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Role of syndecan-4 side chains in turkey satellite cell apoptosis and focal adhesion formation.
Cell Biol Int. 2012 May 01; 36(5):433-40.CB

Abstract

S4 (syndecan-4) is a cell membrane heparan sulfate proteoglycan that functions in muscle growth and development. It is composed of a central core protein and two types of side chains: GAGs (glycosaminoglycans) and N-glycosylated (N-linked glycosylated) chains. The N-glycosylated chains and GAG chains are required for S4 to regulate turkey myogenic satellite cell proliferation. The objective of the current study was to determine whether the S4 side chains regulate cell proliferation through muscle cell focal adhesion formation and apoptosis. S4 mutants with only one or without any N-glycosylated chains attached to the core protein with or without GAG chains were generated to study the function of N-glycosylated chains and the interaction between N-glycosylated chains and GAG chains. The wild-type S4 and all of the S4 side chain mutants were transfected into turkey myogenic satellite cells. Cell apoptosis and focal adhesion formation were measured, and PKCα (protein kinase Cα) cell membrane localization was investigated. S4 increased FAK (focal adhesion kinase) activity and the deletion of the side chains decreased this effect. S4 and the S4 mutants had no effect on β1-integrin expression, but increased the cell membrane localization of β1-integrin and PKCα. Furthermore, cell apoptosis and vinculin containing focal adhesions were not affected by S4 and its mutants. The results suggest that S4 and its side chains play important roles in regulating FAK activity, and PKCα and β1-integrin cell membrane localization, but not cell apoptosis and vinculin-containing focal adhesion formation.

Authors+Show Affiliations

Department of Animal Sciences, Ohio Agricultural Research and Development Center, Ohio State University, Wooster, OH 44691, USA.No 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

22272563

Citation

Song, Yan, et al. "Role of Syndecan-4 Side Chains in Turkey Satellite Cell Apoptosis and Focal Adhesion Formation." Cell Biology International, vol. 36, no. 5, 2012, pp. 433-40.
Song Y, McFarland DC, Velleman SG. Role of syndecan-4 side chains in turkey satellite cell apoptosis and focal adhesion formation. Cell Biol Int. 2012;36(5):433-40.
Song, Y., McFarland, D. C., & Velleman, S. G. (2012). Role of syndecan-4 side chains in turkey satellite cell apoptosis and focal adhesion formation. Cell Biology International, 36(5), 433-40. https://doi.org/10.1042/CBI20110467
Song Y, McFarland DC, Velleman SG. Role of Syndecan-4 Side Chains in Turkey Satellite Cell Apoptosis and Focal Adhesion Formation. Cell Biol Int. 2012 May 1;36(5):433-40. PubMed PMID: 22272563.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Role of syndecan-4 side chains in turkey satellite cell apoptosis and focal adhesion formation. AU - Song,Yan, AU - McFarland,Douglas C, AU - Velleman,Sandra G, PY - 2012/1/26/entrez PY - 2012/1/26/pubmed PY - 2012/8/9/medline SP - 433 EP - 40 JF - Cell biology international JO - Cell Biol Int VL - 36 IS - 5 N2 - S4 (syndecan-4) is a cell membrane heparan sulfate proteoglycan that functions in muscle growth and development. It is composed of a central core protein and two types of side chains: GAGs (glycosaminoglycans) and N-glycosylated (N-linked glycosylated) chains. The N-glycosylated chains and GAG chains are required for S4 to regulate turkey myogenic satellite cell proliferation. The objective of the current study was to determine whether the S4 side chains regulate cell proliferation through muscle cell focal adhesion formation and apoptosis. S4 mutants with only one or without any N-glycosylated chains attached to the core protein with or without GAG chains were generated to study the function of N-glycosylated chains and the interaction between N-glycosylated chains and GAG chains. The wild-type S4 and all of the S4 side chain mutants were transfected into turkey myogenic satellite cells. Cell apoptosis and focal adhesion formation were measured, and PKCα (protein kinase Cα) cell membrane localization was investigated. S4 increased FAK (focal adhesion kinase) activity and the deletion of the side chains decreased this effect. S4 and the S4 mutants had no effect on β1-integrin expression, but increased the cell membrane localization of β1-integrin and PKCα. Furthermore, cell apoptosis and vinculin containing focal adhesions were not affected by S4 and its mutants. The results suggest that S4 and its side chains play important roles in regulating FAK activity, and PKCα and β1-integrin cell membrane localization, but not cell apoptosis and vinculin-containing focal adhesion formation. SN - 1095-8355 UR - https://www.unboundmedicine.com/medline/citation/22272563/Role_of_syndecan_4_side_chains_in_turkey_satellite_cell_apoptosis_and_focal_adhesion_formation_ L2 - https://doi.org/10.1042/CBI20110467 DB - PRIME DP - Unbound Medicine ER -