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Home / Equine Research Bank / Antibodies (Basel) / Binding Analysis of Human Immunoglobulin G as a Zinc-Binding...
Antibodies (Basel, Switzerland)2016; 5(2); 13; doi: 10.3390/antib5020013

Binding Analysis of Human Immunoglobulin G as a Zinc-Binding Protein.

Abstract: Human immunoglobulin G (IgG) binding with zinc ions was examined using zinc ions immobilized on chelating Sepharose beads (Zn-beads). Human IgG bound to Zn-beads but not to Sepharose beads (control beads). Mouse, rat, bovine and equine IgGs also bound to Zn-beads, similar to human IgG. The human IgG F(c) fragment showed zinc ion-binding activity whereas the Fab fragment did not. Ethylenediaminetetraacetic acid (EDTA)-treated Zn-beads no longer bound human IgG; however, washing the beads, followed by the addition of zinc ions, restored the binding activity towards human IgG. Zn-beads saturated with human fibrinogen could bind human IgG, and Zn-beads saturated with human IgG could bind fibrinogen. These results suggest that animal IgGs, including human, specifically bind zinc ions, probably through a zinc-binding site in the F(c) fragment and not in the Fab fragment. In addition, IgG and fibrinogen interact with each other and/or bind zinc ions through different mechanisms.
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Publication Date: 2016-05-19 PubMed ID: 31557994PubMed Central: PMC6698836DOI: 10.3390/antib5020013Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research article investigates how the protein Human Immunoglobulin G (IgG) interacts with zinc ions, suggesting that the IgG molecule has a specific site that enables it to bind with zinc, which could have implications for understanding immune system function.

Research Methodology

  • With the help of zinc ions immobilized on chelating Sepharose beads (Zn-beads), the researchers studied the binding capacity of Human Immunoglobulin G (IgG).
  • A control experiment was also conducted using non-immobilized Sepharose beads.
  • Different animal IgGs (from mouse, rat, cattle, and horse) were also tested to observe their binding phenomenon with Zn-beads.
  • Furthermore, the researchers separated human IgG into two fragments: F(c) and Fab, to identify which of these shows the zinc ion-binding activity.
  • An intervention using Ethylenediaminetetraacetic acid (EDTA) was also used to check if it could influence the binding process.

Findings

  • The research found that human IgG could bind to the Zn-beads, but not to the control beads. This suggests IgG’s affinity towards zinc.
  • Animal IgGs showed a similar binding behavior with the Zn-beads, hinting that this could be a common characteristic across species.
  • Upon dividing the human IgG, only the F(c) fragment demonstrated zinc ion-binding activity, suggesting this segment might be the zinc-binding site.
  • EDTA-treated Zn-beads lost their ability to bind human IgG, indicating the importance of zinc in the binding. But excitingly, this property was reclaimed when the beads were washed and re-exposed to zinc ions.
  • Experiments using human fibrinogen, another protein, revealed an interesting result that Zn-beads already saturated with either human fibrinogen or IgG could bind the other, suggesting an interaction between IgG, fibrinogen, and zinc ions.

Implications

  • The research suggests that animal IgGs, including those of humans, specifically bind with zinc ions likely through a binding site on the F(c) fragment.
  • Another observation was that IgG and fibrinogen interact with each other or bind to zinc ions, possibly through different mechanisms, which could lead to future investigations in understanding their role in the immune system or other biological processes.

Cite This Article

APA
Yamanaka Y, Matsugano S, Yoshikawa Y, Orino K. (2016). Binding Analysis of Human Immunoglobulin G as a Zinc-Binding Protein. Antibodies (Basel), 5(2), 13. https://doi.org/10.3390/antib5020013

Publication

Antibodies (Basel, Switzerland)
ISSN: 2073-4468
NlmUniqueID: 101587489
Country: Switzerland
Language: English
Volume: 5
Issue: 2
PII: 13

Researcher Affiliations

Yamanaka, Yu
  • Laboratory of Veterinary Biochemistry, School of Veterinary Medicine, Kitasato University, Aomori 034-8628, Japan. t-g-i-f@ezweb.ne.jp.
Matsugano, Sho
  • Laboratory of Veterinary Biochemistry, School of Veterinary Medicine, Kitasato University, Aomori 034-8628, Japan. matstgan@outlook.jp.
Yoshikawa, Yasunaga
  • Laboratory of Veterinary Biochemistry, School of Veterinary Medicine, Kitasato University, Aomori 034-8628, Japan. yyoshikawa@vmas.kitasato-u.ac.jp.
Orino, Koichi
  • Laboratory of Veterinary Biochemistry, School of Veterinary Medicine, Kitasato University, Aomori 034-8628, Japan. orino@vmas.kitasato-u.ac.jp.

Conflict of Interest Statement

The authors declare no conflict of interest.

References

This article includes 23 references
  1. Prasad AS. Zinc: A miracle element. Its discovery and impact on human health.. JSM Clin. Oncol. Res. 2014;2:1030–1036.
  2. Prasad AS. Zinc is an Antioxidant and Anti-Inflammatory Agent: Its Role in Human Health.. Front Nutr 2014;1:14.
    doi: 10.3389/fnut.2014.00014pmc: PMC4429650pubmed: 25988117google scholar: lookup
  3. Prasad AS. Zinc: role in immunity, oxidative stress and chronic inflammation.. Curr Opin Clin Nutr Metab Care 2009 Nov;12(6):646-52.
    doi: 10.1097/MCO.0b013e3283312956pubmed: 19710611google scholar: lookup
  4. Haase H, Rink L. The immune system and the impact of zinc during aging.. Immun Ageing 2009 Jun 12;6:9.
    doi: 10.1186/1742-4933-6-9pmc: PMC2702361pubmed: 19523191google scholar: lookup
  5. Bao B, Prasad AS, Beck FW, Bao GW, Singh T, Ali S, Sarkar FH. Intracellular free zinc up-regulates IFN-γ and T-bet essential for Th1 differentiation in Con-A stimulated HUT-78 cells.. Biochem Biophys Res Commun 2011 Apr 22;407(4):703-7.
    doi: 10.1016/j.bbrc.2011.03.084pmc: PMC3142693pubmed: 21439265google scholar: lookup
  6. Haase H, Rink L. Signal transduction in monocytes: the role of zinc ions.. Biometals 2007 Jun;20(3-4):579-85.
    doi: 10.1007/s10534-006-9029-8pubmed: 17453150google scholar: lookup
  7. Margalit O, Simon AJ, Yakubov E, Puca R, Yosepovich A, Avivi C, Jacob-Hirsch J, Gelernter I, Harmelin A, Barshack I, Rechavi G, D'Orazi G, Givol D, Amariglio N. Zinc supplementation augments in vivo antitumor effect of chemotherapy by restoring p53 function.. Int J Cancer 2012 Aug 15;131(4):E562-8.
    doi: 10.1002/ijc.26441pubmed: 21932419google scholar: lookup
  8. Cousins RJ, Liuzzi JP, Lichten LA. Mammalian zinc transport, trafficking, and signals.. J Biol Chem 2006 Aug 25;281(34):24085-9.
    doi: 10.1074/jbc.R600011200pubmed: 16793761google scholar: lookup
  9. Scott BJ, Bradwell AR. Identification of the serum binding proteins for iron, zinc, cadmium, nickel, and calcium.. Clin Chem 1983 Apr;29(4):629-33.
    pubmed: 6831689
  10. Mocchegiani E, Costarelli L, Giacconi R, Cipriano C, Muti E, Malavolta M. Zinc-binding proteins (metallothionein and alpha-2 macroglobulin) and immunosenescence.. Exp Gerontol 2006 Nov;41(11):1094-107.
    doi: 10.1016/j.exger.2006.08.010pubmed: 17030107google scholar: lookup
  11. Babaeva EE, Vorobyova UA, Denisova EA, Medvedeva DA, Cheknev SB. Binding of zinc cations to human serum gamma-globulin.. Bull Exp Biol Med 2006 May;141(5):602-5.
    doi: 10.1007/s10517-006-0232-ypubmed: 17181064google scholar: lookup
  12. Higashi S, Nagasawa K, Yoshikawa Y, Watanabe K, Orino K. Characterization analysis of human anti-ferritin autoantibodies.. Antibodies 2014;3:169–181.
    doi: 10.3390/antib3010169google scholar: lookup
  13. Orino K. Functional binding analysis of human fibrinogen as an iron- and heme-binding protein.. Biometals 2013 Oct;26(5):789-94.
    doi: 10.1007/s10534-013-9657-8pubmed: 23864430google scholar: lookup
  14. Hammarström L, Persson MA, Smith CI. Immunoglobulin subclass distribution of human anti-carbohydrate antibodies: aberrant pattern in IgA-deficient donors.. Immunology 1985 Apr;54(4):821-6.
    pmc: PMC1453556pubmed: 2579900
  15. Boehm TK, DeNardin E. Fibrinogen binds IgG antibody and enhances IgG-mediated phagocytosis.. Hum Antibodies 2008;17(3-4):45-56.
    pubmed: 19029661
  16. Porath J, Olin B. Immobilized metal ion affinity adsorption and immobilized metal ion affinity chromatography of biomaterials. Serum protein affinities for gel-immobilized iron and nickel ions.. Biochemistry 1983 Mar 29;22(7):1621-30.
    doi: 10.1021/bi00276a015pubmed: 6849872google scholar: lookup
  17. Tubek S, Grzanka P, Tubek I. Role of zinc in hemostasis: a review.. Biol Trace Elem Res 2008 Jan;121(1):1-8.
    doi: 10.1007/s12011-007-8038-ypubmed: 17968515google scholar: lookup
  18. Olinescu RM, Kummerow FA. Fibrinogen is an efficient antioxidant.. J Nutr Biochem 2001 Mar;12(3):162-169.
    doi: 10.1016/S0955-2863(00)00147-9pubmed: 11257465google scholar: lookup
  19. Kaplan IV, Attaelmannan M, Levinson SS. Fibrinogen is an antioxidant that protects beta-lipoproteins at physiological concentrations in a cell free system.. Atherosclerosis 2001 Oct;158(2):455-63.
    doi: 10.1016/S0021-9150(01)00452-Xpubmed: 11583726google scholar: lookup
  20. Nowak P, Zbikowska HM, Ponczek M, Kolodziejczyk J, Wachowicz B. Different vulnerability of fibrinogen subunits to oxidative/nitrative modifications induced by peroxynitrite: functional consequences.. Thromb Res 2007;121(2):163-74.
    doi: 10.1016/j.thromres.2007.03.017pubmed: 17467041google scholar: lookup
  21. Prasad AS, Meftah S, Abdallah J, Kaplan J, Brewer GJ, Bach JF, Dardenne M. Serum thymulin in human zinc deficiency.. J Clin Invest 1988 Oct;82(4):1202-10.
    doi: 10.1172/JCI113717pmc: PMC442670pubmed: 3262625google scholar: lookup
  22. Orino K. Physiological implications of mammalian ferritin-binding proteins interacting with circulating ferritin and a new aspect of ferritin- and zinc-binding proteins.. Biometals 2016 Feb;29(1):15-24.
    doi: 10.1007/s10534-015-9897-xpubmed: 26612741google scholar: lookup
  23. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.. Nature 1970 Aug 15;227(5259):680-5.
    doi: 10.1038/227680a0pubmed: 5432063google scholar: lookup

Citations

This article has been cited 3 times.
  1. Nair PM, Srivastava R, Chaudhary P, Kuraichya P, Dhaigude V, Naliyapara HB, Mondal G, Mani V. Impact of zinc, copper, manganese and chromium supplementation on growth performance and blood metabolic profile of Sahiwal (Bos indicus) male calves.. Biometals 2023 Aug 10;.
    doi: 10.1007/s10534-023-00527-4pubmed: 37563359google scholar: lookup
  2. Schloss JV. Nutritional deficiencies that may predispose to long COVID.. Inflammopharmacology 2023 Apr;31(2):573-583.
    doi: 10.1007/s10787-023-01183-3pubmed: 36920723google scholar: lookup
  3. Karunasinghe N. Zinc in Prostate Health and Disease: A Mini Review.. Biomedicines 2022 Dec 10;10(12).
    doi: 10.3390/biomedicines10123206pubmed: 36551962google scholar: lookup
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