Matrix Gla Protein Binds to Fibronectin and Enhances Cell Attachment and Spreading on Fibronectin
Background. Matrix Gla protein (MGP) is a vitamin K-dependent, extracellular matrix protein. MGP is a calcification inhibitor of arteries and cartilage. However MGP is synthesized in many tissues and is especially enriched in embryonic tissues and in cancer cells. The presence of MGP in those instan...
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| Format: | Article |
| Language: | English |
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Wiley
2014-01-01
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| Series: | International Journal of Cell Biology |
| Online Access: | http://dx.doi.org/10.1155/2014/807013 |
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| _version_ | 1832565244886515712 |
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| author | Satoru Ken Nishimoto Miyako Nishimoto |
| author_facet | Satoru Ken Nishimoto Miyako Nishimoto |
| author_sort | Satoru Ken Nishimoto |
| collection | DOAJ |
| description | Background. Matrix Gla protein (MGP) is a vitamin K-dependent, extracellular matrix protein. MGP is a calcification inhibitor of arteries and cartilage. However MGP is synthesized in many tissues and is especially enriched in embryonic tissues and in cancer cells. The presence of MGP in those instances does not correlate well with the calcification inhibitory role. This study explores a potential mechanism for MGP to bind to matrix proteins and alter cell matrix interactions. Methods. To determine whether MGP influences cell behavior through interaction with fibronectin, we studied MGP binding to fibronectin, the effect of MGP on fibronectin mediated cell attachment and spreading and immunolocalized MGP and fibronectin.
Results. First, MGP binds to fibronectin. The binding site for MGP is in a specific fibronectin fragment, called III1-C or anastellin. The binding site for fibronectin is in a MGP C-terminal peptide comprising amino acids 61–77. Second, MGP enhances cell attachment and cell spreading on fibronectin. MGP alone does not promote cell adhesion. Third, MGP is present in fibronectin-rich regions of tissue sections. Conclusions. MGP binds to fibronectin. The presence of MGP increased cell-fibronectin interactions. |
| format | Article |
| id | doaj-art-7c5ca8cdb17e48b4b93179575700d3c5 |
| institution | Kabale University |
| issn | 1687-8876 1687-8884 |
| language | English |
| publishDate | 2014-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | International Journal of Cell Biology |
| spelling | doaj-art-7c5ca8cdb17e48b4b93179575700d3c52025-02-03T01:08:57ZengWileyInternational Journal of Cell Biology1687-88761687-88842014-01-01201410.1155/2014/807013807013Matrix Gla Protein Binds to Fibronectin and Enhances Cell Attachment and Spreading on FibronectinSatoru Ken Nishimoto0Miyako Nishimoto1Department of Microbiology, Immunology, and Biochemistry, University of Tennessee Health Science Center, Memphis, TN, USADepartment of Microbiology, Immunology, and Biochemistry, University of Tennessee Health Science Center, Memphis, TN, USABackground. Matrix Gla protein (MGP) is a vitamin K-dependent, extracellular matrix protein. MGP is a calcification inhibitor of arteries and cartilage. However MGP is synthesized in many tissues and is especially enriched in embryonic tissues and in cancer cells. The presence of MGP in those instances does not correlate well with the calcification inhibitory role. This study explores a potential mechanism for MGP to bind to matrix proteins and alter cell matrix interactions. Methods. To determine whether MGP influences cell behavior through interaction with fibronectin, we studied MGP binding to fibronectin, the effect of MGP on fibronectin mediated cell attachment and spreading and immunolocalized MGP and fibronectin. Results. First, MGP binds to fibronectin. The binding site for MGP is in a specific fibronectin fragment, called III1-C or anastellin. The binding site for fibronectin is in a MGP C-terminal peptide comprising amino acids 61–77. Second, MGP enhances cell attachment and cell spreading on fibronectin. MGP alone does not promote cell adhesion. Third, MGP is present in fibronectin-rich regions of tissue sections. Conclusions. MGP binds to fibronectin. The presence of MGP increased cell-fibronectin interactions.http://dx.doi.org/10.1155/2014/807013 |
| spellingShingle | Satoru Ken Nishimoto Miyako Nishimoto Matrix Gla Protein Binds to Fibronectin and Enhances Cell Attachment and Spreading on Fibronectin International Journal of Cell Biology |
| title | Matrix Gla Protein Binds to Fibronectin and Enhances Cell Attachment and Spreading on Fibronectin |
| title_full | Matrix Gla Protein Binds to Fibronectin and Enhances Cell Attachment and Spreading on Fibronectin |
| title_fullStr | Matrix Gla Protein Binds to Fibronectin and Enhances Cell Attachment and Spreading on Fibronectin |
| title_full_unstemmed | Matrix Gla Protein Binds to Fibronectin and Enhances Cell Attachment and Spreading on Fibronectin |
| title_short | Matrix Gla Protein Binds to Fibronectin and Enhances Cell Attachment and Spreading on Fibronectin |
| title_sort | matrix gla protein binds to fibronectin and enhances cell attachment and spreading on fibronectin |
| url | http://dx.doi.org/10.1155/2014/807013 |
| work_keys_str_mv | AT satorukennishimoto matrixglaproteinbindstofibronectinandenhancescellattachmentandspreadingonfibronectin AT miyakonishimoto matrixglaproteinbindstofibronectinandenhancescellattachmentandspreadingonfibronectin |