The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
A maternal high‐fat diet modulates fetal SIRT1 histone and protein deacetylase activity in nonhuman primates
Open accessAbstract
In nonhuman primates, we previously demonstrated that a maternal high‐fat diet (MHFD) induces fetal nonalcoholic fatty liver disease (NAFLD) and alters the fetal metabolome. These changes are accompanied by altered acetylation of histone H3 (H3K14ac). However, the mechanism behind this alteration in acetylation remains unknown. As SIRT1 is both a lysine deacetylase and a crucial sensor of cellular metabolism, we hypothesized that SIRT1 may be involved in fetal epigenomic alterations. Here we show that in utero exposure to a MHFD, but not maternal obesity per se , increases fetal H3K14ac with concomitant decreased SIRT1 expression and diminished in vitro protein and histone deacetylase activity. MHFD increased H3K14ac and DBC1‐SIRT1 complex formation in fetal livers, both of which were abrogated with diet reversal despite persistent maternal obesity. Moreover, MHFD was associated with altered expression of known downstream effectors deregulated in NAFLD and modulated by SIRT1 ( e.g. , PPARA, PPARG, SREBF1, CYP7A1, FASN, and SCD). Finally, ex vivo purified SIRT1 retains deacetylase activity on an H3K14ac peptide substrate with preferential activity toward acetylated histone H3; mutagenesis of the catalytic domain of SIRT1 (H363Y) abrogates H3K14ac deacetylation. Our data implicate SIRT1 as a likely molecular mediator of the fetal epigenome and metabolome under MHFD conditions.—Suter, M. A., Chen, A., Burdine, M. S., Choudhury, M., Harris, R. A., Lane, R. H., Friedman, J. E., Grove, K. L., Tackett, A. J., Aagaard, K. M. A maternal high‐fat diet modulates fetal SIRT1 histone and protein deacetylase activity in nonhuman primates. FASEB J. 26, 5106–5114 (2012). www.fasebj.org
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan
Howitz, K. T., Bitterman, K. J., Cohen, H. Y., Lamming, D. W., Lavu, S., Wood, J. G., Zipkin, R. E., Chung, P., Kisielewski, A., Zhang, L.-L., et al. (2003) · Nature · doi:10.1038/nature01960 · Cited by 3,796
Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
Imai, S.-I., Armstrong, C. M., Kaeberlein, M., & Guarente, L. (2000) · Nature · doi:10.1038/35001622 · Cited by 3,510
Mechanism of Human SIRT1 Activation by Resveratrol
Borra, M. T., Smith, B. C., & Denu, J. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501250200 · Cited by 1,065
Hirschey, M. D., Shimazu, T., Jing, E., Grueter, C. A., Collins, A. M., Aouizerat, B., Stančáková, A., Goetzman, E., Lam, M. M., Schwer, B., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.07.019 · Cited by 787 · cited 1×
“leading to mitochondrial hyperacetylation (48).”
SIRT1 Regulates Hepatocyte Lipid Metabolism through Activating AMP-activated Protein Kinase
Hou, X., Xu, S., Maitland-Toolan, K. A., Sato, K., Jiang, B., Ido, Y., Lan, F., Walsh, K., Wierzbicki, M., Verbeuren, T. J., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802187200 · Cited by 778
SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation.
Vaquero, A., Scher, M., Erdjument-Bromage, H., Tempst, P., Serrano, L., & Reinberg, D. (2007) · Nature · doi:10.1038/nature06268 · Cited by 439
Inhibition of SIRT1 Reactivates Silenced Cancer Genes without Loss of Promoter DNA Hypermethylation
Pruitt, K., Zinn, R. L., Ohm, J. E., McGarvey, K. M., Kang, S.-H. L., Watkins, D. N., Herman, J. G., & Baylin, S. B. (2006) · PLoS Genetics · doi:10.1371/journal.pgen.0020040 · Cited by 387 · cited 1×
“functioning as an H4K16 and H3K9 deacetylase (13).”
BackgroundFrias, A. E., Morgan, T. K., Evans, A. E., Rasanen, J., Oh, K. Y., Thornburg, K. L., & Grove, K. L. (2011) · Endocrinology · doi:10.1210/en.2010-1332 · Cited by 268
Self-citation
Cited by
MAFLD: a consensus-driven proposed nomenclature for metabolic associated fatty liver disease
Eslam, M., Sanyal, A. J., George, J., Sanyal, A., Neuschwander-Tetri, B., Tiribelli, C., Kleiner, D. E., Brunt, E., Bugianesi, E., Yki-Järvinen, H., et al. (2020) · Gastroenterology · doi:10.1053/j.gastro.2019.11.312 · Cited by 3,286
Nonalcoholic fatty liver disease
Brunt, E. M., Wong, V. W.-S., Nobili, V., Day, C. P., Sookoian, S., Maher, J. J., Bugianesi, E., Sirlin, C. B., Neuschwander-Tetri, B. A., & Rinella, M. E. (2015) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2015.80 · Cited by 818
Ma, J., Prince, A. L., Bader, D., Hu, M., Ganu, R., Baquero, K., Blundell, P., Alan Harris, R., Frias, A. E., Grove, K. L., et al. (2014) · Nature Communications · doi:10.1038/ncomms4889 · Cited by 438
Self-citationEarly Life Nutrition, Epigenetics and Programming of Later Life Disease
Vickers, M. (2014) · Nutrients · doi:10.3390/nu6062165 · Cited by 366
Keating, S. T., & El-Osta, A. (2015) · Circulation Research · doi:10.1161/circresaha.116.303936 · Cited by 317
Metadata
- Authors
- Suter, M. A., Chen, A., Burdine, M. S., Choudhury, M., Harris, R. A., Lane, R. H., Friedman, J. E., Grove, K. L., Tackett, A. J., & Aagaard, K. M.
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 2012-09-14
- Volume
- 26
- Issue
- 12
- Pages
- 5106-5114
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- OpenAlex
- W1981379568
- Cited by
- 171
- References
- 8
- FWCI
- 5.73
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: A maternal high‐fat diet modulates fetal SIRT1 histone and protein deacetylase activity in nonhuman primates. https://app.cochat.ai/papers/10.1096/fj.12-212878
- The paper
- Suter, M. A., Chen, A., Burdine, M. S., Choudhury, M., Harris, R. A., Lane, R. H., Friedman, J. E., Grove, K. L., Tackett, A. J., & Aagaard, K. M. (2012). A maternal high‐fat diet modulates fetal SIRT1 histone and protein deacetylase activity in nonhuman primates. The FASEB Journal. https://doi.org/10.1096/fj.12-212878
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
