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Critical amino acids in syndecan-4 cytoplasmic domain modulation of turkey satellite cell growth and development.

Abstract

Syndecan-4 is composed of a core protein and covalently attached glycosaminoglycan (GAG) and N-linked glycosylated (N-glycosylated) chains. The core protein is divided into extracellular, transmembrane, and cytoplasmic domains. The cytoplasmic domain has two conserved regions and a variable region in the middle. The Ser residue in the conserved region 1 and the Tyr residue in the variable region are important in regulating protein kinase C alpha (PKCα) membrane localization and focal adhesion formation. The objective of the current study was to investigate the role of syndecan-4 Ser and Tyr residues in combination with the GAG and N-glycosylated chains in turkey satellite cell proliferation, differentiation, fibroblast growth factor 2 (FGF2) responsiveness, and PKCα membrane localization. Site-directed mutagenesis was used to generate Ser and Tyr mutants with or without GAG and N-glycosylated chains. The wild type and mutant syndecan-4 constructs were transfected into turkey satellite cells. The over-expression of Ser and Tyr mutants increased cell proliferation and differentiation and decreased membrane localization of PKCα. Furthermore, Ser mutants enhanced cellular responsiveness to FGF2. The results from this study are the first demonstration of a role of syndecan-4 cytoplasmic domain Ser and Tyr residues in regulating satellite cell proliferation, differentiation, and the modulation of cellular responsiveness to FGF2.

Authors+Show Affiliations

Department of Animal Sciences, Ohio Agricultural Research and Development Center, The Ohio State University, Wooster, OH 44691, USA. song.249@osu.eduNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

Language

eng

PubMed ID

22115678

Citation

Song, Yan, et al. "Critical Amino Acids in Syndecan-4 Cytoplasmic Domain Modulation of Turkey Satellite Cell Growth and Development." Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology, vol. 161, no. 2, 2012, pp. 271-8.
Song Y, McFarland DC, Velleman SG. Critical amino acids in syndecan-4 cytoplasmic domain modulation of turkey satellite cell growth and development. Comp Biochem Physiol A Mol Integr Physiol. 2012;161(2):271-8.
Song, Y., McFarland, D. C., & Velleman, S. G. (2012). Critical amino acids in syndecan-4 cytoplasmic domain modulation of turkey satellite cell growth and development. Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology, 161(2), 271-8. https://doi.org/10.1016/j.cbpa.2011.11.007
Song Y, McFarland DC, Velleman SG. Critical Amino Acids in Syndecan-4 Cytoplasmic Domain Modulation of Turkey Satellite Cell Growth and Development. Comp Biochem Physiol A Mol Integr Physiol. 2012;161(2):271-8. PubMed PMID: 22115678.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Critical amino acids in syndecan-4 cytoplasmic domain modulation of turkey satellite cell growth and development. AU - Song,Yan, AU - McFarland,Douglas C, AU - Velleman,Sandra G, Y1 - 2011/11/15/ PY - 2011/09/15/received PY - 2011/10/24/revised PY - 2011/11/08/accepted PY - 2011/11/26/entrez PY - 2011/11/26/pubmed PY - 2012/4/14/medline SP - 271 EP - 8 JF - Comparative biochemistry and physiology. Part A, Molecular & integrative physiology JO - Comp Biochem Physiol A Mol Integr Physiol VL - 161 IS - 2 N2 - Syndecan-4 is composed of a core protein and covalently attached glycosaminoglycan (GAG) and N-linked glycosylated (N-glycosylated) chains. The core protein is divided into extracellular, transmembrane, and cytoplasmic domains. The cytoplasmic domain has two conserved regions and a variable region in the middle. The Ser residue in the conserved region 1 and the Tyr residue in the variable region are important in regulating protein kinase C alpha (PKCα) membrane localization and focal adhesion formation. The objective of the current study was to investigate the role of syndecan-4 Ser and Tyr residues in combination with the GAG and N-glycosylated chains in turkey satellite cell proliferation, differentiation, fibroblast growth factor 2 (FGF2) responsiveness, and PKCα membrane localization. Site-directed mutagenesis was used to generate Ser and Tyr mutants with or without GAG and N-glycosylated chains. The wild type and mutant syndecan-4 constructs were transfected into turkey satellite cells. The over-expression of Ser and Tyr mutants increased cell proliferation and differentiation and decreased membrane localization of PKCα. Furthermore, Ser mutants enhanced cellular responsiveness to FGF2. The results from this study are the first demonstration of a role of syndecan-4 cytoplasmic domain Ser and Tyr residues in regulating satellite cell proliferation, differentiation, and the modulation of cellular responsiveness to FGF2. SN - 1531-4332 UR - https://www.unboundmedicine.com/medline/citation/22115678/Critical_amino_acids_in_syndecan_4_cytoplasmic_domain_modulation_of_turkey_satellite_cell_growth_and_development_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1095-6433(11)00321-7 DB - PRIME DP - Unbound Medicine ER -