Plasminogen-dependent internalization of soluble melanotransferrin involves the low-density lipoprotein receptor-related protein and annexin II
We investigated the effect of plasminogen (Plg) on the internalization of recombinant soluble melanotransferrin (sMTf) using U87 human glioblastoma cells and murine embryonic fibroblasts (MEF) deficient in the low-density lipoprotein receptor-related protein (LRP). Using biospecific interaction anal...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Michaud-Levesque, Jonathan [verfasserIn] Demeule, Michel [verfasserIn] Béliveau, Richard [verfasserIn] |
|---|
| Format: |
E-Artikel |
|---|
| Erschienen: |
Walter de Gruyter ; 2007 |
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| Schlagwörter: |
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| Anmerkung: |
©2007 by Walter de Gruyter Berlin New York |
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| Umfang: |
8 |
| Reproduktion: |
Walter de Gruyter Online Zeitschriften |
|---|---|
| Übergeordnetes Werk: |
Enthalten in: Biological chemistry - Berlin [u.a.] : de Gruyter, 1996, 388(2007), 7 vom: 01. Juli, Seite 747-754 |
| Übergeordnetes Werk: |
volume:388 ; year:2007 ; number:7 ; day:01 ; month:07 ; pages:747-754 ; extent:8 |
| Links: |
|---|
| DOI / URN: |
10.1515/BC.2007.081 |
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NLEJ246523204 |
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| 520 | |a We investigated the effect of plasminogen (Plg) on the internalization of recombinant soluble melanotransferrin (sMTf) using U87 human glioblastoma cells and murine embryonic fibroblasts (MEF) deficient in the low-density lipoprotein receptor-related protein (LRP). Using biospecific interaction analysis, both Glu- and Lys-Plg were shown to interact with immobilized sMTf. The binding of sMTf at the cell surface increased in the presence of both forms of Plg in control and in LRP-deficient MEF cells, whereas the uptake was strongly stimulated only by Lys-Plg in control MEF and U87 cells. In addition, in the presence of Lys-Plg, the internalization of sMTf was a saturable process, sensitive to temperature and dependent on the integrity of lysine residues. The addition of the receptor-associated protein, lactoferrin and aprotinin, as well as a monoclonal antibody (mAb) directed against LRP, inhibited the Lys-Plg-dependent uptake of sMTf. These results suggest an important role for LRP in this process. In addition, using binding and uptake assays in the presence of anti-annexin II mAb, we showed that annexin II might be responsible for the initial binding of sMTf in the presence of Plg. Our results suggest a Plg-mediated internalization mechanism for the clearance of sMTf via annexin II and LRP. | ||
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10.1515/BC.2007.081 doi artikel_Grundlieferung.pp (DE-627)NLEJ246523204 DE-627 ger DE-627 rakwb Michaud-Levesque, Jonathan verfasserin aut Plasminogen-dependent internalization of soluble melanotransferrin involves the low-density lipoprotein receptor-related protein and annexin II Walter de Gruyter 2007 8 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ©2007 by Walter de Gruyter Berlin New York We investigated the effect of plasminogen (Plg) on the internalization of recombinant soluble melanotransferrin (sMTf) using U87 human glioblastoma cells and murine embryonic fibroblasts (MEF) deficient in the low-density lipoprotein receptor-related protein (LRP). Using biospecific interaction analysis, both Glu- and Lys-Plg were shown to interact with immobilized sMTf. The binding of sMTf at the cell surface increased in the presence of both forms of Plg in control and in LRP-deficient MEF cells, whereas the uptake was strongly stimulated only by Lys-Plg in control MEF and U87 cells. In addition, in the presence of Lys-Plg, the internalization of sMTf was a saturable process, sensitive to temperature and dependent on the integrity of lysine residues. The addition of the receptor-associated protein, lactoferrin and aprotinin, as well as a monoclonal antibody (mAb) directed against LRP, inhibited the Lys-Plg-dependent uptake of sMTf. These results suggest an important role for LRP in this process. In addition, using binding and uptake assays in the presence of anti-annexin II mAb, we showed that annexin II might be responsible for the initial binding of sMTf in the presence of Plg. Our results suggest a Plg-mediated internalization mechanism for the clearance of sMTf via annexin II and LRP. Walter de Gruyter Online Zeitschriften annexin II endocytosis low-density lipoprotein receptor-related protein plasminogen soluble melanotransferrin Demeule, Michel verfasserin aut Béliveau, Richard verfasserin aut Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 388(2007), 7 vom: 01. Juli, Seite 747-754 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:388 year:2007 number:7 day:01 month:07 pages:747-754 extent:8 https://doi.org/10.1515/BC.2007.081 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 388 2007 7 01 07 747-754 8 |
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10.1515/BC.2007.081 doi artikel_Grundlieferung.pp (DE-627)NLEJ246523204 DE-627 ger DE-627 rakwb Michaud-Levesque, Jonathan verfasserin aut Plasminogen-dependent internalization of soluble melanotransferrin involves the low-density lipoprotein receptor-related protein and annexin II Walter de Gruyter 2007 8 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ©2007 by Walter de Gruyter Berlin New York We investigated the effect of plasminogen (Plg) on the internalization of recombinant soluble melanotransferrin (sMTf) using U87 human glioblastoma cells and murine embryonic fibroblasts (MEF) deficient in the low-density lipoprotein receptor-related protein (LRP). Using biospecific interaction analysis, both Glu- and Lys-Plg were shown to interact with immobilized sMTf. The binding of sMTf at the cell surface increased in the presence of both forms of Plg in control and in LRP-deficient MEF cells, whereas the uptake was strongly stimulated only by Lys-Plg in control MEF and U87 cells. In addition, in the presence of Lys-Plg, the internalization of sMTf was a saturable process, sensitive to temperature and dependent on the integrity of lysine residues. The addition of the receptor-associated protein, lactoferrin and aprotinin, as well as a monoclonal antibody (mAb) directed against LRP, inhibited the Lys-Plg-dependent uptake of sMTf. These results suggest an important role for LRP in this process. In addition, using binding and uptake assays in the presence of anti-annexin II mAb, we showed that annexin II might be responsible for the initial binding of sMTf in the presence of Plg. Our results suggest a Plg-mediated internalization mechanism for the clearance of sMTf via annexin II and LRP. Walter de Gruyter Online Zeitschriften annexin II endocytosis low-density lipoprotein receptor-related protein plasminogen soluble melanotransferrin Demeule, Michel verfasserin aut Béliveau, Richard verfasserin aut Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 388(2007), 7 vom: 01. Juli, Seite 747-754 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:388 year:2007 number:7 day:01 month:07 pages:747-754 extent:8 https://doi.org/10.1515/BC.2007.081 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 388 2007 7 01 07 747-754 8 |
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10.1515/BC.2007.081 doi artikel_Grundlieferung.pp (DE-627)NLEJ246523204 DE-627 ger DE-627 rakwb Michaud-Levesque, Jonathan verfasserin aut Plasminogen-dependent internalization of soluble melanotransferrin involves the low-density lipoprotein receptor-related protein and annexin II Walter de Gruyter 2007 8 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ©2007 by Walter de Gruyter Berlin New York We investigated the effect of plasminogen (Plg) on the internalization of recombinant soluble melanotransferrin (sMTf) using U87 human glioblastoma cells and murine embryonic fibroblasts (MEF) deficient in the low-density lipoprotein receptor-related protein (LRP). Using biospecific interaction analysis, both Glu- and Lys-Plg were shown to interact with immobilized sMTf. The binding of sMTf at the cell surface increased in the presence of both forms of Plg in control and in LRP-deficient MEF cells, whereas the uptake was strongly stimulated only by Lys-Plg in control MEF and U87 cells. In addition, in the presence of Lys-Plg, the internalization of sMTf was a saturable process, sensitive to temperature and dependent on the integrity of lysine residues. The addition of the receptor-associated protein, lactoferrin and aprotinin, as well as a monoclonal antibody (mAb) directed against LRP, inhibited the Lys-Plg-dependent uptake of sMTf. These results suggest an important role for LRP in this process. In addition, using binding and uptake assays in the presence of anti-annexin II mAb, we showed that annexin II might be responsible for the initial binding of sMTf in the presence of Plg. Our results suggest a Plg-mediated internalization mechanism for the clearance of sMTf via annexin II and LRP. Walter de Gruyter Online Zeitschriften annexin II endocytosis low-density lipoprotein receptor-related protein plasminogen soluble melanotransferrin Demeule, Michel verfasserin aut Béliveau, Richard verfasserin aut Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 388(2007), 7 vom: 01. Juli, Seite 747-754 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:388 year:2007 number:7 day:01 month:07 pages:747-754 extent:8 https://doi.org/10.1515/BC.2007.081 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 388 2007 7 01 07 747-754 8 |
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10.1515/BC.2007.081 doi artikel_Grundlieferung.pp (DE-627)NLEJ246523204 DE-627 ger DE-627 rakwb Michaud-Levesque, Jonathan verfasserin aut Plasminogen-dependent internalization of soluble melanotransferrin involves the low-density lipoprotein receptor-related protein and annexin II Walter de Gruyter 2007 8 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ©2007 by Walter de Gruyter Berlin New York We investigated the effect of plasminogen (Plg) on the internalization of recombinant soluble melanotransferrin (sMTf) using U87 human glioblastoma cells and murine embryonic fibroblasts (MEF) deficient in the low-density lipoprotein receptor-related protein (LRP). Using biospecific interaction analysis, both Glu- and Lys-Plg were shown to interact with immobilized sMTf. The binding of sMTf at the cell surface increased in the presence of both forms of Plg in control and in LRP-deficient MEF cells, whereas the uptake was strongly stimulated only by Lys-Plg in control MEF and U87 cells. In addition, in the presence of Lys-Plg, the internalization of sMTf was a saturable process, sensitive to temperature and dependent on the integrity of lysine residues. The addition of the receptor-associated protein, lactoferrin and aprotinin, as well as a monoclonal antibody (mAb) directed against LRP, inhibited the Lys-Plg-dependent uptake of sMTf. These results suggest an important role for LRP in this process. In addition, using binding and uptake assays in the presence of anti-annexin II mAb, we showed that annexin II might be responsible for the initial binding of sMTf in the presence of Plg. Our results suggest a Plg-mediated internalization mechanism for the clearance of sMTf via annexin II and LRP. Walter de Gruyter Online Zeitschriften annexin II endocytosis low-density lipoprotein receptor-related protein plasminogen soluble melanotransferrin Demeule, Michel verfasserin aut Béliveau, Richard verfasserin aut Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 388(2007), 7 vom: 01. Juli, Seite 747-754 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:388 year:2007 number:7 day:01 month:07 pages:747-754 extent:8 https://doi.org/10.1515/BC.2007.081 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 388 2007 7 01 07 747-754 8 |
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10.1515/BC.2007.081 doi artikel_Grundlieferung.pp (DE-627)NLEJ246523204 DE-627 ger DE-627 rakwb Michaud-Levesque, Jonathan verfasserin aut Plasminogen-dependent internalization of soluble melanotransferrin involves the low-density lipoprotein receptor-related protein and annexin II Walter de Gruyter 2007 8 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ©2007 by Walter de Gruyter Berlin New York We investigated the effect of plasminogen (Plg) on the internalization of recombinant soluble melanotransferrin (sMTf) using U87 human glioblastoma cells and murine embryonic fibroblasts (MEF) deficient in the low-density lipoprotein receptor-related protein (LRP). Using biospecific interaction analysis, both Glu- and Lys-Plg were shown to interact with immobilized sMTf. The binding of sMTf at the cell surface increased in the presence of both forms of Plg in control and in LRP-deficient MEF cells, whereas the uptake was strongly stimulated only by Lys-Plg in control MEF and U87 cells. In addition, in the presence of Lys-Plg, the internalization of sMTf was a saturable process, sensitive to temperature and dependent on the integrity of lysine residues. The addition of the receptor-associated protein, lactoferrin and aprotinin, as well as a monoclonal antibody (mAb) directed against LRP, inhibited the Lys-Plg-dependent uptake of sMTf. These results suggest an important role for LRP in this process. In addition, using binding and uptake assays in the presence of anti-annexin II mAb, we showed that annexin II might be responsible for the initial binding of sMTf in the presence of Plg. Our results suggest a Plg-mediated internalization mechanism for the clearance of sMTf via annexin II and LRP. Walter de Gruyter Online Zeitschriften annexin II endocytosis low-density lipoprotein receptor-related protein plasminogen soluble melanotransferrin Demeule, Michel verfasserin aut Béliveau, Richard verfasserin aut Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 388(2007), 7 vom: 01. Juli, Seite 747-754 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:388 year:2007 number:7 day:01 month:07 pages:747-754 extent:8 https://doi.org/10.1515/BC.2007.081 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 388 2007 7 01 07 747-754 8 |
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Plasminogen-dependent internalization of soluble melanotransferrin involves the low-density lipoprotein receptor-related protein and annexin II |
| abstract |
We investigated the effect of plasminogen (Plg) on the internalization of recombinant soluble melanotransferrin (sMTf) using U87 human glioblastoma cells and murine embryonic fibroblasts (MEF) deficient in the low-density lipoprotein receptor-related protein (LRP). Using biospecific interaction analysis, both Glu- and Lys-Plg were shown to interact with immobilized sMTf. The binding of sMTf at the cell surface increased in the presence of both forms of Plg in control and in LRP-deficient MEF cells, whereas the uptake was strongly stimulated only by Lys-Plg in control MEF and U87 cells. In addition, in the presence of Lys-Plg, the internalization of sMTf was a saturable process, sensitive to temperature and dependent on the integrity of lysine residues. The addition of the receptor-associated protein, lactoferrin and aprotinin, as well as a monoclonal antibody (mAb) directed against LRP, inhibited the Lys-Plg-dependent uptake of sMTf. These results suggest an important role for LRP in this process. In addition, using binding and uptake assays in the presence of anti-annexin II mAb, we showed that annexin II might be responsible for the initial binding of sMTf in the presence of Plg. Our results suggest a Plg-mediated internalization mechanism for the clearance of sMTf via annexin II and LRP. ©2007 by Walter de Gruyter Berlin New York |
| abstractGer |
We investigated the effect of plasminogen (Plg) on the internalization of recombinant soluble melanotransferrin (sMTf) using U87 human glioblastoma cells and murine embryonic fibroblasts (MEF) deficient in the low-density lipoprotein receptor-related protein (LRP). Using biospecific interaction analysis, both Glu- and Lys-Plg were shown to interact with immobilized sMTf. The binding of sMTf at the cell surface increased in the presence of both forms of Plg in control and in LRP-deficient MEF cells, whereas the uptake was strongly stimulated only by Lys-Plg in control MEF and U87 cells. In addition, in the presence of Lys-Plg, the internalization of sMTf was a saturable process, sensitive to temperature and dependent on the integrity of lysine residues. The addition of the receptor-associated protein, lactoferrin and aprotinin, as well as a monoclonal antibody (mAb) directed against LRP, inhibited the Lys-Plg-dependent uptake of sMTf. These results suggest an important role for LRP in this process. In addition, using binding and uptake assays in the presence of anti-annexin II mAb, we showed that annexin II might be responsible for the initial binding of sMTf in the presence of Plg. Our results suggest a Plg-mediated internalization mechanism for the clearance of sMTf via annexin II and LRP. ©2007 by Walter de Gruyter Berlin New York |
| abstract_unstemmed |
We investigated the effect of plasminogen (Plg) on the internalization of recombinant soluble melanotransferrin (sMTf) using U87 human glioblastoma cells and murine embryonic fibroblasts (MEF) deficient in the low-density lipoprotein receptor-related protein (LRP). Using biospecific interaction analysis, both Glu- and Lys-Plg were shown to interact with immobilized sMTf. The binding of sMTf at the cell surface increased in the presence of both forms of Plg in control and in LRP-deficient MEF cells, whereas the uptake was strongly stimulated only by Lys-Plg in control MEF and U87 cells. In addition, in the presence of Lys-Plg, the internalization of sMTf was a saturable process, sensitive to temperature and dependent on the integrity of lysine residues. The addition of the receptor-associated protein, lactoferrin and aprotinin, as well as a monoclonal antibody (mAb) directed against LRP, inhibited the Lys-Plg-dependent uptake of sMTf. These results suggest an important role for LRP in this process. In addition, using binding and uptake assays in the presence of anti-annexin II mAb, we showed that annexin II might be responsible for the initial binding of sMTf in the presence of Plg. Our results suggest a Plg-mediated internalization mechanism for the clearance of sMTf via annexin II and LRP. ©2007 by Walter de Gruyter Berlin New York |
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| title_short |
Plasminogen-dependent internalization of soluble melanotransferrin involves the low-density lipoprotein receptor-related protein and annexin II |
| url |
https://doi.org/10.1515/BC.2007.081 |
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| author2 |
Demeule, Michel Béliveau, Richard |
| author2Str |
Demeule, Michel Béliveau, Richard |
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| doi_str |
10.1515/BC.2007.081 |
| up_date |
2024-07-06T08:43:02.475Z |
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7.401719 |