Tags

Type your tag names separated by a space and hit enter

Syndecan-4 cytoplasmic domain regulation of turkey satellite cell focal adhesions and apoptosis.
Mol Biol Rep. 2012 Aug; 39(8):8251-64.MB

Abstract

Syndecan-4 is a cell membrane proteoglycan composed of a transmembrane core protein and substituted glycosaminoglycan (GAG) and N-linked glycosylated (N-glycosylated) chains. The core protein has three domains: extracellular, transmembrane and cytoplasmic domains. The GAG and N-glycosylated chains and the cytoplasmic domain of syndecan-4, especially the amino acids: Ser(178) and Tyr(187) are critical in regulation of turkey satellite cell growth and development. How these processes are regulated is still unknown. The objective of the current study was to determine whether the syndecan-4 GAG and N-glycosylated chains and the cytoplasmic domain functions through modulating focal adhesion formation and apoptosis. Twelve mutant clones were generated: a truncated syndecan-4 without the cytoplasmic domain with or without GAG and N-glycosylated chains, and Ser(178) and Tyr(187) mutants with or without GAG and N-glycosylated chains. The wild type syndecan-4 and all of the syndecan-4 mutants were transfected into turkey myogenic satellite cells after which cell apoptosis and focal adhesion formation were measured. Syndecan-4 increased cell membrane localization of β1 integrin and the activity of focal adhesion kinase (FAK) whereas the cytoplasmic domain mutation decreased the phosphorylation of FAK. However, syndecan-4 and syndecan-4 mutants did not influence cell apoptosis. They also had no effect on vinculin or paxillin-containing focal adhesion formation. These results suggested that the syndecan-4 cytoplasmic domain plays an important role in regulating FAK activity and β1 integrin cell membrane localization but not cell apoptosis and vinculin or paxillin-containing focal adhesion formation.

Authors+Show Affiliations

Department of Animal Sciences, Ohio Agricultural Research and Development Center, The Ohio State University, 1680 Madison Avenue, 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

22660841

Citation

Song, Yan, et al. "Syndecan-4 Cytoplasmic Domain Regulation of Turkey Satellite Cell Focal Adhesions and Apoptosis." Molecular Biology Reports, vol. 39, no. 8, 2012, pp. 8251-64.
Song Y, McFarland DC, Velleman SG. Syndecan-4 cytoplasmic domain regulation of turkey satellite cell focal adhesions and apoptosis. Mol Biol Rep. 2012;39(8):8251-64.
Song, Y., McFarland, D. C., & Velleman, S. G. (2012). Syndecan-4 cytoplasmic domain regulation of turkey satellite cell focal adhesions and apoptosis. Molecular Biology Reports, 39(8), 8251-64. https://doi.org/10.1007/s11033-012-1673-1
Song Y, McFarland DC, Velleman SG. Syndecan-4 Cytoplasmic Domain Regulation of Turkey Satellite Cell Focal Adhesions and Apoptosis. Mol Biol Rep. 2012;39(8):8251-64. PubMed PMID: 22660841.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Syndecan-4 cytoplasmic domain regulation of turkey satellite cell focal adhesions and apoptosis. AU - Song,Yan, AU - McFarland,Douglas C, AU - Velleman,Sandra G, Y1 - 2012/06/02/ PY - 2011/12/23/received PY - 2012/05/17/accepted PY - 2012/6/5/entrez PY - 2012/6/5/pubmed PY - 2012/11/14/medline SP - 8251 EP - 64 JF - Molecular biology reports JO - Mol Biol Rep VL - 39 IS - 8 N2 - Syndecan-4 is a cell membrane proteoglycan composed of a transmembrane core protein and substituted glycosaminoglycan (GAG) and N-linked glycosylated (N-glycosylated) chains. The core protein has three domains: extracellular, transmembrane and cytoplasmic domains. The GAG and N-glycosylated chains and the cytoplasmic domain of syndecan-4, especially the amino acids: Ser(178) and Tyr(187) are critical in regulation of turkey satellite cell growth and development. How these processes are regulated is still unknown. The objective of the current study was to determine whether the syndecan-4 GAG and N-glycosylated chains and the cytoplasmic domain functions through modulating focal adhesion formation and apoptosis. Twelve mutant clones were generated: a truncated syndecan-4 without the cytoplasmic domain with or without GAG and N-glycosylated chains, and Ser(178) and Tyr(187) mutants with or without GAG and N-glycosylated chains. The wild type syndecan-4 and all of the syndecan-4 mutants were transfected into turkey myogenic satellite cells after which cell apoptosis and focal adhesion formation were measured. Syndecan-4 increased cell membrane localization of β1 integrin and the activity of focal adhesion kinase (FAK) whereas the cytoplasmic domain mutation decreased the phosphorylation of FAK. However, syndecan-4 and syndecan-4 mutants did not influence cell apoptosis. They also had no effect on vinculin or paxillin-containing focal adhesion formation. These results suggested that the syndecan-4 cytoplasmic domain plays an important role in regulating FAK activity and β1 integrin cell membrane localization but not cell apoptosis and vinculin or paxillin-containing focal adhesion formation. SN - 1573-4978 UR - https://www.unboundmedicine.com/medline/citation/22660841/Syndecan_4_cytoplasmic_domain_regulation_of_turkey_satellite_cell_focal_adhesions_and_apoptosis_ L2 - https://doi.org/10.1007/s11033-012-1673-1 DB - PRIME DP - Unbound Medicine ER -