A role for β-catenin in diet-induced skeletal muscle insulin resistance.

dc.citation.issue4
dc.citation.volume11
dc.contributor.authorMasson SWC
dc.contributor.authorDissanayake WC
dc.contributor.authorBroome SC
dc.contributor.authorHedges CP
dc.contributor.authorPeeters WM
dc.contributor.authorGram M
dc.contributor.authorRowlands DS
dc.contributor.authorShepherd PR
dc.contributor.authorMerry TL
dc.coverage.spatialUnited States
dc.date.accessioned2024-06-17T19:55:14Z
dc.date.available2024-06-17T19:55:14Z
dc.date.issued2023-02-17
dc.description.abstractA central characteristic of insulin resistance is the impaired ability for insulin to stimulate glucose uptake into skeletal muscle. While insulin resistance can occur distal to the canonical insulin receptor-PI3k-Akt signaling pathway, the signaling intermediates involved in the dysfunction are yet to be fully elucidated. β-catenin is an emerging distal regulator of skeletal muscle and adipocyte insulin-stimulated GLUT4 trafficking. Here, we investigate its role in skeletal muscle insulin resistance. Short-term (5-week) high-fat diet (HFD) decreased skeletal muscle β-catenin protein expression 27% (p = 0.03), and perturbed insulin-stimulated β-cateninS552 phosphorylation 21% (p = 0.009) without affecting insulin-stimulated Akt phosphorylation relative to chow-fed controls. Under chow conditions, mice with muscle-specific β-catenin deletion had impaired insulin responsiveness, whereas under HFD, both mice exhibited similar levels of insulin resistance (interaction effect of genotype × diet p < 0.05). Treatment of L6-GLUT4-myc myocytes with palmitate lower β-catenin protein expression by 75% (p = 0.02), and attenuated insulin-stimulated β-catenin phosphorylationS552 and actin remodeling (interaction effect of insulin × palmitate p < 0.05). Finally, β-cateninS552 phosphorylation was 45% lower in muscle biopsies from men with type 2 diabetes while total β-catenin expression was unchanged. These findings suggest that β-catenin dysfunction is associated with the development of insulin resistance.
dc.description.confidentialfalse
dc.edition.editionFeb 2023
dc.format.paginatione15536-
dc.identifier.author-urlhttps://www.ncbi.nlm.nih.gov/pubmed/36807886
dc.identifier.citationMasson SWC, Dissanayake WC, Broome SC, Hedges CP, Peeters WM, Gram M, Rowlands DS, Shepherd PR, Merry TL. (2023). A role for β-catenin in diet-induced skeletal muscle insulin resistance.. Physiol Rep. 11. 4. (pp. e15536-).
dc.identifier.doi10.14814/phy2.15536
dc.identifier.eissn2051-817X
dc.identifier.elements-typejournal-article
dc.identifier.issn2051-817X
dc.identifier.numbere15536
dc.identifier.urihttps://mro.massey.ac.nz/handle/10179/69872
dc.languageeng
dc.publisherWiley Periodicals LLC on behalf of The Physiological Society and the American Physiological Society
dc.publisher.urihttps://physoc.onlinelibrary.wiley.com/doi/10.14814/phy2.15536
dc.relation.isPartOfPhysiol Rep
dc.rights(c) 2023 The Author/s
dc.rightsCC BY 4.0
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectWnt-signaling
dc.subjectglucose transport
dc.subjectinsulin resistance
dc.subjectobesity
dc.subjectMice
dc.subjectAnimals
dc.subjectInsulin Resistance
dc.subjectProto-Oncogene Proteins c-akt
dc.subjectDiabetes Mellitus, Type 2
dc.subjectPhosphatidylinositol 3-Kinases
dc.subjectbeta Catenin
dc.subjectGlucose
dc.subjectMuscle, Skeletal
dc.subjectInsulin
dc.subjectDiet, High-Fat
dc.subjectPhosphorylation
dc.subjectGlucose Transporter Type 4
dc.titleA role for β-catenin in diet-induced skeletal muscle insulin resistance.
dc.typeJournal article
pubs.elements-id459830
pubs.organisational-groupCollege of Health
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