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dc.contributor.authorLi, Heen
dc.contributor.authorGuan, Kaifangen
dc.contributor.authorLi, Xuen
dc.contributor.authorMa, Yingen
dc.contributor.authorZhou, Shaoboen
dc.date.accessioned2019-08-19T09:19:29Z
dc.date.available2019-08-19T09:19:29Z
dc.date.issued2018-11-28
dc.identifier.citationLi H, Guan K, Li X, Ma Y, Zhou S (2019) 'MFG-E8 induced differences in proteomic profiles in mouse C2C12 cells and its effect on PI3K/Akt and ERK signal pathways', International Journal of Biological Macromolecules, 124 (), pp.681-688.en
dc.identifier.issn0141-8130
dc.identifier.doi10.1016/j.ijbiomac.2018.11.265
dc.identifier.urihttp://hdl.handle.net/10547/623387
dc.description.abstractMilk fat globule-EGF factor 8 (MFG-E8) is one of the major proteins in milk fat globule membrane. In this study, mouse-derived C2C12 myoblast cells were served as an experimentally tractable model system for investigating the molecular basis of skeletal muscle cell specification and development. To examine the biochemical adaptations associated with myocytes formation comprehensively, a liquid chromatography coupled with tandem mass spectrometry label-free semi-quantitative  approach was used to analyse the myogenic C2C12 proliferation program. Over 1987  proteins were identified in C2C12 cells. The MFG-E8 (200 mg/mL) and MFG-E8 (500 26 mg/mL) with significant differences were compared based on the relative abundance. The result profiles of regulation of MFG-E8 to the expression of proteins in C2C12 cells revealed that differential waves of expression of proteins linked to intracellular signaling, transcription, cytoarchitecture, adhesion, metabolism, and muscle contraction across during the C2C12 cell proliferation process. Based on the analysis of  KEGG and STRING database, further to verification the expression of PI3K and ERK phosphorylation levels by Western blot. This study found that the data of proteomic was complementary to recent MFG-E8 studies of protein expression patterns in developing myotubes and provided a holistic framework for understanding how diverse biochemical processes are coordinated at the cellular level during skeletal muscle development.
dc.language.isoenen
dc.publisherElsevieren
dc.relation.urlhttps://www.sciencedirect.com/science/article/pii/S0141813018346993en
dc.rightsGreen - can archive pre-print and post-print or publisher's version/PDF
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectMFG-E8 induced differences in proteomic profilesen
dc.subjectLC-MS/MSen
dc.subjectlabel-freeen
dc.subjectMFG-E8en
dc.subjectWestern bloten
dc.subjectbiological activityen
dc.subjectC700 Molecular Biology, Biophysics and Biochemistryen
dc.titleMFG-E8 induced differences in proteomic profiles in mouse C2C12 cells and its effect on PI3K/Akt and ERK signal pathwaysen
dc.typeArticleen
dc.contributor.departmentHarbin Institute of Technologyen
dc.contributor.departmentJilin Universityen
dc.contributor.departmentUniversity of Bedfordshireen
dc.identifier.journalInternational Journal of Biological Macromoleculesen
dc.date.updated2019-08-19T09:08:14Z
dc.description.notePlease could you let us have a postprint version of this article for the repository: this is the version after peer review, but before typesetting by the publisher. (We cannot place the publisher's final version in the repository for copyright reasons). Placing a postprint in the repository is necessary to make the article eligible for REF 2021. supplied 19/8/19 1 year embargo
refterms.dateFOA2019-11-28T00:00:00Z
html.description.abstractMilk fat globule-EGF factor 8 (MFG-E8) is one of the major proteins in milk fat globule membrane. In this study, mouse-derived C2C12 myoblast cells were served as an experimentally tractable model system for investigating the molecular basis of skeletal muscle cell specification and development. To examine the biochemical adaptations associated with myocytes formation comprehensively, a liquid chromatography coupled with tandem mass spectrometry label-free semi-quantitative  approach was used to analyse the myogenic C2C12 proliferation program. Over 1987  proteins were identified in C2C12 cells. The MFG-E8 (200 mg/mL) and MFG-E8 (500 26 mg/mL) with significant differences were compared based on the relative abundance. The result profiles of regulation of MFG-E8 to the expression of proteins in C2C12 cells revealed that differential waves of expression of proteins linked to intracellular signaling, transcription, cytoarchitecture, adhesion, metabolism, and muscle contraction across during the C2C12 cell proliferation process. Based on the analysis of  KEGG and STRING database, further to verification the expression of PI3K and ERK phosphorylation levels by Western blot. This study found that the data of proteomic was complementary to recent MFG-E8 studies of protein expression patterns in developing myotubes and provided a holistic framework for understanding how diverse biochemical processes are coordinated at the cellular level during skeletal muscle development.


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