Interactions between bradykinin and plasmin in the endothelial $ Ca^{2+} $ response
Abstract Plasmin is a fibrinolytic factor and a serine protease that activates protease-activated receptors (PARs) to produce endothelium-derived relaxing factors such as nitric oxide and prostacyclin. Nitric oxide and prostacyclin production is regulated, at least in part, by the intracellular $ Ca...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Obata, Yukako [verfasserIn] Takeuchi, Kazuhiko [verfasserIn] Wei, Jiazhang [verfasserIn] Hakamata, Akio [verfasserIn] Odagiri, Keiichi [verfasserIn] Nakajima, Yoshiki [verfasserIn] Watanabe, Hiroshi [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2017 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Molecular and cellular biochemistry - Dordrecht [u.a.] : Springer Science + Business Media B.V, 1973, 445(2017), 1-2 vom: 29. Dez., Seite 179-186 |
|---|---|
| Übergeordnetes Werk: |
volume:445 ; year:2017 ; number:1-2 ; day:29 ; month:12 ; pages:179-186 |
| Links: |
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| DOI / URN: |
10.1007/s11010-017-3263-y |
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| Katalog-ID: |
SPR015658600 |
|---|
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| 245 | 1 | 0 | |a Interactions between bradykinin and plasmin in the endothelial $ Ca^{2+} $ response |
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| 520 | |a Abstract Plasmin is a fibrinolytic factor and a serine protease that activates protease-activated receptors (PARs) to produce endothelium-derived relaxing factors such as nitric oxide and prostacyclin. Nitric oxide and prostacyclin production is regulated, at least in part, by the intracellular $ Ca^{2+} $ concentration in various blood vessel types. Bradykinin and plasmin stimulate vascular endothelial cells and work simultaneously in pathophysiological conditions such as thrombosis and inflammation. Here, we explored the interactions between bradykinin and plasmin in the endothelial $ Ca^{2+} $ response using the fluorescent indicator, Fura-2/AM, in primary cultures of porcine aortic endothelial cells (PAECs). Plasmin (0.15–15 µg/ml) and bradykinin (0.1–10 nM) increased intracellular $ Ca^{2+} $ concentrations in PAECs in a dose-dependent manner, and the plasmin-induced endothelial $ Ca^{2+} $ response occurred only once. Bradykinin (0.1–10 nM) inhibited the plasmin-induced endothelial $ Ca^{2+} $ response in a dose-dependent manner, however, plasmin did not affect the bradykinin-induced endothelial $ Ca^{2+} $ response. Pretreatment with gabexate mesilate (GM, 100 µM), a serine protease inhibitor, that blocks plasmin’s proteolytic activity, fully suppressed the plasmin-induced $ Ca^{2+} $ response. After washout of GM and the first plasmin, the second administration of plasmin caused $ Ca^{2+} $ increases. However, when the first plasmin-induced $ Ca^{2+} $ response was blocked by pretreatment with bradykinin, the second plasmin (15 µg/ml) application did not cause any $ Ca^{2+} $ response, even 30 min after the washout of the first plasmin and bradykinin. Our data suggested that bradykinin regulated the plasmin-induced endothelial $ Ca^{2+} $ response by inhibiting the pathway downstream of the PARs’ N-terminus cleavage. | ||
| 650 | 4 | |a Plasmin |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Endothelial cells |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Calcium |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Bradykinin |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Takeuchi, Kazuhiko |e verfasserin |4 aut | |
| 700 | 1 | |a Wei, Jiazhang |e verfasserin |4 aut | |
| 700 | 1 | |a Hakamata, Akio |e verfasserin |4 aut | |
| 700 | 1 | |a Odagiri, Keiichi |e verfasserin |4 aut | |
| 700 | 1 | |a Nakajima, Yoshiki |e verfasserin |4 aut | |
| 700 | 1 | |a Watanabe, Hiroshi |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Molecular and cellular biochemistry |d Dordrecht [u.a.] : Springer Science + Business Media B.V, 1973 |g 445(2017), 1-2 vom: 29. Dez., Seite 179-186 |w (DE-627)32042975X |w (DE-600)2003615-2 |x 1573-4919 |7 nnns |
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10.1007/s11010-017-3263-y doi (DE-627)SPR015658600 (SPR)s11010-017-3263-y-e DE-627 ger DE-627 rakwb eng 540 ASE 44.00 bkl Obata, Yukako verfasserin aut Interactions between bradykinin and plasmin in the endothelial $ Ca^{2+} $ response 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Plasmin is a fibrinolytic factor and a serine protease that activates protease-activated receptors (PARs) to produce endothelium-derived relaxing factors such as nitric oxide and prostacyclin. Nitric oxide and prostacyclin production is regulated, at least in part, by the intracellular $ Ca^{2+} $ concentration in various blood vessel types. Bradykinin and plasmin stimulate vascular endothelial cells and work simultaneously in pathophysiological conditions such as thrombosis and inflammation. Here, we explored the interactions between bradykinin and plasmin in the endothelial $ Ca^{2+} $ response using the fluorescent indicator, Fura-2/AM, in primary cultures of porcine aortic endothelial cells (PAECs). Plasmin (0.15–15 µg/ml) and bradykinin (0.1–10 nM) increased intracellular $ Ca^{2+} $ concentrations in PAECs in a dose-dependent manner, and the plasmin-induced endothelial $ Ca^{2+} $ response occurred only once. Bradykinin (0.1–10 nM) inhibited the plasmin-induced endothelial $ Ca^{2+} $ response in a dose-dependent manner, however, plasmin did not affect the bradykinin-induced endothelial $ Ca^{2+} $ response. Pretreatment with gabexate mesilate (GM, 100 µM), a serine protease inhibitor, that blocks plasmin’s proteolytic activity, fully suppressed the plasmin-induced $ Ca^{2+} $ response. After washout of GM and the first plasmin, the second administration of plasmin caused $ Ca^{2+} $ increases. However, when the first plasmin-induced $ Ca^{2+} $ response was blocked by pretreatment with bradykinin, the second plasmin (15 µg/ml) application did not cause any $ Ca^{2+} $ response, even 30 min after the washout of the first plasmin and bradykinin. Our data suggested that bradykinin regulated the plasmin-induced endothelial $ Ca^{2+} $ response by inhibiting the pathway downstream of the PARs’ N-terminus cleavage. Plasmin (dpeaa)DE-He213 Endothelial cells (dpeaa)DE-He213 Calcium (dpeaa)DE-He213 Bradykinin (dpeaa)DE-He213 Takeuchi, Kazuhiko verfasserin aut Wei, Jiazhang verfasserin aut Hakamata, Akio verfasserin aut Odagiri, Keiichi verfasserin aut Nakajima, Yoshiki verfasserin aut Watanabe, Hiroshi verfasserin aut Enthalten in Molecular and cellular biochemistry Dordrecht [u.a.] : Springer Science + Business Media B.V, 1973 445(2017), 1-2 vom: 29. Dez., Seite 179-186 (DE-627)32042975X (DE-600)2003615-2 1573-4919 nnns volume:445 year:2017 number:1-2 day:29 month:12 pages:179-186 https://dx.doi.org/10.1007/s11010-017-3263-y lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 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_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 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_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 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_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 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_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 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_4393 GBV_ILN_4700 44.00 ASE AR 445 2017 1-2 29 12 179-186 |
| spelling |
10.1007/s11010-017-3263-y doi (DE-627)SPR015658600 (SPR)s11010-017-3263-y-e DE-627 ger DE-627 rakwb eng 540 ASE 44.00 bkl Obata, Yukako verfasserin aut Interactions between bradykinin and plasmin in the endothelial $ Ca^{2+} $ response 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Plasmin is a fibrinolytic factor and a serine protease that activates protease-activated receptors (PARs) to produce endothelium-derived relaxing factors such as nitric oxide and prostacyclin. Nitric oxide and prostacyclin production is regulated, at least in part, by the intracellular $ Ca^{2+} $ concentration in various blood vessel types. Bradykinin and plasmin stimulate vascular endothelial cells and work simultaneously in pathophysiological conditions such as thrombosis and inflammation. Here, we explored the interactions between bradykinin and plasmin in the endothelial $ Ca^{2+} $ response using the fluorescent indicator, Fura-2/AM, in primary cultures of porcine aortic endothelial cells (PAECs). Plasmin (0.15–15 µg/ml) and bradykinin (0.1–10 nM) increased intracellular $ Ca^{2+} $ concentrations in PAECs in a dose-dependent manner, and the plasmin-induced endothelial $ Ca^{2+} $ response occurred only once. Bradykinin (0.1–10 nM) inhibited the plasmin-induced endothelial $ Ca^{2+} $ response in a dose-dependent manner, however, plasmin did not affect the bradykinin-induced endothelial $ Ca^{2+} $ response. Pretreatment with gabexate mesilate (GM, 100 µM), a serine protease inhibitor, that blocks plasmin’s proteolytic activity, fully suppressed the plasmin-induced $ Ca^{2+} $ response. After washout of GM and the first plasmin, the second administration of plasmin caused $ Ca^{2+} $ increases. However, when the first plasmin-induced $ Ca^{2+} $ response was blocked by pretreatment with bradykinin, the second plasmin (15 µg/ml) application did not cause any $ Ca^{2+} $ response, even 30 min after the washout of the first plasmin and bradykinin. Our data suggested that bradykinin regulated the plasmin-induced endothelial $ Ca^{2+} $ response by inhibiting the pathway downstream of the PARs’ N-terminus cleavage. Plasmin (dpeaa)DE-He213 Endothelial cells (dpeaa)DE-He213 Calcium (dpeaa)DE-He213 Bradykinin (dpeaa)DE-He213 Takeuchi, Kazuhiko verfasserin aut Wei, Jiazhang verfasserin aut Hakamata, Akio verfasserin aut Odagiri, Keiichi verfasserin aut Nakajima, Yoshiki verfasserin aut Watanabe, Hiroshi verfasserin aut Enthalten in Molecular and cellular biochemistry Dordrecht [u.a.] : Springer Science + Business Media B.V, 1973 445(2017), 1-2 vom: 29. Dez., Seite 179-186 (DE-627)32042975X (DE-600)2003615-2 1573-4919 nnns volume:445 year:2017 number:1-2 day:29 month:12 pages:179-186 https://dx.doi.org/10.1007/s11010-017-3263-y lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 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_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 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_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 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_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 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_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 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_4393 GBV_ILN_4700 44.00 ASE AR 445 2017 1-2 29 12 179-186 |
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10.1007/s11010-017-3263-y doi (DE-627)SPR015658600 (SPR)s11010-017-3263-y-e DE-627 ger DE-627 rakwb eng 540 ASE 44.00 bkl Obata, Yukako verfasserin aut Interactions between bradykinin and plasmin in the endothelial $ Ca^{2+} $ response 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Plasmin is a fibrinolytic factor and a serine protease that activates protease-activated receptors (PARs) to produce endothelium-derived relaxing factors such as nitric oxide and prostacyclin. Nitric oxide and prostacyclin production is regulated, at least in part, by the intracellular $ Ca^{2+} $ concentration in various blood vessel types. Bradykinin and plasmin stimulate vascular endothelial cells and work simultaneously in pathophysiological conditions such as thrombosis and inflammation. Here, we explored the interactions between bradykinin and plasmin in the endothelial $ Ca^{2+} $ response using the fluorescent indicator, Fura-2/AM, in primary cultures of porcine aortic endothelial cells (PAECs). Plasmin (0.15–15 µg/ml) and bradykinin (0.1–10 nM) increased intracellular $ Ca^{2+} $ concentrations in PAECs in a dose-dependent manner, and the plasmin-induced endothelial $ Ca^{2+} $ response occurred only once. Bradykinin (0.1–10 nM) inhibited the plasmin-induced endothelial $ Ca^{2+} $ response in a dose-dependent manner, however, plasmin did not affect the bradykinin-induced endothelial $ Ca^{2+} $ response. Pretreatment with gabexate mesilate (GM, 100 µM), a serine protease inhibitor, that blocks plasmin’s proteolytic activity, fully suppressed the plasmin-induced $ Ca^{2+} $ response. After washout of GM and the first plasmin, the second administration of plasmin caused $ Ca^{2+} $ increases. However, when the first plasmin-induced $ Ca^{2+} $ response was blocked by pretreatment with bradykinin, the second plasmin (15 µg/ml) application did not cause any $ Ca^{2+} $ response, even 30 min after the washout of the first plasmin and bradykinin. Our data suggested that bradykinin regulated the plasmin-induced endothelial $ Ca^{2+} $ response by inhibiting the pathway downstream of the PARs’ N-terminus cleavage. Plasmin (dpeaa)DE-He213 Endothelial cells (dpeaa)DE-He213 Calcium (dpeaa)DE-He213 Bradykinin (dpeaa)DE-He213 Takeuchi, Kazuhiko verfasserin aut Wei, Jiazhang verfasserin aut Hakamata, Akio verfasserin aut Odagiri, Keiichi verfasserin aut Nakajima, Yoshiki verfasserin aut Watanabe, Hiroshi verfasserin aut Enthalten in Molecular and cellular biochemistry Dordrecht [u.a.] : Springer Science + Business Media B.V, 1973 445(2017), 1-2 vom: 29. Dez., Seite 179-186 (DE-627)32042975X (DE-600)2003615-2 1573-4919 nnns volume:445 year:2017 number:1-2 day:29 month:12 pages:179-186 https://dx.doi.org/10.1007/s11010-017-3263-y lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 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_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 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_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 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_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 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_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 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_4393 GBV_ILN_4700 44.00 ASE AR 445 2017 1-2 29 12 179-186 |
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10.1007/s11010-017-3263-y doi (DE-627)SPR015658600 (SPR)s11010-017-3263-y-e DE-627 ger DE-627 rakwb eng 540 ASE 44.00 bkl Obata, Yukako verfasserin aut Interactions between bradykinin and plasmin in the endothelial $ Ca^{2+} $ response 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Plasmin is a fibrinolytic factor and a serine protease that activates protease-activated receptors (PARs) to produce endothelium-derived relaxing factors such as nitric oxide and prostacyclin. Nitric oxide and prostacyclin production is regulated, at least in part, by the intracellular $ Ca^{2+} $ concentration in various blood vessel types. Bradykinin and plasmin stimulate vascular endothelial cells and work simultaneously in pathophysiological conditions such as thrombosis and inflammation. Here, we explored the interactions between bradykinin and plasmin in the endothelial $ Ca^{2+} $ response using the fluorescent indicator, Fura-2/AM, in primary cultures of porcine aortic endothelial cells (PAECs). Plasmin (0.15–15 µg/ml) and bradykinin (0.1–10 nM) increased intracellular $ Ca^{2+} $ concentrations in PAECs in a dose-dependent manner, and the plasmin-induced endothelial $ Ca^{2+} $ response occurred only once. Bradykinin (0.1–10 nM) inhibited the plasmin-induced endothelial $ Ca^{2+} $ response in a dose-dependent manner, however, plasmin did not affect the bradykinin-induced endothelial $ Ca^{2+} $ response. Pretreatment with gabexate mesilate (GM, 100 µM), a serine protease inhibitor, that blocks plasmin’s proteolytic activity, fully suppressed the plasmin-induced $ Ca^{2+} $ response. After washout of GM and the first plasmin, the second administration of plasmin caused $ Ca^{2+} $ increases. However, when the first plasmin-induced $ Ca^{2+} $ response was blocked by pretreatment with bradykinin, the second plasmin (15 µg/ml) application did not cause any $ Ca^{2+} $ response, even 30 min after the washout of the first plasmin and bradykinin. Our data suggested that bradykinin regulated the plasmin-induced endothelial $ Ca^{2+} $ response by inhibiting the pathway downstream of the PARs’ N-terminus cleavage. Plasmin (dpeaa)DE-He213 Endothelial cells (dpeaa)DE-He213 Calcium (dpeaa)DE-He213 Bradykinin (dpeaa)DE-He213 Takeuchi, Kazuhiko verfasserin aut Wei, Jiazhang verfasserin aut Hakamata, Akio verfasserin aut Odagiri, Keiichi verfasserin aut Nakajima, Yoshiki verfasserin aut Watanabe, Hiroshi verfasserin aut Enthalten in Molecular and cellular biochemistry Dordrecht [u.a.] : Springer Science + Business Media B.V, 1973 445(2017), 1-2 vom: 29. Dez., Seite 179-186 (DE-627)32042975X (DE-600)2003615-2 1573-4919 nnns volume:445 year:2017 number:1-2 day:29 month:12 pages:179-186 https://dx.doi.org/10.1007/s11010-017-3263-y lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 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_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 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_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 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_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 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_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 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_4393 GBV_ILN_4700 44.00 ASE AR 445 2017 1-2 29 12 179-186 |
| allfieldsSound |
10.1007/s11010-017-3263-y doi (DE-627)SPR015658600 (SPR)s11010-017-3263-y-e DE-627 ger DE-627 rakwb eng 540 ASE 44.00 bkl Obata, Yukako verfasserin aut Interactions between bradykinin and plasmin in the endothelial $ Ca^{2+} $ response 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Plasmin is a fibrinolytic factor and a serine protease that activates protease-activated receptors (PARs) to produce endothelium-derived relaxing factors such as nitric oxide and prostacyclin. Nitric oxide and prostacyclin production is regulated, at least in part, by the intracellular $ Ca^{2+} $ concentration in various blood vessel types. Bradykinin and plasmin stimulate vascular endothelial cells and work simultaneously in pathophysiological conditions such as thrombosis and inflammation. Here, we explored the interactions between bradykinin and plasmin in the endothelial $ Ca^{2+} $ response using the fluorescent indicator, Fura-2/AM, in primary cultures of porcine aortic endothelial cells (PAECs). Plasmin (0.15–15 µg/ml) and bradykinin (0.1–10 nM) increased intracellular $ Ca^{2+} $ concentrations in PAECs in a dose-dependent manner, and the plasmin-induced endothelial $ Ca^{2+} $ response occurred only once. Bradykinin (0.1–10 nM) inhibited the plasmin-induced endothelial $ Ca^{2+} $ response in a dose-dependent manner, however, plasmin did not affect the bradykinin-induced endothelial $ Ca^{2+} $ response. Pretreatment with gabexate mesilate (GM, 100 µM), a serine protease inhibitor, that blocks plasmin’s proteolytic activity, fully suppressed the plasmin-induced $ Ca^{2+} $ response. After washout of GM and the first plasmin, the second administration of plasmin caused $ Ca^{2+} $ increases. However, when the first plasmin-induced $ Ca^{2+} $ response was blocked by pretreatment with bradykinin, the second plasmin (15 µg/ml) application did not cause any $ Ca^{2+} $ response, even 30 min after the washout of the first plasmin and bradykinin. Our data suggested that bradykinin regulated the plasmin-induced endothelial $ Ca^{2+} $ response by inhibiting the pathway downstream of the PARs’ N-terminus cleavage. Plasmin (dpeaa)DE-He213 Endothelial cells (dpeaa)DE-He213 Calcium (dpeaa)DE-He213 Bradykinin (dpeaa)DE-He213 Takeuchi, Kazuhiko verfasserin aut Wei, Jiazhang verfasserin aut Hakamata, Akio verfasserin aut Odagiri, Keiichi verfasserin aut Nakajima, Yoshiki verfasserin aut Watanabe, Hiroshi verfasserin aut Enthalten in Molecular and cellular biochemistry Dordrecht [u.a.] : Springer Science + Business Media B.V, 1973 445(2017), 1-2 vom: 29. Dez., Seite 179-186 (DE-627)32042975X (DE-600)2003615-2 1573-4919 nnns volume:445 year:2017 number:1-2 day:29 month:12 pages:179-186 https://dx.doi.org/10.1007/s11010-017-3263-y lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 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_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 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_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 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_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 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_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 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_4393 GBV_ILN_4700 44.00 ASE AR 445 2017 1-2 29 12 179-186 |
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English |
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Enthalten in Molecular and cellular biochemistry 445(2017), 1-2 vom: 29. Dez., Seite 179-186 volume:445 year:2017 number:1-2 day:29 month:12 pages:179-186 |
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Enthalten in Molecular and cellular biochemistry 445(2017), 1-2 vom: 29. Dez., Seite 179-186 volume:445 year:2017 number:1-2 day:29 month:12 pages:179-186 |
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Plasmin Endothelial cells Calcium Bradykinin |
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Molecular and cellular biochemistry |
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Obata, Yukako @@aut@@ Takeuchi, Kazuhiko @@aut@@ Wei, Jiazhang @@aut@@ Hakamata, Akio @@aut@@ Odagiri, Keiichi @@aut@@ Nakajima, Yoshiki @@aut@@ Watanabe, Hiroshi @@aut@@ |
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Nitric oxide and prostacyclin production is regulated, at least in part, by the intracellular $ Ca^{2+} $ concentration in various blood vessel types. Bradykinin and plasmin stimulate vascular endothelial cells and work simultaneously in pathophysiological conditions such as thrombosis and inflammation. Here, we explored the interactions between bradykinin and plasmin in the endothelial $ Ca^{2+} $ response using the fluorescent indicator, Fura-2/AM, in primary cultures of porcine aortic endothelial cells (PAECs). Plasmin (0.15–15 µg/ml) and bradykinin (0.1–10 nM) increased intracellular $ Ca^{2+} $ concentrations in PAECs in a dose-dependent manner, and the plasmin-induced endothelial $ Ca^{2+} $ response occurred only once. Bradykinin (0.1–10 nM) inhibited the plasmin-induced endothelial $ Ca^{2+} $ response in a dose-dependent manner, however, plasmin did not affect the bradykinin-induced endothelial $ Ca^{2+} $ response. Pretreatment with gabexate mesilate (GM, 100 µM), a serine protease inhibitor, that blocks plasmin’s proteolytic activity, fully suppressed the plasmin-induced $ Ca^{2+} $ response. After washout of GM and the first plasmin, the second administration of plasmin caused $ Ca^{2+} $ increases. However, when the first plasmin-induced $ Ca^{2+} $ response was blocked by pretreatment with bradykinin, the second plasmin (15 µg/ml) application did not cause any $ Ca^{2+} $ response, even 30 min after the washout of the first plasmin and bradykinin. 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|
| author |
Obata, Yukako |
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Obata, Yukako ddc 540 bkl 44.00 misc Plasmin misc Endothelial cells misc Calcium misc Bradykinin Interactions between bradykinin and plasmin in the endothelial $ Ca^{2+} $ response |
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Obata, Yukako |
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540 ASE 44.00 bkl Interactions between bradykinin and plasmin in the endothelial $ Ca^{2+} $ response Plasmin (dpeaa)DE-He213 Endothelial cells (dpeaa)DE-He213 Calcium (dpeaa)DE-He213 Bradykinin (dpeaa)DE-He213 |
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ddc 540 bkl 44.00 misc Plasmin misc Endothelial cells misc Calcium misc Bradykinin |
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ddc 540 bkl 44.00 misc Plasmin misc Endothelial cells misc Calcium misc Bradykinin |
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ddc 540 bkl 44.00 misc Plasmin misc Endothelial cells misc Calcium misc Bradykinin |
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Interactions between bradykinin and plasmin in the endothelial $ Ca^{2+} $ response |
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Interactions between bradykinin and plasmin in the endothelial $ Ca^{2+} $ response |
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Obata, Yukako |
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Molecular and cellular biochemistry |
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Obata, Yukako Takeuchi, Kazuhiko Wei, Jiazhang Hakamata, Akio Odagiri, Keiichi Nakajima, Yoshiki Watanabe, Hiroshi |
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Obata, Yukako |
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10.1007/s11010-017-3263-y |
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| title_sort |
interactions between bradykinin and plasmin in the endothelial $ ca^{2+} $ response |
| title_auth |
Interactions between bradykinin and plasmin in the endothelial $ Ca^{2+} $ response |
| abstract |
Abstract Plasmin is a fibrinolytic factor and a serine protease that activates protease-activated receptors (PARs) to produce endothelium-derived relaxing factors such as nitric oxide and prostacyclin. Nitric oxide and prostacyclin production is regulated, at least in part, by the intracellular $ Ca^{2+} $ concentration in various blood vessel types. Bradykinin and plasmin stimulate vascular endothelial cells and work simultaneously in pathophysiological conditions such as thrombosis and inflammation. Here, we explored the interactions between bradykinin and plasmin in the endothelial $ Ca^{2+} $ response using the fluorescent indicator, Fura-2/AM, in primary cultures of porcine aortic endothelial cells (PAECs). Plasmin (0.15–15 µg/ml) and bradykinin (0.1–10 nM) increased intracellular $ Ca^{2+} $ concentrations in PAECs in a dose-dependent manner, and the plasmin-induced endothelial $ Ca^{2+} $ response occurred only once. Bradykinin (0.1–10 nM) inhibited the plasmin-induced endothelial $ Ca^{2+} $ response in a dose-dependent manner, however, plasmin did not affect the bradykinin-induced endothelial $ Ca^{2+} $ response. Pretreatment with gabexate mesilate (GM, 100 µM), a serine protease inhibitor, that blocks plasmin’s proteolytic activity, fully suppressed the plasmin-induced $ Ca^{2+} $ response. After washout of GM and the first plasmin, the second administration of plasmin caused $ Ca^{2+} $ increases. However, when the first plasmin-induced $ Ca^{2+} $ response was blocked by pretreatment with bradykinin, the second plasmin (15 µg/ml) application did not cause any $ Ca^{2+} $ response, even 30 min after the washout of the first plasmin and bradykinin. Our data suggested that bradykinin regulated the plasmin-induced endothelial $ Ca^{2+} $ response by inhibiting the pathway downstream of the PARs’ N-terminus cleavage. |
| abstractGer |
Abstract Plasmin is a fibrinolytic factor and a serine protease that activates protease-activated receptors (PARs) to produce endothelium-derived relaxing factors such as nitric oxide and prostacyclin. Nitric oxide and prostacyclin production is regulated, at least in part, by the intracellular $ Ca^{2+} $ concentration in various blood vessel types. Bradykinin and plasmin stimulate vascular endothelial cells and work simultaneously in pathophysiological conditions such as thrombosis and inflammation. Here, we explored the interactions between bradykinin and plasmin in the endothelial $ Ca^{2+} $ response using the fluorescent indicator, Fura-2/AM, in primary cultures of porcine aortic endothelial cells (PAECs). Plasmin (0.15–15 µg/ml) and bradykinin (0.1–10 nM) increased intracellular $ Ca^{2+} $ concentrations in PAECs in a dose-dependent manner, and the plasmin-induced endothelial $ Ca^{2+} $ response occurred only once. Bradykinin (0.1–10 nM) inhibited the plasmin-induced endothelial $ Ca^{2+} $ response in a dose-dependent manner, however, plasmin did not affect the bradykinin-induced endothelial $ Ca^{2+} $ response. Pretreatment with gabexate mesilate (GM, 100 µM), a serine protease inhibitor, that blocks plasmin’s proteolytic activity, fully suppressed the plasmin-induced $ Ca^{2+} $ response. After washout of GM and the first plasmin, the second administration of plasmin caused $ Ca^{2+} $ increases. However, when the first plasmin-induced $ Ca^{2+} $ response was blocked by pretreatment with bradykinin, the second plasmin (15 µg/ml) application did not cause any $ Ca^{2+} $ response, even 30 min after the washout of the first plasmin and bradykinin. Our data suggested that bradykinin regulated the plasmin-induced endothelial $ Ca^{2+} $ response by inhibiting the pathway downstream of the PARs’ N-terminus cleavage. |
| abstract_unstemmed |
Abstract Plasmin is a fibrinolytic factor and a serine protease that activates protease-activated receptors (PARs) to produce endothelium-derived relaxing factors such as nitric oxide and prostacyclin. Nitric oxide and prostacyclin production is regulated, at least in part, by the intracellular $ Ca^{2+} $ concentration in various blood vessel types. Bradykinin and plasmin stimulate vascular endothelial cells and work simultaneously in pathophysiological conditions such as thrombosis and inflammation. Here, we explored the interactions between bradykinin and plasmin in the endothelial $ Ca^{2+} $ response using the fluorescent indicator, Fura-2/AM, in primary cultures of porcine aortic endothelial cells (PAECs). Plasmin (0.15–15 µg/ml) and bradykinin (0.1–10 nM) increased intracellular $ Ca^{2+} $ concentrations in PAECs in a dose-dependent manner, and the plasmin-induced endothelial $ Ca^{2+} $ response occurred only once. Bradykinin (0.1–10 nM) inhibited the plasmin-induced endothelial $ Ca^{2+} $ response in a dose-dependent manner, however, plasmin did not affect the bradykinin-induced endothelial $ Ca^{2+} $ response. Pretreatment with gabexate mesilate (GM, 100 µM), a serine protease inhibitor, that blocks plasmin’s proteolytic activity, fully suppressed the plasmin-induced $ Ca^{2+} $ response. After washout of GM and the first plasmin, the second administration of plasmin caused $ Ca^{2+} $ increases. However, when the first plasmin-induced $ Ca^{2+} $ response was blocked by pretreatment with bradykinin, the second plasmin (15 µg/ml) application did not cause any $ Ca^{2+} $ response, even 30 min after the washout of the first plasmin and bradykinin. Our data suggested that bradykinin regulated the plasmin-induced endothelial $ Ca^{2+} $ response by inhibiting the pathway downstream of the PARs’ N-terminus cleavage. |
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Interactions between bradykinin and plasmin in the endothelial $ Ca^{2+} $ response |
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Takeuchi, Kazuhiko Wei, Jiazhang Hakamata, Akio Odagiri, Keiichi Nakajima, Yoshiki Watanabe, Hiroshi |
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| score |
7.4021854 |