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Modulation of turkey myogenic satellite cell differentiation through the shedding of glypican-1.

Abstract

Glypican-1 is a cell membrane heparan sulfate proteoglycan. It is composed of a core protein with covalently attached glycosaminoglycan, and N-linked glycosylated (N-glycosylated) chains, and is attached to the cell membrane by a glycosylphosphatidylinositol (GPI) linkage. Glypican-1 plays a key role in the growth and development of muscle by regulating fibroblast growth factor 2 (FGF2). The GPI anchor of glypican-1 can be cleaved, resulting in glypican-1 being secreted or shed into the extracellular matrix environment. The objective of the current study was to investigate the role of glypican-1 shedding and the glycosaminoglycan and N-glycosylated chains in regulating the differentiation of turkey myogenic satellite cells. A glypican-1 construct without the GPI anchor was cloned into the mammalian expression vector pCMS-EGFP, and glypican-1 without the GPI anchor and glycosaminoglycan and N-glycosylated chains were also cloned. These constructs were co-transfected into turkey myogenic satellite cells with a small interference RNA targeting the GPI anchor of endogenous glypican-1. The soluble glypican-1 mutants were not detected in the satellite cells but in the cell medium, suggesting the secretion of the soluble glypican-1 mutants. Soluble glypican-1 increased satellite cell differentiation and enhanced myotube formation in the presence of exogenous FGF2. The increase in differentiation was supported by the elevated expression of myogenin. In conclusion, the shedding of glypican-1 from the satellite cell surface acts as a positive regulator of satellite cell differentiation and sequesters FGF2, permitting further differentiation.

Authors+Show Affiliations

Department of Animal Sciences, Ohio Agricultural Research and Development Center, The Ohio State University, Wooster, OH 44691, USA. velleman.1@osu.eduNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

23069913

Citation

Velleman, S G., et al. "Modulation of Turkey Myogenic Satellite Cell Differentiation Through the Shedding of Glypican-1." Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology, vol. 164, no. 1, 2013, pp. 36-43.
Velleman SG, Song Y, Shin J, et al. Modulation of turkey myogenic satellite cell differentiation through the shedding of glypican-1. Comp Biochem Physiol A Mol Integr Physiol. 2013;164(1):36-43.
Velleman, S. G., Song, Y., Shin, J., & McFarland, D. C. (2013). Modulation of turkey myogenic satellite cell differentiation through the shedding of glypican-1. Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology, 164(1), 36-43. https://doi.org/10.1016/j.cbpa.2012.10.007
Velleman SG, et al. Modulation of Turkey Myogenic Satellite Cell Differentiation Through the Shedding of Glypican-1. Comp Biochem Physiol A Mol Integr Physiol. 2013;164(1):36-43. PubMed PMID: 23069913.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Modulation of turkey myogenic satellite cell differentiation through the shedding of glypican-1. AU - Velleman,S G, AU - Song,Y, AU - Shin,J, AU - McFarland,D C, Y1 - 2012/10/12/ PY - 2012/09/14/received PY - 2012/10/05/revised PY - 2012/10/05/accepted PY - 2012/10/17/entrez PY - 2012/10/17/pubmed PY - 2013/5/10/medline SP - 36 EP - 43 JF - Comparative biochemistry and physiology. Part A, Molecular & integrative physiology JO - Comp Biochem Physiol A Mol Integr Physiol VL - 164 IS - 1 N2 - Glypican-1 is a cell membrane heparan sulfate proteoglycan. It is composed of a core protein with covalently attached glycosaminoglycan, and N-linked glycosylated (N-glycosylated) chains, and is attached to the cell membrane by a glycosylphosphatidylinositol (GPI) linkage. Glypican-1 plays a key role in the growth and development of muscle by regulating fibroblast growth factor 2 (FGF2). The GPI anchor of glypican-1 can be cleaved, resulting in glypican-1 being secreted or shed into the extracellular matrix environment. The objective of the current study was to investigate the role of glypican-1 shedding and the glycosaminoglycan and N-glycosylated chains in regulating the differentiation of turkey myogenic satellite cells. A glypican-1 construct without the GPI anchor was cloned into the mammalian expression vector pCMS-EGFP, and glypican-1 without the GPI anchor and glycosaminoglycan and N-glycosylated chains were also cloned. These constructs were co-transfected into turkey myogenic satellite cells with a small interference RNA targeting the GPI anchor of endogenous glypican-1. The soluble glypican-1 mutants were not detected in the satellite cells but in the cell medium, suggesting the secretion of the soluble glypican-1 mutants. Soluble glypican-1 increased satellite cell differentiation and enhanced myotube formation in the presence of exogenous FGF2. The increase in differentiation was supported by the elevated expression of myogenin. In conclusion, the shedding of glypican-1 from the satellite cell surface acts as a positive regulator of satellite cell differentiation and sequesters FGF2, permitting further differentiation. SN - 1531-4332 UR - https://www.unboundmedicine.com/medline/citation/23069913/Modulation_of_turkey_myogenic_satellite_cell_differentiation_through_the_shedding_of_glypican_1_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1095-6433(12)00485-0 DB - PRIME DP - Unbound Medicine ER -