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The many faces of interferon tau

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Abstract

Interferon tau (IFNT) was discovered as the pregnancy recognition signal in ruminants, but is now known to have a plethora of physiological functions in the mammalian uterus. The mammalian uterus includes, from the outer surface to the lumen, the serosa, myometrium and endometrium. The endometrium consists of the luminal, superficial glandular, and glandular epithelia, each with a unique phenotype, stromal cells, vascular elements, nerves and immune cells. The uterine epithelia secrete or selectively transport molecules into the uterine lumen that are collectively known as histotroph. Histotroph is required for growth and development of the conceptus (embryo and its associated extra-embryonic membranes) and includes nutrients such as amino acids and glucose, enzymes, growth factors, cytokines, lymphokines, transport proteins for vitamins and minerals and extracellular matrix molecules. Interferon tau and progesterone stimulate transport of amino acids in histotroph, particularly arginine. Arginine stimulates the mechanistic target of rapamycin pathway to induce proliferation, migration and protein synthesis by cells of the conceptus, and arginine is the substrate for synthesis of nitric oxide and polyamines required for growth and development of the conceptus. In ruminants, IFNT also acts in concert with progesterone from the corpus luteum to increase expression of genes for transport of nutrients into the uterine lumen, as well as proteases, protease inhibitors, growth factors for hematopoiesis and angiogenesis and other molecules critical for implantation and placentation. Collectively, the pleiotropic effects of IFNT contribute to survival, growth and development of the ruminant conceptus.

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Acknowledgments

Research in our laboratories was supported by National Research Initiative Competitive Grants from the Animal Reproduction Program (2008-35203-19120, 2009-35206-05211, 2011-67015-20067, and 2011-67015-20028) and Animal Growth & Nutrient Utilization Program (2008-35206-18764) of the USDA National Institute of Food and Agriculture, American Heart Association (10GRNT4480020, 13PRE17050104), National Institute of Health (1R01DK098662), Amercian Diabetes Association(1-13-JF-59), and Texas A&M AgriLife Research (H-8200). The important contributions of our graduate students and colleagues in this research are gratefully acknowledged.

Conflict of interest

The authors declare that there is no conflict of interest that could be perceived as prejudicing the impartiality of this review.

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Authors and Affiliations

  1. Department of Animal Science, Texas A&M University, 2471 TAMU, College Station, TX, 77843-2471, USA

    Fuller W. Bazer, Wei Ying, Xiaoqiu Wang, Kathrin A. Dunlap & Guoyao Wu

  2. Department of Veterinary Physiology and Pharmacology, Texas A&M University, College Station, TX, 77843, USA

    Beiyan Zhou

  3. Department of Veterinary Integrative Biosciences, Texas A&M University, College Station, TX, 77843, USA

    Greg A. Johnson

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  1. Fuller W. Bazer
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  2. Wei Ying
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Correspondence to Fuller W. Bazer.

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Bazer, F.W., Ying, W., Wang, X. et al. The many faces of interferon tau. Amino Acids 47, 449–460 (2015). https://doi.org/10.1007/s00726-014-1905-x

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