Abstract
Zinc is one of the most studied minerals of the twenty-first century as it is practically involved in every function of the body. The importance of zinc has earned it the epithet “calcium of twenty-first century.” However, the bioavailability of zinc depends on the source of zinc and the subsequent processes of digestion, absorption and metabolism. Zinc from organic sources tends to be more available to animals than from inorganic sources. The complex gastrointestinal physiology of ruminants makes these processes even more intricate. Zinc in the rumen interacts with other substances altering its fate. Absorption of zinc from the gastrointestinal tract (GIT) was a mystery until the discovery of zinc transporter proteins. These discoveries opened new gates of wisdom and understanding about the tumultuous journey of zinc molecules through the complex GIT of ruminants. The decade-old concepts of zinc homeostasis largely based on the zinc complexes are jostling through the new theories with the focus on the free zinc ions. The present review briefly elucidates the processes of metabolism and homeostasis of zinc in ruminants.
![](http://media.springernature.com/m312/springer-static/image/art%3A10.1007%2Fs40011-018-1048-z/MediaObjects/40011_2018_1048_Fig1_HTML.png)
![](http://media.springernature.com/m312/springer-static/image/art%3A10.1007%2Fs40011-018-1048-z/MediaObjects/40011_2018_1048_Fig2_HTML.png)
![](http://media.springernature.com/m312/springer-static/image/art%3A10.1007%2Fs40011-018-1048-z/MediaObjects/40011_2018_1048_Fig3_HTML.png)
Similar content being viewed by others
References
Julius MC, Robert EL (2009) Illustrated dictionary of immunology, 3rd edn. CRC Press, USA
Keilin D, Mann T (1940) Carbonic anhydrase: purification and nature of the enzyme. Biochem J 34:1163
Suttle NF (2010) Mineral nutrition of livestock. Cabi, Wallingford
MacDonald RS (2000) The role of zinc in growth and cell proliferation. J Nutr 130:1500S–1508S. https://doi.org/10.1093/jn/130.5.1500S
Welch RM (1993) Zinc concentrations and forms in plants for humans and animals. In: Robson AD (ed) Zinc in soils and plants. Springer, Dordrecht, pp 183–195. https://doi.org/10.1007/978-94-011-0878-2_13
Cakmak I (2008) Enrichment of cereal grains with zinc: agronomic or genetic biofortification? Plant Soil 302:1–17. https://doi.org/10.1007/s11104-007-9466-3
McDonald P, Edward RA, Greenhalgh JFD, Morgan CA, Sinclair LA, Wilkinson RG (2007) Animal nutrition, 7th edn. Pearson, London
Aliarabi H (2005) Technology refinement for the preparation of chelated zinc and effect of its supplementation on growth and vitamin a utilization in cross bred calves. Doctoral dissertation, ICAR-NDRI, Karnal
Mir SH, Malik TA, Pal RP (2018) Necessitation of zinc supplementation to ruminants. Indian Farmer 5:142–146
White CL (1993) The zinc requirements of grazing ruminants. In: Robson AD (ed) Zinc in soils and plants: developments in plant and soil sciences. Academic Publishers, Dordrecht, pp 197–206
ICAR (2013) Nutrient composition of Indian feeds and fodders. Pusa, New Delhi
Malik TA, Mir SH, Pal RP (2017) Chelated versus inorganic zinc supplementation in ruminants. Nutr Food Sci Int J 4:555633. https://doi.org/10.19080/NFSIJ.2017.04.555633
Wright CL, Spears JW (2004) Effect of zinc source and dietary level on zinc metabolism in Holstein Calves. J Dairy Sci 87:1085–1091. https://doi.org/10.3168/jds.S0022-0302(04)73254-3
Cheng K, Lee S, Bae H (1999) Industrial application of rumen microbes. Asian Australas J Anim Sci 12:84–92
Goel G, Dagar SS, Raghav M, Bansal S (2015) Rumen: an underutilised niche for industrially important enzymes. In: Puniya AK, Singh R, Kamra DN (eds) Rumen microbiology: from evolution to revolution. Springer, New Delhi, pp 247–263. https://doi.org/10.1007/978-81-322-2401-3_17
Černík J, Pavlata L, Pechová A, Mišurová Ľ, Jokverová O, Luňáček J, Halouzka R (2013) Effects of peroral supplementation of different forms of zinc on the ruminal mucosa of goat kids—a morphometric study. Acta Vet Brno 82:399–403. https://doi.org/10.2754/avb201382040399
Arelovich H, Amela M, Martínez M, Bravo R, Torrea M (2014) Influence of different sources of zinc and protein supplementation on digestion and rumen fermentation parameters in sheep consuming low-quality hay. Small Rumin Res 121:175–182. https://doi.org/10.1016/j.smallrumres.2014.08.005
Eryavuz A, Dehority B (2009) Effects of supplemental zinc concentration on cellulose digestion and cellulolytic and total bacterial numbers in vitro. Anim Feed Sci Technol 15:175–183. https://doi.org/10.1016/j.anifeedsci.2009.01.008
Gerber J (2018) A review of mineral absorption with special consideration of chelation as a method to improve bioavailability of mineral supplements. Magnesium 21:27
Underwood E, Suttle N (1999) Zinc. In: Underwood E, Suttle N (eds) The mineral nutrition of livestock, 3rd edn. Cabi Publishing, London, pp 477–512
Wright C, Spears J, Webb K (2008) Uptake of zinc from zinc sulfate and zinc proteinate by ovine ruminal and omasal epithelia. J Anim Sci 86:1357–1363. https://doi.org/10.2527/jas.2006-650
Kornegay E, Cheng J, Schell C (1996) Apparent zinc absorption and dry matter digestibility in the stomach, intestine and lower colon of weanling pigs fed an inorganic or organic zinc sources added to adequate and deficient lysine diets. J Anim Sci 74(Suppl 1):182
Quarterman J (1985) Role of intestinal mucus on metal absorption. Trace elements in man and animals: TEMA 5. In: Proceedings of the fifth international symposium on trace elements in man and animals: Farnham Royal. Commonwealth Agricultural Bureaux, Slough, pp 400–401
Menard MP, Cousins RJ (1983) Zinc transport by brush border membrane vesicles from rat intestine. J Nutr 113:1434–1442. https://doi.org/10.1093/jn/113.7.1434
Cousins RJ, Liuzzi JP, Lichten LA (2006) Mammalian zinc transport, trafficking, and signals. J Biol Chem 281:24085–24089
Haney CJ, Grass G, Franke S, Rensing C (2005) New developments in the understanding of the cation diffusion facilitator family. J Ind Microbiol Biotechnol 32:215–226. https://doi.org/10.1007/s10295-005-0224-3
Coudray N, Valvo S, Hu M, Lasala R, Kim C, Vink M, Zhou M, Provasi D, Filizola M, Tao J, Fang J (2013) Inward-facing conformation of the zinc transporter YiiP revealed by cryoelectron microscopy. Proc Natl Acad Sci 110:2140–2145. https://doi.org/10.1073/pnas.1215455110
Podar D, Scherer J, Noordally Z, Herzyk P, Nies D, Sanders D (2012) Metal selectivity determinants in a family of transition metal transporters. J Biol Chem 287:3185–3196. https://doi.org/10.1074/jbc.M111.305649
Nebert DW, Gálvez-Peralta M, Hay EB, Li H, Johansson E, Yin C, Wang B, He L, Soleimani M (2012) ZIP14 and ZIP8 zinc/bicarbonate symporters in Xenopus oocytes: characterization of metal uptake and inhibition. Metallomics 4:1218–1225. https://doi.org/10.1039/c2mt20177a
Taylor KM, Hiscox S, Nicholson RI, Hogstrand C, Kille P (2012) Protein kinase CK2 triggers cytosolic zinc signaling pathways by phosphorylation of zinc channel ZIP7. Sci Signal 5:ra11. https://doi.org/10.1126/scisignal.2002585
Yuzbasiyan-Gurkan V, Bartlett E (2006) Identification of a unique splice site variant in SLC39A4 in bovine hereditary zinc deficiency, lethal trait A46: an animal model of acrodermatitis enteropathica. Genomics 88:521–526. https://doi.org/10.1016/j.ygeno.2006.03.018
Liuzzi JP, Bobo JA, Cui L, McMahon RJ, Cousins RJ (2003) Zinc transporters 1, 2 and 4 are differentially expressed and localized in rats during pregnancy and lactation. J Nutr 133:342–351. https://doi.org/10.1093/jn/133.2.342
Huang D, Hu Q, Fang S, Feng J (2016) Dosage effect of zinc glycine chelate on zinc metabolism and gene expression of zinc transporter in intestinal segments on rat. Biol Trace Elem Res 171:363–370. https://doi.org/10.1007/s12011-015-0535-9
Foote J, Delves H (1984) Albumin bound and alpha 2-macroglobulin bound zinc concentrations in the sera of healthy adults. J Clin Pathol 37:1050–1054. https://doi.org/10.1136/jcp.37.9.1050
Handing KB, Shabalin IG, Kassaar O, Khazaipoul S, Blindauer CA, Stewart AJ, Chruszcz M, Minor W (2016) Circulatory zinc transport is controlled by distinct interdomain sites on mammalian albumins. Chem Sci 7:6635–6648. https://doi.org/10.1039/C6SC02267G
Kassaar O, Schwarz-Linek U, Blindauer CA, Stewart AJ (2015) Plasma free fatty acid levels influence Zn2+-dependent histidine-rich glycoprotein–heparin interactions via an allosteric switch on serum albumin. J Thromb Haemost 13:101–110. https://doi.org/10.1111/jth.12771
Harris WR, Keen C (1989) Calculations of the distribution of zinc in a computer model of human serum. J Nutr 119:1677–1682. https://doi.org/10.1093/jn/119.11.1677
Rowe DJ, Bobilya DJ (2000) Albumin facilitates zinc acquisition by endothelial cells. Proc Soc Exp Biol Med 224:178–186. https://doi.org/10.1111/j.1525-1373.2000.22418.x
Mills CF (1989) Zinc in human biology. Springer, New York
Roohani N, Hurrell R, Kelishadi R, Schulin R (2013) Zinc and its importance for human health: an integrative review. J Res Med Sci 18:144
Lowe NM, Fekete K, Decsi T (2009) Methods of assessment of zinc status in humans: a systematic review. Am J Clin Nutr 89:2040S–2051S. https://doi.org/10.3945/ajcn.2009.27230G
Margoshes M, Vallee BL (1957) A cadmium protein from equine kidney cortex. J Am Chem Soc 79:4813–4814. https://doi.org/10.1021/ja01574a064
Dziegiel P, Pula B, Kobierzycki C, Stasiolek M, Podhorska-Okolow M (eds) (2016) Metallothioneins: structure and functions. In: Metallothioneins in normal and cancer cells. Springer, Cham, pp 3–20. https://doi.org/10.1007/978-3-319-27472-0_2
Bellomo EA, Meur G, Rutter GA (2011) Glucose regulates free cytosolic Zn2+ concentration, Slc39 (ZiP), and metallothionein gene expression in primary pancreatic islet beta-cells. J Biol Chem 286:25778–25789. https://doi.org/10.1074/jbc.M111.246082
National Research Council (2001) Nutrient requirements of dairy cattle: 2001. National Academies Press, Washington
Stake P, Miller W, Blackmon D, Gentry R, Neathery M (1974) Role of pancreas in endogenous zinc excretion in the bovine. J Nutr 104:1279–1284. https://doi.org/10.1093/jn/104.10.1279
King JC, Cousin RJ (2014) Zinc. In: Ross AC, Caballero B, Cousins RJ, Tucker KL, Ziegler TR (eds) Modern nutrition in health and disease, 11th edn. Lippincott, Williams & Wilkins, Baltimore, pp 189–205
Laity JH, Lee BM, Wright PE (2001) Zinc finger proteins: new insights into structural and functional diversity. Curr Opin Struct Biol 11:39–46. https://doi.org/10.1016/S0959-440X(00)00167-6
Colvin RA, Holmes WR, Fontaine CP, Maret W (2010) Cytosolic zinc buffering and muffling: their role in intracellular zinc homeostasis. Metallomics 2:306–317. https://doi.org/10.1039/B926662C
Wellenreuther G, Cianci M, Tucoulou R, Meyer-Klaucke W, Haase H (2009) The ligand environment of zinc stored in vesicles. Biochem Biophys Res Commun 380:198–203. https://doi.org/10.1016/j.bbrc.2009.01.074
Acknowledgements
The authors thank Dr. Bibhudatta SK Panda (PhD Scholar), Animal Physiology Division, ICAR-NDRI, Karnal, and anonymous reviewers for critically evaluating the manuscript.
Author information
Authors and Affiliations
Corresponding author
Ethics declarations
Conflict of interest
The authors declare that there is no conflict of interest to publish this manuscript.
Additional information
Significant statement The review presents a comprehensive outlook on the metabolism and homeostasis of zinc in ruminants. It will help to direct our efforts toward optimizing the zinc nutrition in ruminants.
Rights and permissions
About this article
Cite this article
Mir, S.H., Mani, V., Pal, R.P. et al. Zinc in Ruminants: Metabolism and Homeostasis. Proc. Natl. Acad. Sci., India, Sect. B Biol. Sci. 90, 9–19 (2020). https://doi.org/10.1007/s40011-018-1048-z
Received:
Revised:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s40011-018-1048-z