Source:http://linkedlifedata.com/resource/pubmed/id/15140223
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2004-5-13
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pubmed:abstractText |
The insulin-like growth factor (IGF) system plays an important role in a number of disease states, such as cancer and psoriasis, through its ability to modulate cell proliferation, attachment, and migration. The type-1 IGF and type-2 IGF receptors, as well as six IGF-binding proteins (IGFBP-1-6), have well-established roles in mediating IGF activity. Additionally, it's been demonstrated that IGF-II binds directly to the extracellular matrix protein vitronectin (VN), whereas IGF-I does not. IGFBP-5, however, has been recently demonstrated to facilitate the binding of IGF-I to VN. The aim of this study was to determine whether the interaction between IGF, IGFBP, and VN modulates human keratinocyte function. Functional assays demonstrated that both the IGF-II:VN and IGF-I:IGFBP-5:VN complexes resulted in significantly enhanced protein synthesis and cell migration through 12 microm pore Transwells in skin keratinocytes (HaCAT). Furthermore, the IGF-II:VN complex significantly enhanced human corneal epithelial (HCE) cell protein synthesis. Interestingly, the IGF-II:VN complex did not effect either HCE cell migration or attachment. This is the first study to demonstrate a functional role for the interaction between IGF and VN in human keratinocytes. Moreover, these results suggest that IGF-II:VN and IGF-I:IGFBP-5:VN complexes may be useful in situations where enhanced keratinocyte cell migration and proliferation is required, such as in wound healing and skin regeneration.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Insulin-Like Growth Factor Binding...,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin-Like Growth Factor I,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin-Like Growth Factor II,
http://linkedlifedata.com/resource/pubmed/chemical/Vitronectin
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0022-202X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
122
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1198-206
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:15140223-Cell Adhesion,
pubmed-meshheading:15140223-Cell Movement,
pubmed-meshheading:15140223-Cells, Cultured,
pubmed-meshheading:15140223-Dimerization,
pubmed-meshheading:15140223-Humans,
pubmed-meshheading:15140223-Insulin-Like Growth Factor Binding Protein 5,
pubmed-meshheading:15140223-Insulin-Like Growth Factor I,
pubmed-meshheading:15140223-Insulin-Like Growth Factor II,
pubmed-meshheading:15140223-Keratinocytes,
pubmed-meshheading:15140223-Protein Binding,
pubmed-meshheading:15140223-Protein Biosynthesis,
pubmed-meshheading:15140223-Vitronectin,
pubmed-meshheading:15140223-Wound Healing
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pubmed:year |
2004
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pubmed:articleTitle |
Insulin-like growth factors (IGF) and IGF-binding proteins bound to vitronectin enhance keratinocyte protein synthesis and migration.
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pubmed:affiliation |
Tissue BioRegeneration and Integration Program, Science Research Center, School of Life Sciences, Queensland University of Technology, Brisbane, Qld 4000, Australia. ce.hyde@student.qut.edu.au
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pubmed:publicationType |
Journal Article
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