Source:http://linkedlifedata.com/resource/pubmed/id/20008810
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2009-12-17
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pubmed:abstractText |
Glypican-1 is a cell membrane heparan sulfate proteoglycan that is composed of a core protein and covalently attached glycosaminoglycan (GAG) chains and N-linked glycosylated (N-glycosylated) chains. The glypican-1 GAG chains are required for cell differentiation and responsiveness to fibroblast growth factor 2 (FGF2). The role of glypican-1 N-glycosylated chains in regulating cell activities has not been reported. The objective of the current study was to investigate the role of glypican-1 N-glycosylated chains and the interaction between N-glycosylated and GAG chains in turkey myogenic satellite cell proliferation, differentiation, and FGF2 responsiveness. The wild-type turkey glypican-1 and turkey glypican-1 with mutated GAG chain attachment sites were cloned into the pCMS-EGFP mammalian expression vector and were used as templates to generate glypican-1 N-glycosylated 1-chain and no-chain mutants with or without GAG chains by site-directed mutagenesis. The wild-type glypican-1 and all glypican-1 N-glycosylated 1-chain and no-chain mutants with or without GAG chains were transfected into turkey myogenic satellite cells. Cell proliferation, differentiation, and FGF2 responsiveness were measured. The overexpression of glypican-1 N-glycosylated 1-chain and no-chain mutants without GAG chains increased cell proliferation and differentiation compared with the wild-type glypican-1 but not the glypican-1 N-glycosylated mutants with GAG chains attached. Cells overexpressing glypican-1 N-glycosylated mutants with or without GAG chains increased cell responsiveness to FGF2 compared with wild-type glypican-1. These data suggest that glypican-1 N-glycosylated chains and GAG chains are critical in regulating turkey myogenic satellite cell proliferation, differentiation, and responsivness to FGF2.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0032-5791
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
89
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
123-34
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pubmed:meshHeading |
pubmed-meshheading:20008810-Animals,
pubmed-meshheading:20008810-Cell Differentiation,
pubmed-meshheading:20008810-Cell Proliferation,
pubmed-meshheading:20008810-Cells, Cultured,
pubmed-meshheading:20008810-Fibroblast Growth Factor 2,
pubmed-meshheading:20008810-Gene Expression Regulation,
pubmed-meshheading:20008810-Glypicans,
pubmed-meshheading:20008810-Mutagenesis, Site-Directed,
pubmed-meshheading:20008810-Mutation,
pubmed-meshheading:20008810-Satellite Cells, Skeletal Muscle,
pubmed-meshheading:20008810-Turkeys
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pubmed:year |
2010
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pubmed:articleTitle |
Effect of glypican-1 covalently attached chains on turkey myogenic satellite cell proliferation, differentiation, and fibroblast growth factor 2 responsiveness.
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pubmed:affiliation |
Department of Animal Sciences, Ohio Agricultural Research and Development Center, The Ohio State University, Wooster 44691, USA.
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pubmed:publicationType |
Journal Article
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