCL was performed by using a proper siRNA. Results Endogenous PTN mRNA and protein levels, as well as protein levels of its receptor protein tyrosine phosphatase beta/zeta (RPTPβ/ζ) were maximal at early stages, when CAM angiogenesis is active. Application of AS-PTN onto CAM at days of active angiogenesis was not toxic to the tissue and led to dose-dependent decreased expression of endogenous PTN, ERK1/2 activity and angiogenesis. Interestingly, endogenous PTN was also immunolocalized at the endothelial cell nucleus, possibly through interaction with NCL, a protein that has a significant role in the nuclear translocation of many proteins. Down-regulation of NCL by siRNA in human endothelial cells significantly decreased nuclear PTN, verifying this hypothesis. Moreover, it led to abolishment of PTN-induced endothelial cell migration, suggesting, for the first time, that PTN-NCL interaction has a functional significance. Conclusions Expression of endogenous PTN correlates with and seems to be involved in angiogenesis of the chicken embryo CAM. Our data suggest that NCL may have a role, increasing the number of growth factors whose angiogenic/tumorigenic activities are mediated by NCL. | ||
| 650 | 4 | |a angiogenesis |7 (dpeaa)DE-He213 | |
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| 650 | 4 | |a migration |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a nucleolin |7 (dpeaa)DE-He213 | |
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| 700 | 1 | |a Drosou, Georgia |4 aut | |
| 700 | 1 | |a Mikelis, Constantinos |4 aut | |
| 700 | 1 | |a Theochari, Katerina |4 aut | |
| 700 | 1 | |a Vourtsis, Dionussios |4 aut | |
| 700 | 1 | |a Katsoris, Panagiotis |4 aut | |
| 700 | 1 | |a Giannopoulou, Efstathia |4 aut | |
| 700 | 1 | |a Courty, Jose |4 aut | |
| 700 | 1 | |a Petrou, Christos |4 aut | |
| 700 | 1 | |a Magafa, Vassiliki |4 aut | |
| 700 | 1 | |a Cordopatis, Paul |4 aut | |
| 700 | 1 | |a Papadimitriou, Evangelia |4 aut | |
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10.1186/2045-824X-4-4 doi (DE-627)SPR030901421 (SPR)2045-824X-4-4-e DE-627 ger DE-627 rakwb eng Koutsioumpa, Marina verfasserin aut Pleiotrophin expression and role in physiological angiogenesis in vivo: potential involvement of nucleolin 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Koutsioumpa et al; licensee BioMed Central Ltd. 2012. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background Pleiotrophin (PTN) is a heparin-binding growth factor with significant role(s) in tumour growth and angiogenesis. Although implication of endogenous PTN has been studied in several in vivo models of tumour angiogenesis, its role in physiological angiogenesis has not been addressed. In the present work, we studied expression and functional significance of endogenous PTN during angiogenesis in the chicken embryo chorioallantoic membrane (CAM). Methods Using molecular, cellular and biochemical assays, we studied the expression pattern of PTN in CAM and human endothelial cells and its possible interaction with nucleolin (NCL). CAM cells were transfected with a pCDNA3.1 vector, empty (PC) or containing full length cDNA for PTN in antisense orientation (AS-PTN). Angiogenesis was estimated by measuring total vessel length. In vitro, human endothelial cells migration was studied by using a transwell assay, and down-regulation of NCL was performed by using a proper siRNA. Results Endogenous PTN mRNA and protein levels, as well as protein levels of its receptor protein tyrosine phosphatase beta/zeta (RPTPβ/ζ) were maximal at early stages, when CAM angiogenesis is active. Application of AS-PTN onto CAM at days of active angiogenesis was not toxic to the tissue and led to dose-dependent decreased expression of endogenous PTN, ERK1/2 activity and angiogenesis. Interestingly, endogenous PTN was also immunolocalized at the endothelial cell nucleus, possibly through interaction with NCL, a protein that has a significant role in the nuclear translocation of many proteins. Down-regulation of NCL by siRNA in human endothelial cells significantly decreased nuclear PTN, verifying this hypothesis. Moreover, it led to abolishment of PTN-induced endothelial cell migration, suggesting, for the first time, that PTN-NCL interaction has a functional significance. Conclusions Expression of endogenous PTN correlates with and seems to be involved in angiogenesis of the chicken embryo CAM. Our data suggest that NCL may have a role, increasing the number of growth factors whose angiogenic/tumorigenic activities are mediated by NCL. angiogenesis (dpeaa)DE-He213 endothelial cells (dpeaa)DE-He213 migration (dpeaa)DE-He213 nucleolin (dpeaa)DE-He213 pleiotrophin (dpeaa)DE-He213 receptor protein tyrosine phosphatase (dpeaa)DE-He213 Drosou, Georgia aut Mikelis, Constantinos aut Theochari, Katerina aut Vourtsis, Dionussios aut Katsoris, Panagiotis aut Giannopoulou, Efstathia aut Courty, Jose aut Petrou, Christos aut Magafa, Vassiliki aut Cordopatis, Paul aut Papadimitriou, Evangelia aut Enthalten in Journal of angiogenesis research London : BioMed Central, 2009 4(2012), 1 vom: 16. März (DE-627)609775553 (DE-600)2516062-X 2040-2384 nnns volume:4 year:2012 number:1 day:16 month:03 https://dx.doi.org/10.1186/2045-824X-4-4 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA AR 4 2012 1 16 03 |
| spelling |
10.1186/2045-824X-4-4 doi (DE-627)SPR030901421 (SPR)2045-824X-4-4-e DE-627 ger DE-627 rakwb eng Koutsioumpa, Marina verfasserin aut Pleiotrophin expression and role in physiological angiogenesis in vivo: potential involvement of nucleolin 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Koutsioumpa et al; licensee BioMed Central Ltd. 2012. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background Pleiotrophin (PTN) is a heparin-binding growth factor with significant role(s) in tumour growth and angiogenesis. Although implication of endogenous PTN has been studied in several in vivo models of tumour angiogenesis, its role in physiological angiogenesis has not been addressed. In the present work, we studied expression and functional significance of endogenous PTN during angiogenesis in the chicken embryo chorioallantoic membrane (CAM). Methods Using molecular, cellular and biochemical assays, we studied the expression pattern of PTN in CAM and human endothelial cells and its possible interaction with nucleolin (NCL). CAM cells were transfected with a pCDNA3.1 vector, empty (PC) or containing full length cDNA for PTN in antisense orientation (AS-PTN). Angiogenesis was estimated by measuring total vessel length. In vitro, human endothelial cells migration was studied by using a transwell assay, and down-regulation of NCL was performed by using a proper siRNA. Results Endogenous PTN mRNA and protein levels, as well as protein levels of its receptor protein tyrosine phosphatase beta/zeta (RPTPβ/ζ) were maximal at early stages, when CAM angiogenesis is active. Application of AS-PTN onto CAM at days of active angiogenesis was not toxic to the tissue and led to dose-dependent decreased expression of endogenous PTN, ERK1/2 activity and angiogenesis. Interestingly, endogenous PTN was also immunolocalized at the endothelial cell nucleus, possibly through interaction with NCL, a protein that has a significant role in the nuclear translocation of many proteins. Down-regulation of NCL by siRNA in human endothelial cells significantly decreased nuclear PTN, verifying this hypothesis. Moreover, it led to abolishment of PTN-induced endothelial cell migration, suggesting, for the first time, that PTN-NCL interaction has a functional significance. Conclusions Expression of endogenous PTN correlates with and seems to be involved in angiogenesis of the chicken embryo CAM. Our data suggest that NCL may have a role, increasing the number of growth factors whose angiogenic/tumorigenic activities are mediated by NCL. angiogenesis (dpeaa)DE-He213 endothelial cells (dpeaa)DE-He213 migration (dpeaa)DE-He213 nucleolin (dpeaa)DE-He213 pleiotrophin (dpeaa)DE-He213 receptor protein tyrosine phosphatase (dpeaa)DE-He213 Drosou, Georgia aut Mikelis, Constantinos aut Theochari, Katerina aut Vourtsis, Dionussios aut Katsoris, Panagiotis aut Giannopoulou, Efstathia aut Courty, Jose aut Petrou, Christos aut Magafa, Vassiliki aut Cordopatis, Paul aut Papadimitriou, Evangelia aut Enthalten in Journal of angiogenesis research London : BioMed Central, 2009 4(2012), 1 vom: 16. März (DE-627)609775553 (DE-600)2516062-X 2040-2384 nnns volume:4 year:2012 number:1 day:16 month:03 https://dx.doi.org/10.1186/2045-824X-4-4 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA AR 4 2012 1 16 03 |
| allfields_unstemmed |
10.1186/2045-824X-4-4 doi (DE-627)SPR030901421 (SPR)2045-824X-4-4-e DE-627 ger DE-627 rakwb eng Koutsioumpa, Marina verfasserin aut Pleiotrophin expression and role in physiological angiogenesis in vivo: potential involvement of nucleolin 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Koutsioumpa et al; licensee BioMed Central Ltd. 2012. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background Pleiotrophin (PTN) is a heparin-binding growth factor with significant role(s) in tumour growth and angiogenesis. Although implication of endogenous PTN has been studied in several in vivo models of tumour angiogenesis, its role in physiological angiogenesis has not been addressed. In the present work, we studied expression and functional significance of endogenous PTN during angiogenesis in the chicken embryo chorioallantoic membrane (CAM). Methods Using molecular, cellular and biochemical assays, we studied the expression pattern of PTN in CAM and human endothelial cells and its possible interaction with nucleolin (NCL). CAM cells were transfected with a pCDNA3.1 vector, empty (PC) or containing full length cDNA for PTN in antisense orientation (AS-PTN). Angiogenesis was estimated by measuring total vessel length. In vitro, human endothelial cells migration was studied by using a transwell assay, and down-regulation of NCL was performed by using a proper siRNA. Results Endogenous PTN mRNA and protein levels, as well as protein levels of its receptor protein tyrosine phosphatase beta/zeta (RPTPβ/ζ) were maximal at early stages, when CAM angiogenesis is active. Application of AS-PTN onto CAM at days of active angiogenesis was not toxic to the tissue and led to dose-dependent decreased expression of endogenous PTN, ERK1/2 activity and angiogenesis. Interestingly, endogenous PTN was also immunolocalized at the endothelial cell nucleus, possibly through interaction with NCL, a protein that has a significant role in the nuclear translocation of many proteins. Down-regulation of NCL by siRNA in human endothelial cells significantly decreased nuclear PTN, verifying this hypothesis. Moreover, it led to abolishment of PTN-induced endothelial cell migration, suggesting, for the first time, that PTN-NCL interaction has a functional significance. Conclusions Expression of endogenous PTN correlates with and seems to be involved in angiogenesis of the chicken embryo CAM. Our data suggest that NCL may have a role, increasing the number of growth factors whose angiogenic/tumorigenic activities are mediated by NCL. angiogenesis (dpeaa)DE-He213 endothelial cells (dpeaa)DE-He213 migration (dpeaa)DE-He213 nucleolin (dpeaa)DE-He213 pleiotrophin (dpeaa)DE-He213 receptor protein tyrosine phosphatase (dpeaa)DE-He213 Drosou, Georgia aut Mikelis, Constantinos aut Theochari, Katerina aut Vourtsis, Dionussios aut Katsoris, Panagiotis aut Giannopoulou, Efstathia aut Courty, Jose aut Petrou, Christos aut Magafa, Vassiliki aut Cordopatis, Paul aut Papadimitriou, Evangelia aut Enthalten in Journal of angiogenesis research London : BioMed Central, 2009 4(2012), 1 vom: 16. März (DE-627)609775553 (DE-600)2516062-X 2040-2384 nnns volume:4 year:2012 number:1 day:16 month:03 https://dx.doi.org/10.1186/2045-824X-4-4 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA AR 4 2012 1 16 03 |
| allfieldsGer |
10.1186/2045-824X-4-4 doi (DE-627)SPR030901421 (SPR)2045-824X-4-4-e DE-627 ger DE-627 rakwb eng Koutsioumpa, Marina verfasserin aut Pleiotrophin expression and role in physiological angiogenesis in vivo: potential involvement of nucleolin 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Koutsioumpa et al; licensee BioMed Central Ltd. 2012. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background Pleiotrophin (PTN) is a heparin-binding growth factor with significant role(s) in tumour growth and angiogenesis. Although implication of endogenous PTN has been studied in several in vivo models of tumour angiogenesis, its role in physiological angiogenesis has not been addressed. In the present work, we studied expression and functional significance of endogenous PTN during angiogenesis in the chicken embryo chorioallantoic membrane (CAM). Methods Using molecular, cellular and biochemical assays, we studied the expression pattern of PTN in CAM and human endothelial cells and its possible interaction with nucleolin (NCL). CAM cells were transfected with a pCDNA3.1 vector, empty (PC) or containing full length cDNA for PTN in antisense orientation (AS-PTN). Angiogenesis was estimated by measuring total vessel length. In vitro, human endothelial cells migration was studied by using a transwell assay, and down-regulation of NCL was performed by using a proper siRNA. Results Endogenous PTN mRNA and protein levels, as well as protein levels of its receptor protein tyrosine phosphatase beta/zeta (RPTPβ/ζ) were maximal at early stages, when CAM angiogenesis is active. Application of AS-PTN onto CAM at days of active angiogenesis was not toxic to the tissue and led to dose-dependent decreased expression of endogenous PTN, ERK1/2 activity and angiogenesis. Interestingly, endogenous PTN was also immunolocalized at the endothelial cell nucleus, possibly through interaction with NCL, a protein that has a significant role in the nuclear translocation of many proteins. Down-regulation of NCL by siRNA in human endothelial cells significantly decreased nuclear PTN, verifying this hypothesis. Moreover, it led to abolishment of PTN-induced endothelial cell migration, suggesting, for the first time, that PTN-NCL interaction has a functional significance. Conclusions Expression of endogenous PTN correlates with and seems to be involved in angiogenesis of the chicken embryo CAM. Our data suggest that NCL may have a role, increasing the number of growth factors whose angiogenic/tumorigenic activities are mediated by NCL. angiogenesis (dpeaa)DE-He213 endothelial cells (dpeaa)DE-He213 migration (dpeaa)DE-He213 nucleolin (dpeaa)DE-He213 pleiotrophin (dpeaa)DE-He213 receptor protein tyrosine phosphatase (dpeaa)DE-He213 Drosou, Georgia aut Mikelis, Constantinos aut Theochari, Katerina aut Vourtsis, Dionussios aut Katsoris, Panagiotis aut Giannopoulou, Efstathia aut Courty, Jose aut Petrou, Christos aut Magafa, Vassiliki aut Cordopatis, Paul aut Papadimitriou, Evangelia aut Enthalten in Journal of angiogenesis research London : BioMed Central, 2009 4(2012), 1 vom: 16. März (DE-627)609775553 (DE-600)2516062-X 2040-2384 nnns volume:4 year:2012 number:1 day:16 month:03 https://dx.doi.org/10.1186/2045-824X-4-4 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA AR 4 2012 1 16 03 |
| allfieldsSound |
10.1186/2045-824X-4-4 doi (DE-627)SPR030901421 (SPR)2045-824X-4-4-e DE-627 ger DE-627 rakwb eng Koutsioumpa, Marina verfasserin aut Pleiotrophin expression and role in physiological angiogenesis in vivo: potential involvement of nucleolin 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Koutsioumpa et al; licensee BioMed Central Ltd. 2012. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background Pleiotrophin (PTN) is a heparin-binding growth factor with significant role(s) in tumour growth and angiogenesis. Although implication of endogenous PTN has been studied in several in vivo models of tumour angiogenesis, its role in physiological angiogenesis has not been addressed. In the present work, we studied expression and functional significance of endogenous PTN during angiogenesis in the chicken embryo chorioallantoic membrane (CAM). Methods Using molecular, cellular and biochemical assays, we studied the expression pattern of PTN in CAM and human endothelial cells and its possible interaction with nucleolin (NCL). CAM cells were transfected with a pCDNA3.1 vector, empty (PC) or containing full length cDNA for PTN in antisense orientation (AS-PTN). Angiogenesis was estimated by measuring total vessel length. In vitro, human endothelial cells migration was studied by using a transwell assay, and down-regulation of NCL was performed by using a proper siRNA. Results Endogenous PTN mRNA and protein levels, as well as protein levels of its receptor protein tyrosine phosphatase beta/zeta (RPTPβ/ζ) were maximal at early stages, when CAM angiogenesis is active. Application of AS-PTN onto CAM at days of active angiogenesis was not toxic to the tissue and led to dose-dependent decreased expression of endogenous PTN, ERK1/2 activity and angiogenesis. Interestingly, endogenous PTN was also immunolocalized at the endothelial cell nucleus, possibly through interaction with NCL, a protein that has a significant role in the nuclear translocation of many proteins. Down-regulation of NCL by siRNA in human endothelial cells significantly decreased nuclear PTN, verifying this hypothesis. Moreover, it led to abolishment of PTN-induced endothelial cell migration, suggesting, for the first time, that PTN-NCL interaction has a functional significance. Conclusions Expression of endogenous PTN correlates with and seems to be involved in angiogenesis of the chicken embryo CAM. Our data suggest that NCL may have a role, increasing the number of growth factors whose angiogenic/tumorigenic activities are mediated by NCL. angiogenesis (dpeaa)DE-He213 endothelial cells (dpeaa)DE-He213 migration (dpeaa)DE-He213 nucleolin (dpeaa)DE-He213 pleiotrophin (dpeaa)DE-He213 receptor protein tyrosine phosphatase (dpeaa)DE-He213 Drosou, Georgia aut Mikelis, Constantinos aut Theochari, Katerina aut Vourtsis, Dionussios aut Katsoris, Panagiotis aut Giannopoulou, Efstathia aut Courty, Jose aut Petrou, Christos aut Magafa, Vassiliki aut Cordopatis, Paul aut Papadimitriou, Evangelia aut Enthalten in Journal of angiogenesis research London : BioMed Central, 2009 4(2012), 1 vom: 16. März (DE-627)609775553 (DE-600)2516062-X 2040-2384 nnns volume:4 year:2012 number:1 day:16 month:03 https://dx.doi.org/10.1186/2045-824X-4-4 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA AR 4 2012 1 16 03 |
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Koutsioumpa, Marina @@aut@@ Drosou, Georgia @@aut@@ Mikelis, Constantinos @@aut@@ Theochari, Katerina @@aut@@ Vourtsis, Dionussios @@aut@@ Katsoris, Panagiotis @@aut@@ Giannopoulou, Efstathia @@aut@@ Courty, Jose @@aut@@ Petrou, Christos @@aut@@ Magafa, Vassiliki @@aut@@ Cordopatis, Paul @@aut@@ Papadimitriou, Evangelia @@aut@@ |
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This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Background Pleiotrophin (PTN) is a heparin-binding growth factor with significant role(s) in tumour growth and angiogenesis. Although implication of endogenous PTN has been studied in several in vivo models of tumour angiogenesis, its role in physiological angiogenesis has not been addressed. In the present work, we studied expression and functional significance of endogenous PTN during angiogenesis in the chicken embryo chorioallantoic membrane (CAM). Methods Using molecular, cellular and biochemical assays, we studied the expression pattern of PTN in CAM and human endothelial cells and its possible interaction with nucleolin (NCL). CAM cells were transfected with a pCDNA3.1 vector, empty (PC) or containing full length cDNA for PTN in antisense orientation (AS-PTN). Angiogenesis was estimated by measuring total vessel length. In vitro, human endothelial cells migration was studied by using a transwell assay, and down-regulation of NCL was performed by using a proper siRNA. Results Endogenous PTN mRNA and protein levels, as well as protein levels of its receptor protein tyrosine phosphatase beta/zeta (RPTPβ/ζ) were maximal at early stages, when CAM angiogenesis is active. Application of AS-PTN onto CAM at days of active angiogenesis was not toxic to the tissue and led to dose-dependent decreased expression of endogenous PTN, ERK1/2 activity and angiogenesis. Interestingly, endogenous PTN was also immunolocalized at the endothelial cell nucleus, possibly through interaction with NCL, a protein that has a significant role in the nuclear translocation of many proteins. Down-regulation of NCL by siRNA in human endothelial cells significantly decreased nuclear PTN, verifying this hypothesis. Moreover, it led to abolishment of PTN-induced endothelial cell migration, suggesting, for the first time, that PTN-NCL interaction has a functional significance. Conclusions Expression of endogenous PTN correlates with and seems to be involved in angiogenesis of the chicken embryo CAM. 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Koutsioumpa, Marina |
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Pleiotrophin expression and role in physiological angiogenesis in vivo: potential involvement of nucleolin angiogenesis (dpeaa)DE-He213 endothelial cells (dpeaa)DE-He213 migration (dpeaa)DE-He213 nucleolin (dpeaa)DE-He213 pleiotrophin (dpeaa)DE-He213 receptor protein tyrosine phosphatase (dpeaa)DE-He213 |
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Koutsioumpa, Marina Drosou, Georgia Mikelis, Constantinos Theochari, Katerina Vourtsis, Dionussios Katsoris, Panagiotis Giannopoulou, Efstathia Courty, Jose Petrou, Christos Magafa, Vassiliki Cordopatis, Paul Papadimitriou, Evangelia |
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pleiotrophin expression and role in physiological angiogenesis in vivo: potential involvement of nucleolin |
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Pleiotrophin expression and role in physiological angiogenesis in vivo: potential involvement of nucleolin |
| abstract |
Background Pleiotrophin (PTN) is a heparin-binding growth factor with significant role(s) in tumour growth and angiogenesis. Although implication of endogenous PTN has been studied in several in vivo models of tumour angiogenesis, its role in physiological angiogenesis has not been addressed. In the present work, we studied expression and functional significance of endogenous PTN during angiogenesis in the chicken embryo chorioallantoic membrane (CAM). Methods Using molecular, cellular and biochemical assays, we studied the expression pattern of PTN in CAM and human endothelial cells and its possible interaction with nucleolin (NCL). CAM cells were transfected with a pCDNA3.1 vector, empty (PC) or containing full length cDNA for PTN in antisense orientation (AS-PTN). Angiogenesis was estimated by measuring total vessel length. In vitro, human endothelial cells migration was studied by using a transwell assay, and down-regulation of NCL was performed by using a proper siRNA. Results Endogenous PTN mRNA and protein levels, as well as protein levels of its receptor protein tyrosine phosphatase beta/zeta (RPTPβ/ζ) were maximal at early stages, when CAM angiogenesis is active. Application of AS-PTN onto CAM at days of active angiogenesis was not toxic to the tissue and led to dose-dependent decreased expression of endogenous PTN, ERK1/2 activity and angiogenesis. Interestingly, endogenous PTN was also immunolocalized at the endothelial cell nucleus, possibly through interaction with NCL, a protein that has a significant role in the nuclear translocation of many proteins. Down-regulation of NCL by siRNA in human endothelial cells significantly decreased nuclear PTN, verifying this hypothesis. Moreover, it led to abolishment of PTN-induced endothelial cell migration, suggesting, for the first time, that PTN-NCL interaction has a functional significance. Conclusions Expression of endogenous PTN correlates with and seems to be involved in angiogenesis of the chicken embryo CAM. Our data suggest that NCL may have a role, increasing the number of growth factors whose angiogenic/tumorigenic activities are mediated by NCL. © Koutsioumpa et al; licensee BioMed Central Ltd. 2012. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( |
| abstractGer |
Background Pleiotrophin (PTN) is a heparin-binding growth factor with significant role(s) in tumour growth and angiogenesis. Although implication of endogenous PTN has been studied in several in vivo models of tumour angiogenesis, its role in physiological angiogenesis has not been addressed. In the present work, we studied expression and functional significance of endogenous PTN during angiogenesis in the chicken embryo chorioallantoic membrane (CAM). Methods Using molecular, cellular and biochemical assays, we studied the expression pattern of PTN in CAM and human endothelial cells and its possible interaction with nucleolin (NCL). CAM cells were transfected with a pCDNA3.1 vector, empty (PC) or containing full length cDNA for PTN in antisense orientation (AS-PTN). Angiogenesis was estimated by measuring total vessel length. In vitro, human endothelial cells migration was studied by using a transwell assay, and down-regulation of NCL was performed by using a proper siRNA. Results Endogenous PTN mRNA and protein levels, as well as protein levels of its receptor protein tyrosine phosphatase beta/zeta (RPTPβ/ζ) were maximal at early stages, when CAM angiogenesis is active. Application of AS-PTN onto CAM at days of active angiogenesis was not toxic to the tissue and led to dose-dependent decreased expression of endogenous PTN, ERK1/2 activity and angiogenesis. Interestingly, endogenous PTN was also immunolocalized at the endothelial cell nucleus, possibly through interaction with NCL, a protein that has a significant role in the nuclear translocation of many proteins. Down-regulation of NCL by siRNA in human endothelial cells significantly decreased nuclear PTN, verifying this hypothesis. Moreover, it led to abolishment of PTN-induced endothelial cell migration, suggesting, for the first time, that PTN-NCL interaction has a functional significance. Conclusions Expression of endogenous PTN correlates with and seems to be involved in angiogenesis of the chicken embryo CAM. Our data suggest that NCL may have a role, increasing the number of growth factors whose angiogenic/tumorigenic activities are mediated by NCL. © Koutsioumpa et al; licensee BioMed Central Ltd. 2012. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( |
| abstract_unstemmed |
Background Pleiotrophin (PTN) is a heparin-binding growth factor with significant role(s) in tumour growth and angiogenesis. Although implication of endogenous PTN has been studied in several in vivo models of tumour angiogenesis, its role in physiological angiogenesis has not been addressed. In the present work, we studied expression and functional significance of endogenous PTN during angiogenesis in the chicken embryo chorioallantoic membrane (CAM). Methods Using molecular, cellular and biochemical assays, we studied the expression pattern of PTN in CAM and human endothelial cells and its possible interaction with nucleolin (NCL). CAM cells were transfected with a pCDNA3.1 vector, empty (PC) or containing full length cDNA for PTN in antisense orientation (AS-PTN). Angiogenesis was estimated by measuring total vessel length. In vitro, human endothelial cells migration was studied by using a transwell assay, and down-regulation of NCL was performed by using a proper siRNA. Results Endogenous PTN mRNA and protein levels, as well as protein levels of its receptor protein tyrosine phosphatase beta/zeta (RPTPβ/ζ) were maximal at early stages, when CAM angiogenesis is active. Application of AS-PTN onto CAM at days of active angiogenesis was not toxic to the tissue and led to dose-dependent decreased expression of endogenous PTN, ERK1/2 activity and angiogenesis. Interestingly, endogenous PTN was also immunolocalized at the endothelial cell nucleus, possibly through interaction with NCL, a protein that has a significant role in the nuclear translocation of many proteins. Down-regulation of NCL by siRNA in human endothelial cells significantly decreased nuclear PTN, verifying this hypothesis. Moreover, it led to abolishment of PTN-induced endothelial cell migration, suggesting, for the first time, that PTN-NCL interaction has a functional significance. Conclusions Expression of endogenous PTN correlates with and seems to be involved in angiogenesis of the chicken embryo CAM. Our data suggest that NCL may have a role, increasing the number of growth factors whose angiogenic/tumorigenic activities are mediated by NCL. © Koutsioumpa et al; licensee BioMed Central Ltd. 2012. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( |
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