Tracy G. Anthony, Ph.D.

Professor of Nutritional Sciences

Environmental and Occupational Health Sciences Institute

Division of Toxicology

Rutgers School of Environmental and Biological Sciences

Foran Hall

59 Dudley Road – Room 166

New Brunswick, NJ 08901

Work Phone: 848-932-6331(office)


Tracy G Anthony, Ph.D.


Research Areas

The Anthony Lab studies homeostatic responses to changes in nutrient supply and environmental stress. Our experiments aim to identify dietary components and cellular processes that prevent and treat serious diseases and promote healthspan. Over the years my group has published numerous high impact publications which delineate mechanisms of metabolic and proteostasis control by diet, drugs, genetics and environmental stressors. These works have spanned many organ systems including endocrine, gastrointestinal, hepatobiliary, immune, lymphatic, muscular and the central nervous system. With respect to diet and nutrient supply, we study how amino acid insufficiency or imbalance alters tissue proteostasis in the whole animal. We use experimental models that alter amino acid availability and work to understand how altering the supply of amino acids, in total or individually, is sensed and communicated under different metabolic states. We also are interested in metabolic and molecular responses to exercise and the crosstalk between diet and physical activity. Current projects in the laboratory may be grouped into the following areas:

Homeostatic responses to amino acid insufficiency

Alterations in amino acid availability and balance are sensed by overlapping signal transduction cascades. Two major signaling nodes responsive to amino acid supply in mammals are the: 1) Integrated Stress Response (ISR), also called the Amino Acid Response (AAR) and 2) mechanistic Target Of Rapamycin Complex 1 (mTORC1) pathway. While the mTORC1 pathway functions as a sensor of amino acid abundance to stimulate growth, the ISR/AAR is activated by amino acid deprivation to slow growth and instead favor cytoprotective and adaptive processes. How these signaling pathways work together to regulate gene-specific translation and promote cellular resilience is a major research focus of the lab. This project uses genetic strains of mice with targeted deficiencies in the ISR/AAR in combination of sophisticated molecular biology and stable isotope techniques to assess control of proteostasis and metabolism in tissues of mice.

Mechanisms of toxicity by asparaginase

Asparaginase is an important part of the remission induction regimen for treating acute lymphoblastic leukemia, the most common childhood cancer. The enzyme breaks down circulating asparagine and glutamine, creating a physiologically relevant model of amino acid deficiency. In leukemic cells which express very little asparagine synthetase (the enzyme that makes asparagine), asparaginase inflicts a lethal amino acid starvation. Yet for reasons not completely understood, cancer patients may unpredictably suffer severe complications, such as thromboembolism, liver failure and pancreatitis. Our lab was the first to report that phosphorylation of the translation factor, eIF2, by the amino acid sensor, GCN2, is activated by asparaginase. We were also the first to describe the ISR as the body’s first responder to asparaginase exposure. Since then we have gone on to show the impact of obesity and age on liver responses to asparaginase and we continue to use this agent as a research tool and study it to improve its efficacy to treat cancer and other diseases. This project utilizes a combination of biochemical, dietary, metabolic and molecular approaches in mice to identify mechanisms by which asparaginase causes metabolic complications and cell death. These results will be used to increase the safety and efficacy of asparaginase and to develop improved personalized approaches to the treatment of serious diseases.

ER stress and the Unfolded Protein Response

Chemical, environmental or nutritional perturbations that disrupt homeostasis within the endoplasmic reticulum (ER) activate a mechanism called the Unfolded Protein Response (UPR, also called the ER Stress Response). Phosphorylation of the translation factor eIF2 by PERK constitutes one arm of the UPR which serves to alleviate cell stress and re-establish homeostasis through a reprogramming of gene expression driven by the transcription factor ATF4. My laboratory is interested in exploring how the PERK-eIF2-ATF4 arm of the UPR contributes to the overall cellular effort to promote cellular adaptation and survival in response to a wide variety of environmental insults and proteotoxic stress agents.

Dietary protein, exercise, muscle growth and metabolic homeostasis

The interface of dietary protein and exercise as it relates to optimization of lean body mass is a longstanding area of interest and study. Previous projects in the lab include identifying metabolic and transcriptional signatures in the muscle of exercised horses, and varying the composition, distribution, source and/or timing of dietary protein on mTORC1 signaling and protein synthesis in mice. Information gained in this area will be targeted to relevant populations to improve performance and promote recovery and resilience.

Recent Publications

Nofal M, Wang T, Yang L, Jankowski CSR, Hsin-Jung Li S, Han S, Parsons L, Frese AN, Gitai Z, Anthony TG, Wühr M, Sabatini DM, Rabinowitz JD. GCN2 adapts protein synthesis to scavenging-dependent growth. Cell Syst. 2022 Feb 16;13(2):158-172.e9. doi: 10.1016/j.cels.2021.09.014. Epub 2021 Oct 26. PubMed PMID: 34706266; PubMed Central PMCID: PMC8961722.

Misra J, Holmes MJ, T Mirek E, Langevin M, Kim HG, Carlson KR, Watford M, Dong XC, Anthony TG, Wek RC. Discordant regulation of eIF2 kinase GCN2 and mTORC1 during nutrient stress. Nucleic Acids Res. 2021 Jun 4;49(10):5726-5742. doi: 10.1093/nar/gkab362. PubMed PMID: 34023907; PubMed Central PMCID: PMC8191763.
Jonsson WO, Margolies NS, Mirek ET, Zhang Q, Linden MA, Hill CM, Link C, Bithi N, Zalma B, Levy JL, Pettit AP, Miller JW, Hine C, Morrison CD, Gettys TW, Miller BF, Hamilton KL, Wek RC, Anthony TG. Physiologic Responses to Dietary Sulfur Amino Acid Restriction in Mice Are Influenced by Atf4 Status and Biological Sex. J Nutr. 2021 Apr 8;151(4):785-799. doi: 10.1093/jn/nxaa396. PubMed PMID: 33512502; PubMed Central PMCID: PMC8030708.
Lackey AI, Chen T, Zhou YX, Bottasso Arias NM, Doran JM, Zacharisen SM, Gajda AM, Jonsson WO, Córsico B, Anthony TG, Joseph LB, Storch J. Mechanisms underlying reduced weight gain in intestinal fatty acid-binding protein (IFABP) null mice. Am J Physiol Gastrointest Liver Physiol. 2020 Mar 1;318(3):G518-G530. doi: 10.1152/ajpgi.00120.2019. Epub 2020 Jan 6. PubMed PMID: 31905021; PubMed Central PMCID: PMC7099495.
Klein DJ, McKeever KH, Mirek ET, Anthony TG. Metabolomic Response of Equine Skeletal Muscle to Acute Fatiguing Exercise and Training. Front Physiol. 2020;11:110. doi: 10.3389/fphys.2020.00110. eCollection 2020. PubMed PMID: 32132934; PubMed Central PMCID: PMC7040365.
Bott AJ, Shen J, Tonelli C, Zhan L, Sivaram N, Jiang YP, Yu X, Bhatt V, Chiles E, Zhong H, Maimouni S, Dai W, Velasquez S, Pan JA, Muthalagu N, Morton J, Anthony TG, Feng H, Lamers WH, Murphy DJ, Guo JY, Jin J, Crawford HC, Zhang L, White E, Lin RZ, Su X, Tuveson DA, Zong WX. Glutamine Anabolism Plays a Critical Role in Pancreatic Cancer by Coupling Carbon and Nitrogen Metabolism. Cell Rep. 2019 Oct 29;29(5):1287-1298.e6. doi: 10.1016/j.celrep.2019.09.056. PubMed PMID: 31665640; PubMed Central PMCID: PMC6886125.
Park J, Zhu Q, Mirek E, Na L, Raduwan H, Anthony TG, Belden WJ. BMAL1 associates with chromosome ends to control rhythms in TERRA and telomeric heterochromatin. PLoS One. 2019;14(10):e0223803. doi: 10.1371/journal.pone.0223803. eCollection 2019. PubMed PMID: 31634367; PubMed Central PMCID: PMC6802832.
Nikonorova IA, Zhu Q, Signore CC, Mirek ET, Jonsson WO, Kong B, Guo GL, Belden WJ, Anthony TG. Age modulates liver responses to asparaginase-induced amino acid stress in mice. J Biol Chem. 2019 Sep 20;294(38):13864-13875. doi: 10.1074/jbc.RA119.009864. Epub 2019 Aug 14. PubMed PMID: 31413113; PubMed Central PMCID: PMC6755797.
Jonsson WO, Margolies NS, Anthony TG. Dietary Sulfur Amino Acid Restriction and the Integrated Stress Response: Mechanistic Insights. Nutrients. 2019 Jun 15;11(6). doi: 10.3390/nu11061349. Review. PubMed PMID: 31208042; PubMed Central PMCID: PMC6627990.
Neinast MD, Jang C, Hui S, Murashige DS, Chu Q, Morscher RJ, Li X, Zhan L, White E, Anthony TG, Rabinowitz JD, Arany Z. Quantitative Analysis of the Whole-Body Metabolic Fate of Branched-Chain Amino Acids. Cell Metab. 2019 Feb 5;29(2):417-429.e4. doi: 10.1016/j.cmet.2018.10.013. Epub 2018 Nov 15. PubMed PMID: 30449684; PubMed Central PMCID: PMC6365191.
Yimcharoen M, Kittikunnathum S, Suknikorn C, Nak-On W, Yeethong P, Anthony TG, Bunpo P. Effects of ascorbic acid supplementation on oxidative stress markers in healthy women following a single bout of exercise. J Int Soc Sports Nutr. 2019 Jan 21;16(1):2. doi: 10.1186/s12970-019-0269-8. PubMed PMID: 30665439; PubMed Central PMCID: PMC6341721.
Articles indexed in PubMed

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