Remodeling of skeletal muscle mitochondrial proteome with high-fat diet involves greater changes to β-oxidation than electron transfer proteins in mice

Dasari, Surendra; Newsom, Sean A.; Ehrlicher, Sarah E.; Stierwalt, Harrison D.; Robinson, Matthew M.

doi:10.1152/ajpendo.00051.2018

Cited by 15 publications

(18 citation statements)

References 44 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Quadriceps and gastrocnemius muscle were homogenized as whole tissue (~40 mg) or mitochondrial isolations (~70 mg) for immunoblotting as previously described . We previously reported, using proteomics, that the isolation yields a mitochondrial enriched fraction, but still has contamination of other fractions . Immunoblotting of the Myo, Cyto and Mito fractions demonstrate a high abundance of VDAC in the Mito fraction with some contamination of tubulin (Figure D).…”

Section: Methodsmentioning

confidence: 94%

“…22 We previously reported, using proteomics, that the isolation yields a mitochondrial enriched fraction, but still has contamination of other fractions. 28 Immunoblotting of the Myo, Cyto and Mito fractions demonstrate a high abundance of VDAC in the Mito fraction with some contamination of tubulin ( Figure 2D). Approximately 35 μg of protein was resolved on 10%-15% Bis-Tris gels and transferred to nitrocellulose membranes.…”

Section: Immunoblottingmentioning

confidence: 97%

See 1 more Smart Citation

Mitochondrial adaptations to exercise do not require Bcl2‐mediated autophagy but occur with BNIP3/Parkin activation

et al. 2020

Self Cite

View full text Add to dashboard Cite

Understanding the mechanisms regulating mitochondrial respiratory function and adaptations to metabolic challenges, such as exercise and high dietary fat, is necessary to promote skeletal muscle health and attenuate metabolic disease. Autophagy is a constitutively active degradation pathway that promotes mitochondrial turnover and transiently increases postexercise. Recent evidence indicates Bcl2 mediates exercise‐induced autophagy and skeletal muscle adaptions to training during high‐fat diet. We determined if improvements in mitochondrial respiration due to exercise training required Bcl2‐mediated autophagy using a transgenic mouse model of impaired inducible autophagy (Bcl2AAA). Mitochondrial adaptations to a treadmill exercise training protocol, in either low‐fat or high‐fat diet fed mice, did not require Bcl2‐mediated autophagy activation. Instead, training increased protein synthesis rates and basal autophagy in the Bcl2AAA mice, while acute exercise activated BNIP3 and Parkin autophagy. High‐fat diet stimulated lipid‐specific mitochondrial adaptations. These data demonstrate increases in basal mitochondrial turnover, not transient activation with exercise, mediate adaptations to exercise and high‐fat diet.

show abstract

Section: Methodsmentioning

confidence: 94%

Section: Immunoblottingmentioning

confidence: 97%

Mitochondrial adaptations to exercise do not require Bcl2‐mediated autophagy but occur with BNIP3/Parkin activation

et al. 2020

Self Cite

View full text Add to dashboard Cite

show abstract

“…STAT3 has been identified in mitochondria from heart, liver (42,45), Pro-B cells (45), astrocytes (34), and Ras-transformed MEFS (12). Moreover, recent proteomic analysis in a crude, mitochondrial-enriched fraction from gastrocnemius of C57BL/6J mice also identified STAT3, suggesting that STAT3 may also localize to mitochondria in skeletal muscle (7). A limitation of this latter study, however, is that nuclear proteins were also identified in the proteomic analysis (e.g., histones 1, 2A, 2B, 3, and lamin A), which indicates that nuclei were likely present in the crude fraction; as such, detected STAT3 could have been from mitochondria and/or nuclei.…”

Section: Discussionmentioning

confidence: 99%

“…We sought to confirm the presence of STAT3 in skeletal muscle mitochondria, as has previously been demonstrated in heart and liver (42,45), Pro-B cells (45), astrocytes (34), Ras-transformed MEFS (12), and a mitochondrial-enriched fraction from mouse skeletal muscle (7). As previous literature suggests that the mitochondrial-localized pool of STAT3 is 10-fold smaller than that of other cellular compartments [e.g., cytosol (45)], and given that STAT3 has a strong presence in the nucleus (18, 43), we developed a novel flow cytometrybased approach to assess mitochondrial STAT3.…”

Section: Stat3 Protein Is Localized In Skeletal Muscle Mitochondriamentioning

confidence: 90%

“…To this end, recent studies demonstrate that signal transducer and activator of transcription 3 (STAT3), which has historically been considered for its cytokine-induced nuclear transcriptional activity (21), can localize to the mitochondria in a number of tissues and cells, including heart, liver, brain, kidney (42,45), Pro-B cells (45), astrocytes (34), and Rastransformed mouse embryonic fibroblasts (MEFS) (12). Interestingly, recent proteomics-based analysis extend this finding to skeletal muscle with STAT3 detected in a mitochondrialenriched fraction obtained from gastrocnemius of C57BL/6J mice (7). Within mitochondria, STAT3 influences oxidative phosphorylation at the level of the electron transport chain (ETC) complexes I and II and does so in a manner that is independent of its canonical transcriptional activity (12,25,34,42,45).…”

Section: Introductionmentioning

confidence: 95%

See 1 more Smart Citation

Skeletal muscle mitochondrial function and exercise capacity are not impaired in mice with knockout of STAT3

Dent

Hetrick

Tahvilian

et al. 2019

Journal of Applied Physiology

View full text Add to dashboard Cite

Signal transducer and activator of transcription 3 (STAT3) was recently found to be localized to mitochondria in a number of tissues and cell types, where it modulates oxidative phosphorylation via interactions with the electron transport proteins, complex I and complex II. Skeletal muscle is densely populated with mitochondria although whether STAT3 contributes to skeletal muscle oxidative capacity is unknown. In the present study, we sought to elucidate the contribution of STAT3 to mitochondrial and skeletal muscle function by studying mice with muscle-specific knockout of STAT3 (mKO). First, we developed a novel flow cytometry-based approach to confirm that STAT3 is present in skeletal muscle mitochondria. However, contrary to findings in other tissue types, complex I and complex II activity and maximal mitochondrial respiratory capacity in skeletal muscle were comparable between mKO mice and floxed/wild-type littermates. Moreover, there were no genotype differences in endurance exercise performance, skeletal muscle force-generating capacity, or the adaptive response of skeletal muscle to voluntary wheel running. Collectively, although we confirm the presence of STAT3 in skeletal muscle mitochondria, our data establish that STAT3 is dispensable for mitochondrial and physiological function in skeletal muscle. NEW & NOTEWORTHY Whether signal transducer and activator of transcription 3 (STAT3) can regulate the activity of complex I and II of the electron transport chain and mitochondrial oxidative capacity in skeletal muscle, as it can in other tissues, is unknown. By using a mouse model lacking STAT3 in muscle, we demonstrate that skeletal muscle mitochondrial and physiological function, both in vivo and ex vivo, is not impacted by the loss of STAT3.

show abstract

Insulin resistance is improved in high‐fat fed mice by photobiomodulation therapy at 630 nm

Silva

Ferraresi

Almeida

et al. 2020

Journal of Biophotonics

View full text Add to dashboard Cite

Photobiomodulation therapy (PBMT) in the infrared spectrum exerts positive effects on glucose metabolism, but the use of PBMT at the red spectrum has not been assessed. Male Swiss albino mice were divided into low‐fat control and high‐fat diet (HFD) for 12 weeks and were treated with red (630 nm) PBMT or no treatment (Sham) during weeks 9 to 12. PBMT was delivered at 31.19 J/cm2, 60 J total dose per day for 20 days. In HFD‐fed mice, PBMT improved glucose tolerance, insulin resistance and fasting hyperinsulinemia. PBMT also reduced adiposity and inflammatory infiltrate in adipose tissue. Phosphorylation of Akt in epididymal adipose tissue and rectus femoralis muscle was improved by PBMT. In epididymal fat PBMT reversed the reduced phosphorylation of AS160 and the reduced Glut4 content. In addition, PBMT reversed the alterations caused by HFD in rectus femoralis muscle on proteins involved in mitochondrial dynamics and β‐oxidation. In conclusion, PBMT at red spectrum improved insulin resistance and glucose metabolism in HFD‐fed mice.

show abstract

Remodeling of skeletal muscle mitochondrial proteome with high-fat diet involves greater changes to β-oxidation than electron transfer proteins in mice

Cited by 15 publications

References 44 publications

Mitochondrial adaptations to exercise do not require Bcl2‐mediated autophagy but occur with BNIP3/Parkin activation

Mitochondrial adaptations to exercise do not require Bcl2‐mediated autophagy but occur with BNIP3/Parkin activation

Skeletal muscle mitochondrial function and exercise capacity are not impaired in mice with knockout of STAT3

Insulin resistance is improved in high‐fat fed mice by photobiomodulation therapy at 630 nm

Contact Info

Product

Resources

About