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Effect of glypican-1 covalently attached chains on turkey myogenic satellite cell proliferation, differentiation, and fibroblast growth factor 2 responsiveness.
Poult Sci. 2010 Jan; 89(1):123-34.PS

Abstract

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.

Authors+Show Affiliations

Department of Animal Sciences, Ohio Agricultural Research and Development Center, The Ohio State University, Wooster 44691, USA.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

20008810

Citation

Song, Y, et al. "Effect of Glypican-1 Covalently Attached Chains On Turkey Myogenic Satellite Cell Proliferation, Differentiation, and Fibroblast Growth Factor 2 Responsiveness." Poultry Science, vol. 89, no. 1, 2010, pp. 123-34.
Song Y, Nestor KE, McFarland DC, et al. Effect of glypican-1 covalently attached chains on turkey myogenic satellite cell proliferation, differentiation, and fibroblast growth factor 2 responsiveness. Poult Sci. 2010;89(1):123-34.
Song, Y., Nestor, K. E., McFarland, D. C., & Velleman, S. G. (2010). Effect of glypican-1 covalently attached chains on turkey myogenic satellite cell proliferation, differentiation, and fibroblast growth factor 2 responsiveness. Poultry Science, 89(1), 123-34. https://doi.org/10.3382/ps.2009-00325
Song Y, et al. Effect of Glypican-1 Covalently Attached Chains On Turkey Myogenic Satellite Cell Proliferation, Differentiation, and Fibroblast Growth Factor 2 Responsiveness. Poult Sci. 2010;89(1):123-34. PubMed PMID: 20008810.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Effect of glypican-1 covalently attached chains on turkey myogenic satellite cell proliferation, differentiation, and fibroblast growth factor 2 responsiveness. AU - Song,Y, AU - Nestor,K E, AU - McFarland,D C, AU - Velleman,S G, PY - 2009/12/17/entrez PY - 2009/12/17/pubmed PY - 2010/2/25/medline SP - 123 EP - 34 JF - Poultry science JO - Poult Sci VL - 89 IS - 1 N2 - 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. SN - 0032-5791 UR - https://www.unboundmedicine.com/medline/citation/20008810/Effect_of_glypican_1_covalently_attached_chains_on_turkey_myogenic_satellite_cell_proliferation_differentiation_and_fibroblast_growth_factor_2_responsiveness_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0032-5791(19)42413-9 DB - PRIME DP - Unbound Medicine ER -