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Regulation of GLUT4 translocation in an in vitro cell model using postprandial human serum ex vivo

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dc.contributor.author Cogan, Karl E.
dc.contributor.author Carson, Brian P.
dc.contributor.author Patel, Bijal
dc.contributor.author Amigo-Benavent, Miryam
dc.contributor.author Jakeman, Philip M.
dc.contributor.author Egan, Brendan
dc.date.accessioned 2019-09-25T10:48:21Z
dc.date.issued 2019
dc.identifier.issn 0958-0670
dc.identifier.uri http://hdl.handle.net/10344/8070
dc.description peer-reviewed en_US
dc.description.abstract Individual amino acids, amino acid mixtures and protein hydrolysates stimulate glucose uptake in many experimental models. To replicate better in vitro the dynamic postprandial response to feeding in vivo, in the present study we investigated the effects of culture media conditioned with fasted and postprandial human serum on GLUT4 translocation in L6‐GLUT4myc myotubes. Serum samples were collected from healthy male participants (n = 8) at baseline (T0), 60 (T60) and 120 min (T120) after the ingestion of 0.33 g (kg body mass)−1 of intact (WPC) or hydrolysed (WPH) whey protein and an isonitrogenous non‐essential amino acid (NEAA) control. L6‐GLUT4myc myotubes were starved of serum and amino acids for 1 h before incubation for 1 h in medium containing 1% postprandial human serum, after which GLUT4 translocation was determined via colorimetric assay. Medium conditioned with fasted human serum at concentrations of 5–20% increased cell surface GLUT4myc abundance. Incubation with serum collected after the ingestion of WPH increased cell surface GLUT4myc at T60 relative to T0 [mean (lower, upper 95% confidence interval)]; [1.13 (1.05, 1.22)], whereas WPC [0.98 (0.90, 1.07)] or NEAA [1.02 (0.94, 1.11)] did not. The differential increases in cell surface GLUT4myc abundance were not explained by differences in serum concentrations of total, essential and branched‐chain amino acids or insulin, glucagon‐like peptide 1 (GLP‐1) and gastric inhibitory polypeptide (GIP). Using a new ex vivo, in vitro approach, cell culture medium conditioned with postprandial serum after the ingestion of a whey protein hydrolysate increased GLUT4 translocation in skeletal muscle cells. en_US
dc.language.iso eng en_US
dc.publisher Wiley and Sons Ltd en_US
dc.relation.ispartofseries Experimental Physiology;104 (6), pp. 800-807
dc.relation.uri http://dx.doi.org/10.1113/EP087356
dc.rights This is the author accepted peer reviewed version of the following article: Regulation of GLUT4 translocation in an in vitro cell model using postprandial human serum ex vivo, Experimental Physiology, 2019 104 (6), pp 800-807, http://dx.doi.org/10.1113/EP087356 which has been published in final form at [Link to final article using the DOI]. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving. http://olabout.wiley.com/WileyCDA/Section/id-828039.html#terms en_US
dc.subject bioactive en_US
dc.subject GLUT4 translocation en_US
dc.subject serum en_US
dc.subject skeletal muscle en_US
dc.subject whey en_US
dc.title Regulation of GLUT4 translocation in an in vitro cell model using postprandial human serum ex vivo en_US
dc.type info:eu-repo/semantics/article en_US
dc.type.supercollection all_ul_research en_US
dc.type.supercollection ul_published_reviewed en_US
dc.date.updated 2019-09-25T10:34:57Z
dc.description.version ACCEPTED
dc.identifier.doi 10.1113/EP087356
dc.contributor.sponsor Food for Health Ireland en_US
dc.contributor.sponsor EI en_US
dc.relation.projectid TC2013001 en_US
dc.date.embargoEndDate 2020-06-01
dc.embargo.terms 2020-06-01 en_US
dc.rights.accessrights info:eu-repo/semantics/openAccess en_US
dc.internal.rssid 2903134
dc.internal.copyrightchecked Yes
dc.identifier.journaltitle Experimental Physiology
dc.description.status peer-reviewed


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