P15 peptide stimulates chondrogenic commitment and endochondral ossification View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2017-07

AUTHORS

Jun Zhang, Peter Eisenhauer, Ozҫan Kaya, Alexander R. Vaccaro, Carol Diallo, Andrzej Fertala, Theresa A. Freeman

ABSTRACT

PURPOSE: The synthetic 15 amino acid biomimetic peptide sequence (P15) derived from a region of the alpha (α)-1 chain of collagen I, has been shown to promote α2 integrin activation and enhance intramembranous ossification. In this study, we ask if the P15 peptide also enhances bone formation through endochondral ossification, and determine if direct binding of α2 integrin with P15 mediates integrin activation. METHODS: Mesenchymal cells (C3H10T1/2) were cultured in chondrogenic media and the expression of chondrogenic markers and integrin activation was determined by Western blot and fluorescent immunohistochemistry. A biosensor assay was used to determine if binding occurred between P15 and α2 β1 integrin. Finally, an in vivo model of endochondral ossification was used to determine the effect of P15 on bone formation. RESULTS: In the presence of P15, chondrogenesis and activation of α5 integrin were enhanced, as observed by both Western blot analysis and immunoflourescent staining. A biosensor assay investigating the specificity of the interaction between P15 with α2β1 integrin determined direct binding does not occur. When P15 was added to Matrigel implanted in a murine endochondral ossification model, in the presence of bone morphogenic protein-2 (BMP-2), a significant increase in chondrocyte differentiation and mineralization was observed. CONCLUSION: P15 does not directly activate integrins by binding, but does upregulate integrin signaling to enhance differentiation of both osteoblasts and chondrocytes to increase both intramembranous and endochondral bone formation. More... »

PAGES

1413-1422

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00264-017-3464-8

DOI

http://dx.doi.org/10.1007/s00264-017-3464-8

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1084517484

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/28389839


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    "description": "PURPOSE: The synthetic 15 amino acid biomimetic peptide sequence (P15) derived from a region of the alpha (\u03b1)-1 chain of collagen I, has been shown to promote \u03b12 integrin activation and enhance intramembranous ossification. In this study, we ask if the P15 peptide also enhances bone formation through endochondral ossification, and determine if direct binding of \u03b12 integrin with P15 mediates integrin activation.\nMETHODS: Mesenchymal cells (C3H10T1/2) were cultured in chondrogenic media and the expression of chondrogenic markers and integrin activation was determined by Western blot and fluorescent immunohistochemistry. A biosensor assay was used to determine if binding occurred between P15 and \u03b12 \u03b21 integrin. Finally, an in vivo model of endochondral ossification was used to determine the effect of P15 on bone formation.\nRESULTS: In the presence of P15, chondrogenesis and activation of \u03b15 integrin were enhanced, as observed by both Western blot analysis and immunoflourescent staining. A biosensor assay investigating the specificity of the interaction between P15 with \u03b12\u03b21 integrin determined direct binding does not occur. When P15 was added to Matrigel implanted in a murine endochondral ossification model, in the presence of bone morphogenic protein-2 (BMP-2), a significant increase in chondrocyte differentiation and mineralization was observed.\nCONCLUSION: P15 does not directly activate integrins by binding, but does upregulate integrin signaling to enhance differentiation of both osteoblasts and chondrocytes to increase both intramembranous and endochondral bone formation.", 
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Download the RDF metadata as:  json-ld nt turtle xml License info

HOW TO GET THIS DATA PROGRAMMATICALLY:

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curl -H 'Accept: application/ld+json' 'https://scigraph.springernature.com/pub.10.1007/s00264-017-3464-8'

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Turtle is a human-readable linked data format.

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RDF/XML is a standard XML format for linked data.

curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1007/s00264-017-3464-8'


 

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