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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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Autores principales: Nishimoto, Satoru Ken, Nishimoto, Miyako
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4158265/
https://www.ncbi.nlm.nih.gov/pubmed/25210519
http://dx.doi.org/10.1155/2014/807013
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author Nishimoto, Satoru Ken
Nishimoto, Miyako
author_facet Nishimoto, Satoru Ken
Nishimoto, Miyako
author_sort Nishimoto, Satoru Ken
collection PubMed
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.
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spelling pubmed-41582652014-09-10 Matrix Gla Protein Binds to Fibronectin and Enhances Cell Attachment and Spreading on Fibronectin Nishimoto, Satoru Ken Nishimoto, Miyako Int J Cell Biol Research Article 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. Hindawi Publishing Corporation 2014 2014-08-21 /pmc/articles/PMC4158265/ /pubmed/25210519 http://dx.doi.org/10.1155/2014/807013 Text en Copyright © 2014 S. K. Nishimoto and M. Nishimoto. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Nishimoto, Satoru Ken
Nishimoto, Miyako
Matrix Gla Protein Binds to Fibronectin and Enhances Cell Attachment and Spreading on Fibronectin
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
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4158265/
https://www.ncbi.nlm.nih.gov/pubmed/25210519
http://dx.doi.org/10.1155/2014/807013
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