MMP‐2 inhibits PCSK9‐induced degradation of the LDL receptor in Hepa1‐c1c7 cells
Low‐density lipoprotein receptor (LDLR) catalyzes the uptake of LDL‐cholesterol by liver and peripheral organs. The function of the LDLR is antagonized by pro‐protein convertase subtilisin/kexin type 9 (PCSK9), which binds to LDLR at the plasma membrane inducing LDLR degradation. Here, we report tha...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Wang, Xiang [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2015 |
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| Rechteinformationen: |
Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. |
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| Schlagwörter: |
Low density lipoprotein receptor Pro-protein convertase subtilisin/kexin type 9 Sterol-regulatory element binding protein Matrix Metalloproteinase 2 - physiology |
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| Übergeordnetes Werk: |
Enthalten in: FEBS letters - Amsterdam [u.a.] : Elsevier, 1968, 589(2015), 4, Seite 490-496 |
|---|---|
| Übergeordnetes Werk: |
volume:589 ; year:2015 ; number:4 ; pages:490-496 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.febslet.2015.01.007 |
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| 520 | |a Low‐density lipoprotein receptor (LDLR) catalyzes the uptake of LDL‐cholesterol by liver and peripheral organs. The function of the LDLR is antagonized by pro‐protein convertase subtilisin/kexin type 9 (PCSK9), which binds to LDLR at the plasma membrane inducing LDLR degradation. Here, we report that matrix metalloproteinase‐2 (MMP‐2) interacts with and cleaves PCSK9, as evidenced by proteomic, chemical cross‐linkage, blue native‐PAGE and domain‐specific antibodies Western blot analyses. Furthermore, MMP‐2 overexpression renders Hepa1‐c1c7 cells resistant to PCSK9‐induced LDLR degradation. The data suggest that pathological MMP‐2 overexpression may protect the LDLR from PCSK‐9‐induced degradation. We have identified a novel biological action of MMP‐2 in lipid metabolism. MMP‐2 binds and cleaves PCSK9 to reduce PCSK9‐induced degradation of LDLR. MMP‐2 overexpression may protect the LDLR from PCSK9‐induced degradation and increase LDL cholesterol uptake. | ||
| 540 | |a Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies | ||
| 540 | |a Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. | ||
| 650 | 4 | |a Atherosclerosis | |
| 650 | 4 | |a Low density lipoprotein receptor | |
| 650 | 4 | |a Pro-protein convertase subtilisin/kexin type 9 | |
| 650 | 4 | |a Sterol-regulatory element binding protein | |
| 650 | 4 | |a Cholesterol | |
| 650 | 4 | |a Matrix metalloproteinase-2 | |
| 650 | 4 | |a Matrix Metalloproteinase 2 - physiology | |
| 650 | 4 | |a Receptors, LDL - metabolism | |
| 650 | 4 | |a Serine Endopeptidases - physiology | |
| 650 | 4 | |a Proprotein Convertases - physiology | |
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| 700 | 1 | |a Sun, Difei |4 oth | |
| 700 | 1 | |a Adijiang, Ayinuer |4 oth | |
| 700 | 1 | |a Li, Liang |4 oth | |
| 700 | 1 | |a Zhang, Dawei |4 oth | |
| 700 | 1 | |a Fernandez-Patron, Carlos |4 oth | |
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10.1016/j.febslet.2015.01.007 doi PQ20160617 (DE-627)OLC196554584X (DE-599)GBVOLC196554584X (PRQ)c170X-138362f51e95f7b94b6f6b1ec528b3f293af255bc36284ba91ec819c0a3b39700 (KEY)0045922420150000589000400490mmp2inhibitspcsk9induceddegradationoftheldlrecepto DE-627 ger DE-627 rakwb eng 570 530 610 DNB Wang, Xiang verfasserin aut MMP‐2 inhibits PCSK9‐induced degradation of the LDL receptor in Hepa1‐c1c7 cells 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Low‐density lipoprotein receptor (LDLR) catalyzes the uptake of LDL‐cholesterol by liver and peripheral organs. The function of the LDLR is antagonized by pro‐protein convertase subtilisin/kexin type 9 (PCSK9), which binds to LDLR at the plasma membrane inducing LDLR degradation. Here, we report that matrix metalloproteinase‐2 (MMP‐2) interacts with and cleaves PCSK9, as evidenced by proteomic, chemical cross‐linkage, blue native‐PAGE and domain‐specific antibodies Western blot analyses. Furthermore, MMP‐2 overexpression renders Hepa1‐c1c7 cells resistant to PCSK9‐induced LDLR degradation. The data suggest that pathological MMP‐2 overexpression may protect the LDLR from PCSK‐9‐induced degradation. We have identified a novel biological action of MMP‐2 in lipid metabolism. MMP‐2 binds and cleaves PCSK9 to reduce PCSK9‐induced degradation of LDLR. MMP‐2 overexpression may protect the LDLR from PCSK9‐induced degradation and increase LDL cholesterol uptake. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Atherosclerosis Low density lipoprotein receptor Pro-protein convertase subtilisin/kexin type 9 Sterol-regulatory element binding protein Cholesterol Matrix metalloproteinase-2 Matrix Metalloproteinase 2 - physiology Receptors, LDL - metabolism Serine Endopeptidases - physiology Proprotein Convertases - physiology Berry, Evan oth Hernandez-Anzaldo, Samuel oth Sun, Difei oth Adijiang, Ayinuer oth Li, Liang oth Zhang, Dawei oth Fernandez-Patron, Carlos oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 4, Seite 490-496 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:4 pages:490-496 http://dx.doi.org/10.1016/j.febslet.2015.01.007 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.01.007/abstract http://www.ncbi.nlm.nih.gov/pubmed/25613181 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 4 490-496 |
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10.1016/j.febslet.2015.01.007 doi PQ20160617 (DE-627)OLC196554584X (DE-599)GBVOLC196554584X (PRQ)c170X-138362f51e95f7b94b6f6b1ec528b3f293af255bc36284ba91ec819c0a3b39700 (KEY)0045922420150000589000400490mmp2inhibitspcsk9induceddegradationoftheldlrecepto DE-627 ger DE-627 rakwb eng 570 530 610 DNB Wang, Xiang verfasserin aut MMP‐2 inhibits PCSK9‐induced degradation of the LDL receptor in Hepa1‐c1c7 cells 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Low‐density lipoprotein receptor (LDLR) catalyzes the uptake of LDL‐cholesterol by liver and peripheral organs. The function of the LDLR is antagonized by pro‐protein convertase subtilisin/kexin type 9 (PCSK9), which binds to LDLR at the plasma membrane inducing LDLR degradation. Here, we report that matrix metalloproteinase‐2 (MMP‐2) interacts with and cleaves PCSK9, as evidenced by proteomic, chemical cross‐linkage, blue native‐PAGE and domain‐specific antibodies Western blot analyses. Furthermore, MMP‐2 overexpression renders Hepa1‐c1c7 cells resistant to PCSK9‐induced LDLR degradation. The data suggest that pathological MMP‐2 overexpression may protect the LDLR from PCSK‐9‐induced degradation. We have identified a novel biological action of MMP‐2 in lipid metabolism. MMP‐2 binds and cleaves PCSK9 to reduce PCSK9‐induced degradation of LDLR. MMP‐2 overexpression may protect the LDLR from PCSK9‐induced degradation and increase LDL cholesterol uptake. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Atherosclerosis Low density lipoprotein receptor Pro-protein convertase subtilisin/kexin type 9 Sterol-regulatory element binding protein Cholesterol Matrix metalloproteinase-2 Matrix Metalloproteinase 2 - physiology Receptors, LDL - metabolism Serine Endopeptidases - physiology Proprotein Convertases - physiology Berry, Evan oth Hernandez-Anzaldo, Samuel oth Sun, Difei oth Adijiang, Ayinuer oth Li, Liang oth Zhang, Dawei oth Fernandez-Patron, Carlos oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 4, Seite 490-496 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:4 pages:490-496 http://dx.doi.org/10.1016/j.febslet.2015.01.007 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.01.007/abstract http://www.ncbi.nlm.nih.gov/pubmed/25613181 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 4 490-496 |
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10.1016/j.febslet.2015.01.007 doi PQ20160617 (DE-627)OLC196554584X (DE-599)GBVOLC196554584X (PRQ)c170X-138362f51e95f7b94b6f6b1ec528b3f293af255bc36284ba91ec819c0a3b39700 (KEY)0045922420150000589000400490mmp2inhibitspcsk9induceddegradationoftheldlrecepto DE-627 ger DE-627 rakwb eng 570 530 610 DNB Wang, Xiang verfasserin aut MMP‐2 inhibits PCSK9‐induced degradation of the LDL receptor in Hepa1‐c1c7 cells 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Low‐density lipoprotein receptor (LDLR) catalyzes the uptake of LDL‐cholesterol by liver and peripheral organs. The function of the LDLR is antagonized by pro‐protein convertase subtilisin/kexin type 9 (PCSK9), which binds to LDLR at the plasma membrane inducing LDLR degradation. Here, we report that matrix metalloproteinase‐2 (MMP‐2) interacts with and cleaves PCSK9, as evidenced by proteomic, chemical cross‐linkage, blue native‐PAGE and domain‐specific antibodies Western blot analyses. Furthermore, MMP‐2 overexpression renders Hepa1‐c1c7 cells resistant to PCSK9‐induced LDLR degradation. The data suggest that pathological MMP‐2 overexpression may protect the LDLR from PCSK‐9‐induced degradation. We have identified a novel biological action of MMP‐2 in lipid metabolism. MMP‐2 binds and cleaves PCSK9 to reduce PCSK9‐induced degradation of LDLR. MMP‐2 overexpression may protect the LDLR from PCSK9‐induced degradation and increase LDL cholesterol uptake. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Atherosclerosis Low density lipoprotein receptor Pro-protein convertase subtilisin/kexin type 9 Sterol-regulatory element binding protein Cholesterol Matrix metalloproteinase-2 Matrix Metalloproteinase 2 - physiology Receptors, LDL - metabolism Serine Endopeptidases - physiology Proprotein Convertases - physiology Berry, Evan oth Hernandez-Anzaldo, Samuel oth Sun, Difei oth Adijiang, Ayinuer oth Li, Liang oth Zhang, Dawei oth Fernandez-Patron, Carlos oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 4, Seite 490-496 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:4 pages:490-496 http://dx.doi.org/10.1016/j.febslet.2015.01.007 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.01.007/abstract http://www.ncbi.nlm.nih.gov/pubmed/25613181 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 4 490-496 |
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10.1016/j.febslet.2015.01.007 doi PQ20160617 (DE-627)OLC196554584X (DE-599)GBVOLC196554584X (PRQ)c170X-138362f51e95f7b94b6f6b1ec528b3f293af255bc36284ba91ec819c0a3b39700 (KEY)0045922420150000589000400490mmp2inhibitspcsk9induceddegradationoftheldlrecepto DE-627 ger DE-627 rakwb eng 570 530 610 DNB Wang, Xiang verfasserin aut MMP‐2 inhibits PCSK9‐induced degradation of the LDL receptor in Hepa1‐c1c7 cells 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Low‐density lipoprotein receptor (LDLR) catalyzes the uptake of LDL‐cholesterol by liver and peripheral organs. The function of the LDLR is antagonized by pro‐protein convertase subtilisin/kexin type 9 (PCSK9), which binds to LDLR at the plasma membrane inducing LDLR degradation. Here, we report that matrix metalloproteinase‐2 (MMP‐2) interacts with and cleaves PCSK9, as evidenced by proteomic, chemical cross‐linkage, blue native‐PAGE and domain‐specific antibodies Western blot analyses. Furthermore, MMP‐2 overexpression renders Hepa1‐c1c7 cells resistant to PCSK9‐induced LDLR degradation. The data suggest that pathological MMP‐2 overexpression may protect the LDLR from PCSK‐9‐induced degradation. We have identified a novel biological action of MMP‐2 in lipid metabolism. MMP‐2 binds and cleaves PCSK9 to reduce PCSK9‐induced degradation of LDLR. MMP‐2 overexpression may protect the LDLR from PCSK9‐induced degradation and increase LDL cholesterol uptake. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Atherosclerosis Low density lipoprotein receptor Pro-protein convertase subtilisin/kexin type 9 Sterol-regulatory element binding protein Cholesterol Matrix metalloproteinase-2 Matrix Metalloproteinase 2 - physiology Receptors, LDL - metabolism Serine Endopeptidases - physiology Proprotein Convertases - physiology Berry, Evan oth Hernandez-Anzaldo, Samuel oth Sun, Difei oth Adijiang, Ayinuer oth Li, Liang oth Zhang, Dawei oth Fernandez-Patron, Carlos oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 4, Seite 490-496 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:4 pages:490-496 http://dx.doi.org/10.1016/j.febslet.2015.01.007 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.01.007/abstract http://www.ncbi.nlm.nih.gov/pubmed/25613181 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 4 490-496 |
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10.1016/j.febslet.2015.01.007 doi PQ20160617 (DE-627)OLC196554584X (DE-599)GBVOLC196554584X (PRQ)c170X-138362f51e95f7b94b6f6b1ec528b3f293af255bc36284ba91ec819c0a3b39700 (KEY)0045922420150000589000400490mmp2inhibitspcsk9induceddegradationoftheldlrecepto DE-627 ger DE-627 rakwb eng 570 530 610 DNB Wang, Xiang verfasserin aut MMP‐2 inhibits PCSK9‐induced degradation of the LDL receptor in Hepa1‐c1c7 cells 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Low‐density lipoprotein receptor (LDLR) catalyzes the uptake of LDL‐cholesterol by liver and peripheral organs. The function of the LDLR is antagonized by pro‐protein convertase subtilisin/kexin type 9 (PCSK9), which binds to LDLR at the plasma membrane inducing LDLR degradation. Here, we report that matrix metalloproteinase‐2 (MMP‐2) interacts with and cleaves PCSK9, as evidenced by proteomic, chemical cross‐linkage, blue native‐PAGE and domain‐specific antibodies Western blot analyses. Furthermore, MMP‐2 overexpression renders Hepa1‐c1c7 cells resistant to PCSK9‐induced LDLR degradation. The data suggest that pathological MMP‐2 overexpression may protect the LDLR from PCSK‐9‐induced degradation. We have identified a novel biological action of MMP‐2 in lipid metabolism. MMP‐2 binds and cleaves PCSK9 to reduce PCSK9‐induced degradation of LDLR. MMP‐2 overexpression may protect the LDLR from PCSK9‐induced degradation and increase LDL cholesterol uptake. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Atherosclerosis Low density lipoprotein receptor Pro-protein convertase subtilisin/kexin type 9 Sterol-regulatory element binding protein Cholesterol Matrix metalloproteinase-2 Matrix Metalloproteinase 2 - physiology Receptors, LDL - metabolism Serine Endopeptidases - physiology Proprotein Convertases - physiology Berry, Evan oth Hernandez-Anzaldo, Samuel oth Sun, Difei oth Adijiang, Ayinuer oth Li, Liang oth Zhang, Dawei oth Fernandez-Patron, Carlos oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 4, Seite 490-496 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:4 pages:490-496 http://dx.doi.org/10.1016/j.febslet.2015.01.007 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.01.007/abstract http://www.ncbi.nlm.nih.gov/pubmed/25613181 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 4 490-496 |
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MMP‐2 inhibits PCSK9‐induced degradation of the LDL receptor in Hepa1‐c1c7 cells |
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mmp‐2 inhibits pcsk9‐induced degradation of the ldl receptor in hepa1‐c1c7 cells |
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MMP‐2 inhibits PCSK9‐induced degradation of the LDL receptor in Hepa1‐c1c7 cells |
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Low‐density lipoprotein receptor (LDLR) catalyzes the uptake of LDL‐cholesterol by liver and peripheral organs. The function of the LDLR is antagonized by pro‐protein convertase subtilisin/kexin type 9 (PCSK9), which binds to LDLR at the plasma membrane inducing LDLR degradation. Here, we report that matrix metalloproteinase‐2 (MMP‐2) interacts with and cleaves PCSK9, as evidenced by proteomic, chemical cross‐linkage, blue native‐PAGE and domain‐specific antibodies Western blot analyses. Furthermore, MMP‐2 overexpression renders Hepa1‐c1c7 cells resistant to PCSK9‐induced LDLR degradation. The data suggest that pathological MMP‐2 overexpression may protect the LDLR from PCSK‐9‐induced degradation. We have identified a novel biological action of MMP‐2 in lipid metabolism. MMP‐2 binds and cleaves PCSK9 to reduce PCSK9‐induced degradation of LDLR. MMP‐2 overexpression may protect the LDLR from PCSK9‐induced degradation and increase LDL cholesterol uptake. |
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Low‐density lipoprotein receptor (LDLR) catalyzes the uptake of LDL‐cholesterol by liver and peripheral organs. The function of the LDLR is antagonized by pro‐protein convertase subtilisin/kexin type 9 (PCSK9), which binds to LDLR at the plasma membrane inducing LDLR degradation. Here, we report that matrix metalloproteinase‐2 (MMP‐2) interacts with and cleaves PCSK9, as evidenced by proteomic, chemical cross‐linkage, blue native‐PAGE and domain‐specific antibodies Western blot analyses. Furthermore, MMP‐2 overexpression renders Hepa1‐c1c7 cells resistant to PCSK9‐induced LDLR degradation. The data suggest that pathological MMP‐2 overexpression may protect the LDLR from PCSK‐9‐induced degradation. We have identified a novel biological action of MMP‐2 in lipid metabolism. MMP‐2 binds and cleaves PCSK9 to reduce PCSK9‐induced degradation of LDLR. MMP‐2 overexpression may protect the LDLR from PCSK9‐induced degradation and increase LDL cholesterol uptake. |
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Low‐density lipoprotein receptor (LDLR) catalyzes the uptake of LDL‐cholesterol by liver and peripheral organs. The function of the LDLR is antagonized by pro‐protein convertase subtilisin/kexin type 9 (PCSK9), which binds to LDLR at the plasma membrane inducing LDLR degradation. Here, we report that matrix metalloproteinase‐2 (MMP‐2) interacts with and cleaves PCSK9, as evidenced by proteomic, chemical cross‐linkage, blue native‐PAGE and domain‐specific antibodies Western blot analyses. Furthermore, MMP‐2 overexpression renders Hepa1‐c1c7 cells resistant to PCSK9‐induced LDLR degradation. The data suggest that pathological MMP‐2 overexpression may protect the LDLR from PCSK‐9‐induced degradation. We have identified a novel biological action of MMP‐2 in lipid metabolism. MMP‐2 binds and cleaves PCSK9 to reduce PCSK9‐induced degradation of LDLR. MMP‐2 overexpression may protect the LDLR from PCSK9‐induced degradation and increase LDL cholesterol uptake. |
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MMP‐2 inhibits PCSK9‐induced degradation of the LDL receptor in Hepa1‐c1c7 cells |
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The function of the LDLR is antagonized by pro‐protein convertase subtilisin/kexin type 9 (PCSK9), which binds to LDLR at the plasma membrane inducing LDLR degradation. Here, we report that matrix metalloproteinase‐2 (MMP‐2) interacts with and cleaves PCSK9, as evidenced by proteomic, chemical cross‐linkage, blue native‐PAGE and domain‐specific antibodies Western blot analyses. Furthermore, MMP‐2 overexpression renders Hepa1‐c1c7 cells resistant to PCSK9‐induced LDLR degradation. The data suggest that pathological MMP‐2 overexpression may protect the LDLR from PCSK‐9‐induced degradation. We have identified a novel biological action of MMP‐2 in lipid metabolism. MMP‐2 binds and cleaves PCSK9 to reduce PCSK9‐induced degradation of LDLR. MMP‐2 overexpression may protect the LDLR from PCSK9‐induced degradation and increase LDL cholesterol uptake.</subfield></datafield><datafield tag="540" ind1=" " ind2=" "><subfield code="a">Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies</subfield></datafield><datafield tag="540" ind1=" " ind2=" "><subfield code="a">Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Atherosclerosis</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Low density lipoprotein receptor</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Pro-protein convertase subtilisin/kexin type 9</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Sterol-regulatory element binding protein</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Cholesterol</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Matrix metalloproteinase-2</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Matrix Metalloproteinase 2 - physiology</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Receptors, LDL - metabolism</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Serine Endopeptidases - physiology</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Proprotein Convertases - physiology</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Berry, Evan</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Hernandez-Anzaldo, Samuel</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Sun, Difei</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Adijiang, Ayinuer</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Li, Liang</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Zhang, Dawei</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Fernandez-Patron, Carlos</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">FEBS letters</subfield><subfield code="d">Amsterdam [u.a.] : Elsevier, 1968</subfield><subfield code="g">589(2015), 4, Seite 490-496</subfield><subfield code="w">(DE-627)129522023</subfield><subfield code="w">(DE-600)212746-5</subfield><subfield code="w">(DE-576)014938014</subfield><subfield code="x">0014-5793</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:589</subfield><subfield code="g">year:2015</subfield><subfield code="g">number:4</subfield><subfield code="g">pages:490-496</subfield></datafield><datafield tag="856" ind1="4" ind2="1"><subfield code="u">http://dx.doi.org/10.1016/j.febslet.2015.01.007</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.01.007/abstract</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">http://www.ncbi.nlm.nih.gov/pubmed/25613181</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_OLC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHY</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-CHE</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHA</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-DE-84</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_21</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_70</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_211</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2219</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4012</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4125</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4219</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4305</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">589</subfield><subfield code="j">2015</subfield><subfield code="e">4</subfield><subfield code="h">490-496</subfield></datafield></record></collection>
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