Show simple item record

dc.contributor.authorLi, Heen
dc.contributor.authorXu, Weilien
dc.contributor.authorMa, Yingen
dc.contributor.authorZhou, Shaoboen
dc.date.accessioned2017-09-28T12:39:13Z
dc.date.available2017-09-28T12:39:13Z
dc.date.issued2017-06-07
dc.identifier.citationLi H, Xu W, Ma Y, Zhou S (2017) 'Separation and purification of the bovine milk fat globule membrane protein and its effect on improvement of C2C12 mouse skeletal muscle cell proliferation', New Journal of Chemistry, 41, pp.6530-6539.en
dc.identifier.issn1144-0546
dc.identifier.doi10.1039/C7NJ00560A
dc.identifier.urihttp://hdl.handle.net/10547/622257
dc.description.abstractA novel method to improve the proliferation activity of C2C12 cells by the bovine milk fat globule membrane (MFGM) protein was established in this study. The MFGM protein was extracted and isolated into 4 fractions using an electric cream separator, and purified by a cellulose DEAE-52 column. Fraction 2 accounted for 57.8% of the total MFGM protein, and was used in the following study. The MTT assay showed that it induced cell proliferation activity, increased the cell survival rate and the cell number using flow cytometry and fluorescence microscopy analysis. There were only subtle changes in the morphology as observed using confocal scanning laser microscopy, but the number of mitochondria was significantly increased as observed using transmission electron microscopy analysis. Furthermore, the mRNA expression of MyoD, cyclin D1, p70S6K and mTOR was up-regulated as determined utilizing the quantitative real-time PCR assay, and the activation of Akt and mTOR phosphorylation was up regulated as determined using the Western blot assay. The main protein in fraction 2, assayed by 1-D gel electrophoresis and MALDI TOF-TOF, was identified as milk fat globule-EGF factor 8, the content was 65.6% of the total protein in fraction 2. The results elucidate a new molecular mechanism of the MFGM protein fraction 2: the activation of the Akt signal pathway in promoting cell proliferation.
dc.description.sponsorshipNational Natural Science Foundation of China grant (NO. 31501481)en
dc.language.isoenen
dc.publisherRoyal Society of Chemistryen
dc.relation.urlhttp://pubs.rsc.org/is/content/articlelanding/2017/nj/c7nj00560a/unauth#!divAbstracten
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.subjectc2c12en
dc.subjectsacoponiaen
dc.subjectC910 Applied Biological Sciencesen
dc.titleSeparation and purification of the bovine milk fat globule membrane protein and its effect on improvement of C2C12 mouse skeletal muscle cell proliferationen
dc.typeArticleen
dc.contributor.departmentHarbin Institute of Technologyen
dc.contributor.departmentUniversity of Bedfordshireen
dc.identifier.journalNew Journal of Chemistryen
dc.date.updated2017-09-28T12:35:01Z
dc.description.noteI can provide reprint, if someone needs it. If this is to be eligible for REF, we will need the preprint file (final draft post-refereeing) please! RVO 25-9-17
html.description.abstractA novel method to improve the proliferation activity of C2C12 cells by the bovine milk fat globule membrane (MFGM) protein was established in this study. The MFGM protein was extracted and isolated into 4 fractions using an electric cream separator, and purified by a cellulose DEAE-52 column. Fraction 2 accounted for 57.8% of the total MFGM protein, and was used in the following study. The MTT assay showed that it induced cell proliferation activity, increased the cell survival rate and the cell number using flow cytometry and fluorescence microscopy analysis. There were only subtle changes in the morphology as observed using confocal scanning laser microscopy, but the number of mitochondria was significantly increased as observed using transmission electron microscopy analysis. Furthermore, the mRNA expression of MyoD, cyclin D1, p70S6K and mTOR was up-regulated as determined utilizing the quantitative real-time PCR assay, and the activation of Akt and mTOR phosphorylation was up regulated as determined using the Western blot assay. The main protein in fraction 2, assayed by 1-D gel electrophoresis and MALDI TOF-TOF, was identified as milk fat globule-EGF factor 8, the content was 65.6% of the total protein in fraction 2. The results elucidate a new molecular mechanism of the MFGM protein fraction 2: the activation of the Akt signal pathway in promoting cell proliferation.


Files in this item

Thumbnail
Name:
Li He paper 1 final.pdf
Size:
1.067Mb
Format:
PDF
Description:
author's version

This item appears in the following Collection(s)

Show simple item record

Green - can archive pre-print and post-print or publisher's version/PDF
Except where otherwise noted, this item's license is described as Green - can archive pre-print and post-print or publisher's version/PDF