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Fibroblast growth factor 2 and protein kinase C alpha are involved in syndecan-4 cytoplasmic domain modulation of turkey myogenic satellite cell proliferation.

Abstract

Syndecan-4 core protein is composed of extracellular, transmembrane, and cytoplasmic domains. The cytoplasmic domain functions in transmitting signals into the cell through the protein kinase C alpha (PKCα) pathway. The glycosaminoglycan (GAG) and N-linked glycosylated (N-glycosylated) chains attached to the extracellular domain influence cell proliferation. The current study investigated the function of syndecan-4 cytoplasmic domain in combination with GAG and N-glycosylated chains in turkey muscle cell proliferation, differentiation, fibroblast growth factor 2 (FGF2) responsiveness, and PKCα membrane localization. Syndecan-4 or syndecan-4 without the cytoplasmic domain and with or without the GAG and N-glycosylated chains were transfected or co-transfected with a small interfering RNA targeting syndecan-4 cytoplasmic domain into turkey muscle satellite cells. The overexpression of syndecan-4 mutants increased cell proliferation but did not change differentiation. Syndecan-4 mutants had increased cellular responsiveness to FGF2 during proliferation. Syndecan-4 increased PKCα cell membrane localization, whereas the syndecan-4 mutants decreased PKCα cell membrane localization compared to syndecan-4. However, compared to the cells without transfection, syndecan-4 mutants increased cell membrane localization of PKCα. These data indicated that the syndecan-4 cytoplasmic domain and the GAG and N-glycosylated chains are critical in syndecan-4 regulating satellite cell proliferation, responsiveness to FGF2, and PKCα cell membrane localization.

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

21939780

Citation

Song, Yan, et al. "Fibroblast Growth Factor 2 and Protein Kinase C Alpha Are Involved in Syndecan-4 Cytoplasmic Domain Modulation of Turkey Myogenic Satellite Cell Proliferation." Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology, vol. 161, no. 1, 2012, pp. 44-52.
Song Y, McFarland DC, Velleman SG. Fibroblast growth factor 2 and protein kinase C alpha are involved in syndecan-4 cytoplasmic domain modulation of turkey myogenic satellite cell proliferation. Comp Biochem Physiol A Mol Integr Physiol. 2012;161(1):44-52.
Song, Y., McFarland, D. C., & Velleman, S. G. (2012). Fibroblast growth factor 2 and protein kinase C alpha are involved in syndecan-4 cytoplasmic domain modulation of turkey myogenic satellite cell proliferation. Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology, 161(1), 44-52. https://doi.org/10.1016/j.cbpa.2011.09.001
Song Y, McFarland DC, Velleman SG. Fibroblast Growth Factor 2 and Protein Kinase C Alpha Are Involved in Syndecan-4 Cytoplasmic Domain Modulation of Turkey Myogenic Satellite Cell Proliferation. Comp Biochem Physiol A Mol Integr Physiol. 2012;161(1):44-52. PubMed PMID: 21939780.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Fibroblast growth factor 2 and protein kinase C alpha are involved in syndecan-4 cytoplasmic domain modulation of turkey myogenic satellite cell proliferation. AU - Song,Yan, AU - McFarland,Douglas C, AU - Velleman,Sandra G, Y1 - 2011/09/10/ PY - 2011/06/08/received PY - 2011/09/02/revised PY - 2011/09/04/accepted PY - 2011/9/24/entrez PY - 2011/9/24/pubmed PY - 2012/3/16/medline SP - 44 EP - 52 JF - Comparative biochemistry and physiology. Part A, Molecular & integrative physiology JO - Comp Biochem Physiol A Mol Integr Physiol VL - 161 IS - 1 N2 - Syndecan-4 core protein is composed of extracellular, transmembrane, and cytoplasmic domains. The cytoplasmic domain functions in transmitting signals into the cell through the protein kinase C alpha (PKCα) pathway. The glycosaminoglycan (GAG) and N-linked glycosylated (N-glycosylated) chains attached to the extracellular domain influence cell proliferation. The current study investigated the function of syndecan-4 cytoplasmic domain in combination with GAG and N-glycosylated chains in turkey muscle cell proliferation, differentiation, fibroblast growth factor 2 (FGF2) responsiveness, and PKCα membrane localization. Syndecan-4 or syndecan-4 without the cytoplasmic domain and with or without the GAG and N-glycosylated chains were transfected or co-transfected with a small interfering RNA targeting syndecan-4 cytoplasmic domain into turkey muscle satellite cells. The overexpression of syndecan-4 mutants increased cell proliferation but did not change differentiation. Syndecan-4 mutants had increased cellular responsiveness to FGF2 during proliferation. Syndecan-4 increased PKCα cell membrane localization, whereas the syndecan-4 mutants decreased PKCα cell membrane localization compared to syndecan-4. However, compared to the cells without transfection, syndecan-4 mutants increased cell membrane localization of PKCα. These data indicated that the syndecan-4 cytoplasmic domain and the GAG and N-glycosylated chains are critical in syndecan-4 regulating satellite cell proliferation, responsiveness to FGF2, and PKCα cell membrane localization. SN - 1531-4332 UR - https://www.unboundmedicine.com/medline/citation/21939780/Fibroblast_growth_factor_2_and_protein_kinase_C_alpha_are_involved_in_syndecan_4_cytoplasmic_domain_modulation_of_turkey_myogenic_satellite_cell_proliferation_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1095-6433(11)00265-0 DB - PRIME DP - Unbound Medicine ER -