The guanylate binding protein‐1 GTPase controls the invasive and angiogenic capability of endothelial cells through inhibition of MMP‐1 expression
Abstract Expression of the large GTPase guanylate binding protein‐1 (GBP‐1) is induced by inflammatory cytokines (ICs) in endothelial cells (ECs), and the helical domain of the molecule mediates the repression of EC proliferation by ICs. Here we show that the expression of GBP‐1 and of the matrix me...
Ausführliche Beschreibung
Autor*in: |
Guenzi, Eric [verfasserIn] Töpolt, Kristin [verfasserIn] Lubeseder‐Martellato, Clara [verfasserIn] Jörg, Anita [verfasserIn] Naschberger, Elisabeth [verfasserIn] Benelli, Roberto [verfasserIn] Albini, Adriana [verfasserIn] Stürzl, Michael [verfasserIn] |
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E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2003 |
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Schlagwörter: |
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Anmerkung: |
© European Molecular Biology Organization 2003 |
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Übergeordnetes Werk: |
Enthalten in: The EMBO Journal - Nature Publishing Group UK, 2023, 22(2003), 15 vom: 01. Aug., Seite 3772-3782 |
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Übergeordnetes Werk: |
volume:22 ; year:2003 ; number:15 ; day:01 ; month:08 ; pages:3772-3782 |
Links: |
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DOI / URN: |
10.1093/emboj/cdg382 |
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Katalog-ID: |
SPR057948305 |
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100 | 1 | |a Guenzi, Eric |e verfasserin |4 aut | |
245 | 1 | 0 | |a The guanylate binding protein‐1 GTPase controls the invasive and angiogenic capability of endothelial cells through inhibition of MMP‐1 expression |
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520 | |a Abstract Expression of the large GTPase guanylate binding protein‐1 (GBP‐1) is induced by inflammatory cytokines (ICs) in endothelial cells (ECs), and the helical domain of the molecule mediates the repression of EC proliferation by ICs. Here we show that the expression of GBP‐1 and of the matrix metalloproteinase‐1 (MMP‐1) are inversely related in vitro and in vivo, and that GBP‐1 selectively inhibits the expression of MMP‐1 in ECs, but not the expression of other proteases. The GTPase activity of GBP‐1 was necessary for this effect, which inhibited invasiveness and tube‐forming capability of ECs in three‐dimensional collagen‐I matrices. A GTPase‐deficient mutant (D184N‐GBP‐1) operated as a transdominant inhibitor of wild‐type GBP‐1 and rescued MMP‐1 expression in the presence of ICs. Expression of D184N‐GBP‐1, as well as paracrine supplementation of MMP‐1, restored the tube‐forming capability of ECs in the presence of wild‐type GBP‐1. The latter finding indicated that the inhibition of capillary formation is specifically due to the repression of MMP‐1 expression by GBP‐1, and is not affected by the anti‐proliferative activity of the helical domain of GBP‐1. These findings substantiate the role of GBP‐1 as a major regulator of the anti‐angiogenic response of ECs to ICs. | ||
650 | 4 | |a angiogenesis |7 (dpeaa)DE-He213 | |
650 | 4 | |a collagenase |7 (dpeaa)DE-He213 | |
650 | 4 | |a inflammation |7 (dpeaa)DE-He213 | |
650 | 4 | |a invasion |7 (dpeaa)DE-He213 | |
650 | 4 | |a MMP |7 (dpeaa)DE-He213 | |
700 | 1 | |a Töpolt, Kristin |e verfasserin |4 aut | |
700 | 1 | |a Lubeseder‐Martellato, Clara |e verfasserin |4 aut | |
700 | 1 | |a Jörg, Anita |e verfasserin |4 aut | |
700 | 1 | |a Naschberger, Elisabeth |e verfasserin |4 aut | |
700 | 1 | |a Benelli, Roberto |e verfasserin |4 aut | |
700 | 1 | |a Albini, Adriana |e verfasserin |4 aut | |
700 | 1 | |a Stürzl, Michael |e verfasserin |4 aut | |
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773 | 1 | 8 | |g volume:22 |g year:2003 |g number:15 |g day:01 |g month:08 |g pages:3772-3782 |
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10.1093/emboj/cdg382 doi (DE-627)SPR057948305 (SPR)cdg382-e DE-627 ger DE-627 rakwb eng Guenzi, Eric verfasserin aut The guanylate binding protein‐1 GTPase controls the invasive and angiogenic capability of endothelial cells through inhibition of MMP‐1 expression 2003 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2003 Abstract Expression of the large GTPase guanylate binding protein‐1 (GBP‐1) is induced by inflammatory cytokines (ICs) in endothelial cells (ECs), and the helical domain of the molecule mediates the repression of EC proliferation by ICs. Here we show that the expression of GBP‐1 and of the matrix metalloproteinase‐1 (MMP‐1) are inversely related in vitro and in vivo, and that GBP‐1 selectively inhibits the expression of MMP‐1 in ECs, but not the expression of other proteases. The GTPase activity of GBP‐1 was necessary for this effect, which inhibited invasiveness and tube‐forming capability of ECs in three‐dimensional collagen‐I matrices. A GTPase‐deficient mutant (D184N‐GBP‐1) operated as a transdominant inhibitor of wild‐type GBP‐1 and rescued MMP‐1 expression in the presence of ICs. Expression of D184N‐GBP‐1, as well as paracrine supplementation of MMP‐1, restored the tube‐forming capability of ECs in the presence of wild‐type GBP‐1. The latter finding indicated that the inhibition of capillary formation is specifically due to the repression of MMP‐1 expression by GBP‐1, and is not affected by the anti‐proliferative activity of the helical domain of GBP‐1. These findings substantiate the role of GBP‐1 as a major regulator of the anti‐angiogenic response of ECs to ICs. angiogenesis (dpeaa)DE-He213 collagenase (dpeaa)DE-He213 inflammation (dpeaa)DE-He213 invasion (dpeaa)DE-He213 MMP (dpeaa)DE-He213 Töpolt, Kristin verfasserin aut Lubeseder‐Martellato, Clara verfasserin aut Jörg, Anita verfasserin aut Naschberger, Elisabeth verfasserin aut Benelli, Roberto verfasserin aut Albini, Adriana verfasserin aut Stürzl, Michael verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 22(2003), 15 vom: 01. Aug., Seite 3772-3782 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:22 year:2003 number:15 day:01 month:08 pages:3772-3782 https://dx.doi.org/10.1093/emboj/cdg382 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 22 2003 15 01 08 3772-3782 |
spelling |
10.1093/emboj/cdg382 doi (DE-627)SPR057948305 (SPR)cdg382-e DE-627 ger DE-627 rakwb eng Guenzi, Eric verfasserin aut The guanylate binding protein‐1 GTPase controls the invasive and angiogenic capability of endothelial cells through inhibition of MMP‐1 expression 2003 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2003 Abstract Expression of the large GTPase guanylate binding protein‐1 (GBP‐1) is induced by inflammatory cytokines (ICs) in endothelial cells (ECs), and the helical domain of the molecule mediates the repression of EC proliferation by ICs. Here we show that the expression of GBP‐1 and of the matrix metalloproteinase‐1 (MMP‐1) are inversely related in vitro and in vivo, and that GBP‐1 selectively inhibits the expression of MMP‐1 in ECs, but not the expression of other proteases. The GTPase activity of GBP‐1 was necessary for this effect, which inhibited invasiveness and tube‐forming capability of ECs in three‐dimensional collagen‐I matrices. A GTPase‐deficient mutant (D184N‐GBP‐1) operated as a transdominant inhibitor of wild‐type GBP‐1 and rescued MMP‐1 expression in the presence of ICs. Expression of D184N‐GBP‐1, as well as paracrine supplementation of MMP‐1, restored the tube‐forming capability of ECs in the presence of wild‐type GBP‐1. The latter finding indicated that the inhibition of capillary formation is specifically due to the repression of MMP‐1 expression by GBP‐1, and is not affected by the anti‐proliferative activity of the helical domain of GBP‐1. These findings substantiate the role of GBP‐1 as a major regulator of the anti‐angiogenic response of ECs to ICs. angiogenesis (dpeaa)DE-He213 collagenase (dpeaa)DE-He213 inflammation (dpeaa)DE-He213 invasion (dpeaa)DE-He213 MMP (dpeaa)DE-He213 Töpolt, Kristin verfasserin aut Lubeseder‐Martellato, Clara verfasserin aut Jörg, Anita verfasserin aut Naschberger, Elisabeth verfasserin aut Benelli, Roberto verfasserin aut Albini, Adriana verfasserin aut Stürzl, Michael verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 22(2003), 15 vom: 01. Aug., Seite 3772-3782 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:22 year:2003 number:15 day:01 month:08 pages:3772-3782 https://dx.doi.org/10.1093/emboj/cdg382 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 22 2003 15 01 08 3772-3782 |
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10.1093/emboj/cdg382 doi (DE-627)SPR057948305 (SPR)cdg382-e DE-627 ger DE-627 rakwb eng Guenzi, Eric verfasserin aut The guanylate binding protein‐1 GTPase controls the invasive and angiogenic capability of endothelial cells through inhibition of MMP‐1 expression 2003 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2003 Abstract Expression of the large GTPase guanylate binding protein‐1 (GBP‐1) is induced by inflammatory cytokines (ICs) in endothelial cells (ECs), and the helical domain of the molecule mediates the repression of EC proliferation by ICs. Here we show that the expression of GBP‐1 and of the matrix metalloproteinase‐1 (MMP‐1) are inversely related in vitro and in vivo, and that GBP‐1 selectively inhibits the expression of MMP‐1 in ECs, but not the expression of other proteases. The GTPase activity of GBP‐1 was necessary for this effect, which inhibited invasiveness and tube‐forming capability of ECs in three‐dimensional collagen‐I matrices. A GTPase‐deficient mutant (D184N‐GBP‐1) operated as a transdominant inhibitor of wild‐type GBP‐1 and rescued MMP‐1 expression in the presence of ICs. Expression of D184N‐GBP‐1, as well as paracrine supplementation of MMP‐1, restored the tube‐forming capability of ECs in the presence of wild‐type GBP‐1. The latter finding indicated that the inhibition of capillary formation is specifically due to the repression of MMP‐1 expression by GBP‐1, and is not affected by the anti‐proliferative activity of the helical domain of GBP‐1. These findings substantiate the role of GBP‐1 as a major regulator of the anti‐angiogenic response of ECs to ICs. angiogenesis (dpeaa)DE-He213 collagenase (dpeaa)DE-He213 inflammation (dpeaa)DE-He213 invasion (dpeaa)DE-He213 MMP (dpeaa)DE-He213 Töpolt, Kristin verfasserin aut Lubeseder‐Martellato, Clara verfasserin aut Jörg, Anita verfasserin aut Naschberger, Elisabeth verfasserin aut Benelli, Roberto verfasserin aut Albini, Adriana verfasserin aut Stürzl, Michael verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 22(2003), 15 vom: 01. Aug., Seite 3772-3782 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:22 year:2003 number:15 day:01 month:08 pages:3772-3782 https://dx.doi.org/10.1093/emboj/cdg382 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 22 2003 15 01 08 3772-3782 |
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10.1093/emboj/cdg382 doi (DE-627)SPR057948305 (SPR)cdg382-e DE-627 ger DE-627 rakwb eng Guenzi, Eric verfasserin aut The guanylate binding protein‐1 GTPase controls the invasive and angiogenic capability of endothelial cells through inhibition of MMP‐1 expression 2003 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2003 Abstract Expression of the large GTPase guanylate binding protein‐1 (GBP‐1) is induced by inflammatory cytokines (ICs) in endothelial cells (ECs), and the helical domain of the molecule mediates the repression of EC proliferation by ICs. Here we show that the expression of GBP‐1 and of the matrix metalloproteinase‐1 (MMP‐1) are inversely related in vitro and in vivo, and that GBP‐1 selectively inhibits the expression of MMP‐1 in ECs, but not the expression of other proteases. The GTPase activity of GBP‐1 was necessary for this effect, which inhibited invasiveness and tube‐forming capability of ECs in three‐dimensional collagen‐I matrices. A GTPase‐deficient mutant (D184N‐GBP‐1) operated as a transdominant inhibitor of wild‐type GBP‐1 and rescued MMP‐1 expression in the presence of ICs. Expression of D184N‐GBP‐1, as well as paracrine supplementation of MMP‐1, restored the tube‐forming capability of ECs in the presence of wild‐type GBP‐1. The latter finding indicated that the inhibition of capillary formation is specifically due to the repression of MMP‐1 expression by GBP‐1, and is not affected by the anti‐proliferative activity of the helical domain of GBP‐1. These findings substantiate the role of GBP‐1 as a major regulator of the anti‐angiogenic response of ECs to ICs. angiogenesis (dpeaa)DE-He213 collagenase (dpeaa)DE-He213 inflammation (dpeaa)DE-He213 invasion (dpeaa)DE-He213 MMP (dpeaa)DE-He213 Töpolt, Kristin verfasserin aut Lubeseder‐Martellato, Clara verfasserin aut Jörg, Anita verfasserin aut Naschberger, Elisabeth verfasserin aut Benelli, Roberto verfasserin aut Albini, Adriana verfasserin aut Stürzl, Michael verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 22(2003), 15 vom: 01. Aug., Seite 3772-3782 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:22 year:2003 number:15 day:01 month:08 pages:3772-3782 https://dx.doi.org/10.1093/emboj/cdg382 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 22 2003 15 01 08 3772-3782 |
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10.1093/emboj/cdg382 doi (DE-627)SPR057948305 (SPR)cdg382-e DE-627 ger DE-627 rakwb eng Guenzi, Eric verfasserin aut The guanylate binding protein‐1 GTPase controls the invasive and angiogenic capability of endothelial cells through inhibition of MMP‐1 expression 2003 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2003 Abstract Expression of the large GTPase guanylate binding protein‐1 (GBP‐1) is induced by inflammatory cytokines (ICs) in endothelial cells (ECs), and the helical domain of the molecule mediates the repression of EC proliferation by ICs. Here we show that the expression of GBP‐1 and of the matrix metalloproteinase‐1 (MMP‐1) are inversely related in vitro and in vivo, and that GBP‐1 selectively inhibits the expression of MMP‐1 in ECs, but not the expression of other proteases. The GTPase activity of GBP‐1 was necessary for this effect, which inhibited invasiveness and tube‐forming capability of ECs in three‐dimensional collagen‐I matrices. A GTPase‐deficient mutant (D184N‐GBP‐1) operated as a transdominant inhibitor of wild‐type GBP‐1 and rescued MMP‐1 expression in the presence of ICs. Expression of D184N‐GBP‐1, as well as paracrine supplementation of MMP‐1, restored the tube‐forming capability of ECs in the presence of wild‐type GBP‐1. The latter finding indicated that the inhibition of capillary formation is specifically due to the repression of MMP‐1 expression by GBP‐1, and is not affected by the anti‐proliferative activity of the helical domain of GBP‐1. These findings substantiate the role of GBP‐1 as a major regulator of the anti‐angiogenic response of ECs to ICs. angiogenesis (dpeaa)DE-He213 collagenase (dpeaa)DE-He213 inflammation (dpeaa)DE-He213 invasion (dpeaa)DE-He213 MMP (dpeaa)DE-He213 Töpolt, Kristin verfasserin aut Lubeseder‐Martellato, Clara verfasserin aut Jörg, Anita verfasserin aut Naschberger, Elisabeth verfasserin aut Benelli, Roberto verfasserin aut Albini, Adriana verfasserin aut Stürzl, Michael verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 22(2003), 15 vom: 01. Aug., Seite 3772-3782 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:22 year:2003 number:15 day:01 month:08 pages:3772-3782 https://dx.doi.org/10.1093/emboj/cdg382 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 22 2003 15 01 08 3772-3782 |
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Enthalten in The EMBO Journal 22(2003), 15 vom: 01. Aug., Seite 3772-3782 volume:22 year:2003 number:15 day:01 month:08 pages:3772-3782 |
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Enthalten in The EMBO Journal 22(2003), 15 vom: 01. Aug., Seite 3772-3782 volume:22 year:2003 number:15 day:01 month:08 pages:3772-3782 |
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Guenzi, Eric @@aut@@ Töpolt, Kristin @@aut@@ Lubeseder‐Martellato, Clara @@aut@@ Jörg, Anita @@aut@@ Naschberger, Elisabeth @@aut@@ Benelli, Roberto @@aut@@ Albini, Adriana @@aut@@ Stürzl, Michael @@aut@@ |
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Here we show that the expression of GBP‐1 and of the matrix metalloproteinase‐1 (MMP‐1) are inversely related in vitro and in vivo, and that GBP‐1 selectively inhibits the expression of MMP‐1 in ECs, but not the expression of other proteases. The GTPase activity of GBP‐1 was necessary for this effect, which inhibited invasiveness and tube‐forming capability of ECs in three‐dimensional collagen‐I matrices. A GTPase‐deficient mutant (D184N‐GBP‐1) operated as a transdominant inhibitor of wild‐type GBP‐1 and rescued MMP‐1 expression in the presence of ICs. Expression of D184N‐GBP‐1, as well as paracrine supplementation of MMP‐1, restored the tube‐forming capability of ECs in the presence of wild‐type GBP‐1. The latter finding indicated that the inhibition of capillary formation is specifically due to the repression of MMP‐1 expression by GBP‐1, and is not affected by the anti‐proliferative activity of the helical domain of GBP‐1. 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|
author |
Guenzi, Eric |
spellingShingle |
Guenzi, Eric misc angiogenesis misc collagenase misc inflammation misc invasion misc MMP The guanylate binding protein‐1 GTPase controls the invasive and angiogenic capability of endothelial cells through inhibition of MMP‐1 expression |
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1460-2075 |
topic_title |
The guanylate binding protein‐1 GTPase controls the invasive and angiogenic capability of endothelial cells through inhibition of MMP‐1 expression angiogenesis (dpeaa)DE-He213 collagenase (dpeaa)DE-He213 inflammation (dpeaa)DE-He213 invasion (dpeaa)DE-He213 MMP (dpeaa)DE-He213 |
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misc angiogenesis misc collagenase misc inflammation misc invasion misc MMP |
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misc angiogenesis misc collagenase misc inflammation misc invasion misc MMP |
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misc angiogenesis misc collagenase misc inflammation misc invasion misc MMP |
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Elektronische Aufsätze Aufsätze Elektronische Ressource |
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title |
The guanylate binding protein‐1 GTPase controls the invasive and angiogenic capability of endothelial cells through inhibition of MMP‐1 expression |
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The guanylate binding protein‐1 GTPase controls the invasive and angiogenic capability of endothelial cells through inhibition of MMP‐1 expression |
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Guenzi, Eric |
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The EMBO Journal |
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2003 |
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Guenzi, Eric Töpolt, Kristin Lubeseder‐Martellato, Clara Jörg, Anita Naschberger, Elisabeth Benelli, Roberto Albini, Adriana Stürzl, Michael |
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Guenzi, Eric |
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10.1093/emboj/cdg382 |
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title_sort |
the guanylate binding protein‐1 gtpase controls the invasive and angiogenic capability of endothelial cells through inhibition of mmp‐1 expression |
title_auth |
The guanylate binding protein‐1 GTPase controls the invasive and angiogenic capability of endothelial cells through inhibition of MMP‐1 expression |
abstract |
Abstract Expression of the large GTPase guanylate binding protein‐1 (GBP‐1) is induced by inflammatory cytokines (ICs) in endothelial cells (ECs), and the helical domain of the molecule mediates the repression of EC proliferation by ICs. Here we show that the expression of GBP‐1 and of the matrix metalloproteinase‐1 (MMP‐1) are inversely related in vitro and in vivo, and that GBP‐1 selectively inhibits the expression of MMP‐1 in ECs, but not the expression of other proteases. The GTPase activity of GBP‐1 was necessary for this effect, which inhibited invasiveness and tube‐forming capability of ECs in three‐dimensional collagen‐I matrices. A GTPase‐deficient mutant (D184N‐GBP‐1) operated as a transdominant inhibitor of wild‐type GBP‐1 and rescued MMP‐1 expression in the presence of ICs. Expression of D184N‐GBP‐1, as well as paracrine supplementation of MMP‐1, restored the tube‐forming capability of ECs in the presence of wild‐type GBP‐1. The latter finding indicated that the inhibition of capillary formation is specifically due to the repression of MMP‐1 expression by GBP‐1, and is not affected by the anti‐proliferative activity of the helical domain of GBP‐1. These findings substantiate the role of GBP‐1 as a major regulator of the anti‐angiogenic response of ECs to ICs. © European Molecular Biology Organization 2003 |
abstractGer |
Abstract Expression of the large GTPase guanylate binding protein‐1 (GBP‐1) is induced by inflammatory cytokines (ICs) in endothelial cells (ECs), and the helical domain of the molecule mediates the repression of EC proliferation by ICs. Here we show that the expression of GBP‐1 and of the matrix metalloproteinase‐1 (MMP‐1) are inversely related in vitro and in vivo, and that GBP‐1 selectively inhibits the expression of MMP‐1 in ECs, but not the expression of other proteases. The GTPase activity of GBP‐1 was necessary for this effect, which inhibited invasiveness and tube‐forming capability of ECs in three‐dimensional collagen‐I matrices. A GTPase‐deficient mutant (D184N‐GBP‐1) operated as a transdominant inhibitor of wild‐type GBP‐1 and rescued MMP‐1 expression in the presence of ICs. Expression of D184N‐GBP‐1, as well as paracrine supplementation of MMP‐1, restored the tube‐forming capability of ECs in the presence of wild‐type GBP‐1. The latter finding indicated that the inhibition of capillary formation is specifically due to the repression of MMP‐1 expression by GBP‐1, and is not affected by the anti‐proliferative activity of the helical domain of GBP‐1. These findings substantiate the role of GBP‐1 as a major regulator of the anti‐angiogenic response of ECs to ICs. © European Molecular Biology Organization 2003 |
abstract_unstemmed |
Abstract Expression of the large GTPase guanylate binding protein‐1 (GBP‐1) is induced by inflammatory cytokines (ICs) in endothelial cells (ECs), and the helical domain of the molecule mediates the repression of EC proliferation by ICs. Here we show that the expression of GBP‐1 and of the matrix metalloproteinase‐1 (MMP‐1) are inversely related in vitro and in vivo, and that GBP‐1 selectively inhibits the expression of MMP‐1 in ECs, but not the expression of other proteases. The GTPase activity of GBP‐1 was necessary for this effect, which inhibited invasiveness and tube‐forming capability of ECs in three‐dimensional collagen‐I matrices. A GTPase‐deficient mutant (D184N‐GBP‐1) operated as a transdominant inhibitor of wild‐type GBP‐1 and rescued MMP‐1 expression in the presence of ICs. Expression of D184N‐GBP‐1, as well as paracrine supplementation of MMP‐1, restored the tube‐forming capability of ECs in the presence of wild‐type GBP‐1. The latter finding indicated that the inhibition of capillary formation is specifically due to the repression of MMP‐1 expression by GBP‐1, and is not affected by the anti‐proliferative activity of the helical domain of GBP‐1. These findings substantiate the role of GBP‐1 as a major regulator of the anti‐angiogenic response of ECs to ICs. © European Molecular Biology Organization 2003 |
collection_details |
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container_issue |
15 |
title_short |
The guanylate binding protein‐1 GTPase controls the invasive and angiogenic capability of endothelial cells through inhibition of MMP‐1 expression |
url |
https://dx.doi.org/10.1093/emboj/cdg382 |
remote_bool |
true |
author2 |
Töpolt, Kristin Lubeseder‐Martellato, Clara Jörg, Anita Naschberger, Elisabeth Benelli, Roberto Albini, Adriana Stürzl, Michael |
author2Str |
Töpolt, Kristin Lubeseder‐Martellato, Clara Jörg, Anita Naschberger, Elisabeth Benelli, Roberto Albini, Adriana Stürzl, Michael |
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doi_str |
10.1093/emboj/cdg382 |
up_date |
2024-10-22T04:52:04.844Z |
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|
score |
7.401016 |